|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
44-565 |
6.45e-176 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 530.89 E-value: 6.45e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 44 TRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVG 123
Cdd:COG1132 61 LLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 124 MFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQN 203
Cdd:COG1132 141 QLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 204 KELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPC 283
Cdd:COG1132 221 RELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 284 IDAFANARGAAYVIFDIIDNNPKIDSfSERGHKPDSIKGNLEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGC 363
Cdd:COG1132 301 LNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGS 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 364 GKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYD 443
Cdd:COG1132 378 GKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHE 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 444 FIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLST 523
Cdd:COG1132 458 FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLST 537
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 564345546 524 VRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQTSGS 565
Cdd:COG1132 538 IRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
76-1204 |
5.52e-175 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 555.79 E-value: 5.52e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 76 IRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISP 155
Cdd:PTZ00265 129 LKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 156 ILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAF 235
Cdd:PTZ00265 209 LIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMIN 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 236 LLIYASYALAFWYGSTLVIS--------KEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKI 307
Cdd:PTZ00265 289 GFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 308 DSfSERGHKPDSIKgNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISI-D 386
Cdd:PTZ00265 369 EN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInD 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 387 GQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYG----------------RGNVTMD-------------------- 430
Cdd:PTZ00265 447 SHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndms 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 431 ---------------------EIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 489
Cdd:PTZ00265 527 nttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 490 TSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRNADVI------------------------------------- 530
Cdd:PTZ00265 607 TSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdnkennnknnkddn 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 531 ----------AGFEDGVIVEQGSHSELIK-KEGIYFRLVNMQTSGSQILSEEFEVELSDEKAAG-GVAPNGWKARIFRNS 598
Cdd:PTZ00265 687 nnnnnnnnnkINNAGSYIIEQGTHDALMKnKNGIYYTMINNQKVSSKKSSNNDNDKDSDMKSSAyKDSERGYDPDEMNGN 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 599 TKKSLKSSRAHQNRLDVETNELDANV-PPVSFLKVLRLNKTEWPY---------------FVVGTLCAIANGALQPAFSI 662
Cdd:PTZ00265 767 SKHENESASNKKSCKMSDENASENNAgGKLPFLRNLFKRKPKAPNnlrivyreifsykkdVTIIALSILVAGGLYPVFAL 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 663 ILSEMIA-IFgpgDDTVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKNS 741
Cdd:PTZ00265 847 LYAKYVStLF---DFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHA 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 742 TGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFiYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEM 821
Cdd:PTZ00265 924 PGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSF-YFCPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEI 1002
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 822 EAAGKI----------------ATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYA 885
Cdd:PTZ00265 1003 NQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINS 1082
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 886 GCFRFGSYLIVNGHMRFKDVI-LVFSAIVLGAVAlGHASSFAPDYAKAKLSAAYLFSLFERQPLIDSYSREGMW---PDK 961
Cdd:PTZ00265 1083 FAYWFGSFLIRRGTILVDDFMkSLFTFLFTGSYA-GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKND 1161
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 962 FEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD---------------------- 1019
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqd 1241
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1020 --------------------------------PMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDN 1067
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1068 SrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQE 1147
Cdd:PTZ00265 1322 D--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1148 AL----DKAreGRTCIVIAHRLSTIQNADLIVVIDNGK-----VKEHGTHQQLL-AQKGIYFSMVNI 1204
Cdd:PTZ00265 1400 TIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGVYKKYVKL 1464
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
628-1209 |
1.25e-169 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 514.33 E-value: 1.25e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 628 SFLKVLRLNKTEWPYFVVGTLCAIANGALQPAFSIILSEMI-AIFGPGDdtvkQQKCNMFSLVFLGLGVLSFFTFFLQGF 706
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGD----LSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 707 TFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGW 786
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 787 QLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKA 866
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 867 HIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQ 946
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 947 PLIDSYSREGMwPDKFEGSVTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVL 1026
Cdd:COG1132 322 PEIPDPPGAVP-LPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1027 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQ 1106
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1107 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHG 1186
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|...
gi 564345546 1187 THQQLLAQKGIYFSMVNIQAGTQ 1209
Cdd:COG1132 557 THEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
325-561 |
1.09e-151 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 454.31 E-value: 1.09e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 325 EFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 404
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 405 VSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKIL 484
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 485 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 561
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
966-1205 |
2.42e-150 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 450.45 E-value: 2.42e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1045
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFDCSIAENIAYGDNSRvvSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQP 1125
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1126 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQ 1205
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
53-562 |
3.49e-142 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 447.36 E-value: 3.49e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 53 LGGGVLLAAYIQV------SFWTLAAGRQI-RKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdISKISEGIGDKVGMF 125
Cdd:COG2274 198 LAIGLLLALLFEGllrllrSYLLLRLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 126 FQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 205
Cdd:COG2274 277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 206 LERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF--SVGQAAPC 283
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLG--QLIAFNILSGRFlaPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 284 IDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDsIKGNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGC 363
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 364 GKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYD 443
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 444 FIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLST 523
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
490 500 510
....*....|....*....|....*....|....*....
gi 564345546 524 VRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQT 562
Cdd:COG2274 673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
633-949 |
1.29e-139 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 425.71 E-value: 1.29e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 633 LRLNKTEWPYFVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAG 712
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 713 EILTTRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLL 792
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 793 LSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGIT 872
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 873 FSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLI 949
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
52-558 |
2.03e-131 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 418.74 E-value: 2.03e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 52 GLGGGVLLAAYiqvsfwtlaaGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIAT 131
Cdd:TIGR00958 219 GLRGGSFNYTM----------ARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVM 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 132 FFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQK 211
Cdd:TIGR00958 289 LLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 212 HLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVGQAAPCIDAFAN-- 289
Cdd:TIGR00958 369 ALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGN----LVSFLLYQEQLGEAVRVLSYVYSgm 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 290 --ARGAAYVIFDIIDNNPKIDSfsERGHKPDSIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKST 367
Cdd:TIGR00958 445 mqAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKST 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 368 TVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMK 447
Cdd:TIGR00958 523 VAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIME 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 448 LPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAalDKAREGRTTIVIAHRLSTVRNA 527
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERA 680
|
490 500 510
....*....|....*....|....*....|.
gi 564345546 528 DVIAGFEDGVIVEQGSHSELIKKEGIYFRLV 558
Cdd:TIGR00958 681 DQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
625-1206 |
2.51e-131 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 418.47 E-value: 2.51e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 625 PPVSFLKVLRLNKTEWPYFVVGTLCAIANGALQPAFSIILseMIAIfgpgdDTVKQQKcNMFSLVFLGLGVLSFFTF--- 701
Cdd:COG2274 140 KPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFT--QVVI-----DRVLPNQ-DLSTLWVLAIGLLLALLFegl 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 702 --FLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLaTDAAQVQGATGTRLALIAQNTANLGTGII 779
Cdd:COG2274 212 lrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 780 ISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAgnaKRDKKEMEAAGKIAT---EAIENIRTVVSLTQERKFESMYVEKLH 856
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLR---RLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWENLLA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 857 GPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFkDVILVFSAIVLGAVA-LGHASSFAPDYAKAKLS 935
Cdd:COG2274 366 KYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQLIGLLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 936 AAYLFSLFERQPLIDSySREGMWPDKFEGSVTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE 1015
Cdd:COG2274 445 LERLDDILDLPPEREE-GRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1016 RFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQK 1095
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEALPMG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1096 YETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIV 1175
Cdd:COG2274 601 YDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII 680
|
570 580 590
....*....|....*....|....*....|.
gi 564345546 1176 VIDNGKVKEHGTHQQLLAQKGIYFSMVNIQA 1206
Cdd:COG2274 681 VLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
49-561 |
1.75e-125 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 398.30 E-value: 1.75e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 49 YYSGLGGGVL---LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMF 125
Cdd:TIGR02204 60 YFAFLLVVALvlaLGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 126 FQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 205
Cdd:TIGR02204 140 LRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 206 LERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIGAfSVGQAAPCI 284
Cdd:TIGR02204 220 RSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTlGQFVFYAVMVAG-SIGTLSEVW 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 285 DAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCG 364
Cdd:TIGR02204 299 GELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 365 KSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDF 444
Cdd:TIGR02204 379 KSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 445 IMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV 524
Cdd:TIGR02204 459 ISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538
|
490 500 510
....*....|....*....|....*....|....*..
gi 564345546 525 RNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 561
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
39-297 |
2.56e-122 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 380.08 E-value: 2.56e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 39 LEEEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGI 118
Cdd:cd18558 54 LEEEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 119 GDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIA 198
Cdd:cd18558 134 GDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 199 FGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVG 278
Cdd:cd18558 214 FGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAG 293
|
250
....*....|....*....
gi 564345546 279 QAAPCIDAFANARGAAYVI 297
Cdd:cd18558 294 QQVPSIEAFANARGAAYHI 312
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
616-1202 |
1.15e-120 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 389.85 E-value: 1.15e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 616 ETNELDANVPPVSFlKVLRLNKTEWPYFVVGTL---CAIANGALQPAFSiilSEMIAIFGpGDDTVKQQKCNMFSLVFLG 692
Cdd:TIGR00958 137 EAEQGQSETADLLF-RLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYT---GRVIDTLG-GDKGPPALASAIFFMCLLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 693 LGvlSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTA 772
Cdd:TIGR00958 212 IA--SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENK--TGELTSRLSSDTQTMSRSLSLNVNVLLRNLV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 773 NLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYV 852
Cdd:TIGR00958 288 MLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 853 EKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRfKDVILVFsaiVLGAVALGHA----SSFAPD 928
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVS-SGNLVSF---LLYQEQLGEAvrvlSYVYSG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 929 YAKAKLSAAYLFSLFERQPLIdsySREGMW-PDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGK 1007
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPNI---PLTGTLaPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGK 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1008 STVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHP 1087
Cdd:TIGR00958 521 STVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAAKAANAHD 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1088 FIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEalDKAREGRTCIVIAHRLST 1167
Cdd:TIGR00958 599 FIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLST 676
|
570 580 590
....*....|....*....|....*....|....*
gi 564345546 1168 IQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMV 1202
Cdd:TIGR00958 677 VERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
685-1205 |
1.07e-114 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 369.41 E-value: 1.07e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 685 MFSLVFLGLGVLSFFTFFLqgftFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 764
Cdd:TIGR02204 63 FLLVVALVLALGTAARFYL----VTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSSL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 765 ALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE 844
Cdd:TIGR02204 137 SMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 845 RKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDV-ILVFSAIVLGAvALGHAS 923
Cdd:TIGR02204 217 DAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgQFVFYAVMVAG-SIGTLS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 924 SFAPDYAKAKLSAAYLFSLFERQPLIDSYSREGMWPDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSS 1003
Cdd:TIGR02204 296 EVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1004 GCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGdnsRV-VSQDEIVRAAKE 1082
Cdd:TIGR02204 376 GAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG---RPdATDEEVEAAARA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1083 ANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIA 1162
Cdd:TIGR02204 453 AHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIA 532
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 564345546 1163 HRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQ 1205
Cdd:TIGR02204 533 HRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
59-561 |
1.22e-114 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 369.05 E-value: 1.22e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 59 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 138
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 139 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 218
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 219 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNaMTVFFSiligafSVGQAAPCIDAFANARG------ 292
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFIT------AMIALIRPLKSLTNVNApmqrgl 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 293 -AAYVIFDIIDNNPKIDsfsERGHKPDSIKGNLEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQL 371
Cdd:TIGR02203 302 aAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 372 LQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGR-GNVTMDEIKKAVKEANAYDFIMKLPQ 450
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 451 KFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVI 530
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
490 500 510
....*....|....*....|....*....|.
gi 564345546 531 AGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 561
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
324-557 |
1.27e-112 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 350.76 E-value: 1.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKI 483
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 484 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRL 557
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
195-566 |
3.77e-112 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 363.37 E-value: 3.77e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 195 TVIAFGGQNKELERYQKHLENAKKIGIKKAISAN---------ISMGIAFLLIYASYAlafwygstlVISKEYTIGNamt 265
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAllnfgqaliIALGLTAMMLMAAQG---------VVAGTMTVGD--- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 266 vfFsILIGAFSVGQAAPCidafaNARGAAY-----------VIFDIIDNNPKIDSfserghKPDSI-----KGNLEFSDV 329
Cdd:COG5265 298 --F-VLVNAYLIQLYIPL-----NFLGFVYreirqaladmeRMFDLLDQPPEVAD------APDAPplvvgGGEVRFENV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 330 HFSY-PSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQE 408
Cdd:COG5265 364 SFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 409 PVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:COG5265 441 TVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 489 ATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQTSGSQ 566
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEE 598
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
16-297 |
7.62e-108 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 340.61 E-value: 7.62e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 16 ILFSNIFHKCLNFSLSMLNPgRILEEEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWF 95
Cdd:cd18577 20 IVFGDLFDAFTDFGSGESSP-DEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 96 DIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKE 175
Cdd:cd18577 99 DKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 176 LAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVIS 255
Cdd:cd18577 179 QEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRD 258
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564345546 256 KEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVI 297
Cdd:cd18577 259 GEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
72-561 |
1.59e-107 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 350.47 E-value: 1.59e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 72 AGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDD------------ISKISEGigdkvgmffqaiATFFAGFIVG 139
Cdd:PRK11176 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREG------------ASIIGLFIMM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 140 FIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKI 219
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 220 GIKKAISANISMGIAFLLiyASYALAF--WYGSTLVISKEYTIGnAMTVFFSILIGAFSVGQAAPCIDA-FANARGAAYV 296
Cdd:PRK11176 241 GMKMVSASSISDPIIQLI--ASLALAFvlYAASFPSVMDTLTAG-TITVVFSSMIALMRPLKSLTNVNAqFQRGMAACQT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 297 IFDIIDNNPKIDsfsERGHKPDSIKGNLEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY 376
Cdd:PRK11176 318 LFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 377 DPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNV-TMDEIKKAVKEANAYDFIMKLPQKFDTL 455
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 456 VGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFED 535
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
490 500
....*....|....*....|....*.
gi 564345546 536 GVIVEQGSHSELIKKEGIYFRLVNMQ 561
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
628-1208 |
3.22e-107 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 349.02 E-value: 3.22e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 628 SFLKVLRLNKTEWPYFVVGTLCAIANGALQPAFSIILSEMI-AIFGPGDdtvkQQKCNMFSLVFLGLGVLSFFTFFLQGF 706
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRD----RSVLWWVPLVVIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 707 TFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGW 786
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 787 QLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE----RKFESMYVEKLhgpyRNS 862
Cdd:TIGR02203 155 QLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQayetRRFDAVSNRNR----RLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 863 VRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSL 942
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 943 FERQPLIDSYSREgmwPDKFEGSVTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA 1022
Cdd:TIGR02203 311 LDSPPEKDTGTRA---IERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1023 GTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQdEIVRAAKEANIHPFIETLPQKYETRVGD 1102
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRA-EIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1103 KGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKV 1182
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570 580
....*....|....*....|....*.
gi 564345546 1183 KEHGTHQQLLAQKGIYFSMVNIQAGT 1208
Cdd:TIGR02203 546 VERGTHNELLARNGLYAQLHNMQFRE 571
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
966-1198 |
1.46e-106 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 334.58 E-value: 1.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1045
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFDCSIAENIAYGDnsRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQP 1125
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1126 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIY 1198
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
324-561 |
1.47e-105 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 331.89 E-value: 1.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSY-PSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFI 402
Cdd:cd03253 1 IEFENVTFAYdPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPK 482
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 483 ILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 561
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
939-1206 |
2.17e-104 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 342.57 E-value: 2.17e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 939 LFSLFERQPLIdsYSREGMWPDKF-EGSVTFNEVVFNY-PTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLER 1016
Cdd:COG5265 332 MFDLLDQPPEV--ADAPDAPPLVVgGGEVRFENVSFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1017 FYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKY 1096
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDFIESLPDGY 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1097 ETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVV 1176
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
250 260 270
....*....|....*....|....*....|
gi 564345546 1177 IDNGKVKEHGTHQQLLAQKGIYFSMVNIQA 1206
Cdd:COG5265 565 LEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
643-939 |
2.47e-104 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 331.93 E-value: 2.47e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVK-----------------QQKCNMFSLVFLGLGVLSFFTFFLQG 705
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNItgnssglnssagpfeklEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 706 FTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYG 785
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 786 WQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRK 865
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 866 AHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMR-FKDVILVFSAIVLGAVALGHASSFAPdYAKAKLSAAYL 939
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSiGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
966-1205 |
4.43e-101 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 319.95 E-value: 4.43e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1045
Cdd:cd03253 1 IEFENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQP 1125
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1126 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQ 1205
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
322-552 |
2.91e-99 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 314.93 E-value: 2.91e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 322 GNLEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF 401
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 481
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 482 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEG 552
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
225-561 |
6.52e-97 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 321.53 E-value: 6.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 225 ISANISMGIAFLLiyasyalafwyGSTLVISKEYTIGN--AMTVFFSILIG------AF--SVGQAAPCIDAFanargaa 294
Cdd:PRK13657 248 AASTITMLAILVL-----------GAALVQKGQLRVGEvvAFVGFATLLIGrldqvvAFinQVFMAAPKLEEF------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 295 yviFDIIDNNPKIDsfsERGHKPD--SIKGNLEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL 372
Cdd:PRK13657 310 ---FEVEDAVPDVR---DPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 373 QRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKF 452
Cdd:PRK13657 382 QRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 453 DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAG 532
Cdd:PRK13657 462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541
|
330 340
....*....|....*....|....*....
gi 564345546 533 FEDGVIVEQGSHSELIKKEGIYFRLVNMQ 561
Cdd:PRK13657 542 FDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
964-1196 |
7.23e-97 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 308.39 E-value: 7.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 964 GSVTFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQ 1043
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1044 LGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIR 1123
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1124 QPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKG 1196
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
288-552 |
6.06e-95 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 315.54 E-value: 6.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 288 ANARGAAYVIFDIIDNNPKIdsfSERGHKPDSIKGN--LEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGK 365
Cdd:COG4988 302 ANGIAAAEKIFALLDAPEPA---APAGTAPLPAAGPpsIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 366 STTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFI 445
Cdd:COG4988 377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 446 MKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVR 525
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
250 260
....*....|....*....|....*..
gi 564345546 526 NADVIAGFEDGVIVEQGSHSELIKKEG 552
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
719-1207 |
2.41e-93 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 311.57 E-value: 2.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 719 LRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPF 798
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 799 IAVAgiveMKMLAGNAKRDKKEMEAA-GKIATEAIENIR--TVVSLTQERKFESMYVEKLHGPYR-NSVRKAHIYGITFS 874
Cdd:PRK11176 178 VSIA----IRVVSKRFRNISKNMQNTmGQVTTSAEQMLKghKEVLIFGGQEVETKRFDKVSNRMRqQGMKMVSASSISDP 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 875 ISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLIDSYSR 954
Cdd:PRK11176 254 IIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKR 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 955 EgmwPDKFEGSVTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKK 1034
Cdd:PRK11176 334 V---IERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1035 LNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVvSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQR 1114
Cdd:PRK11176 410 YTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQY-SREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQR 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1115 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
490
....*....|...
gi 564345546 1195 KGIYFSMVNIQAG 1207
Cdd:PRK11176 569 NGVYAQLHKMQFG 581
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
68-557 |
1.71e-91 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 305.92 E-value: 1.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 68 WTLaagRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDIskisegigDKVGMFF-QAIATFFAGFIVGFIrgwkL 146
Cdd:COG4987 82 ATL---RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlRVLLPLLVALLVILA----A 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 147 TLVIMAISPILGLSTA-------VWAKILSTFSDKELAAYAKAG-----AVAEEALGAIRTVIAFGGQNKELERYQKHLE 214
Cdd:COG4987 147 VAFLAFFSPALALVLAlglllagLLLPLLAARLGRRAGRRLAAAraalrARLTDLLQGAAELAAYGALDRALARLDAAEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 215 NAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVFFSILIGAFSVgqAAPCIDAFAN---AR 291
Cdd:COG4987 227 RLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALALFEA--LAPLPAAAQHlgrVR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 292 GAAYVIFDIIDNNPKIDSFSERGHKPDSikGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQL 371
Cdd:COG4987 304 AAARRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 372 LQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQK 451
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 452 FDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIA 531
Cdd:COG4987 461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
490 500
....*....|....*....|....*.
gi 564345546 532 GFEDGVIVEQGSHSELIKKEGIYFRL 557
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
921-1196 |
8.58e-88 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 295.51 E-value: 8.58e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 921 HASsfapdyAKAKLSAAYLFSLFErQPLIDSYSREGMWPDKFEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALV 1000
Cdd:COG4988 299 HAR------ANGIAAAEKIFALLD-APEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1001 GSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVSQDEIVRAA 1080
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAAL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1081 KEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV 1160
Cdd:COG4988 448 EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527
|
250 260 270
....*....|....*....|....*....|....*.
gi 564345546 1161 IAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKG 1196
Cdd:COG4988 528 ITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
959-1182 |
1.26e-87 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 282.82 E-value: 1.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 959 PDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQ 1038
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1039 WLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIA 1118
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1119 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKV 1182
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
131-562 |
1.89e-84 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 290.11 E-value: 1.89e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 131 TFFAgfiVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQ 210
Cdd:TIGR01846 268 VFLA---VMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 211 KHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAFS--VGQAAPCIDAFA 288
Cdd:TIGR01846 345 RQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQ--LVAFNMLAGRVTqpVLRLAQLWQDFQ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 289 NARGAAYVIFDIIdNNPKIDSFSERGHKPDsIKGNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTT 368
Cdd:TIGR01846 423 QTGIALERLGDIL-NSPTEPRSAGLAALPE-LRGAITFENIRFRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKSTL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 369 VQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKL 448
Cdd:TIGR01846 500 TKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISEL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 449 PQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNAD 528
Cdd:TIGR01846 580 PQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACD 659
|
410 420 430
....*....|....*....|....*....|....
gi 564345546 529 VIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQT 562
Cdd:TIGR01846 660 RIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
317-538 |
7.70e-83 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 269.73 E-value: 7.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 317 PDSIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR 396
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 397 CLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARA 476
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 477 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVI 538
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
324-536 |
1.23e-82 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 266.94 E-value: 1.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFSTTIAENIrygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 483
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564345546 484 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDG 536
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
715-1204 |
1.30e-82 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 281.27 E-value: 1.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 715 LTTRLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATgtrLALIAQNTANLGTGIIISFIYGWQLTLLLLS 794
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGL--ARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 795 VVPFIAVAGIVeMKMLAG--NAKRDKKEMEAAGKIATEAIENIRTVVSLT----QERKFESmyVEKLHGPYRNSVRKAHI 868
Cdd:COG4987 161 LALGLLLAGLL-LPLLAArlGRRAGRRLAAARAALRARLTDLLQGAAELAaygaLDRALAR--LDAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 869 Y-GITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDV-ILVFSAIVLGAVALGHASSFApDYAKAKLSAAYLFSLFERQ 946
Cdd:COG4987 238 LsALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLaLLVLAALALFEALAPLPAAAQ-HLGRVRAAARRLNELLDAP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 947 PLIdSYSREGMWPDKFeGSVTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVL 1026
Cdd:COG4987 317 PAV-TEPAEPAPAPGG-PSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1027 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQ 1106
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1107 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHG 1186
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
490
....*....|....*...
gi 564345546 1187 THQQLLAQKGIYFSMVNI 1204
Cdd:COG4987 552 THEELLAQNGRYRQLYQR 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
324-561 |
3.89e-82 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 268.20 E-value: 3.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKI 483
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 484 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 561
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
966-1205 |
5.16e-81 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 265.12 E-value: 5.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQL 1044
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 GIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQ 1124
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1125 PRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNI 1204
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 564345546 1205 Q 1205
Cdd:cd03252 237 Q 237
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
643-939 |
6.76e-81 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 267.03 E-value: 6.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMIAIF-----GPGDDTVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTT 717
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 718 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 797
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 798 FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 877
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 878 AFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYL 939
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
780-1196 |
1.30e-79 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 273.76 E-value: 1.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 780 ISFIYGWQLTLLLLS-VVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKiATEAIENIRTVVSLTQERKfesmYVEKLHGp 858
Cdd:PRK13657 150 LALFMNWRLSLVLVVlGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAH-VSDAIGNVSVVQSYNRIEA----ETQALRD- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 859 YRNSVRKAHI-----YGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFApdyAKAK 933
Cdd:PRK13657 224 IADNLLAAQMpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFI---NQVF 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 934 LSAAYLFSLF----------ERQPLIDsysregmwPDKFEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSS 1003
Cdd:PRK13657 301 MAAPKLEEFFevedavpdvrDPPGAID--------LGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1004 GCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEA 1083
Cdd:PRK13657 371 GAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1084 NIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1163
Cdd:PRK13657 449 QAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAH 528
|
410 420 430
....*....|....*....|....*....|...
gi 564345546 1164 RLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKG 1196
Cdd:PRK13657 529 RLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
641-1198 |
3.27e-79 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 276.05 E-value: 3.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 641 PYFVVGTLCAIANGALQPAFSIILSEMIAIfgpgddtvkQQKCNMFSLVFLGLGVLSFFTFFLQGFTfgkagEILTTRLR 720
Cdd:TIGR03796 157 LYLLLAGLLLVLPGLVIPAFSQIFVDEILV---------QGRQDWLRPLLLGMGLTALLQGVLTWLQ-----LYYLRRLE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 721 ---SMAFKA-----MLRQDMSWFDdhKNSTGALSTRLATdAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLL 792
Cdd:TIGR03796 223 iklAVGMSArflwhILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 793 lsvvpfIAVAGIVEMKMLAGNAKR---DKKEMEAAGKIATEAIENIRTVVSLtQERKFESMYVEKLHGPYRNSVRKAHIY 869
Cdd:TIGR03796 300 ------IAFAAINVLALQLVSRRRvdaNRRLQQDAGKLTGVAISGLQSIETL-KASGLESDFFSRWAGYQAKLLNAQQEL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 870 GITFSI----SQAFMYFSYAGCFRFGSYLIVNGHMR------FKDVILVFSAIVLGAVALGHA-SSFAPDYAKAKLSAAY 938
Cdd:TIGR03796 373 GVLTQIlgvlPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGTlQELEGDLNRLDDVLRN 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 939 -LFSLFERQPLIDSYSREgmwPDKFEGSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF 1017
Cdd:TIGR03796 453 pVDPLLEEPEGSAATSEP---PRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1018 YDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYE 1097
Cdd:TIGR03796 529 YQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSRPGGYD 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1098 TRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALdkAREGRTCIVIAHRLSTIQNADLIVVI 1177
Cdd:TIGR03796 607 AELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVL 684
|
570 580
....*....|....*....|.
gi 564345546 1178 DNGKVKEHGTHQQLLAQKGIY 1198
Cdd:TIGR03796 685 ERGKVVQRGTHEELWAVGGAY 705
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
966-1181 |
1.18e-78 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 255.77 E-value: 1.18e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1045
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFDCSIAENIaygdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkgtqLSGGQKQRIAIARALIRQP 1125
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1126 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGK 1181
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
782-1207 |
2.69e-75 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 264.30 E-value: 2.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 782 FIYGWQLTLLLLSVVPF-----IAVAGIVEMKMlagnakRDKKEMEAAGK-IATEAIENIRTVVSLTQERKFESMYVEKL 855
Cdd:TIGR01846 274 FFYSPTLTGVVIGSLVCyallsVFVGPILRKRV------EDKFERSAAATsFLVESVTGIETIKATATEPQFQNRWDRQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 856 HGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVIL--VFSAIVLGAVAlgHASSFAPDYAKAK 933
Cdd:TIGR01846 348 AAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAfnMLAGRVTQPVL--RLAQLWQDFQQTG 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 934 LSAAYLFSLFErQPlIDSYSREGMWPDKFEGSVTFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL 1013
Cdd:TIGR01846 426 IALERLGDILN-SP-TEPRSAGLAALPELRGAITFENIRFRYAPDS-PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1014 LERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAKEANIHPFIETLP 1093
Cdd:TIGR01846 503 LQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELP 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1094 QKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADL 1173
Cdd:TIGR01846 581 QGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDR 660
|
410 420 430
....*....|....*....|....*....|....
gi 564345546 1174 IVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQAG 1207
Cdd:TIGR01846 661 IIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
645-1210 |
3.51e-74 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 271.13 E-value: 3.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 645 VGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKQqkcnMFSLVFLGLG--VLSFFTFFLQGFTFGKageILTTrLRSM 722
Cdd:PTZ00265 64 VSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDI----IFSLVLIGIFqfILSFISSFCMDVVTTK---ILKT-LKLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 723 AFKAMLRQDMSWFDDHKNSTgaLSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 802
Cdd:PTZ00265 136 FLKSVFYQDGQFHDNNPGSK--LTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 803 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMY--VEKLHGPY---RNSVRKAHIYGItfsisQ 877
Cdd:PTZ00265 214 GVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFnlSEKLYSKYilkANFMESLHIGMI-----N 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 878 AFMYFSYAGCFRFGSYLIV--------NGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLI 949
Cdd:PTZ00265 289 GFILASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 950 DSYSREGMWPDKfeGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLL-D 1028
Cdd:PTZ00265 369 ENNDDGKKLKDI--KKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInD 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1029 GQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAY------------------------GDNSR--------------- 1069
Cdd:PTZ00265 447 SHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRnscrakcagdlndms 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1070 ----------------VVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:PTZ00265 527 nttdsneliemrknyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEA 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1134 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQNADLIVVIDNGK------------------------------ 1181
Cdd:PTZ00265 607 TSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddn 686
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 564345546 1182 -----------------VKEHGTHQQLLAQK-GIYFSMVNIQAGTQN 1210
Cdd:PTZ00265 687 nnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYYTMINNQKVSSK 733
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
225-571 |
2.64e-73 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 255.58 E-value: 2.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 225 ISANISMGIAFLLiyasyalafwyGSTLVISKEYTIGNAMTV--FFSILIGAFSvgQAAPCIDAFANARGAAYVIFDIID 302
Cdd:TIGR01192 248 MASTISMMCILVI-----------GTVLVIKGELSVGEVIAFigFANLLIGRLD--QMSGFITQIFEARAKLEDFFDLED 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 303 NNPKIDSFSERGHKPDsIKGNLEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGT 382
Cdd:TIGR01192 315 SVFQREEPADAPELPN-VKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 383 ISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQ 462
Cdd:TIGR01192 392 ILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNR 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 463 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 542
Cdd:TIGR01192 472 LSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKG 551
|
330 340
....*....|....*....|....*....
gi 564345546 543 SHSELIKKEGIYFRLvnMQTSGsqILSEE 571
Cdd:TIGR01192 552 SFQELIQKDGRFYKL--LRRSG--LLTNQ 576
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
16-275 |
1.83e-72 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 242.55 E-value: 1.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 16 ILFSNIFHKCLNFSLSMLNpGRILE----------EEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFH 85
Cdd:pfam00664 4 AILLAILSGAISPAFPLVL-GRILDvllpdgdpetQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 86 AILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWA 165
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 166 KILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALA 245
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 564345546 246 FWYGSTLVISKEYTIGN--AMTVFFSILIGAF 275
Cdd:pfam00664 243 LWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
17-307 |
4.48e-70 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 237.35 E-value: 4.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 17 LFSNIFHKCLNfSLSMLNPGRILEEeMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFD 96
Cdd:cd18578 27 VFAILFSKLIS-VFSLPDDDELRSE-ANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 97 IKG--TTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDK 174
Cdd:cd18578 105 DPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 175 ELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVI 254
Cdd:cd18578 185 NKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVA 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 564345546 255 SKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKI 307
Cdd:cd18578 265 NGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
643-917 |
3.81e-69 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 233.30 E-value: 3.81e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKQqKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 722
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ-ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 723 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 802
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 803 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYF 882
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 564345546 883 SYAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAV 917
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVafLSLFAQLFGPL 274
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
782-1205 |
1.26e-68 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 244.87 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 782 FIYGWQLTL----LLLSVVPFIAVAGIVEMKMLagnakrdKKEMEAAGKIATEAIENIRTVVSL----TQERKFesMYVE 853
Cdd:TIGR03797 271 FYYSWKLALvavaLALVAIAVTLVLGLLQVRKE-------RRLLELSGKISGLTVQLINGISKLrvagAENRAF--ARWA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 854 KLHGPYRNSVRKAH-IYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDvILVFSAivlgavALGHASSFAPDYAKA 932
Cdd:TIGR03797 342 KLFSRQRKLELSAQrIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGS-FLAFNT------AFGSFSGAVTQLSNT 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 933 KLSAAYLFSLFER-QPLIDS---YSREGMWPDKFEGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGK 1007
Cdd:TIGR03797 415 LISILAVIPLWERaKPILEAlpeVDEAKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1008 STVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsrVVSQDEIVRAAKEANIHP 1087
Cdd:TIGR03797 493 STLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1088 FIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLST 1167
Cdd:TIGR03797 570 DIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLST 647
|
410 420 430
....*....|....*....|....*....|....*...
gi 564345546 1168 IQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQ 1205
Cdd:TIGR03797 648 IRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
322-542 |
3.55e-68 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 228.24 E-value: 3.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 322 GNLEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF 401
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 481
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 482 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 542
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
286-530 |
4.57e-67 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 236.03 E-value: 4.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 286 AFANARGAAYVIFDIIDNNPKIdsFSERGHKPDSIKGNLEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGK 365
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 366 STTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFI 445
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 446 MKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVR 525
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
....*
gi 564345546 526 NADVI 530
Cdd:TIGR02857 522 LADRI 526
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
964-1182 |
1.35e-66 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 224.01 E-value: 1.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 964 GSVTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQ 1043
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1044 LGIVSQEPILFDCSIAENIAYGDnsRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIR 1123
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1124 QPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKV 1182
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
322-543 |
2.03e-65 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 220.44 E-value: 2.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 322 GNLEFSDVHFSYpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 400
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFSTTIAENI----RYgrgnvTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARA 476
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 477 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 543
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
88-561 |
3.53e-65 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 234.85 E-value: 3.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 88 LRQEMGWFDIKGTTELNTRlTDDISKISEGIGDKvgMFFQAIATFFAGFIVG--FIRGWKLTLVIMAISPILGLSTAVWA 165
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASR-AMGISQIRRILSGS--TLTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLVLG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 166 KILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANI-SMGIAFLLIYASYAL 244
Cdd:TIGR03797 297 LLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLlTVFNAVLPVLTSAAL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 245 aFWYGSTLVISKEYTIGNAMTvfFSILIGAFSVGqaapcIDAFANARGAAYVIF-------DIIDNNPKIDsfsERGHKP 317
Cdd:TIGR03797 377 -FAAAISLLGGAGLSLGSFLA--FNTAFGSFSGA-----VTQLSNTLISILAVIplwerakPILEALPEVD---EAKTDP 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 318 DSIKGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRC 397
Cdd:TIGR03797 446 GKLSGAIEVDRVTFRYRPDGPL-ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 398 LREFIGVVSQEPVLFSTTIAENIrYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARAL 477
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 478 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRttIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRL 557
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
....
gi 564345546 558 VNMQ 561
Cdd:TIGR03797 682 ARRQ 685
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
62-559 |
3.87e-64 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 232.32 E-value: 3.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 62 YIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdISKISEGIGDKV-GMFFQAIATFFAGFIVGF 140
Cdd:TIGR01193 214 YIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTIlSLFLDMWILVIVGLFLVR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 141 iRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGqnkELERYQK-------HL 213
Cdd:TIGR01193 293 -QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS---EAERYSKidsefgdYL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 214 ENAKKIGIKKAISANISMGIAFLLIyasyALAFWYGSTLVISKEYTIGNAMTvfFSILIGAFsvgqaapcIDAFANarga 293
Cdd:TIGR01193 369 NKSFKYQKADQGQQAIKAVTKLILN----VVILWTGAYLVMRGKLTLGQLIT--FNALLSYF--------LTPLEN---- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 294 ayvifdIIDNNPK----------------IDSFSERGHKPDS---IKGNLEFSDVHFSYPSRANIkiLKGLNLKVKSGQT 354
Cdd:TIGR01193 431 ------IINLQPKlqaarvannrlnevylVDSEFINKKKRTElnnLNGDIVINDVSYSYGYGSNI--LSDISLTIKMNSK 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 355 VALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYG-RGNVTMDEIK 433
Cdd:TIGR01193 503 TTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIW 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 434 KAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREgRT 513
Cdd:TIGR01193 583 AACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KT 661
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 564345546 514 TIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVN 559
Cdd:TIGR01193 662 IIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
936-1194 |
5.47e-64 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 228.09 E-value: 5.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 936 AAY--LFSLFERQPLidsySREGMWPDKFEGSVTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL 1013
Cdd:COG4618 303 QAYrrLNELLAAVPA----EPERMPLPRPKGRLSVENLTVVPP-GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1014 LERFYDPMAGTVLLDGQEAKklnvQWLRAQLG--I--VSQEPILFDCSIAENIA-YGDnsrvVSQDEIVRAAKEANIHPF 1088
Cdd:COG4618 378 LVGVWPPTAGSVRLDGADLS----QWDREELGrhIgyLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEM 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1089 IETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLST 1167
Cdd:COG4618 450 ILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSL 529
|
250 260
....*....|....*....|....*..
gi 564345546 1168 IQNADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:COG4618 530 LAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
715-1205 |
8.43e-64 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 227.67 E-value: 8.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 715 LTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR-LALIAQNTANLGTGIIISFIYGWQLTLLLL 793
Cdd:PRK10789 67 LAVELREDFYRQLSRQHPEFYLRHR--TGDLMARATNDVDRVVFAAGEGvLTLVDSLVMGCAVLIVMSTQISWQLTLLAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 794 SVVPFIAVAgivemkmlagnAKRDKKEMEAAGKIATEAIE--NIRTVVSLTQERKFESMYVEKLHGPY---------RNS 862
Cdd:PRK10789 145 LPMPVMAIM-----------IKRYGDQLHERFKLAQAAFSslNDRTQESLTSIRMIKAFGLEDRQSALfaadaedtgKKN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 863 VRKAHI---YGITFSISQAFMYFSYAGCfrfGSYLIVNGHMrfkdvilvfsaivlgavALGHASSFA--------PDYAK 931
Cdd:PRK10789 214 MRVARIdarFDPTIYIAIGMANLLAIGG---GSWMVVNGSL-----------------TLGQLTSFVmylglmiwPMLAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 932 AKL-------SAAY--LFSLFERQPLIDsysrEGMWP-DKFEGSVTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVG 1001
Cdd:PRK10789 274 AWMfnivergSAAYsrIRAMLAEAPVVK----DGSEPvPEGRGELDVNIRQFTYPQ-TDHPALENVNFTLKPGQMLGICG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1002 SSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVRAAK 1081
Cdd:PRK10789 349 PTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD--ATQQEIEHVAR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1082 EANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVI 1161
Cdd:PRK10789 427 LASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIIS 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 564345546 1162 AHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQ 1205
Cdd:PRK10789 507 AHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
330-1210 |
8.91e-64 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 238.34 E-value: 8.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 330 HFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEgTISIDgqdirnfnvrcLREFIGVVSQEP 409
Cdd:PLN03232 621 YFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV-----------IRGSVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 410 VLFSTTIAENIRYGrGNVTMDEIKKAVK-EANAYDFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:PLN03232 689 WIFNATVRENILFG-SDFESERYWRAIDvTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 489 ATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLvnMQTSGSqi 567
Cdd:PLN03232 767 PLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL--MENAGK-- 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 568 LSEEFEVELSDEKaaggVAPNGWKARIfrNSTKKSLKSSRAHQNRLDVETNELDANVPPVSFLKVLRLNKTEWPYFVVGT 647
Cdd:PLN03232 843 MDATQEVNTNDEN----ILKLGPTVTI--DVSERNLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMI 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 648 L--CAIANGALQPAFSIILSemiaiFGPGDDTVKQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFK 725
Cdd:PLN03232 917 LlvCYLTTEVLRVSSSTWLS-----IWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLN 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 726 AMLRQDMSWFddHKNSTGALSTRLATDAAQvqgatgtrlalIAQNTANLGTGIIISFiygWQL--TLLLLSVVPFIAVAG 803
Cdd:PLN03232 992 SILRAPMLFF--HTNPTGRVINRFSKDIGD-----------IDRNVANLMNMFMNQL---WQLlsTFALIGTVSTISLWA 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 804 IVEMKML-------AGNAKRDKKEMEAAGKIATEAI--ENIRTVVSLTQERKFESMyvEKLHGPYRN------------- 861
Cdd:PLN03232 1056 IMPLLILfyaaylyYQSTSREVRRLDSVTRSPIYAQfgEALNGLSSIRAYKAYDRM--AKINGKSMDnnirftlantssn 1133
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 862 ---SVRKAHIYGITFSISQAFMYFSYAGcfrfgsyliVNGHMRFKDVILVFSAIVLGAVALghASSFAPDYAKAKLS--- 935
Cdd:PLN03232 1134 rwlTIRLETLGGVMIWLTATFAVLRNGN---------AENQAGFASTMGLLLSYTLNITTL--LSGVLRQASKAENSlns 1202
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 936 ---AAYLFSLFERQPLIDSYSRE-GMWPDKfeGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTV 1010
Cdd:PLN03232 1203 verVGNYIDLPSEATAIIENNRPvSGWPSR--GSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSM 1278
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1011 VQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVRAAKEANIHPFIE 1090
Cdd:PLN03232 1279 LNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVID 1355
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1091 TLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN 1170
Cdd:PLN03232 1356 RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID 1435
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 564345546 1171 ADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQAGTQN 1210
Cdd:PLN03232 1436 CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
928-1177 |
9.66e-64 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 226.40 E-value: 9.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 928 DYAKAKLSAAYLFSLFERQPLIDSYSREGMWPDkfEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGK 1007
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAPVTAAP--ASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1008 STVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVSQDEIVRAAKEANIHP 1087
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1088 FIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1167
Cdd:TIGR02857 440 FVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLAL 519
|
250
....*....|
gi 564345546 1168 IQNADLIVVI 1177
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
39-560 |
1.10e-63 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 238.00 E-value: 1.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 39 LEEEMTRYAYYYSGLGGGVLLAAYIQvSFWTLAAGRQIRK-IRQKFFHAILRQEMGWFDIKGTTE--LNTRLTDDISKIS 115
Cdd:PTZ00265 861 LEANSNKYSLYILVIAIAMFISETLK-NYYNNVIGEKVEKtMKRRLFENILYQEISFFDQDKHAPglLSAHINRDVHLLK 939
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 116 EGIGDKVGMFFQAIATFFAGFIVGF----IRGWKLTLV------IMAISPILGLSTAVWAK-------ILSTFSDKELAA 178
Cdd:PTZ00265 940 TGLVNNIVIFTHFIVLFLVSMVMSFyfcpIVAAVLTGTyfifmrVFAIRARLTANKDVEKKeinqpgtVFAYNSDDEIFK 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 179 YAKAGAvaEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEY 258
Cdd:PTZ00265 1020 DPSFLI--QEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTI 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 259 TIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGHK---PDSIKGNLEFSDVHFSYPS 335
Cdd:PTZ00265 1098 LVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYIS 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 336 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-------------------------------------- 377
Cdd:PTZ00265 1178 RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvne 1257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 378 ----------------PTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANA 441
Cdd:PTZ00265 1258 fsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAI 1337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 442 YDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL----DKAreGRTTIVI 517
Cdd:PTZ00265 1338 DEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITI 1415
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 564345546 518 AHRLSTVRNADVIAGFED----GVIVE-QGSHSELIK-KEGIYFRLVNM 560
Cdd:PTZ00265 1416 AHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
55-589 |
2.10e-62 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 223.82 E-value: 2.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 55 GGVLLAA---YIQVSFWTL----AAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQ 127
Cdd:PRK10789 40 GTMVLIAvvvYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 128 AIATFFAGFIVGFIR-GWKLTLVIMAISPILGLSTAVWAKIL-----------STFSDKelaayakagavAEEALGAIRT 195
Cdd:PRK10789 120 SLVMGCAVLIVMSTQiSWQLTLLALLPMPVMAIMIKRYGDQLherfklaqaafSSLNDR-----------TQESLTSIRM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 196 VIAFGgqnkeLERYQKHL--ENAKKIGIKKA----ISANISMGIaFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFS 269
Cdd:PRK10789 189 IKAFG-----LEDRQSALfaADAEDTGKKNMrvarIDARFDPTI-YIAIGMANLLAIGGGSWMVVNGSLTLG-QLTSFVM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 270 ILigafsvGQAAPCIDAFA---N--ARG-AAYV-IFDIIDNNPKIDSfserGHKP-DSIKGNLEFSDVHFSYPsRANIKI 341
Cdd:PRK10789 262 YL------GLMIWPMLALAwmfNivERGsAAYSrIRAMLAEAPVVKD----GSEPvPEGRGELDVNIRQFTYP-QTDHPA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIR 421
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 422 YGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV 501
Cdd:PRK10789 411 LGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 502 QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQtsgsqilseEFEVELSDEKA 581
Cdd:PRK10789 491 LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ---------QLEAALDDAPE 561
|
....*...
gi 564345546 582 AGGVAPNG 589
Cdd:PRK10789 562 IREEAVDA 569
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
342-1201 |
4.96e-62 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 232.91 E-value: 4.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnvrclrefIGVVSQEPVLFSTTIAENIR 421
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 422 YGRGnvTMDEIKKAVKEANAY--DFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 499
Cdd:TIGR00957 721 FGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 500 EVqaaLDKA------REGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQTSGSQILSEEfe 573
Cdd:TIGR00957 798 HI---FEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLE-- 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 574 velsdEKAAGGVAPNGWKARIFRNST----------KKSLKSSRAH---QNRLDVETNELDANVPPVSFLKVLRLNKTE- 639
Cdd:TIGR00957 873 -----DSWTALVSGEGKEAKLIENGMlvtdvvgkqlQRQLSASSSDsgdQSRHHGSSAELQKAEAKEETWKLMEADKAQt 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 640 --------WPYFVVGTLCA--------IANGALQPAFSIILSEMIaifgpgDDTV---KQQKCNMFSLVFLGLGVLSFFT 700
Cdd:TIGR00957 948 gqvelsvyWDYMKAIGLFItflsiflfVCNHVSALASNYWLSLWT------DDPMvngTQNNTSLRLSVYGALGILQGFA 1021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 701 FFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTAN-LGTGII 779
Cdd:TIGR00957 1022 VFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvIGALIV 1099
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 780 ISFIygwqlTLLLLSVVPFIAVAGIVEMKMLAGNAkRDKKEMEAAGKIATEAIENiRTVVSLTQERKFEsmyveklhgpy 859
Cdd:TIGR00957 1100 ILLA-----TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLESVSRSPVYSHFN-ETLLGVSVIRAFE----------- 1161
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 860 rNSVRKAHIYGITFSISQAFMYfsyagcfrfgSYLIVNGHMRFKdVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYL 939
Cdd:TIGR00957 1162 -EQERFIHQSDLKVDENQKAYY----------PSIVANRWLAVR-LECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYS 1229
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 940 FSL--------------------FERQPLIDSYSREGMW-------PDKF--EGSVTFNEVVFNYPTRANVpVLQGLSLE 990
Cdd:TIGR00957 1230 LQVtfylnwlvrmssemetnivaVERLKEYSETEKEAPWqiqetapPSGWppRGRVEFRNYCLRYREDLDL-VLRHINVT 1308
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 991 VKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRV 1070
Cdd:TIGR00957 1309 IHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPFSQ 1385
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1071 VSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD 1150
Cdd:TIGR00957 1386 YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR 1465
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1151 KAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSM 1201
Cdd:TIGR00957 1466 TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
964-1187 |
5.64e-61 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 207.73 E-value: 5.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 964 GSVTFNEVVFNYptRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRA 1042
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALI 1122
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1123 RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGT 1187
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
321-550 |
6.94e-61 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 219.23 E-value: 6.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 321 KGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 400
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFSTTIAENI-RYGrgNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVR 479
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 480 NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKK 550
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
263-557 |
9.55e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 218.93 E-value: 9.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 263 AMTVF-----FSILI---GAFS-VGQaapCIdafanarGAAYVIFDIIDNNPKIdSFSERgHKPDSIKGNLEFSDVHFSY 333
Cdd:PRK11160 281 ALFVFaalaaFEALMpvaGAFQhLGQ---VI-------ASARRINEITEQKPEV-TFPTT-STAAADQVSLTLNNVSFTY 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 334 PSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFS 413
Cdd:PRK11160 349 PDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 414 TTIAENIRYGRGNVTmDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 493
Cdd:PRK11160 428 ATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 494 DTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRL 557
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
690-1211 |
2.29e-59 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 215.35 E-value: 2.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 690 FLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQ 769
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 770 NTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF-E 848
Cdd:PRK10790 149 SAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFgE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 849 SMyveklhgpyrNSVRKAHiygitfsisqafmYFSYAGCFRFGSYLIvnghmrfKDVILVFSAIVL------------GA 916
Cdd:PRK10790 229 RM----------GEASRSH-------------YMARMQTLRLDGFLL-------RPLLSLFSALILcgllmlfgfsasGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 917 VALGHASSFApdyakaklsaAYLFSLFErqPLIDSYSREGMWPDK-------FE------------------GSVTFNEV 971
Cdd:PRK10790 279 IEVGVLYAFI----------SYLGRLNE--PLIELTTQQSMLQQAvvagervFElmdgprqqygnddrplqsGRIDIDNV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 972 VFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEP 1051
Cdd:PRK10790 347 SFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1052 ILFDCSIAENIAYGdnsRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLD 1131
Cdd:PRK10790 425 VVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1132 EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQAGTQNL 1211
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEEL 581
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
656-1203 |
5.99e-59 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 216.91 E-value: 5.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 656 LQPAFSIILSEMIAIFGPgddtvkQQKCNMFSLVFLGL-------GVLSFFtfflQGFTFGKAGEILTTRLRSMAFKAML 728
Cdd:TIGR01193 171 ISIAGSYYLQKIIDTYIP------HKMMGTLGIISIGLiiayiiqQILSYI----QIFLLNVLGQRLSIDIILSYIKHLF 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 729 RQDMSWFDDHKnsTGALSTRLaTDAAQVQGATG-TRLALIAqntaNLGTGIIISFIYGWQ---LTLLLLSVVPFIAVAGI 804
Cdd:TIGR01193 241 ELPMSFFSTRR--TGEIVSRF-TDASSIIDALAsTILSLFL----DMWILVIVGLFLVRQnmlLFLLSLLSIPVYAVIII 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 805 VEMKMLAgnaKRDKKEMEAAGKIATEAIEN---IRTVVSLTQE----RKFESMYVEKLHGPYRNS----VRKAHIYGITF 873
Cdd:TIGR01193 314 LFKRTFN---KLNHDAMQANAVLNSSIIEDlngIETIKSLTSEaerySKIDSEFGDYLNKSFKYQkadqGQQAIKAVTKL 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 874 SISQAFMYFsyagcfrfGSYLIVNGHMRFKDVIlVFSAIV-LGAVALGHASSFAPDYAKAKLSAAYLFSLFerqpLIDSY 952
Cdd:TIGR01193 391 ILNVVILWT--------GAYLVMRGKLTLGQLI-TFNALLsYFLTPLENIINLQPKLQAARVANNRLNEVY----LVDSE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 953 SREGMWPDKFE---GSVTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDG 1029
Cdd:TIGR01193 458 FINKKKRTELNnlnGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1030 QEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGdNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSG 1109
Cdd:TIGR01193 536 FSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISG 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1110 GQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREgRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQ 1189
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHD 693
|
570
....*....|....
gi 564345546 1190 QLLAQKGIYFSMVN 1203
Cdd:TIGR01193 694 ELLDRNGFYASLIH 707
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
319-1202 |
1.54e-58 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 221.92 E-value: 1.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 319 SIKgnlefsDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LLQRLYDPTEGTISIDGQdirnfnvrc 397
Cdd:PLN03130 616 SIK------NGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT--------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 398 lrefIGVVSQEPVLFSTTIAENIRYGrGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARAL 477
Cdd:PLN03130 681 ----VAYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 478 VRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFR 556
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQK 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 557 LvnMQTSGSQILSEEFEVELSDEKAAGGVAPNGWKARIFRNStkkSLKSSRAHQNRLDVETNELDANVppVSFLKVLRLN 636
Cdd:PLN03130 836 L--MENAGKMEEYVEENGEEEDDQTSSKPVANGNANNLKKDS---SSKKKSKEGKSVLIKQEERETGV--VSWKVLERYK 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 637 KTEWPYFVVGTL--CAIANGALQPAFSIILSEMIaifgpGDDTVKQQKCNMFSLVFlglGVLSFftfflqgftfgkaGEI 714
Cdd:PLN03130 909 NALGGAWVVMILflCYVLTEVFRVSSSTWLSEWT-----DQGTPKTHGPLFYNLIY---ALLSF-------------GQV 967
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 715 LTT----------------RLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDaaqvqgatgtrLALIAQNTANLGTGI 778
Cdd:PLN03130 968 LVTllnsywlimsslyaakRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKD-----------LGDIDRNVAVFVNMF 1034
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 779 IISFiygWQL--TLLLLSVVPFIAVAGIveMKMLAG---------NAKRDKKEMEaagkiateaienirtvvSLTQERKF 847
Cdd:PLN03130 1035 LGQI---FQLlsTFVLIGIVSTISLWAI--MPLLVLfygaylyyqSTAREVKRLD-----------------SITRSPVY 1092
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 848 eSMYVEKLHG-----PYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYL-IVNGHMrfkdVILVFSAIVLGAVALGH 921
Cdd:PLN03130 1093 -AQFGEALNGlstirAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLeTLGGLM----IWLTASFAVMQNGRAEN 1167
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 922 ASSFAP------DYA-------KAKLSAAYL----FSLFER-----------QPLIDSYSREGMWPDKfeGSVTFNEVVF 973
Cdd:PLN03130 1168 QAAFAStmglllSYAlnitsllTAVLRLASLaensLNAVERvgtyidlpseaPLVIENNRPPPGWPSS--GSIKFEDVVL 1245
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 974 NYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPI 1052
Cdd:PLN03130 1246 RY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPV 1323
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1053 LFDCSIAENIaygDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDE 1132
Cdd:PLN03130 1324 LFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1133 ATSALDTESEKVVQEALDKarEGRTC--IVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFS-MV 1202
Cdd:PLN03130 1401 ATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkMV 1471
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
935-1201 |
1.80e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 206.60 E-value: 1.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 935 SAAYLFSLFERQPLIdSYSREGMWPDKfEGSVTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1014
Cdd:PRK11160 310 SARRINEITEQKPEV-TFPTTSTAAAD-QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1015 ERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYgdnsrvvsqdeivrAAKEANIHPFIETL-- 1092
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL--------------AAPNASDEALIEVLqq 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1093 ---------PQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1163
Cdd:PRK11160 453 vgleklledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH 532
|
250 260 270
....*....|....*....|....*....|....*...
gi 564345546 1164 RLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSM 1201
Cdd:PRK11160 533 RLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
188-550 |
4.90e-54 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 198.34 E-value: 4.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 188 EALGAIRTViafggQNKELERYQKHLENAKKIGIKKAISANISMgiAFLLIYASYALAFwyGSTLVISKEYTIGnaMTVF 267
Cdd:TIGR01842 194 EAMGMMGNL-----TKRWGRFHSKYLSAQSAASDRAGMLSNLSK--YFRIVLQSLVLGL--GAYLAIDGEITPG--MMIA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 268 FSILigafsVGQAAPCID-------AFANARGAAYVIFDIIDNNPkidsFSERGHKPDSIKGNLEFSDVHFSYPSrANIK 340
Cdd:TIGR01842 263 GSIL-----VGRALAPIDgaiggwkQFSGARQAYKRLNELLANYP----SRDPAMPLPEPEGHLSVENVTIVPPG-GKKP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENI 420
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 421 -RYGRgNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 499
Cdd:TIGR01842 413 aRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 564345546 500 EVQAALDKAR-EGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKK 550
Cdd:TIGR01842 492 ALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
188-521 |
6.09e-54 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 197.97 E-value: 6.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 188 EALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVF 267
Cdd:TIGR02868 198 DALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 268 FSILIGAFSVGQAAP-CIDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKG-NLEFSDVHFSYPSRAniKILKGL 345
Cdd:TIGR02868 277 VLLPLAAFEAFAALPaAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PVLDGV 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 346 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRG 425
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARP 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 426 NVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL 505
Cdd:TIGR02868 435 DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL 514
|
330
....*....|....*.
gi 564345546 506 DKAREGRTTIVIAHRL 521
Cdd:TIGR02868 515 LAALSGRTVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
322-577 |
8.79e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 198.79 E-value: 8.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 322 GNLEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF 401
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEPVLFSTTIAENIRYGRgNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 481
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 482 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 561
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
250
....*....|....*.
gi 564345546 562 TSGSQILSEEFEVELS 577
Cdd:PRK10790 576 LAGEELAASVREEESL 591
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
286-557 |
8.70e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 195.83 E-value: 8.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 286 AFANARGAAYVIFDIIDNNpkiDSFSERGHKPDSIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGK 365
Cdd:PRK11174 313 AKAQAVGAAESLVTFLETP---LAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 366 STTVQLLqrL-YDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDF 444
Cdd:PRK11174 390 TSLLNAL--LgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 445 IMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV 524
Cdd:PRK11174 468 LPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDL 547
|
250 260 270
....*....|....*....|....*....|...
gi 564345546 525 RNADVIAGFEDGVIVEQGSHSELIKKEGIYFRL 557
Cdd:PRK11174 548 AQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
324-551 |
1.36e-52 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 184.07 E-value: 1.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPV--LFSTTIAENIRYG---RGnVTMDEIKKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIA 474
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenLG-LPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 475 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIKKE 551
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
324-547 |
1.43e-52 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 183.92 E-value: 1.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGTISIDGQDIR--NFNVR 396
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYdlDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 397 CLREFIGVVSQEPVLFSTTIAENIRYG---RGNVTMDEIKKAVKEANAydfIMKLPQKfdtlVGDR--GAQLSGGQKQRI 471
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlHGIKLKEELDERVEEALR---KAALWDE----VKDRlhALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 472 AIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 547
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
324-548 |
3.10e-52 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 192.43 E-value: 3.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAN--IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF 401
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 ---IGVVSQEPV--LF-STTIAENIRYG---RGNVTMDEIKKAVKEAnaydfiMK---LPQKFdtlvGDR-GAQLSGGQK 468
Cdd:COG1123 341 rrrVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAEL------LErvgLPPDL----ADRyPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 469 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 545
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
...
gi 564345546 546 ELI 548
Cdd:COG1123 491 EVF 493
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
684-1194 |
4.20e-52 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 192.95 E-value: 4.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 684 NMFSLVFLGLGVLSFFTFF-----LQGFTFGKAGEILTTRLRSMAFKAMLRQDMswfddhkNSTGALSTRLATDAAQVQG 758
Cdd:TIGR01842 41 SVPTLLMLTVLALGLYLFLglldaLRSFVLVRIGEKLDGALNQPIFAASFSATL-------RRGSGDGLQALRDLDQLRQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 759 ATGtrlaliaqntanlGTGIIISFIYGWQLTLLLLSVV--PFIAVAGIVEMKMLAG----NAKRDKKEME-------AAG 825
Cdd:TIGR01842 114 FLT-------------GPGLFAFFDAPWMPIYLLVCFLlhPWIGILALGGAVVLVGlallNNRATKKPLKeateasiRAN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 826 KIATEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHMRFKD 904
Cdd:TIGR01842 181 NLADSALRNAEVIEAMGMMGNLTKRW-GRFHSKYLSAQSAASDRAGMLSnLSKYFRIVLQSLVLGLGAYLAIDGEITPGM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 905 VILvfSAIVLGAvALG---HASSFAPDYAKAKLSAAYLFSLFERQPLidsySREGMWPDKFEGSVTFNEVVFnYPTRANV 981
Cdd:TIGR01842 260 MIA--GSILVGR-ALApidGAIGGWKQFSGARQAYKRLNELLANYPS----RDPAMPLPEPEGHLSVENVTI-VPPGGKK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKklnvQWLRAQLG----IVSQEPILFDCS 1057
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK----QWDRETFGkhigYLPQDVELFPGT 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIA-YGDNsrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:TIGR01842 408 VAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1137 LDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:TIGR01842 485 LDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
987-1201 |
7.72e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 193.14 E-value: 7.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 987 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGD 1066
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1067 NSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQ 1146
Cdd:PRK11174 448 PD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1147 EALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSM 1201
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
325-536 |
5.33e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 178.81 E-value: 5.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 325 EFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 404
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 405 VSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEANAydfimklpqkfdtLVGDRG------AQLSGGQKQRIAIA 474
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlgLPEEEIEERVEEALE-------------LVGLEGlrdrspFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 475 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDG 536
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
324-538 |
3.02e-49 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 172.40 E-value: 3.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFSTTIAENIrygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 483
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 484 LLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVI 538
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
966-1195 |
1.93e-48 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 172.13 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1045
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPI--LFDCSIAENIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIAR 1119
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1120 ALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLAQK 1195
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
983-1191 |
3.67e-48 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 171.21 E-value: 3.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFD 1055
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENIAYGDNSRVVSQ----DEIVRAA-KEANIHPfietlpqkyetRVGDK--GTQLSGGQKQRIAIARALIRQPRVL 1128
Cdd:cd03260 95 GSIYDNVAYGLRLHGIKLkeelDERVEEAlRKAALWD-----------EVKDRlhALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1129 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1191
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
324-550 |
5.81e-48 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 171.22 E-value: 5.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF- 401
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 --IGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIKKAVKEanaydfimklpqkFDTLVG--DRG----AQLSGGQKQR 470
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPLeiAGVPKAEIEERVLE-------------LLELVGleDKAdaypAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 564345546 548 IKK 550
Cdd:cd03258 229 FAN 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
342-491 |
6.49e-48 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 167.82 E-value: 6.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFS-TTIAENI 420
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 421 RYGRgnvTMDEIKKAVKEANAYDFIMKLPQKF--DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 491
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
324-543 |
1.05e-47 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 174.11 E-value: 1.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF- 401
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 --IGVVSQEPVLFST-TIAENIRY-----GrgnVTMDEIKKAVKE----------ANAYdfimklPqkfdtlvgdrgAQL 463
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALpleiaG---VPKAEIRKRVAEllelvglsdkADAY------P-----------SQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 464 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVE 540
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 564345546 541 QGS 543
Cdd:COG1135 222 QGP 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
966-1194 |
1.11e-47 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 178.94 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRAN--VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWL 1040
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1041 RAQLGIVSQEPIL-FDC--SIAENIAYG-DNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRvgdKGTQLSGGQKQR 1114
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-----LERvgLPPDLADR---YPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1115 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1191
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
...
gi 564345546 1192 LAQ 1194
Cdd:COG1123 493 FAN 495
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
324-542 |
1.91e-47 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 167.49 E-value: 1.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNvRCLREFIG 403
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFSTTIAENIrygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrGAQLSGGQKQRIAIARALVRNPKI 483
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 484 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 542
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
971-1182 |
2.18e-47 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 167.01 E-value: 2.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 971 VVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1050
Cdd:cd03246 6 VSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1051 PILFDCSIAENIaygdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLL 1130
Cdd:cd03246 85 DELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1131 DEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIDNGKV 1182
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
324-542 |
2.26e-47 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 169.22 E-value: 2.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF- 401
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 --IGVVSQEPV-----LFS--TTIAENIRYGRGNVTMDEIKKAVKEA-----NAYDFIMKLPqkfdtlvgdrgAQLSGGQ 467
Cdd:cd03257 82 keIQMVFQDPMsslnpRMTigEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYP-----------HELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 468 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 542
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
324-519 |
6.47e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 167.30 E-value: 6.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:COG4619 1 LELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFSTTIAENI----RYGRGNVTMDEIKKAVKEANaydfimkLPQKF-DTLVgdrgAQLSGGQKQRIAIARALV 478
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPV----ERLSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564345546 479 RNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 519
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
982-1182 |
1.13e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.53 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1061
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1062 IA--YGDNSRVVSQDEIVRAAKEANIHPFIetlpqkYETRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1139
Cdd:COG4619 94 LPfpFQLRERKFDRERALELLERLGLPPDI------LDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564345546 1140 ESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:COG4619 164 ENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
968-1181 |
1.48e-46 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 166.10 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 968 FNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIV 1047
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1048 SQEP--ILFDCSIAENIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARAL 1121
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1122 IRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGK 1181
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
958-1187 |
1.53e-46 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 166.05 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 958 WPDkfEGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN 1036
Cdd:cd03369 1 WPE--HGEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1037 VQWLRAQLGIVSQEPILFDCSIAENI-AYGDNSrvvsqDEIVRAAkeanihpfietlpqkyeTRVGDKGTQLSGGQKQRI 1115
Cdd:cd03369 77 LEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEYS-----DEEIYGA-----------------LRVSEGGLNLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGT 1187
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
324-548 |
2.82e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 166.32 E-value: 2.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI--RNFNVRCLREF 401
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEPVLFS-TTIAENIRYG----RGnvtMDEiKKAVKEAnaydfiMKLPQKfdtlVG--DRG----AQLSGGQKQR 470
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvKK---MSK-AEAEERA------MELLER----VGlaDKAdaypAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELI 548
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFF 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
324-541 |
3.21e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 165.60 E-value: 3.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL---- 398
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 399 REFIGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIKKAVKEANAY----DFIMKLPqkfdtlvgdrgAQLSGGQKQRI 471
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLllAGVSRKERRERARELLERvglgDRLDHRP-----------SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 472 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIA-HRLSTVRNADVIAGFEDGVIVEQ 541
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
324-559 |
3.35e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.01 E-value: 3.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRcLREFIG 403
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFST-TIAENIRYGRG--NVTMDEIKKAVKEANAydfIMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRN 480
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 481 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFEDGVIVEQGSHSELIKK--EGIYFR 556
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARllEDVFLE 229
|
...
gi 564345546 557 LVN 559
Cdd:COG1131 230 LTG 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
966-1186 |
1.87e-45 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 161.71 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLG 1045
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFDCSIAENIaygdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkGTQLSGGQKQRIAIARALIRQP 1125
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1126 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHG 1186
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
324-538 |
3.16e-45 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 162.66 E-value: 3.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF- 401
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 ---IGVVSQEPVLFST-TIAENIRYGrgnVTMDEIKKAVKEANAYDFI--MKLPQKFDTLVgdrgAQLSGGQKQRIAIAR 475
Cdd:cd03255 81 rrhIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTVRNADVIAGFEDGVI 538
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
324-536 |
7.25e-45 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 160.05 E-value: 7.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR--NFNVRCLREF 401
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEPVLFST-TIAENIRYGrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRN 480
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 481 PKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 536
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
324-548 |
1.32e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 169.70 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPT---EGTISIDGQDIRNFNVRCLRE 400
Cdd:COG1123 5 LEVRDLSVRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEP--VLFSTTIAENIRYG--RGNVTMDEIKKAVKEANAYDFImklpqkfDTLVGDRGAQLSGGQKQRIAIARA 476
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGL-------ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 477 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELI 548
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
324-553 |
1.73e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 162.21 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF-NVRCLREFI 402
Cdd:TIGR04520 1 IEVENVSFSYPE-SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIA 474
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 475 RALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG------SHSE 546
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228
|
....*..
gi 564345546 547 LIKKEGI 553
Cdd:TIGR04520 229 LLKEIGL 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
322-543 |
1.75e-44 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 160.27 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 322 GNLEFSDVHFSYpsRANI-KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 400
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFSTTIAENI-RYGRgnVTMDEIKKAVKeanaydfimklpqkfdtlVGDRGAQLSGGQKQRIAIARALVR 479
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 480 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 543
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
324-542 |
2.52e-44 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 159.99 E-value: 2.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclREFIG 403
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFST-TIAENIRYG--RGNVTMDEIKKAVKEANAydfimklpqkfdtLVGDRG------AQLSGGQKQRIAIA 474
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLE-------------LVGLEGllnrypHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 475 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 542
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
965-1165 |
4.35e-44 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 168.69 E-value: 4.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQL 1044
Cdd:TIGR02868 334 TLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 GIVSQEPILFDCSIAEN--IAYGDnsrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALI 1122
Cdd:TIGR02868 412 SVCAQDAHLFDTTVRENlrLARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564345546 1123 RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRL 1165
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
324-549 |
6.29e-44 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 159.76 E-value: 6.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-- 401
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 -IGVVSQEPVLFST-TIAENIRYG---RGNVTMDEIKKAVkeanaydfIMKLpqkfdTLVGDRGA------QLSGGQKQR 470
Cdd:COG1127 83 rIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 564345546 548 IK 549
Cdd:COG1127 230 LA 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
324-547 |
1.72e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 162.19 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------RNfnvr 396
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 397 clrefIGVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIKKAVKEANAydfIMKLPQkfdtlVGDRG-AQLSGGQKQRI 471
Cdd:COG3842 79 -----VGMVFQDYALFPhLTVAENVAFGlrmRG-VPKAEIRARVAELLE---LVGLEG-----LADRYpHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 472 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSE 546
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222
|
.
gi 564345546 547 L 547
Cdd:COG3842 223 I 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
975-1186 |
3.20e-43 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 157.28 E-value: 3.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 975 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL---RAQLGIVSQE 1050
Cdd:cd03257 11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1051 PI-----LFdcSIAENIAygdnsrvvsqdEIVRAAKEANIHPFIETLPQKYETRVGDKGT-------QLSGGQKQRIAIA 1118
Cdd:cd03257 91 PMsslnpRM--TIGEQIA-----------EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryphELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1119 RALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1186
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
324-548 |
3.75e-43 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 157.46 E-value: 3.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFS-TTIAENIrygrGNV-TMDEIKKAVKEANAYDfIMKL----PQKFdtlvGDR-GAQLSGGQKQRIAIARA 476
Cdd:cd03295 79 YVIQQIGLFPhMTVEENI----ALVpKLLKWPKEKIRERADE-LLALvgldPAEF----ADRyPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 477 LVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRL-STVRNADVIAGFEDGVIVEQGSHSELI 548
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
325-536 |
6.52e-43 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 153.55 E-value: 6.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 325 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 404
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 405 VSQepvlfsttiaenirygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKIL 484
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 485 LLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFEDG 536
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
977-1186 |
6.98e-43 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 155.76 E-value: 6.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILFD- 1055
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPqkyetrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLD 1131
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1132 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHG 1186
Cdd:cd03259 156 EPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
324-547 |
9.49e-43 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 156.50 E-value: 9.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRA-NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFI 402
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVL-----FS--TTIAENIR-YGRGNVtMDEIKKAVKEANaydfimkLPqkfDTLVGDRGAQLSGGQKQRIAIA 474
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRiHGLPDR-EERIAELLEQVG-------LP---PSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 475 RALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 547
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADL 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
46-559 |
1.31e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 170.54 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 46 YAYYYSGLGGGVLLAAYIQvSFWTLAAG-RQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGM 124
Cdd:PLN03232 952 YIVVYALLGFGQVAVTFTN-SFWLISSSlHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 125 F----FQAIATFFAGFIVGFIRGWkltlvimAISPILGLSTAVWAKILSTFSD-KELAAYAKAGAVAE--EALGAIRTVI 197
Cdd:PLN03232 1031 FmnqlWQLLSTFALIGTVSTISLW-------AIMPLLILFYAAYLYYQSTSREvRRLDSVTRSPIYAQfgEALNGLSSIR 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 198 AFGGQNKELERYQKHLENAKKIGIKkAISAN-------ISMGIAFLLIYASYALAFW--------YGSTLVISKEYTIgN 262
Cdd:PLN03232 1104 AYKAYDRMAKINGKSMDNNIRFTLA-NTSSNrwltirlETLGGVMIWLTATFAVLRNgnaenqagFASTMGLLLSYTL-N 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 263 AMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGhkpdSIKgnleFSDVHFSYpsRANIK-I 341
Cdd:PLN03232 1182 ITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG----SIK----FEDVHLRY--RPGLPpV 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIR 421
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 422 -YGRGNVTmdEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAE 500
Cdd:PLN03232 1332 pFSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 501 VQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEG-IYFRLVN 559
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVH 1469
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
324-551 |
1.55e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 156.36 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVL-FSTTIAENIRYGR-------GNVT---MDEIKKAVKEANAYDFIMKLpqkFDTlvgdrgaqLSGGQKQRIA 472
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfGRPSaedREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 473 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELIK 549
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
..
gi 564345546 550 KE 551
Cdd:COG1120 228 PE 229
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
980-1194 |
1.65e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 155.54 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF 1054
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 -DCSIAENIAYGdnSRVV---SQDEIVRAAKEAnihpfietLpqkyeTRVG--DKG----TQLSGGQKQRIAIARALIRQ 1124
Cdd:COG1126 90 pHLTVLENVTLA--PIKVkkmSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1125 PRVLLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:COG1126 155 PKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
984-1135 |
3.10e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 151.26 E-value: 3.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILF-DCSIAENI 1062
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1063 AYGDNSRvvsqdEIVRAAKEANIHPFIETLPQKY--ETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:pfam00005 81 RLGLLLK-----GLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
324-519 |
4.44e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 155.25 E-value: 4.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclrefI 402
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVLFS-TTIAENIRYGrgnVTMDEIKKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIAIAR 475
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALG---LELRGVPKAERRERARELL--------ELVGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 519
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
966-1184 |
6.11e-42 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 153.40 E-value: 6.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEakklnVQWLRAQL 1044
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 GIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVRAAKEAnihpfIEtlpqkyetRVGDKGT------QLSGGQKQRIAI 1117
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-----LE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1118 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDN--GKVKE 1184
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
324-519 |
6.60e-42 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 153.01 E-value: 6.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPS-RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclrefI 402
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIKKAVKEANA----YDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIA 474
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelQG-VPKAEARERAEELLElvglSGFENAYP-----------HQLSGGMRQRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564345546 475 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 519
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
978-1193 |
7.09e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 154.19 E-value: 7.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 978 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL---- 1053
Cdd:COG1124 15 GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAslhp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 ---FDCSIAE--NIAYGDNSrvvsQDEIVRAAKEANihpfietLPQKYETRVGDkgtQLSGGQKQRIAIARALIRQPRVL 1128
Cdd:COG1124 95 rhtVDRILAEplRIHGLPDR----EERIAELLEQVG-------LPPSFLDRYPH---QLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1129 LLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:COG1124 161 LLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
324-538 |
1.15e-41 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 152.30 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRN--FNVRCLREF 401
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEPVLFS-TTIAENIRYGRgnVTMDEIKKAVKEANAYDFIMK--LPQKFDtlvgDRGAQLSGGQKQRIAIARALV 478
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 479 RNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVI 538
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
965-1187 |
3.69e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.26 E-value: 3.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQL 1044
Cdd:COG3842 5 ALELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 GIVSQEPILF-DCSIAENIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPqkyetrvgdkgTQLSGGQKQRIAIAR 1119
Cdd:COG3842 80 GMVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYP-----------HQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1120 ALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVIDNGKVKEHGT 1187
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
966-1194 |
6.55e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 158.91 E-value: 6.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGTVLLDGQEAKKLNVQWLRA 1042
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQEPI--LFDCSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETrvgdkgtQLSGGQKQRIAIARA 1120
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1121 LIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
324-549 |
7.79e-41 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 150.73 E-value: 7.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-- 401
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 -IGVVSQEPVLF-STTIAENIRYG---RGNVTMDEIKKAVKeanaydfiMKLpqkfdTLVGDRG------AQLSGGQKQR 470
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlreHTRLSEEEIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEVQA-ALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDlIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 564345546 548 IK 549
Cdd:cd03261 225 RA 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
966-1184 |
1.41e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.42 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGTVLLDGQEAKKLN----V 1037
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1038 QWLRAQLGIVSQEPILFDC-SIAENIA----YGDNSRVVSQDEIVRAAKEANIHPFIETLPqkyetrvgdkgTQLSGGQK 1112
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1113 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIDNGKVKE 1184
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
966-1194 |
2.73e-40 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 148.88 E-value: 2.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGTVLLDGQEAKKLN---VQ 1038
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1039 WLRAQLGIVSQEPILFDC-SIAENIAYGDNSRVVSQDEIVRAAKEanihpfieTLPQkyetrVG--DKG----TQLSGGQ 1111
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLE--------LLEL-----VGleDKAdaypAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1112 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTH 1188
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 564345546 1189 QQLLAQ 1194
Cdd:cd03258 226 EEVFAN 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
980-1194 |
3.04e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.06 E-value: 3.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlRAQLGIVSQEPILF-DCSI 1058
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGYVPQEPALYpDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 AENIAYGDNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDEL-----LELfgLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1137 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:COG1131 162 LDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
324-547 |
6.60e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 151.76 E-value: 6.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------RNfnvr 396
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdRN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 397 clrefIGVVSQEPVLF-STTIAENIRYG---RGnVTMDEIKKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIA 472
Cdd:COG3839 77 -----IAMVFQSYALYpHMTVYENIAFPlklRK-VPKAEIDRRVREAAE---LLGL----EDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 473 IARALVRNPKILLLDEATSALD------TESE-AEVQAALdkareGRTTIVIAH------RLstvrnADVIAGFEDGVIV 539
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHdqveamTL-----ADRIAVMNDGRIQ 213
|
....*...
gi 564345546 540 EQGSHSEL 547
Cdd:COG3839 214 QVGTPEEL 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
324-549 |
6.81e-40 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 150.59 E-value: 6.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGTISIDGQDIRNFNVRCLR 399
Cdd:COG0444 2 LEVRNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 400 EF----IGVVSQEPvlFS---------TTIAENIRYGRGnVTMDEIKKAVKEA-------NAYDFIMKLPQkfdtlvgdr 459
Cdd:COG0444 82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRIHGG-LSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 460 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIA- 531
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAv 223
|
250 260
....*....|....*....|
gi 564345546 532 --GfedGVIVEQGSHSELIK 549
Cdd:COG0444 224 myA---GRIVEEGPVEELFE 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
324-552 |
6.87e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 148.08 E-value: 6.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREfIG 403
Cdd:COG4555 2 IEVENLSKKYGKV---PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFST-TIAENIRY-GRGNvtmdEIKKAVKEANAYDFI--MKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVR 479
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfAELY----GLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 480 NPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKEG 552
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
966-1195 |
7.69e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 148.73 E-value: 7.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAK-KLNVQWLRAQL 1044
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 GIVSQEPilfD----CSIAEN-IAYGDNSRVVSQDEIVR----AAKEANIHPFIETLPQKyetrvgdkgtqLSGGQKQRI 1115
Cdd:TIGR04520 80 GMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHL-----------LSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 564345546 1194 QK 1195
Cdd:TIGR04520 226 QV 227
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
44-297 |
1.38e-39 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 148.86 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 44 TRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVG 123
Cdd:cd18557 36 NELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 124 MFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQN 203
Cdd:cd18557 116 QLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 204 KELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMT-VFFSILIgAFSVGQAAP 282
Cdd:cd18557 196 KEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSfILYTIMV-ASSVGGLSS 274
|
250
....*....|....*
gi 564345546 283 CIDAFANARGAAYVI 297
Cdd:cd18557 275 LLADIMKALGASERV 289
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
971-1192 |
1.58e-39 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 147.50 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 971 VVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1050
Cdd:COG1120 7 LSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1051 PIL-FDCSIAENIAYG------DNSRVVSQD-EIVRAA-KEANIHPFIEtlpQKYetrvgdkgTQLSGGQKQRIAIARAL 1121
Cdd:COG1120 84 PPApFGLTVRELVALGryphlgLFGRPSAEDrEAVEEAlERTGLEHLAD---RPV--------DELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1122 IRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
325-553 |
2.34e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.44 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 325 EFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 404
Cdd:PRK13632 9 KVENVSFSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 405 VSQEP--VLFSTTIAENIRYGRGN--VTMDEIKK----AVKEANAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIARA 476
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGLENkkVPPKKMKDiiddLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 477 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGI 553
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
325-546 |
4.52e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 149.18 E-value: 4.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 325 EFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-- 401
Cdd:PRK11153 3 ELKNISKVFPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 -IGVVSQE-PVLFSTTIAENIRYGR--GNVTMDEIKKAVKE----------ANAYdfimklPqkfdtlvgdrgAQLSGGQ 467
Cdd:PRK11153 83 qIGMIFQHfNLLSSRTVFDNVALPLelAGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 468 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIV-IAHRLSTVRN-ADVIAGFEDGVIVEQGSH 544
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQGTV 225
|
..
gi 564345546 545 SE 546
Cdd:PRK11153 226 SE 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
966-1184 |
5.28e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 146.39 E-value: 5.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEakklnVQWLRAQL 1044
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 GIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVRAAKEAnihpfIEtlpqkyetRVGDKG------TQLSGGQKQRIAI 1117
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERAREL-----LE--------LVGLAGfedaypHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1118 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVIDN--GKVKE 1184
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
324-538 |
8.09e-39 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 142.54 E-value: 8.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIG 403
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFST-TIAENIRYgrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqlSGGQKQRIAIARALVRNPK 482
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 483 ILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVI 538
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
966-1181 |
1.77e-38 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 142.61 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRANV--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPMAGTVLLDGQEAkklnvqwlr 1041
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGSIA--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1042 aqlgIVSQEPILFDCSIAENIAYG---DNSRVvsqDEIVRAAKeanIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIA 1118
Cdd:cd03250 70 ----YVSQEPWIQNGTIRENILFGkpfDEERY---EKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1119 RALIRQPRVLLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVIDNGK 1181
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
969-1194 |
2.17e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.16 E-value: 2.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 969 NEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVS 1048
Cdd:PRK13635 9 EHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1049 QEPilfD-----CSIAENIAYGDNSRVVSQDEIVR----AAKEANIHPFIETLPQKyetrvgdkgtqLSGGQKQRIAIAR 1119
Cdd:PRK13635 88 QNP---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1120 ALIRQPRVLLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
975-1187 |
2.28e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 146.76 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 975 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGTVLLDGQEAKKLNVQWLRA---QLGIV 1047
Cdd:COG1135 11 FPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELRAarrKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1048 SQEPILFD-CSIAENIAY-----GdnsrvVSQDEIvraakEANIHPFIEtlpqkyetRVG--DKG----TQLSGGQKQRI 1115
Cdd:COG1135 88 FQHFNLLSsRTVAENVALpleiaG-----VPKAEI-----RKRVAELLE--------LVGlsDKAdaypSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1187
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
324-540 |
2.76e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.88 E-value: 2.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQD---IRNFNVRCLRE 400
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQE-PVLFSTTIAENIRY-----GRgnvTMDEIKKAVKEAnaydfIMK--LPQKFDTLVgdrgAQLSGGQKQRIA 472
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGK---SRKEIRRRVREV-----LDLvgLSDKAKALP----HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 473 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRNAD--VIAgFEDGVIVE 540
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
324-542 |
3.15e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 144.02 E-value: 3.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD--P---TEGTISIDGQDI--RNFNVR 396
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 397 CLREFIGVVSQEPVLFSTTIAENIRYG------RGNVTMDEI-KKAVKEANAYDfimklpqkfdtLVGDR----GAQLSG 465
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWD-----------EVKDRlkksALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 466 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREgRTTIVI-------AHRLStvrnaDVIAGFEDGVI 538
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGEL 231
|
....
gi 564345546 539 VEQG 542
Cdd:COG1117 232 VEFG 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
324-547 |
4.67e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 143.27 E-value: 4.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-- 401
Cdd:COG3638 3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 -IGVVSQEPVLFS-TTIAENI-----------RYGRGNVTMDEIKKAvkeanaydfimklpqkFDTL--VG------DRG 460
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVlagrlgrtstwRSLLGLFPPEDRERA----------------LEALerVGladkayQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 461 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGV 537
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
250
....*....|
gi 564345546 538 IVEQGSHSEL 547
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
340-1203 |
1.37e-37 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 154.17 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGtisidgqdirnfnvRCLRE-FIGVVSQEPVLFSTTIAE 418
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG--------------RVWAErSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 419 NIRYgrgnvtMDE-----IKKAVK----EANaydfIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 489
Cdd:PTZ00243 740 NILF------FDEedaarLADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 490 TSALDTE-SEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEgIYFRL-----VNMQTS 563
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLaaelkENKDSK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 564 GSQILSEEFEVELSDEkaaGGVAPNGWKARIFRNSTKKSLKSSRAHQNRLDVETNELDANVPPVSFLKVLRL--NKTEWP 641
Cdd:PTZ00243 889 EGDADAEVAEVDAAPG---GAVDHEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFcgGLHAAG 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 642 Y----FVVGTLCAIANGalqpafsIILSEMIA-IFGPGDDTvkqqkcnmFSLVFLGLGVLSFFTFFLQGFTFGKAGEILT 716
Cdd:PTZ00243 966 FvlatFAVTELVTVSSG-------VWLSMWSTrSFKLSAAT--------YLYVYLGIVLLGTFSVPLRFFLSYEAMRRGS 1030
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 717 TRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAqvqgatgtrlalIAQNTANLGTGIIISFIYGWQLTLLLLSVV 796
Cdd:PTZ00243 1031 RNMHRDLLRSVSRGTMSFFD--TTPLGRILNRFSRDID------------ILDNTLPMSYLYLLQCLFSICSSILVTSAS 1096
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 797 -PFIAVA----GIVEMK-MLAGNAkrdkkemeaagkiateAIENIRTVVSLTQERKFeSMYVEKLHGpyrnsvrKAHI-- 868
Cdd:PTZ00243 1097 qPFVLVAlvpcGYLYYRlMQFYNS----------------ANREIRRIKSVAKSPVF-TLLEEALQG-------SATIta 1152
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 869 YGITFSISQ-AFMYFSYAgcfrFGSYLIVNGHMRFKDVILVF-SAIVLGAVAL-------GHASSfaPDYAKAKLSAAYL 939
Cdd:PTZ00243 1153 YGKAHLVMQeALRRLDVV----YSCSYLENVANRWLGVRVEFlSNIVVTVIALigvigtmLRATS--QEIGLVSLSLTMA 1226
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 940 FSLFE------RQ--------------------------PLIDSY-----SREGMWPDKF-------------------E 963
Cdd:PTZ00243 1227 MQTTAtlnwlvRQvatveadmnsverllyytdevphedmPELDEEvdaleRRTGMAADVTgtvviepasptsaaphpvqA 1306
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 964 GSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRA 1042
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALI 1122
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1123 -RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQL-LAQKGIYFS 1200
Cdd:PTZ00243 1462 kKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHS 1541
|
...
gi 564345546 1201 MVN 1203
Cdd:PTZ00243 1542 MVE 1544
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
983-1191 |
1.68e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 141.71 E-value: 1.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--P---MAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFD 1055
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDiyDPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENIAYG-----DNSRVVsQDEIVRAA-KEANihpfietLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLL 1129
Cdd:COG1117 106 KSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1130 LDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVIDNGKVKEHGTHQQL 1191
Cdd:COG1117 178 MDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
967-1196 |
1.89e-37 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 141.15 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 967 TFNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNvQWLRAQLGI 1046
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1047 VSQEPILFD-CSIAENI-----AYGDNSRVVSQ--DEIVRAAKeanihpfietLPQKYETRVGDkgtqLSGGQKQRIAIA 1118
Cdd:COG4555 79 LPDERGLYDrLTVRENIryfaeLYGLFDEELKKriEELIELLG----------LEEFLDRRVGE----LSTGMKKKVALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1119 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQKG 1196
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
977-1181 |
2.71e-37 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 138.47 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN--VQWLRAQLGIVSQEPILF 1054
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 -DCSIAENIAYGdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:cd03229 89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1134 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGK 1181
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
982-1193 |
3.21e-37 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 140.50 E-value: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNV---QWLRAQLGIVSQEPILFDC-S 1057
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAYG-DNSRVVSQDEIVRAAKEAnihpfIEtlpqkyetRVGDKGT------QLSGGQKQRIAIARALIRQPRVLLL 1130
Cdd:COG1127 99 VFENVAFPlREHTDLSEAEIRELVLEK-----LE--------LVGLPGAadkmpsELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1131 DEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
967-1181 |
3.31e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.38 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 967 TFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGI 1046
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1047 VSQepilfdcsiaeniaygdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkgtqLSGGQKQRIAIARALIRQPR 1126
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1127 VLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIDNGK 1181
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
331-1198 |
5.62e-37 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 152.37 E-value: 5.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 331 FSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnvrclrefIGVVSQEPV 410
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 411 LFSTTIAENIRYGrgnVTMDEIK--KAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:TIGR01271 498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 489 ATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL-------------------- 547
Cdd:TIGR01271 575 PFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELqakrpdfsslllgleafdnf 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 548 -----------------IKKEGIYFR------------------------------------LVNMQTSGSQILSEEFEV 574
Cdd:TIGR01271 655 saerrnsiltetlrrvsIDGDSTVFSgpetikqsfkqpppefaekrkqsiilnpiasarkfsFVQMGPQKAQATTIEDAV 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 575 -ELSDEKAA--------------GGVAPNGW----------------------KARIFRNSTKKSLKSSRAHQ--NRLDV 615
Cdd:TIGR01271 735 rEPSERKFSlvpedeqgeeslprGNQYHHGLqhqaqrrqsvlqlmthsnrgenRREQLQTSFRKKSSITQQNElaSELDI 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 616 ---------------ETNELD---------ANVPPV-SFLKVLRLNKTEWPYFVVGTLCAIANGAlQPAFSIILSEMIAI 670
Cdd:TIGR01271 815 ysrrlskdsvyeiseEINEEDlkecfaderENVFETtTWNTYLRYITTNRNLVFVLIFCLVIFLA-EVAASLLGLWLITD 893
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 671 FGPGDDTVKQQKCNMFS------------------LVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDM 732
Cdd:TIGR01271 894 NPSAPNYVDQQHANASSpdvqkpviitptsayyifYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPM 973
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 733 SWFDDHKnsTGALSTRLATDAAQVQGATG-TRLALIAQNTANLGTGIIISFIYGWqltlLLLSVVPFIAVAGIVEMKMLA 811
Cdd:TIGR01271 974 AVLNTMK--AGRILNRFTKDMAIIDDMLPlTLFDFIQLTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIMLRAYFLR 1047
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 812 GNAKRDKKEMEAAGKIATEAIENIR---TVVSLTQERKFESMYVEKLHGPYRN-SVRKAHIYGITFSISQAFMYFSYAGC 887
Cdd:TIGR01271 1048 TSQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHTANwFLYLSTLRWFQMRIDIIFVFFFIAVT 1127
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 888 F-RFGSYLIVNGHMrfkDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLF-SLFERQP---------------LID 950
Cdd:TIGR01271 1128 FiAIGTNQDGEGEV---GIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFiDLPQEEPrpsggggkyqlstvlVIE 1204
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 951 SYSREGMWPDkfEGSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGTVLLDGQ 1030
Cdd:TIGR01271 1205 NPHAQKCWPS--GGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGV 1280
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1031 EAKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGG 1110
Cdd:TIGR01271 1281 SWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNG 1357
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1111 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQ 1190
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQK 1437
|
....*...
gi 564345546 1191 LLAQKGIY 1198
Cdd:TIGR01271 1438 LLNETSLF 1445
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
321-557 |
5.77e-37 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 152.41 E-value: 5.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 321 KGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 400
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFSTTIAENIRyGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 480
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 481 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRL 557
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
324-547 |
7.12e-37 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 139.24 E-value: 7.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-- 401
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 -IGVVSQEPVLFS-TTIAENIRYGR-----------GNVTMDEIKKAVKEANAYDFIMKLPQkfdtlvgdRGAQLSGGQK 468
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAALERVGLLDKAYQ--------RADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 469 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTVR-NADVIAGFEDGVIVEQGSHS 545
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 564345546 546 EL 547
Cdd:cd03256 231 EL 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
968-1197 |
1.14e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 139.74 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 968 FNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIV 1047
Cdd:PRK13632 10 VENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1048 SQEPilfD-----CSIAENIAYGDNSRVVSQDE----IVRAAKEANIHPFIETLPQKyetrvgdkgtqLSGGQKQRIAIA 1118
Cdd:PRK13632 89 FQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1119 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKG 1196
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
.
gi 564345546 1197 I 1197
Cdd:PRK13632 235 I 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
983-1182 |
1.51e-36 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 137.66 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF-DCSIA 1059
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltDDKKNINELRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1060 ENIAYGD-NSRVVSQDEIVRAAKEanihpfietlpqkYETRVG--DKGT----QLSGGQKQRIAIARALIRQPRVLLLDE 1132
Cdd:cd03262 95 ENITLAPiKVKGMSKAEAEERALE-------------LLEKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1133 ATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:cd03262 162 PTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
38-294 |
1.98e-36 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 139.99 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 38 ILEEEMTRYAYYYSGLGGGVLLAA---YIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKI 114
Cdd:cd07346 30 IPAGDLSLLLWIALLLLLLALLRAllsYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 115 SEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIR 194
Cdd:cd07346 110 QNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 195 TVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGA 274
Cdd:cd07346 190 VVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG-ELVAFLAYLGML 268
|
250 260
....*....|....*....|.
gi 564345546 275 FS-VGQAAPCIDAFANARGAA 294
Cdd:cd07346 269 FGpIQRLANLYNQLQQALASL 289
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
324-536 |
2.43e-36 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 136.45 E-value: 2.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL---YDPTEGTISIDGQdirnfnvrcl 398
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 399 refIGVVSQEPVLFSTTIAENIRYGRgnvTMDEIK-KAVKEANA--YDFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIAR 475
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGK---PFDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEV--QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDG 536
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
346-548 |
2.55e-36 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 138.93 E-value: 2.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 346 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF----IGVVSQEPVLF-STTIAENI 420
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 421 RYG---RGnvtmdeIKKAVKEANAY---------DFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:cd03294 124 AFGlevQG------VPRAEREERAAealelvgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 489 ATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELI 548
Cdd:cd03294 187 AFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
982-1202 |
2.56e-36 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 138.50 E-value: 2.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1061
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1062 IaygDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1141
Cdd:cd03288 115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1142 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQK-GIYFSMV 1202
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
336-547 |
2.59e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 140.64 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 336 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF---IGVVSQEPvlF 412
Cdd:COG4608 28 VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 413 S---------TTIAENIRYgRGNVTMDEIKKAVKEanaydfIMklpqkfdTLVG------DRGA-QLSGGQKQRIAIARA 476
Cdd:COG4608 106 AslnprmtvgDIIAEPLRI-HGLASKAERRERVAE------LL-------ELVGlrpehaDRYPhEFSGGQRQRIGIARA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 477 LVRNPKILLLDEATSALDTESEAEV-------QAALdkareGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:COG4608 172 LALNPKLIVCDEPVSALDVSIQAQVlnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
324-538 |
2.76e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.91 E-value: 2.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnvrcLREFIG 403
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVL---FSTTIAENI---RYGRGNVTM---DEIKKAVKEA----NAYDFImklpqkfDTLVGdrgaQLSGGQKQR 470
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsRADREAVDEAlervGLEDLA-------DRPIG----ELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVR-NADVIAGFEDGVI 538
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLV 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
966-1182 |
3.01e-36 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 136.85 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL---- 1040
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1041 RAQLGIVSQE----PILfdcSIAENIAYGDNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRVGdkgtQLSGGQKQR 1114
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1115 IAIARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVIDNGKV 1182
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
643-936 |
3.90e-36 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 138.84 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDtvkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 722
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD---LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 723 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 802
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 803 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYF 882
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 883 SYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSA 936
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
966-1193 |
4.20e-36 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 136.86 E-value: 4.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNV---QWLRA 1042
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQEPILFDC-SIAENIAYG--DNSRvVSQDEIVRAAKE----ANIHPFIETLPqkyetrvgdkgTQLSGGQKQRI 1115
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlrEHTR-LSEEEIREIVLEkleaVGLRGAEDLYP-----------AELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1116 AIARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELR 225
|
.
gi 564345546 1193 A 1193
Cdd:cd03261 226 A 226
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
646-938 |
4.60e-36 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 138.85 E-value: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 646 GTLCAIANGALQPAFSIILSEMIAIFGPGDDtvkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFK 725
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGD---LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 726 AMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIV 805
Cdd:cd18557 78 SLLRQEIAFFDKHK--TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 806 EMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYA 885
Cdd:cd18557 156 YGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 886 GCFRFGSYLIVNGHMRFKDVI--LVFSAIVlgAVALGHASSFAPDYAKAkLSAAY 938
Cdd:cd18557 236 LVLWYGGYLVLSGQLTVGELTsfILYTIMV--ASSVGGLSSLLADIMKA-LGASE 287
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
965-1194 |
5.71e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 140.28 E-value: 5.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGTVLLDGQEAK-KLNVQwl 1040
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1041 RAQLGIVSQEPILF-DCSIAENIAYGDNSRVVSQDEIVRAAKE----ANIHPFIETLPqkyetrvgdkgTQLSGGQKQRI 1115
Cdd:COG1118 74 ERRVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVIDNGKVKEH 1185
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQV 215
|
....*....
gi 564345546 1186 GTHQQLLAQ 1194
Cdd:COG1118 216 GTPDEVYDR 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
964-1191 |
1.12e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 139.44 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 964 GSVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQeakklNVQWLRAQ 1043
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-----DVTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1044 ---LGIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPqkyetrvgdkgTQLSGGQKQRI 1115
Cdd:COG3839 74 drnIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKP-----------KQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1116 AIARALIRQPRVLLLDEATSALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVIDNGKVKEH 1185
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQV 215
|
....*.
gi 564345546 1186 GTHQQL 1191
Cdd:COG3839 216 GTPEEL 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
324-518 |
1.20e-35 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 134.84 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRC---LRE 400
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIKKAVKEANAydfIMKLPQKFDTLvgdrGAQLSGGQKQRIAIARAL 477
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALevTGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564345546 478 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA 518
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
46-619 |
1.39e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 147.96 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 46 YAYYYSGLGGGVLLAAYIQvSFW----TLAAGRqirKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDK 121
Cdd:PLN03130 955 YNLIYALLSFGQVLVTLLN-SYWlimsSLYAAK---RLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVF 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 122 VGMF----FQAIATFFagfIVGFIRgwklTLVIMAISPILGLSTAVWAKILSTFSD-KELAAYAKAGAVAE--EALGAIR 194
Cdd:PLN03130 1031 VNMFlgqiFQLLSTFV---LIGIVS----TISLWAIMPLLVLFYGAYLYYQSTAREvKRLDSITRSPVYAQfgEALNGLS 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 195 TVIAFGGQNKELERYQKHLENAKKIGIKKaISANISMGIAF-----LLIY--ASYAL----------AFWYGSTLVISKE 257
Cdd:PLN03130 1104 TIRAYKAYDRMAEINGRSMDNNIRFTLVN-MSSNRWLAIRLetlggLMIWltASFAVmqngraenqaAFASTMGLLLSYA 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 258 YTIGNAMTvffsiligafSVGQAAPCIDAFANA--RGAAYVifDIIDNNPKIdsfsERGHKPDS---IKGNLEFSDVHFS 332
Cdd:PLN03130 1183 LNITSLLT----------AVLRLASLAENSLNAveRVGTYI--DLPSEAPLV----IENNRPPPgwpSSGSIKFEDVVLR 1246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 333 YpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVL 411
Cdd:PLN03130 1247 Y--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVL 1324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 412 FSTTIAENIR-YGRGNVTmdEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEAT 490
Cdd:PLN03130 1325 FSGTVRFNLDpFNEHNDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 491 SALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYF-RLVnmQTSGS---- 565
Cdd:PLN03130 1403 AAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFsKMV--QSTGAanaq 1480
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 566 ---QILSEEFEVELSDEKAAG------GVAPNGWkARIFRNSTKKSLKSSRAHQNRLDVETNE 619
Cdd:PLN03130 1481 ylrSLVFGGDEDRLAREESKAldgqrkWLASSRW-AAAAQFALAVSLTSSQNDLQSLEIEDEN 1542
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
966-1193 |
1.66e-35 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 135.51 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1045
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILF-DCSIAENIAYgdnsrVVSQDEIVRAAKEANIHPFIETL---PQKYETRVGDkgtQLSGGQKQRIAIARAL 1121
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIAL-----VPKLLKWPKEKIRERADELLALVgldPAEFADRYPH---ELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1122 IRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
325-527 |
3.25e-35 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 133.81 E-value: 3.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 325 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclrefIGV 404
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 405 VSQEPVL---FSTTIAENI---RYGRGNVTMdEIKKAVKEA--NAYDFimklpqkfdtlVG-----DRG-AQLSGGQKQR 470
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmgLYGHKGLFR-RLSKADKAKvdEALER-----------VGlselaDRQiGELSGGQQQR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA 527
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEY 198
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
328-519 |
5.35e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 132.77 E-value: 5.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 328 DVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGqdiRNFNVRCLREFIGVVSQ 407
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 408 EP--VLFSTTIAENIRYGRGNVTMD--EIKKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKI 483
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 564345546 484 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH 519
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
324-547 |
6.84e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.82 E-value: 6.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIrNFNVRCLREFIG 403
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLF-STTIAENIRYG--RGNVTMDEIKKAVKE----------ANAYdfimklPqkfdtlvgdrgAQLSGGQKQR 470
Cdd:COG1118 79 FVFQHYALFpHMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------P-----------SQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQGSHSEL 547
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhDELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
322-558 |
7.62e-35 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 134.27 E-value: 7.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 322 GNLEFSDVHFSYPSraNIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 400
Cdd:cd03288 18 GEIKIHDLCVRYEN--NLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFSTTIAENIRYGRgNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 480
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 481 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELI-KKEGIYFRLV 558
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
980-1191 |
8.67e-35 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 133.13 E-value: 8.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAkkLNVQWLRAQLGIVSQEPILF-DCSI 1058
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 AENIAYGDNSRVVSQDEIVRAAKEAnihpfietLPQ----KYETRvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1134
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEA--------LDLvqleGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1135 SALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQL 1191
Cdd:cd03300 159 GALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
41-262 |
9.01e-35 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 134.98 E-value: 9.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 41 EEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGD 120
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 121 KVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFG 200
Cdd:cd18572 113 NLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 201 GQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 262
Cdd:cd18572 193 TEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
966-1182 |
1.20e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 133.26 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRA 1042
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQEPILFD-CSIAENI---AYGDNS------RVVSQDEIVRAAkEAnihpfIET--LPQKYETRVGdkgtQLSGG 1110
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERAL-EA-----LERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1111 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
325-542 |
1.24e-34 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 130.63 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 325 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 404
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 405 VSQepvlfsttiaenirygrgnvtmdeikkAVKEANAYDFIMKLpqkFDTlvgdrgaqLSGGQKQRIAIARALVRNPKIL 484
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 485 LLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 542
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
40-280 |
2.10e-34 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 133.91 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 40 EEEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIG 119
Cdd:cd18780 38 LRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 120 DKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAF 199
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 200 GGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFfsiLIGAFSVGQ 279
Cdd:cd18780 198 AKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTG-LLTSF---LLYTLTVAM 273
|
.
gi 564345546 280 A 280
Cdd:cd18780 274 S 274
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
966-1186 |
4.72e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.56 E-value: 4.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRA 1042
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQE-PILFDCSIAENIAY-----GdnsrvVSQDEIVRAAKEAnihpfietLpqkyeTRVG--DKG----TQLSGG 1110
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREV--------L-----DLVGlsDKAkalpHELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1111 QKQRIAIARALIRQPRVLLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVIDNGKVKEHG 1186
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
342-550 |
8.66e-34 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 130.53 E-value: 8.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclREFIGVVSQEPVLF-STTIAENI 420
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 421 RYGRGNVTMD--EIKKAVKEanaydfIMKLpQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 498
Cdd:cd03299 93 AYGLKKRKVDkkEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 499 AEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKK 550
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
324-542 |
9.61e-34 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 129.30 E-value: 9.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------RNfnvr 396
Cdd:cd03301 1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppkdRD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 397 clrefIGVVSQEPVLF-STTIAENIRYG--RGNVTMDEIKKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIAI 473
Cdd:cd03301 74 -----IAMVFQNYALYpHMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQI----EHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 474 ARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQG 542
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
324-549 |
1.60e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.91 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:PRK13635 6 IRVEHISFRYPD-AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEP--VLFSTTIAENIRYGRGN--VTMDE----IKKAVKEANAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 475
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIK 549
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
324-543 |
1.97e-33 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 136.74 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANI--------KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLyDPTEGTISIDGQDIRNFN- 394
Cdd:COG4172 276 LEARDLKVWFPIKRGLfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 395 --VRCLREFIGVVSQEPvlFST-----TIAENIRYG----RGNVTMDEIKKAVKEAnaydfimkLPQkfdtlVG-DRGA- 461
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEA--------LEE-----VGlDPAAr 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 462 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADV 529
Cdd:COG4172 420 hryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVVRAlAHR 495
|
250
....*....|....
gi 564345546 530 IAGFEDGVIVEQGS 543
Cdd:COG4172 496 VMVMKDGKVVEQGP 509
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
324-547 |
2.13e-33 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 128.71 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV-RCLREFI 402
Cdd:cd03224 1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVLFST-TIAENIRYGRGNVTMDEIKKAVKEAnaYDFIMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNP 481
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 482 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVI----AHRLSTVrnADVIAGFEDGVIVEQGSHSEL 547
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
969-1182 |
2.22e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 126.74 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 969 NEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGIVS 1048
Cdd:cd03230 4 RNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1049 QEPILF-DCSIAENIaygdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkgtQLSGGQKQRIAIARALIRQPRV 1127
Cdd:cd03230 80 EEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1128 LLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
341-547 |
4.42e-33 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 128.12 E-value: 4.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnVRCLREFIGVVSQEPVLFS-TTIAEN 419
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTVFQNYALFPhLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 420 IRYG--RGNVTMDEIKKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 497
Cdd:cd03300 93 IAFGlrLKKLPKAEIKERVAEA------LDLVQ-LEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 498 EAEVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSEL 547
Cdd:cd03300 166 RKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
324-548 |
5.18e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 128.29 E-value: 5.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDV--HFsypsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR--NFNVRCLR 399
Cdd:PRK09493 2 IEFKNVskHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 400 EFIGVVSQEPVLFSTTIA-ENIRYG----RGnvtmdeIKKAVKEANAYDFIMKlpqkfdtlVG--DRG----AQLSGGQK 468
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFGplrvRG------ASKEEAEKQARELLAK--------VGlaERAhhypSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 469 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSE 546
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
..
gi 564345546 547 LI 548
Cdd:PRK09493 223 LI 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
981-1182 |
6.59e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.38 E-value: 6.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQ-LGI--VSQEPILF-DC 1056
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPR--DAQaAGIaiIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1057 SIAENIAYGD---NSRVVSQDEIVRAAKEA------NIHPfietlpqkyETRVGDkgtqLSGGQKQRIAIARALIRQPRV 1127
Cdd:COG1129 95 SVAENIFLGReprRGGLIDWRAMRRRARELlarlglDIDP---------DTPVGD----LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1128 LLLDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:COG1129 162 LILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
983-1192 |
7.45e-33 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 127.84 E-value: 7.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1061
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1062 IAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1141
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1142 EKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:cd03299 165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
966-1194 |
1.35e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLnvqwlRAQLG 1045
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQE-------PIlfdcSIAENIAYGDNSRV-------VSQDEIVRAA-KEANIHPFIETlpqkyetRVGdkgtQLSGG 1110
Cdd:COG1121 79 YVPQRaevdwdfPI----TVRDVVLMGRYGRRglfrrpsRADREAVDEAlERVGLEDLADR-------PIG----ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1111 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIdNGKVKEHGTH 1188
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222
|
....*.
gi 564345546 1189 QQLLAQ 1194
Cdd:COG1121 223 EEVLTP 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
324-560 |
1.36e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 130.84 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnVRCLREFIG 403
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--VPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFS-TTIAENIRYG--RGNVTMDEIKKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRN 480
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMVQ-LEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 481 PKILLLDEATSALDTESEAEVQAALdKA--RE-GRTTIVIAH----RLSTvrnADVIAGFEDGVIVEQGSHSElikkegI 553
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPRE------I 232
|
....*..
gi 564345546 554 YFRLVNM 560
Cdd:PRK09452 233 YEEPKNL 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
981-1193 |
1.79e-32 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 126.01 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILF-DCS 1057
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAYGDNSRVvsqdeivRAAKEANIHPFIETLPQKYEtRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1137
Cdd:cd03224 92 VEENLLLGAYARR-------RAKRKARLERVYELFPRLKE-RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1138 dteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVIDNGKVKEHGTHQQLLA 1193
Cdd:cd03224 164 ---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
324-547 |
1.89e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.22 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-I 402
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVLFST-TIAENI---RYGRGNVTMDEiKKAVKEANAydfIMK---LPQKFDTLVGDrgaqLSGGQKQRIAIAR 475
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIflgREPRRGGLIDW-RAMRRRARE---LLArlgLDIDPDTPVGD----LSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 476 ALVRNPKILLLDEATSALdteSEAEVQAALD-----KAReGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:COG1129 154 ALSRDARVLILDEPTASL---TEREVERLFRiirrlKAQ-GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
980-1191 |
2.24e-32 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 126.30 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSI 1058
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 AENIAYG----DNSRVVSQDEIVRAAKEANIHPFIETLPQKYETrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEAT 1134
Cdd:cd03296 92 FDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1135 SALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQL 1191
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
340-542 |
2.44e-32 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 125.49 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVK---SGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ---DIR-NFNVRCLREFIGVVSQEPVLF 412
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 413 S-TTIAENIRYGRGNVTMDEIKKAVKEANAYdfiMKLpqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 491
Cdd:cd03297 88 PhLNVRENLAFGLKRKRNREDRISVDELLDL---LGL----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 492 ALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 542
Cdd:cd03297 161 ALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
977-1191 |
3.07e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 128.70 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEPil 1053
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 FDC-----SIAENIAYG-DNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRVGDkgtQLSGGQKQRIAIARALIRQP 1125
Cdd:COG4608 105 YASlnprmTVGDIIAEPlRIHGLASKAERRERVAEL-----LELvgLRPEHADRYPH---EFSGGQRQRIGIARALALNP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1126 RVLLLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1191
Cdd:COG4608 177 KLIVCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
341-547 |
3.79e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 126.02 E-value: 3.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTI-----SIDGQdiRNFN-----VRCLREFIGVVSQEPV 410
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSqqkglIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 411 LFS-TTIAENIRygRGNVTMDEIKKAVKEANAYDFIMKLpqkfdTLVGDRGA---QLSGGQKQRIAIARALVRNPKILLL 486
Cdd:PRK11264 96 LFPhRTVLENII--EGPVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 487 DEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
982-1187 |
3.97e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 129.68 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAE 1060
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1061 NIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKyetrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1140
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQR-------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1141 SEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVIDNGKVKEHGT 1187
Cdd:PRK09452 179 LRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
981-1194 |
4.07e-32 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 126.60 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRA----QLGIVSQEPILF-D 1055
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLD 1131
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1132 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
340-549 |
5.07e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 127.09 E-value: 5.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI--RNFNVRCLREFIGVVSQEP--VLFSTT 415
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 416 IAENIRYGRGNVTM--DEIKKAVKEANAydfIMKLPqkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 493
Cdd:PRK13637 101 IEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 494 DTESEAEVQAALDKARE--GRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIK 549
Cdd:PRK13637 176 DPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
975-1187 |
8.73e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 127.61 E-value: 8.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 975 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPMAGTVLLDGQEAKKLNVQWLRA---QLGIV 1047
Cdd:PRK11153 11 FPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1048 SQE-PILFDCSIAENIAY-----GdnsrvVSQDEIvraakEANIHPFIEtlpqkyetRVG--DKG----TQLSGGQKQRI 1115
Cdd:PRK11153 88 FQHfNLLSSRTVFDNVALplelaG-----TPKAEI-----KARVTELLE--------LVGlsDKAdrypAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGT 1187
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
975-1194 |
9.64e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 127.09 E-value: 9.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 975 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GTVLLDGQEAKKLNVQWLRA----QLGI 1046
Cdd:COG0444 11 FPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1047 VSQEP---------ILFdcSIAENI-AYGDNSRVVSQDEIVRAAKEANIHPfietlPqkyETRVGDKGTQLSGGQKQRIA 1116
Cdd:COG0444 91 IFQDPmtslnpvmtVGD--QIAEPLrIHGGLSKAEARERAIELLERVGLPD-----P---ERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1117 IARALIRQPRVLLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQ 1189
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVE 236
|
....*
gi 564345546 1190 QLLAQ 1194
Cdd:COG0444 237 ELFEN 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
977-1194 |
1.14e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 131.35 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPMAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEPil 1053
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 FDC-----SIAENIAYGdnsRVVSQDEIVRAAKEANIhpfIETLpqkyeTRVG-DKGT------QLSGGQKQRIAIARAL 1121
Cdd:COG4172 372 FGSlsprmTVGQIIAEG---LRVHGPGLSAAERRARV---AEAL-----EEVGlDPAArhryphEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1122 IRQPRVLLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:COG4172 441 ILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
977-1176 |
1.82e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 122.59 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlRAQLGIVSQEPILF-D 1055
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENIA-----YGdnsRVVSQDEIVRAAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLL 1130
Cdd:COG4133 90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564345546 1131 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1176
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
324-547 |
1.83e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 124.80 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL--REF 401
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEP--VLFSTTIAENIRYGRGNV--TMDEIKKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAI 473
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 474 ARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
967-1182 |
2.54e-31 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 123.45 E-value: 2.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 967 TFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE---AKKLNVQWLRAQ 1043
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1044 LGIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQ-----KYETRVGdkgtQLSGGQKQRIAI 1117
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERvglldKAYQRAD----QLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1118 ARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVIDNGKV 1182
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
684-900 |
2.58e-31 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 124.93 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 684 NMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR 763
Cdd:cd18573 41 KTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNK--TGELVSRLSSDTSVVGKSLTQN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 764 LALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQ 843
Cdd:cd18573 119 LSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 844 ERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18573 199 ERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGEL 255
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
324-547 |
2.92e-31 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 122.61 E-value: 2.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREfIG 403
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS-LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFST-TIAENIRY-----GRGNVTMDEIKKAVKEanaydfIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 477
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRART----LSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 478 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
966-1192 |
3.21e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 123.28 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAK--KLNVQWLRAQ 1043
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1044 LGIVSQEPILFDCSIA-ENIAYGDNSrvvsqdeiVRAAKEANIHPFIETLPQK--YETRVGDKGTQLSGGQKQRIAIARA 1120
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGPLR--------VRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1121 LIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
324-547 |
3.22e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.35 E-value: 3.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGTISIDGQDI---RNFNV 395
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 396 RcLREFIGVVSQEPVLFSTTIAENIRYG------RGNVTMDE-IKKAVKEANAYDFIMklpqkfDTLvGDRGAQLSGGQK 468
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVK------DRL-HDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 469 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
342-547 |
5.38e-31 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 122.45 E-value: 5.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclREFIGVVSQEPVLFS-TTIAENI 420
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 421 RYG------RGNVTMDEIKKAVKEanaydfIMKLPQkFDTLvGDR-GAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 493
Cdd:cd03296 96 AFGlrvkprSERPPEAEIRAKVHE------LLKLVQ-LDWL-ADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 494 DTESEAEVQAALDKARE--GRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 547
Cdd:cd03296 168 DAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
966-1194 |
6.66e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.30 E-value: 6.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1045
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVRAAKEAnihpfIETLP-QKYETRvgdKGTQLSGGQKQRIAIARALI 1122
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEA-----LELVGmQDFKER---EPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1123 RQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
324-530 |
7.14e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 121.05 E-value: 7.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRcLREFIG 403
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFST-TIAENIR-----YGRgNVTMDEIKKAVKEanaydfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARAL 477
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 478 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRNADVI 530
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
988-1194 |
7.24e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.79 E-value: 7.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 988 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVqwlrAQ--LGIVSQEPILFD-CSIAENIAY 1064
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErpVSMLFQENNLFPhLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1065 GDNSR----VVSQDEIVRAAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD-- 1138
Cdd:COG3840 95 GLRPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1139 --TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:COG3840 164 lrQEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
971-1186 |
8.83e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 119.85 E-value: 8.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 971 VVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQe 1050
Cdd:cd03214 5 LSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1051 pilfdcsiaeniaygdnsrvvsqdeivrAAKEANIHPFIEtlpQKYetrvgdkgTQLSGGQKQRIAIARALIRQPRVLLL 1130
Cdd:cd03214 81 ----------------------------ALELLGLAHLAD---RPF--------NELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1131 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHG 1186
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
324-547 |
1.26e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.53 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 475
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
968-1186 |
2.16e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.95 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 968 FNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLnvqwlRAQLGIV 1047
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1048 SQEPIL---FDCSIAENIAYGDNSRVVSQDEIVRAAKEAnihpFIETLpqkyeTRVGDKG------TQLSGGQKQRIAIA 1118
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK----VDEAL-----ERVGLSEladrqiGELSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1119 RALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIdNGKVKEHG 1186
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
324-539 |
2.33e-30 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 117.91 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPsraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREFI 402
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQepvlfsttiaenirygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPK 482
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 483 ILLLDEATSALdteSEAEVQAALD----KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIV 539
Cdd:cd03216 103 LLILDEPTAAL---TPAEVERLFKvirrLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
984-1182 |
3.03e-30 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 119.32 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-D 1055
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENIAYG-----DNSRVVSQDEIVRAAkeaNIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLL 1130
Cdd:cd03297 90 LNVRENLAFGlkrkrNREDRISVDELLDLL---GLDHLLNRYPA-----------QLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1131 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
983-1183 |
3.19e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 118.90 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeaKKLNVQWLRAQLGIVSQEP--ILFDCSIAE 1060
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDVdyQLFTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1061 NIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1140
Cdd:cd03226 92 ELLLGLKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564345546 1141 SEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVK 1183
Cdd:cd03226 161 NMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
983-1187 |
4.34e-30 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 119.85 E-value: 4.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGIVS--QEPILF-DCSIA 1059
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1060 ENI----------AYGDNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRV 1127
Cdd:cd03219 94 ENVmvaaqartgsGLLLARARREEREARERAEEL-----LERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1128 LLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1187
Cdd:cd03219 165 LLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
324-547 |
4.56e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 120.97 E-value: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 475
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
324-551 |
5.20e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 120.63 E-value: 5.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANIKiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 475
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKE 551
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
966-1182 |
6.06e-30 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 118.66 E-value: 6.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRA 1042
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQE-PILFDCSIAENIAYGDNSRVVSQDEIVRAAKEAnihpfIETLPQKYETRvgDKGTQLSGGQKQRIAIARAL 1121
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAA-----LELVGLSHKHR--ALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1122 IRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNA--DLIVVIDNGKV 1182
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
980-1186 |
9.92e-30 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 117.74 E-value: 9.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ-----EAKKLNVqwlraqlGIVSQEPILF 1054
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlPPKDRDI-------AMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 -DCSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:cd03301 85 pHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPK-------QLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1134 TSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVIDNGKVKEHG 1186
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
973-1202 |
1.03e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.84 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 973 FNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1050
Cdd:PRK13647 12 FRYKdgTKA----LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1051 P--ILFDCSIAENIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQ 1124
Cdd:PRK13647 88 PddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1125 PRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHG-----THQQLLAQKGI 1197
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGL 236
|
....*
gi 564345546 1198 YFSMV 1202
Cdd:PRK13647 237 RLPLV 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
324-551 |
1.17e-29 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 119.03 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEG-TISIDGQDIRNFNVRCLREFI 402
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVS---------QEPVL-------FSTTiaeniryGRGNVTMDEIKKAVKEANAYdfiMKLPQKFDTLVGdrgaQLSGG 466
Cdd:COG1119 81 GLVSpalqlrfprDETVLdvvlsgfFDSI-------GLYREPTDEQRERARELLEL---LGLAHLADRPFG----TLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 467 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStvrnaDVIAGF------EDGVI 538
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIthvlllKDGRV 221
|
250
....*....|...
gi 564345546 539 VEQGSHSELIKKE 551
Cdd:COG1119 222 VAAGPKEEVLTSE 234
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
688-900 |
1.25e-29 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 120.05 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 688 LVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALI 767
Cdd:cd18780 46 LILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 768 AQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF 847
Cdd:cd18780 124 LRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564345546 848 ESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18780 204 VSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGEL 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
324-551 |
1.35e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.46 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 475
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKE 551
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
980-1182 |
1.46e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 115.60 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQ-LGIvsqepilfdcsi 1058
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARrAGI------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 aeniaygdnsrvvsqdeivraakeANIHpfietlpqkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL- 1137
Cdd:cd03216 78 ------------------------AMVY-------------------QLSVGERQMVEIARALARNARLLILDEPTAALt 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564345546 1138 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
966-1193 |
2.08e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 118.94 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN-VQWLRAQL 1044
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 GIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVRAAKEAnihpFIETLPQKYETRvgdKGTQLSGGQKQRIAIARALI 1122
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1123 RQPRVLLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
324-540 |
2.24e-29 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 117.53 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN------VR 396
Cdd:COG4181 9 IELRGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 397 clREFIGVVSQ-EPVLFSTTIAENI-----RYGRGNVTmdeiKKAVKEANAYDfimklpqkfdtlVGDRG----AQLSGG 466
Cdd:COG4181 89 --ARHVGFVFQsFQLLPTLTALENVmlpleLAGRRDAR----ARARALLERVG------------LGHRLdhypAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 467 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTVRNADVIAGFEDGVIVE 540
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
41-261 |
2.73e-29 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 119.16 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 41 EEMTRYAYYYSGLGGGVLL----AAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISE 116
Cdd:cd18573 34 EIFGLSLKTFALALLGVFVvgaaANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 117 GIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTV 196
Cdd:cd18573 114 SLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTV 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 197 IAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 261
Cdd:cd18573 194 RAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVG 258
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
983-1194 |
5.15e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.82 E-value: 5.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1061
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1062 IAYGDNSRVVSQDEIVRAAKEAnihpfIETLP-QKYETRVGDkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1140
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEA-----LELVDlAGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1141 SEKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:PRK11432 171 LRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
336-540 |
5.20e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.48 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 336 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF---IGVVSQEP--- 409
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrdIQMVFQDSisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 410 VLFSTTIAENIRYG-RGNVTMDEikkAVKEANAYDFI--MKLPqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 486
Cdd:PRK10419 102 VNPRKTVREIIREPlRHLLSLDK---AERLARASEMLraVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 487 DEATSALDTESEAEVQAALDKAREGRTT--IVIAHRLSTV-RNADVIAGFEDGVIVE 540
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
324-541 |
8.06e-29 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 116.83 E-value: 8.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPS------RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN--- 394
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 395 VRCLREFIGVVSQE---PVLFSTTIAENIRYGRGNVT-MDEIKKAVKEANAYDfIMKLPqkfDTLVGDRGAQLSGGQKQR 470
Cdd:TIGR02769 83 RRAFRRDVQLVFQDspsAVNPRMTVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQ 541
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
324-547 |
9.48e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.61 E-value: 9.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR------------ 391
Cdd:PRK10619 6 LNVIDLHKRYGEH---EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 392 -NFNVRCLREFIGVVSQEPVLFS-TTIAENIRygRGNVTMDEIKKAVKEANAYDFIMKLPQKfDTLVGDRGAQLSGGQKQ 469
Cdd:PRK10619 83 dKNQLRLLRTRLTMVFQHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 470 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNADVIAGF-EDGVIVEQGSHSEL 547
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
984-1187 |
1.12e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 117.07 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEP--ILFDCSIA 1059
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1060 ENIAYGDNSRVVSQDEIVRAAKEAnihpfIETLPQKYETrVGDKGT-QLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1138
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1139 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1187
Cdd:PRK13637 177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
323-551 |
1.12e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 115.62 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 323 NLEFSDVHFSYPSRAnikilKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV--RClre 400
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaeRP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 fIGVVSQEPVLFS-TTIAENIRYG---RGNVTMDEiKKAVKEANA----YDFIMKLPqkfdtlvgdrgAQLSGGQKQRIA 472
Cdd:COG3840 73 -VSMLFQENNLFPhLTVAQNIGLGlrpGLKLTAEQ-RAQVEQALErvglAGLLDRLP-----------GQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 473 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIK 549
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
..
gi 564345546 550 KE 551
Cdd:COG3840 220 GE 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
953-1210 |
1.21e-28 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 125.06 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 953 SREGMWPDKFE---------GSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG 1023
Cdd:TIGR00957 615 SHEELEPDSIErrtikpgegNSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1024 TVLLDGQEAkklnvqwlraqlgIVSQEPILFDCSIAENIAYGDNSrvvsQDEIVRAAKEA-NIHPFIETLPQKYETRVGD 1102
Cdd:TIGR00957 694 HVHMKGSVA-------------YVPQQAWIQNDSLRENILFGKAL----NEKYYQQVLEAcALLPDLEILPSGDRTEIGE 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1103 KGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL---DKAREGRTCIVIAHRLSTIQNADLIVVIDN 1179
Cdd:TIGR00957 757 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSG 836
|
250 260 270
....*....|....*....|....*....|.
gi 564345546 1180 GKVKEHGTHQQLLAQKGIYFSMVNIQAGTQN 1210
Cdd:TIGR00957 837 GKISEMGSYQELLQRDGAFAEFLRTYAPDEQ 867
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
977-1179 |
1.29e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.50 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPIL 1053
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 FD-CSIAENIAYG---DNSRVVSQDEIVRAAKEANIHPFIETLPqkyetrvgdkgTQLSGGQKQRIAIARALIRQPRVLL 1129
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1130 LDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIDN 1179
Cdd:COG4136 157 LDEPFSKLDAAlRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
324-550 |
1.62e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.80 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRA--NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI----RNFNVRC 397
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 398 LREFIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDeIKKAvkEANAYDFIMKLPQKFDTLvGDRGAQLSGGQKQRIAIAR 475
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIKK 550
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
324-551 |
1.76e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.44 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGTISIDGQDIRNFNVRCLRE 400
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEANA----YDFIMKLPQkfdtlvgdrgaQLSGGQKQRIA 472
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 473 IARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKK 550
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 564345546 551 E 551
Cdd:PRK13640 234 V 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
345-550 |
2.17e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.90 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 345 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclREFIGVVSQEPVLFS-TTIAENIRYG 423
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPhMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 424 RG--NVTMDEIKKAVKEANAydfimklpqkfdtLV-----GDRGA-QLSGGQKQRIAIARALVRNPKILLLDEATSALDt 495
Cdd:PRK11432 103 LKmlGVPKEERKQRVKEALE-------------LVdlagfEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLD- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 496 eseAEVQAAL-DKARE-----GRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSELIKK 550
Cdd:PRK11432 169 ---ANLRRSMrEKIRElqqqfNITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
324-553 |
2.29e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 114.69 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPsraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV-RCLREFI 402
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVLFST-TIAENIR---YGRGNVtmDEIKKAVKEAnaYDFIMKLPQKFDTlvgdRGAQLSGGQKQRIAIARALV 478
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLlgaYARRDR--AEVRADLERV--YELFPRLKERRRQ----RAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 479 RNPKILLLDEATSALdteseA-----EVQAALDKAREGRTTIVI----AHRLSTVrnADVIAGFEDGVIVEQGSHSELIK 549
Cdd:COG0410 153 SRPKLLLLDEPSLGL-----ApliveEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
....
gi 564345546 550 KEGI 553
Cdd:COG0410 226 DPEV 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
317-561 |
2.39e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.10 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 317 PDSIkgnLEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ--DIRNFN 394
Cdd:PRK13636 2 EDYI---LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 395 VRCLREFIGVVSQEP--VLFSTTIAENIRYGRGNVTM--DEIKKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQR 470
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIA-HRLSTVR-NADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEImKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
250
....*....|....*
gi 564345546 548 I-KKEGIyfRLVNMQ 561
Cdd:PRK13636 230 FaEKEML--RKVNLR 242
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
643-900 |
2.43e-28 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 116.10 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALqPAFsiiLSEMI-AIFGPGDDTVKQQKCNMFSLVFLGLGVLSFftffLQGFTFGKAGEILTTRLRS 721
Cdd:cd18572 2 FVFLVVAALSELAI-PHY---TGAVIdAVVADGSREAFYRAVLLLLLLSVLSGLFSG----LRGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 722 MAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAV 801
Cdd:cd18572 74 DLFRSLLRQDIAFFDATK--TGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 802 AGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMY 881
Cdd:cd18572 152 ITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQN 231
|
250
....*....|....*....
gi 564345546 882 FSYAGCFRFGSYLIVNGHM 900
Cdd:cd18572 232 GTQVLVLFYGGHLVLSGRM 250
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
324-550 |
2.75e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.27 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI----RNFNVRC 397
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 398 LREFIGVVSQ--EPVLFSTTIAENIRYGRGN--VTMDEIKKAVKEANAydfIMKLPQKfdtlVGDRGA-QLSGGQKQRIA 472
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPEE----LLARSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 473 IARALVRNPKILLLDEATSALDTESEAEVQ---AALDKaREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELI 548
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIF 234
|
..
gi 564345546 549 KK 550
Cdd:PRK13634 235 AD 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
324-569 |
3.67e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 121.75 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPS-RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL---- 398
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 399 REFIGVVSQEPVLFSTTIAENirygrgNVTMDEI----KKAVKEANAYDFIMKLpqKFDTLVGDRGAQLSGGQKQRIAIA 474
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQ------NVEVPAVyaglERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 475 RALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGI 553
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGG 236
|
250
....*....|....*.
gi 564345546 554 YFRLVNMQTSGSQILS 569
Cdd:PRK10535 237 TEPVVNTASGWRQFVS 252
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
646-918 |
4.40e-28 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 115.27 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 646 GTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKqqkCNMFSLVFLGLGVL-SFFTFFlQGFTFGKAGEILTTRLRSMAF 724
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTAS---LNQIALLLLGLFLLqAVFSFF-RIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 725 KAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGI 804
Cdd:cd18576 77 RHLQRLPLSFFHERR--VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 805 VEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERkFESM-YVEKLHGPYRNSVRKAHIYGITFSISQAFMYFS 883
Cdd:cd18576 155 LFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLLFGA 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 564345546 884 YAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAVA 918
Cdd:cd18576 234 IVAVLWYGGRLVLAGELTAGDLVafLLYTLFIAGSIG 270
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
966-1191 |
5.03e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.85 E-value: 5.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1045
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPI-LFDCSIAE-NIAYGDNSRVVSQDEIVR----AAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIAR 1119
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRrvseALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1120 ALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQL 1191
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-534 |
6.47e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.36 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGTISIDGQDI--RNFNVR 396
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 397 CLREFIGVVSQEPVLFSTTIAENIRYG------RGNVTMDEI-KKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQ 469
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 470 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFE 534
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFK 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
980-1193 |
8.05e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 113.15 E-value: 8.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVqWLRAQLGI--VSQEPILF-DC 1056
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1057 SIAENIAYGdnSRVVSQDEIVRAAKEAnIHpfiETLPQKYEtRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:COG0410 94 TVEENLLLG--AYARRDRAEVRADLER-VY---ELFPRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1137 LdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:COG0410 167 L---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
987-1195 |
9.77e-28 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 115.98 E-value: 9.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 987 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-DCSIAEN 1061
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1062 IAYG-----DNSRVVSQDEIVRAAkeaNIHPFIETLPQKyetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:TIGR02142 96 LRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1137 LDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQK 1195
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
197-520 |
1.10e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 119.53 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 197 IAF-GGQNKELERYQKHLENAKKIgIKKAISANISMGiAFLLIYASYALAFWY--GSTLVISKEYTIGNAMTV--FFSIL 271
Cdd:COG4178 234 IALyRGEAAERRRLRRRFDAVIAN-WRRLIRRQRNLT-FFTTGYGQLAVIFPIlvAAPRYFAGEITLGGLMQAasAFGQV 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 272 IGAFSVgqaapCIDAFAN-ARGAAYVI-----FDIIDNNPKIDSFSERGHKPDSikGNLEFSDVHFSYPSRAniKILKGL 345
Cdd:COG4178 312 QGALSW-----FVDNYQSlAEWRATVDrlagfEEALEAADALPEAASRIETSED--GALALEDLTLRTPDGR--PLLEDL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 346 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISI-DGQDIrnfnvrcLrefigVVSQEPVLFSTTIAENIRY-- 422
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------L-----FLPQRPYLPLGTLREALLYpa 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 423 GRGNVTMDEIKKAVKEANaydfIMKLPQKFDTlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQ 502
Cdd:COG4178 451 TAEAFSDAELREALEAVG----LGHLAERLDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
330
....*....|....*...
gi 564345546 503 AALDKAREGRTTIVIAHR 520
Cdd:COG4178 526 QLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
324-549 |
1.36e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.16 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYP--SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR----NFNVRC 397
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 398 LREFIGVVSQ--EPVLFSTTIAENIRYGRGN--VTMDEIK-KAVKeanaydFIMKLPQKfDTLVGDRGAQLSGGQKQRIA 472
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKeKALK------WLKKVGLS-EDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 473 IARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHrlstvrNADVIAGFEDGVIVEQgsHSELIK 549
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVLE--HGKLIK 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
324-542 |
1.37e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 111.10 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHF---SYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGTISIDGQDIRNFNVRCL 398
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 399 refIGVVSQEPVLFST-TIAENIrygrgnvtmdeikkavkeanayDFIMKLpqkfdtlvgdRGaqLSGGQKQRIAIARAL 477
Cdd:cd03213 84 ---IGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 478 VRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTvrnaDVIAGFEDGVIVEQG 542
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQG 188
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
323-545 |
1.38e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.80 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 323 NLEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIrNFN-------V 395
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSqkpsekaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 396 RCLREFIGVVSQE----PVLfstTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLvgdrGAQLSGGQKQRI 471
Cdd:COG4161 78 RLLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 472 AIARALVRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 545
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQvVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
971-1193 |
1.57e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 113.65 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 971 VVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1050
Cdd:PRK13642 10 LVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1051 P--ILFDCSIAENIAYGDNSRVVSQDEIVRAAKEAnihpFIETLPQKYETRvgdKGTQLSGGQKQRIAIARALIRQPRVL 1128
Cdd:PRK13642 90 PdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEA----LLAVNMLDFKTR---EPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1129 LLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
984-1165 |
1.94e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 112.95 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA-----GTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFDC 1056
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1057 SIAENIAYGD--NSRVVSQDEIV-RAAKEAnihpfieTLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVeRSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 564345546 1134 TSALDTESEKVVQEALDKAREGRTCIVIAHRL 1165
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
56-294 |
2.21e-27 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 113.35 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 56 GVLLA----AYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIAT 131
Cdd:cd18576 44 GLFLLqavfSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 132 FFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQK 211
Cdd:cd18576 124 LIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 212 HLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMT-VFFSILIGAfSVGQAAPCIDAFANA 290
Cdd:cd18576 204 ALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQKA 282
|
....
gi 564345546 291 RGAA 294
Cdd:cd18576 283 LGAS 286
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
324-556 |
3.36e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.91 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSR-------ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN-- 394
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 395 -VRCLREFIGVVSQ-----------------EPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYdfimklPQKFdtlv 456
Cdd:PRK11308 86 aQKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY------PHMF---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 457 gdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIV-IAHRLSTVRN-ADVIAGF 533
Cdd:PRK11308 156 -------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQELGLSYVfISHDLSVVEHiADEVMVM 228
|
250 260
....*....|....*....|...
gi 564345546 534 EDGVIVEQGShselikKEGIYFR 556
Cdd:PRK11308 229 YLGRCVEKGT------KEQIFNN 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
983-1193 |
3.62e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.77 E-value: 3.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV-----LLDGQE---AKKLNVQWLRAQLGIVSQEPILF 1054
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARslsQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 DC-SIAENIAYGDnsrVVSQDEiVRAAKEAnihpfietLPQKYETRVGDKGTQ------LSGGQKQRIAIARALIRQPRV 1127
Cdd:PRK11264 98 PHrTVLENIIEGP---VIVKGE-PKEEATA--------RARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1128 LLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:PRK11264 166 ILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
982-1200 |
3.70e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 114.93 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKklNVQWLRAQLGIVSQEPILF-DCSIAE 1060
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1061 NIAYGdnsrvVSQDEIVRAAKEANIHPFIETLP-QKYETRvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1139
Cdd:PRK11607 111 NIAFG-----LKQDKLPKAEIASRVNEMLGLVHmQEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1140 ESEKVVQ-EALD-KAREGRTCIVIAH-RLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFS 1200
Cdd:PRK11607 183 KLRDRMQlEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
984-1194 |
4.22e-27 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 114.43 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPMAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEP 1051
Cdd:COG4148 11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1052 ILFD-CSIAENIAYG-----DNSRVVSQDEIVRAakeANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQP 1125
Cdd:COG4148 87 RLFPhLSVRGNLLYGrkrapRAERRISFDEVVEL---LGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1126 RVLLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:COG4148 153 RLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
966-1187 |
4.78e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.20 E-value: 4.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GTVLLDGQEAKKLNVQWLRA 1042
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVR----AAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIA 1116
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1117 IARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGT 1187
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
966-1194 |
5.38e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.10 E-value: 5.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPT---RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQW-LR 1041
Cdd:PRK13633 5 IKCKNVSYKYESneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1042 AQLGIVSQEPilfDCSIA-----ENIAYGDNSRVVSQDEIVR----AAKEANIHPFietlpQKYETRVgdkgtqLSGGQK 1112
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVativeEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEY-----RRHAPHL------LSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1113 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQ 1190
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
....
gi 564345546 1191 LLAQ 1194
Cdd:PRK13633 231 IFKE 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
324-547 |
5.39e-27 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 117.09 E-value: 5.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLLQRLYDPTEGTISIDGQDIRNFNVRCL 398
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVeAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 399 REF----IGVVSQEPV-----LFS--TTIAENIRYGRGnVTMDEIKKAVKEAnaydfimkLpqkfdTLVGDRGA------ 461
Cdd:COG4172 87 RRIrgnrIAMIFQEPMtslnpLHTigKQIAEVLRLHRG-LSGAAARARALEL--------L-----ERVGIPDPerrlda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 462 ---QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFED 535
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKdlQRELGMALLLITHDLGVVRRfADRVAVMRQ 232
|
250
....*....|..
gi 564345546 536 GVIVEQGSHSEL 547
Cdd:COG4172 233 GEIVEQGPTAEL 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
324-547 |
6.43e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 113.26 E-value: 6.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSD--VHFSYPSR--------ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF 393
Cdd:PRK15079 9 LEVADlkVHFDIKDGkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 394 N---VRCLREFIGVVSQEPvLFSTT--------IAENIRYGRGNVTMDEIKKAVKEanaydFIMK---LPQkfdtLVGDR 459
Cdd:PRK15079 89 KddeWRAVRSDIQMIFQDP-LASLNprmtigeiIAEPLRTYHPKLSRQEVKDRVKA-----MMLKvglLPN----LINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 460 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLSTVRN-ADVIAGFEDG 536
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlQREmGLSLIFIAHDLAVVKHiSDRVLVMYLG 238
|
250
....*....|.
gi 564345546 537 VIVEQGSHSEL 547
Cdd:PRK15079 239 HAVELGTYDEV 249
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-547 |
7.15e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.77 E-value: 7.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 338 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLF 412
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 413 ST-TIAENIRYG----RGNVTMDEIKKAVKEAnaydfiMKLPQKFDTlVGDR----GAQLSGGQKQRIAIARALVRNPKI 483
Cdd:PRK14247 95 PNlSIFENVALGlklnRLVKSKKELQERVRWA------LEKAQLWDE-VKDRldapAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 484 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
978-1195 |
7.20e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 111.44 E-value: 7.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 978 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRA---QLGIVSQepilf 1054
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 DC--------SIAENIA-----YGDNSRVVSQDEIVRAAKEANIHPFI-ETLPQkyetrvgdkgtQLSGGQKQRIAIARA 1120
Cdd:TIGR02769 96 DSpsavnprmTVRQIIGeplrhLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QLSGGQLQRINIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1121 LIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQK 1195
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
964-1198 |
7.58e-27 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 111.48 E-value: 7.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 964 GSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGTVLLDGQEAKKLNVQWLRAQ 1043
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1044 LGIVSQEPILFDCSIAENI-AYGDNSrvvsQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALI 1122
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1123 RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIY 1198
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
328-550 |
8.17e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.72 E-value: 8.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 328 DVHFSYPSRANIK---ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF-NVRCLREFIG 403
Cdd:PRK13633 9 NVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 475
Cdd:PRK13633 89 MVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKK 550
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
337-551 |
1.29e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.10 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 337 ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVL-FSTT 415
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 416 IAENIRYGR-------GNVTMDEiKKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:PRK11231 93 VRELVAYGRspwlslwGRLSAED-NARVNQA------MEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 489 ATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIKKE 551
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
982-1180 |
1.39e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.06 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLL-DGQEAkklnvqwlraqLgIVSQEPILFDCSIAE 1060
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------L-FLPQRPYLPLGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1061 NIAYGDNSRVVSQDEIVRAAKEANIHPFIETLpqkyeTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1140
Cdd:COG4178 445 ALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564345546 1141 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNG 1180
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
981-1194 |
2.37e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 115.17 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRA----QLGIVSQEPI 1052
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1053 -----LFdcSIAENIAygdnsrvvsqdEIVR---------AAKEAnihpfIETL-----PQKyETRVGDKGTQLSGGQKQ 1113
Cdd:COG4172 103 tslnpLH--TIGKQIA-----------EVLRlhrglsgaaARARA-----LELLervgiPDP-ERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1114 RIAIARALIRQPRVLLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1186
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQG 239
|
....*...
gi 564345546 1187 THQQLLAQ 1194
Cdd:COG4172 240 PTAELFAA 247
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
324-550 |
2.53e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.22 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPS------RAnikiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI----RNF 393
Cdd:PRK13649 3 INLQNVSYTYQAgtpfegRA----LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 394 NVRCLREFIGVVSQ--EPVLFSTTIAENIRYGRGN--VTMDEIKKAVKEanaydfimKLpqkfdTLVG------DRGA-Q 462
Cdd:PRK13649 79 DIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALARE--------KL-----ALVGiseslfEKNPfE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 463 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFEDGVIVE 540
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVL 225
|
250
....*....|
gi 564345546 541 QGSHSELIKK 550
Cdd:PRK13649 226 SGKPKDIFQD 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
970-1195 |
2.54e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.32 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 970 EVVFNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ--EAKKLNVQWLRAQLG 1045
Cdd:PRK13636 10 ELNYNYSdgTHA----LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPqkyetrvgDKGTQ-LSGGQKQRIAIARALI 1122
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK--------DKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1123 RQPRVLLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVIDNGKVKEHGTHQQLLAQK 1195
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
979-1194 |
2.69e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.21 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 979 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEPilfd 1055
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 csiaeniaYGD-NSR-VVSQ---------DEIVRAAKEANIHPFIEtlpqkyetRVGDKGTQ-------LSGGQKQRIAI 1117
Cdd:PRK11308 102 --------YGSlNPRkKVGQileepllinTSLSAAERREKALAMMA--------KVGLRPEHydryphmFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1118 ARALIRQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
987-1186 |
2.91e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 107.96 E-value: 2.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 987 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAENIAYG 1065
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1066 DNSRV----VSQDEIVRAAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1141
Cdd:cd03298 95 LSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564345546 1142 EKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1186
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
965-1168 |
3.91e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.97 E-value: 3.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGTVLLDGQ--------EAKKLN 1036
Cdd:PRK14258 7 AIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1037 VQWLRAQLGIVSQEPILFDCSIAENIAYGDN----SRVVSQDEIVRAA-KEANihpfietLPQKYETRVGDKGTQLSGGQ 1111
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESAlKDAD-------LWDEIKHKIHKSALDLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1112 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTI 1168
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
966-1193 |
3.95e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.72 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYptRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLL------DGQEAKKL 1035
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1036 NVqwLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRvgdKGTQLSGGQ 1111
Cdd:PRK13634 81 KP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IELvgLPEELLAR---SPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1112 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1187
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....*.
gi 564345546 1188 HQQLLA 1193
Cdd:PRK13634 230 PREIFA 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
342-533 |
3.98e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.10 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD--PT---EGTISIDGQDIRNFNVRC--LREFIGVVSQEPVLFST 414
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDPveVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 415 TIAENIRYG------RGNvtMDE-IKKAVKEANAYDFIM-KLPQKfdtlvgdrGAQLSGGQKQRIAIARALVRNPKILLL 486
Cdd:PRK14243 106 SIYDNIAYGaringyKGD--MDElVERSLRQAALWDEVKdKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564345546 487 DEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGF 533
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFF 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
967-1163 |
4.03e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.80 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 967 TFNEVVFNYP-TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEakklnVQWLRAQLG 1045
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVRAAKEanihpfietlpqkYETRVGDKGT------QLSGGQKQRIAIA 1118
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEE-------------LLALVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564345546 1119 RALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1163
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
324-551 |
4.10e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.51 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEP--VLFSTTIAENIRYGRGNVTMDE------IKKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 475
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKE 551
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
324-525 |
4.56e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.97 E-value: 4.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPS-RANikilKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ--DIRNFNVrCLRE 400
Cdd:COG3845 6 LELRGITKRFGGvVAN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRD-AIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFST-TIAENIRYGR-----GNVTMDEIKKAVKE-ANAYDFIMKLpqkfDTLVGDrgaqLSGGQKQRIAI 473
Cdd:COG3845 81 GIGMVHQHFMLVPNlTVAENIVLGLeptkgGRLDRKAARARIRElSERYGLDVDP----DAKVED----LSVGEQQRVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 474 ARALVRNPKILLLDEATSALdTESEA-EVQAALDK-AREGRTTIVIAHRLSTVR 525
Cdd:COG3845 153 LKALYRGARILILDEPTAVL-TPQEAdELFEILRRlAAEGKSIIFITHKLREVM 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
324-542 |
4.73e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 107.28 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTvALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIG 403
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFST-TIAENIRY-GR-GNVTMDEIKKAVKEA----NAYDFimklpqkfdtlVGDRGAQLSGGQKQRIAIARA 476
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiAWlKGIPSKEVKARVDEVlelvNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 477 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 542
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
338-542 |
5.37e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 106.92 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 338 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREfIGVVSQEPVLFST-TI 416
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRR-IGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 417 AENIR-----YGRGNVTMDEIKKAVKEANAYDfimklpqkfdtlvgDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 491
Cdd:cd03268 90 RENLRllarlLGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564345546 492 ALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 542
Cdd:cd03268 156 GLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
324-530 |
5.90e-26 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 107.52 E-value: 5.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF--NVRCLRef 401
Cdd:cd03219 1 LEVRGLTKRF---GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLppHEIARL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 iGVVS--QEPVLFST-TIAENIRYG-----RGNVTMDEIKKAVKEANAYDF----IMKLPQKFDTLVGDrgaqLSGGQKQ 469
Cdd:cd03219 76 -GIGRtfQIPRLFPElTVLENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 470 RIAIARALVRNPKILLLDEATSALdteSEAEVQAALDK----AREGRTTIVIAHRLSTVRN-ADVI 530
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGL---NPEETEELAELirelRERGITVLLVEHDMDVVMSlADRV 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
342-547 |
6.83e-26 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 107.07 E-value: 6.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIGVVSQEPvlfsttIAENIR 421
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL------SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 422 YGRGNVTM---------DEIKKAVKEANAYdfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSA 492
Cdd:cd03265 89 TGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 493 LDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:cd03265 162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
324-545 |
6.85e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.79 E-value: 6.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirNFN--------- 394
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDfsktpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 395 VRCLREFIGVVSQEPVLFS-TTIAENIRYGRGNVT-MDEiKKAVKEAnaydfiMKLPQKFD-TLVGDR-GAQLSGGQKQR 470
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPhLTVQQNLIEAPCRVLgLSK-DQALARA------EKLLERLRlKPYADRfPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 545
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
980-1186 |
8.32e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.69 E-value: 8.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEP-IL 1053
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 FDCSIAENIAYGD--NSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLL 1129
Cdd:PRK14247 95 PNLSIFENVALGLklNRLVKSKKELQERVRWA-----LEKaqLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1130 LDEATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVIDNGKVKEHG 1186
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
983-1186 |
9.09e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 106.51 E-value: 9.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD-CSIAEN 1061
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPnFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1062 IAY-----GDNSRVVSQdEIVRAAKEANIHPFietlpqkYETRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:cd03264 93 LDYiawlkGIPSKEVKA-RVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1137 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1186
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
981-1182 |
1.07e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 107.43 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVqWLRAQLGIVS--QEPILF-DCS 1057
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFpELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIA----YGDNSRVVSQ-----------DEIVRAAKEAnihpfIET--LPQKYETRVGDkgtqLSGGQKQRIAIARA 1120
Cdd:COG0411 96 VLENVLvaahARLGRGLLAAllrlprarreeREARERAEEL-----LERvgLADRADEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1121 LIRQPRVLLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
356-547 |
1.20e-25 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 110.19 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 356 ALVGNSGCGKSTTVQLLQRLYDPTEGTISIDG---QDI-RNFNVRCLREFIGVVSQEPVLFST-TIAENIRYGRgnvtmd 430
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSaRGIFLPPHRRRIGYVFQEARLFPHlSVRGNLLYGR------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 431 eiKKAVKEANAYDFimklpqkfDTLVG--------DRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV 501
Cdd:COG4148 103 --KRAPRAERRISF--------DEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564345546 502 QAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 547
Cdd:COG4148 173 LPYLERlRDELDIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPLAEV 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
340-521 |
1.28e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.48 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnvrcLRE-----FIGVVSQEPVL--- 411
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-----LPEykrakYIGRVFQDPMMgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 412 FSTTIAEN--IRYGRGN-------VT---MDEIKKAVKEANaydfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVR 479
Cdd:COG1101 95 PSMTIEENlaLAYRRGKrrglrrgLTkkrRELFRELLATLG-----LGLENRLDTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564345546 480 NPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRL 521
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
979-1180 |
1.40e-25 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 106.26 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 979 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVL----LDGQEAKKLNVQWLRAQLGIVSQEPILF 1054
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 DCSIAENIAYGDNSRVVSQDEIVRAAkeaNIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1134
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564345546 1135 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIDNG 1180
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
323-494 |
1.46e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.93 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 323 NLEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------RNfnv 395
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelepadRD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 396 rclrefIGVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIKKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRI 471
Cdd:PRK11650 78 ------IAMVFQNYALYPhMSVRENMAYGlkiRG-MPKAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRV 143
|
170 180
....*....|....*....|...
gi 564345546 472 AIARALVRNPKILLLDEATSALD 494
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
965-1187 |
1.84e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.52 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVVFNYptRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE----AKKLN 1036
Cdd:PRK13649 2 GINLQNVSYTY--QAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1037 VQWLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVRAAKEAnihpfiETLPQKYETRVGDKGTQLSGGQKQR 1114
Cdd:PRK13649 80 IKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1115 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1187
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
324-542 |
2.23e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 105.27 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpSRANIKilkgLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclREFIG 403
Cdd:cd03298 1 VRLDKIRFSY-GEQPMH----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFS-TTIAENIRYGRG------NVTMDEIKKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARA 476
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 477 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 542
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
984-1174 |
2.26e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.40 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFDC 1056
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1057 SIAENIAYGDNSRVVSQDEIVRAAKEANIHPfiETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:PRK14239 101 SIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 564345546 1137 LDTESEKVVQEALDKAREGRTCIVIAHrlsTIQNADLI 1174
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
969-1195 |
2.89e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 969 NEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL--RAQLGI 1046
Cdd:PRK13639 5 RDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1047 VSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVRAAKEAnihpfietlpqkyETRVGDKGTQ------LSGGQKQRIAIA 1118
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEA-------------LKAVGMEGFEnkpphhLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1119 RALIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVIDNGKVKEHGTHQQLLAQK 1195
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
324-494 |
2.92e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.57 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFSTTIAENIRYGRgnvtmdEIKKAVKEANAY-DFIMK--LPqkfDTLVGDRGAQLSGGQKQRIAIARALVRN 480
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170
....*....|....
gi 564345546 481 PKILLLDEATSALD 494
Cdd:PRK10247 156 PKVLLLDEITSALD 169
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
338-510 |
3.02e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 338 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRefIGVVSQEPVLFS-TTI 416
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 417 AENIRYG------RGNVTMDEIKKAVkeanaydfiMKLPQ--KFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:PRK10851 92 FDNIAFGltvlprRERPNAAAIKAKV---------TQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180
....*....|....*....|..
gi 564345546 489 ATSALDTESEAEVQAALDKARE 510
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHE 184
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-547 |
4.10e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.90 E-value: 4.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ------DIRNFNVRCLREFIGVVSQEPVLFS- 413
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 414 TTIAENIRY---GRGNVTMDEIKKAVKEANAYDFIMKlpQKFDTLvGDRGAQLSGGQKQRIAIARALVRNPKILLLDEAT 490
Cdd:PRK14246 105 LSIYDNIAYplkSHGIKEKREIKKIVEECLRKVGLWK--EVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 491 SALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
324-519 |
7.43e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 105.33 E-value: 7.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYP-SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclRefi 402
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVLFS-TTIAENIRYG---RGnvtmdeIKKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIA 472
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGlrlRG------VPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564345546 473 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 519
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
339-554 |
7.66e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.86 E-value: 7.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 339 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISID----GQD--------------IRNFnvRCLRE 400
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKknnhelitnpyskkIKNF--KELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEP--VLFSTTIAENIRYGrgNVTMDEIKKAVKEANAYdFIMKLPQKFDTLvgDRGA-QLSGGQKQRIAIARAL 477
Cdd:PRK13631 117 RVSMVFQFPeyQLFKDTIEKDIMFG--PVALGVKKSEAKKLAKF-YLNKMGLDDSYL--ERSPfGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 478 VRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKEGIY 554
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
977-1192 |
8.58e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.39 E-value: 8.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FD 1055
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENIAYGDN---SRVVSQDEIVRAAKEanihpfiETLPQKYETRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLD 1131
Cdd:PRK09536 92 FDVRQVVEMGRTphrSRFDTWTETDRAAVE-------RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1132 EATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:PRK09536 165 EPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
975-1191 |
8.86e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 103.74 E-value: 8.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 975 YPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILF 1054
Cdd:cd03263 10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 D-CSIAENIAYgdNSRV--VSQDEIvraakEANIHPFIET--LPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLL 1129
Cdd:cd03263 88 DeLTVREHLRF--YARLkgLPKSEI-----KEEVELLLRVlgLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1130 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1191
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
984-1180 |
9.81e-25 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 104.08 E-value: 9.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLraqlgIVSQEPILFD-CSIAENI 1062
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1063 AYGDNS-----RVVSQDEIVRaakeanihpfiETLPQKYETRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:TIGR01184 76 ALAVDRvlpdlSKSERRAIVE-----------EHIALVGLTEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564345546 1137 LDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIDNG 1180
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
981-1184 |
1.15e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 104.05 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGTVLLDGQEAKKLN----VQWLRAQLGIVSQE--- 1050
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfql 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1051 -PILfdcSIAENIAY-----GDNsrvvsqDEIVRAAKEanihpfietLpqkyeTRVGDKG------TQLSGGQKQRIAIA 1118
Cdd:COG4181 102 lPTL---TALENVMLplelaGRR------DARARARAL---------L-----ERVGLGHrldhypAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1119 RALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVIDNGKVKE 1184
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
340-542 |
1.18e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 103.50 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLYDP--TEGTISIDGQDIRNFNVRclrEFIGVVSQEPVLFST-T 415
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRKPDQFQ---KCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 416 IAENIRYGRGNVTMDEIKKAVKEANAYDFIMKlpQKFDTLVGD-RGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 494
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKKRVEDVLLR--DLALTRIGGnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 495 TESEAEVQAAL-DKAREGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQG 542
Cdd:cd03234 176 SFTALNLVSTLsQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
322-559 |
1.38e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 111.79 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 322 GNLEFSDVHFSYpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 400
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFSTTIAENIRyGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALV-R 479
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 480 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELI-KKEGIYFRLV 558
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVmNRQSIFHSMV 1543
|
.
gi 564345546 559 N 559
Cdd:PTZ00243 1544 E 1544
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
976-1186 |
1.41e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 102.24 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 976 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGTVLLDGqeaKKLNVQWLRAQLGIVSQEPIL 1053
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 FDC-SIAENIAYgdnsrvvsqdeivrAAKeanihpfietLpqkyetrvgdKGtqLSGGQKQRIAIARALIRQPRVLLLDE 1132
Cdd:cd03213 94 HPTlTVRETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1133 ATSALDTESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVIDNGKVKEHG 1186
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
324-547 |
1.67e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 103.37 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------Rnfnvr 396
Cdd:TIGR03410 1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklppheR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 397 cLREFIGVVSQEPVLFST-TIAENIRYGrgnvtMDEIKKAVKEANayDFIMKL-PQKFDTLvGDRGAQLSGGQKQRIAIA 474
Cdd:TIGR03410 73 -ARAGIAYVPQGREIFPRlTVEENLLTG-----LAALPRRSRKIP--DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 475 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
983-1194 |
1.74e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 104.28 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE-------------AKKLNVQWLRAQLGIVSQ 1049
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1050 EPILFD-CSIAENIAYGDN-----SRVVSQDEIVRAAKEANIHpfiETLPQKYETrvgdkgtQLSGGQKQRIAIARALIR 1123
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPIqvlglSKQEARERAVKYLAKVGID---ERAQGKYPV-------HLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1124 QPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-542 |
1.85e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 103.77 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGTISIDGQDIRNFNVRCL--REFIGVVSQEPVLFS 413
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 414 -TTIAENIRYG-------RGNVTMDE-IKKAVKEANAYDFIMklpqkfDTLvGDRGAQLSGGQKQRIAIARALVRNPKIL 484
Cdd:PRK14267 99 hLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWDEVK------DRL-NDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 485 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHR-LSTVRNADVIAGFEDGVIVEQG 542
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
59-277 |
2.24e-24 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 104.81 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 59 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 138
Cdd:cd18552 54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 139 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 218
Cdd:cd18552 134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 219 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSV 277
Cdd:cd18552 214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
972-1198 |
2.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 105.32 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 972 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV---------------LLDGQEAKKL- 1035
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnheLITNPYSKKIk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1036 NVQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEivrAAKEANIH--------PFIETLPqkyetrvgdkgT 1105
Cdd:PRK13631 110 NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYlnkmglddSYLERSP-----------F 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1106 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVK 1183
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKIL 255
|
250
....*....|....*
gi 564345546 1184 EHGTHQQLLAQKGIY 1198
Cdd:PRK13631 256 KTGTPYEIFTDQHII 270
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
976-1186 |
2.69e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 102.45 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 976 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD 1055
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 -CSIAENIAYGDNSRVVSQDEIVRAAKE-ANIHPFIETLpqkyETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:cd03266 92 rLTARENLEYFAGLYGLKGDELTARLEElADRLGMEELL----DRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1134 TSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIDNGKVKEHG 1186
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
966-1186 |
3.44e-24 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 101.91 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlrAQLG 1045
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVRAAKEANIHpfietlpqkyeTRVGDKGTQLSGGQKQRIAIARALIRQ 1124
Cdd:cd03268 76 ALIEAPGFYPnLTARENLRLLARLLGIRKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1125 PRVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1186
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
324-543 |
4.20e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.25 E-value: 4.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANIK--------ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPTEGTISIDGQDIRNFNV 395
Cdd:PRK15134 276 LDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 396 RCL---REFIGVVSQEP---------VLfsTTIAENIRYGRGNVTMDEIKKAVKEAnaydfiMKlPQKFDTLVGDR-GAQ 462
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------ME-EVGLDPETRHRyPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 463 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNA--DVIAgFEDGVI 538
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALchQVIV-LRQGEV 504
|
....*
gi 564345546 539 VEQGS 543
Cdd:PRK15134 505 VEQGD 509
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
965-1188 |
4.42e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE---AKKLN---VQ 1038
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSekaIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1039 WLRAQLGIVSQE----PILfdcSIAENIAYGDnSRVVSQdeivraAKEANIHPFIETLPQkyeTRVGDKGT----QLSGG 1110
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLIEAP-CKVLGL------SKEQAREKAMKLLAR---LRLTDKADrfplHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1111 QKQRIAIARALIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTH 1188
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
334-542 |
4.78e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 101.68 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 334 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIrNFNVRCLREFIGVVSQEPVLFS 413
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 414 -TTIAENIRY--GRGNVTMDEIKKAVKEanaydfimkLPQKFDT--LVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:cd03266 92 rLTARENLEYfaGLYGLKGDELTARLEE---------LADRLGMeeLLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 489 ATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFEDGVIVEQG 542
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
983-1182 |
5.04e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 101.96 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GTVLLDGQEAKKlnVQWLRaQLGIVSQEPILFDC-SI 1058
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 AENIAYGDNSRV-VSQDEIVRAAKEAnihpfIETLPQKYETRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:cd03234 99 RETLTYTAILRLpRKSSDAIRKKRVE-----DVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564345546 1137 LDTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVIDNGKV 1182
Cdd:cd03234 174 LDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
345-547 |
7.18e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 104.81 E-value: 7.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 345 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGqdirnfnvRCL------------REFIGVVSQEPVLF 412
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG--------RTLfdsrkgiflppeKRRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 413 S-TTIAENIRYGRGNVTMDEikKAVKEANAYDFImklpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 491
Cdd:TIGR02142 88 PhLSVRGNLRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 492 ALDTESEAEVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 547
Cdd:TIGR02142 161 ALDDPRKYEILPYLERlHAEFGIPILyVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
978-1192 |
7.24e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.16 E-value: 7.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 978 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDC 1056
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1057 SIAENIAYG--DNSRVVSQD-EIVRAA-KEANIHPFIEtlpQKYetrvgdkgTQLSGGQKQRIAIARALIR------QPR 1126
Cdd:PRK13548 92 TVEEVVAMGraPHGLSRAEDdALVAAAlAQVDLAHLAG---RDY--------PQLSGGEQQRVQLARVLAQlwepdgPPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1127 VLLLDEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:PRK13548 161 WLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
965-1138 |
8.06e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 104.54 E-value: 8.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpMAGTVLLDGQeakklnvqwlr 1041
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGR----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1042 aqlgIVSQ-EPILFDC-------------SIAENIAYGDNSRVVSQDEIVR----AAKEANIHPFIETLPQkyetrvgdk 1103
Cdd:PRK11650 67 ----VVNElEPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIEErvaeAARILELEPLLDRKPR--------- 133
|
170 180 190
....*....|....*....|....*....|....*
gi 564345546 1104 gtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1138
Cdd:PRK11650 134 --ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
342-569 |
1.18e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.12 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF----IGVVSQEPVLFS-TTI 416
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 417 AENIRYGrgnVTMDEIKKAVKEANAYDFIMKLpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 496
Cdd:PRK10070 124 LDNTAFG---MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 497 SEAEVQAALDK--AREGRTTIVIAHRL-STVRNADVIAGFEDGVIVEQGSHSELIKKEG-----IYFRLVNMqtsgSQIL 568
Cdd:PRK10070 199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyvrTFFRGVDI----SQVF 274
|
.
gi 564345546 569 S 569
Cdd:PRK10070 275 S 275
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
326-519 |
1.41e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 326 FSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGqdirnfNVRclrefIGVV 405
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 406 SQEPVLFST-TIAENIRYGRGNV--TMDEIKKAVK--------------------EANAYDF------IMK---LPQK-F 452
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELraLEAELEELEAklaepdedlerlaelqeefeALGGWEAearaeeILSglgFPEEdL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 453 DTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAEVqaaldKAREGrTTIVIAH 519
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
983-1184 |
1.44e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 101.69 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN----------VQWL----------RA 1042
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsisavnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQEPI--LFDCSIAENIAygdnsRVvsqDEIVRAAKEANIHpfIETLPQkyetrvgdkgtQLSGGQKQRIAIARA 1120
Cdd:PRK10419 107 TVREIIREPLrhLLSLDKAERLA-----RA---SEMLRAVDLDDSV--LDKRPP-----------QLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1121 LIRQPRVLLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKE 1184
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
342-519 |
1.63e-23 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 100.62 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLrefigVVSQEPVLFS-TTIAENI 420
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 421 RYGRGNVtMDEIKKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIAIARALVRNPKILLLDEATSALD 494
Cdd:TIGR01184 76 ALAVDRV-LPDLSKSERRAIVEEHI--------ALVGLTEAadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*..
gi 564345546 495 TESEAEVQAALDKARE--GRTTIVIAH 519
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEehRVTVLMVTH 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
984-1195 |
1.79e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.83 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQ--EPILFDCS 1057
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAYGDNSRVVSQDEivraAKEANIhpfietlpqKYETRVG------DKGT-QLSGGQKQRIAIARALIRQPRVLLL 1130
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1131 DEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLAQK 1195
Cdd:PRK13641 170 DEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
988-1195 |
1.83e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.43 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 988 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILFD-CSIAENIAYGD 1066
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1067 NSRV---VSQDEIVRA-AKEANIHPFIETLPqkyetrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD---- 1138
Cdd:PRK10771 97 NPGLklnAAQREKLHAiARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1139 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLLAQK 1195
Cdd:PRK10771 166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
983-1192 |
2.01e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.89 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---MAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILF-D 1055
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFieTLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1136 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
324-536 |
2.11e-23 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 99.71 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKST----TVQLLQRLYDPTEGTISIDGQDIRNFNVRCLR 399
Cdd:cd03290 1 VQVTNGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSlllaILGEMQTLEGKVHWSNKNESEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 400 EFIGVVSQEPVLFSTTIAENIRYGrgNVTMDEIKKAVKEANAYD-FIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALV 478
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 479 RNPKILLLDEATSALDTE-SEAEVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFEDG 536
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
978-1192 |
2.30e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 100.54 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 978 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-TVLLDGQEAKKLNVQWLRAQLGIVSQEpilfdc 1056
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLVSPA------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1057 sIAENIAYGDNSR--VVS------------QDEIVRAAKEAnihpfIETLpqkyetRVGDKG----TQLSGGQKQRIAIA 1118
Cdd:COG1119 87 -LQLRFPRDETVLdvVLSgffdsiglyrepTDEQRERAREL-----LELL------GLAHLAdrpfGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1119 RALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVIDNGKVKEHGTHQQLL 1192
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAGPKEEVL 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
324-551 |
2.62e-23 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 99.92 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV-RCLREFI 402
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVLF-STTIAENIRygrgnVTMDEIKKAVKEANaydfimklpQKFDTLVGD---------RGAQLSGGQKQRIA 472
Cdd:cd03218 78 GYLPQEASIFrKLTVEENIL-----AVLEIRGLSKKERE---------EKLEELLEEfhithlrksKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 473 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HR----LSTVRNADVIAgfeDGVIVEQGSHSEL 547
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRAYIIY---EGKVLAEGTPEEI 220
|
....
gi 564345546 548 IKKE 551
Cdd:cd03218 221 AANE 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
981-1163 |
2.65e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 99.82 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE-----AKKLNVQWL---RAQLGIVSQ--- 1049
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQASPREILalrRRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1050 ------------EPILfdcsiaeniaygdnSRVVSQDEIVRAAKEA----NIHPFIETLPQkyetrvgdkgTQLSGGQKQ 1113
Cdd:COG4778 104 viprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLPERLWDLPP----------ATFSGGEQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1114 RIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH 1163
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
324-551 |
2.80e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVL-FSTTIAENIRYGRGnvTMDEIKKAVKEanaydfimkLPQKFDTLVG-----DRG-AQLSGGQKQRIAIARA 476
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRA--PHGLSRAEDDA---------LVAAALAQVDlahlaGRDyPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 477 LVR------NPKILLLDEATSALDTESEAEV-QAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVlRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEV 228
|
....
gi 564345546 548 IKKE 551
Cdd:PRK13548 229 LTPE 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
982-1163 |
2.86e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.54 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEakklnVQWLRAQLGIVSQ-EPILFDCSIAE 1060
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQnEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1061 NIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1140
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*
gi 564345546 1141 SEKVVQEALDK--AREGRTCIVIAH 1163
Cdd:PRK11248 163 TREQMQTLLLKlwQETGKQVLLITH 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
324-550 |
3.34e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.35 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDgqDI------RNFNV 395
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 396 RCLREFIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKE-----ANAYDFIMKLPqkfdtlvgdrgAQLSGG 466
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 467 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSH 544
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*.
gi 564345546 545 SELIKK 550
Cdd:PRK13643 229 SDVFQE 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
322-580 |
3.69e-23 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 100.70 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 322 GNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDpTEGTISIDGQDIRNFNVRCLREF 401
Cdd:cd03289 1 GQMTVKDLTAKYTEGGN-AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEPVLFSTTIAENIR-YGRGNvtMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 480
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 481 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL--------------STVRNADVIAGF--EDGVIVEQGSH 544
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIeamlecqrflvieeNKVRQYDSIQKLlnEKSHFKQAISP 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 564345546 545 SELIKKEGIYFRLVNMQTSGSQI--LSEEFEVELSDEK 580
Cdd:cd03289 237 SDRLKLFPRRNSSKSKRKPRPQIqaLQEETEEEVQDTR 274
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
324-543 |
3.94e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.83 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN-VRCLREFI 402
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEP--VLFSTTIAENIRYGRGNVTMD--EIKKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQRIAIARALV 478
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 479 RNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 543
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
967-1182 |
4.18e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.72 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 967 TFNEVVfnyptrANvpvlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEakklnVQW------L 1040
Cdd:COG3845 14 RFGGVV------AN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP-----VRIrsprdaI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1041 RAQLGIVSQEPILFDC-SIAENIAYG-DNSRVVSQDeIVRAAKEanihpfIETLPQKY------ETRVGDkgtqLSGGQK 1112
Cdd:COG3845 79 ALGIGMVHQHFMLVPNlTVAENIVLGlEPTKGGRLD-RKAARAR------IRELSERYgldvdpDAKVED----LSVGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1113 QRIAIARALIRQPRVLLLDEATSAL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIDNGKV 1182
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
983-1186 |
4.59e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.92 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF- 1054
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 DCSIAENIAYGD--NSRVVSQ---DEIVR-AAKEAnihpfieTLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVL 1128
Cdd:PRK14267 99 HLTIYDNVAIGVklNGLVKSKkelDERVEwALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1129 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlSTIQNA---DLIVVIDNGKVKEHG 1186
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
983-1187 |
5.13e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 99.14 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlRAQLGI--VSQEPILF-DCSIA 1059
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1060 ENIAYGDNsrvvsqdeiVRAAKEANIHPFIETL-PQKYETRvGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1138
Cdd:TIGR03410 94 ENLLTGLA---------ALPRRSRKIPDEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1139 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGT 1187
Cdd:TIGR03410 164 PSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
982-1193 |
8.17e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 99.70 E-value: 8.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ--EAKKLNVQWLRAQLGIVSQEP--ILFDCS 1057
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAYGDNSRVVSQDEIVRAAKEAnihpfiETLPQKYETRvgDKGTQ-LSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEA------LTLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1137 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:PRK13638 167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
41-294 |
8.22e-23 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 99.87 E-value: 8.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 41 EEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGD 120
Cdd:cd18575 33 ALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 121 KVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFG 200
Cdd:cd18575 113 SLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 201 GQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIgAFSVGQ 279
Cdd:cd18575 193 REDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGElSQFVFYAVLA-AGSVGA 271
|
250
....*....|....*
gi 564345546 280 AAPCIDAFANARGAA 294
Cdd:cd18575 272 LSEVWGDLQRAAGAA 286
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
979-1195 |
8.46e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 8.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 979 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDCS 1057
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAYGDN------SRVVSQDE-IVRAAKEANihpFIETLPQKyetRVgdkgTQLSGGQKQRIAIARALIRQPRVLLL 1130
Cdd:PRK11231 93 VRELVAYGRSpwlslwGRLSAEDNaRVNQAMEQT---RINHLADR---RL----TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1131 DEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLLAQK 1195
Cdd:PRK11231 163 DEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
324-550 |
8.53e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.99 E-value: 8.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGTISIDGQDIRNFNV--RClR 399
Cdd:COG0396 1 LEIKNLHVSVEGK---EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPdeRA-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 400 EFIGVVSQEPV--------LFSTTIAENIRygRGNVTMDEIKKAVKEANAydfIMKLPQKFdtlvGDRG--AQLSGGQKQ 469
Cdd:COG0396 77 AGIFLAFQYPVeipgvsvsNFLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 470 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGShSE 546
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KE 226
|
....
gi 564345546 547 LIKK 550
Cdd:COG0396 227 LALE 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
982-1175 |
1.36e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.86 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1061
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1062 IAYGDNSRVVSQDEivrAAKEANIHPFieTLPqkyETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1141
Cdd:PRK10247 101 LIFPWQIRNQQPDP---AIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 564345546 1142 EKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIV 1175
Cdd:PRK10247 173 KHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVI 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
333-547 |
1.38e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 101.26 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 333 YPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdiRNFNVRCLREFIGVVSQEPVLF 412
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 413 S-TTIAENIRYGR--GNVTMDEIKKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 489
Cdd:PRK11000 88 PhLSVAENMSFGLklAGAKKEEINQRVNQVAE---VLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 490 TSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
983-1189 |
1.44e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDG------QEAKKLNVQWLRAQLGIVSQE----PI 1052
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1053 LfdcSIAENIAYGDnSRV--VSQDEIVRAAKEanihpFIETLpqkyetRVGDKGT----QLSGGQKQRIAIARALIRQPR 1126
Cdd:PRK11124 97 L---TVQQNLIEAP-CRVlgLSKDQALARAEK-----LLERL------RLKPYADrfplHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1127 VLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQ 1189
Cdd:PRK11124 162 VLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
345-519 |
1.60e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.07 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 345 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnVRCLREFIGVVSQEPVLFS-TTIAENIRYG 423
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFPhMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 424 --RGNVTMDEIKKAVKE----ANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE- 496
Cdd:PRK11607 116 lkQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKl 184
|
170 180
....*....|....*....|....*.
gi 564345546 497 ---SEAEVQAALDkaREGRTTIVIAH 519
Cdd:PRK11607 185 rdrMQLEVVDILE--RVGVTCVMVTH 208
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
329-547 |
2.00e-22 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 98.78 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 329 VHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnvrclrefIGVVSQE 408
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 409 PVLFSTTIAENIRYGrgnVTMDEI--KKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 486
Cdd:cd03291 107 SWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 487 DEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 547
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
983-1191 |
2.11e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAEN 1061
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1062 IAYG---------DNSRVVSQD-----EIVRAAKEANIHPfietlpqkyetrvgdkgTQLSGGQKQRIAIARALIRQPRV 1127
Cdd:PRK10851 95 IAFGltvlprrerPNAAAIKAKvtqllEMVQLAHLADRYP-----------------AQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1128 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVIDNGKVKEHGTHQQL 1191
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
982-1193 |
2.62e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 96.84 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVqWLRAQLGI--VSQEPILF-DCSI 1058
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 AENIAYGDNSRVVSQDEIVRAAkEANIHPF-IETLPQKyetrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1137
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1138 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
975-1194 |
2.67e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.34 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 975 YPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEP--I 1052
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1053 LFDCSIAENIAYGDNSRVVSQDEIVRAAKEAnihpfIETLP-QKYETRVGDkgtQLSGGQKQRIAIARALIRQPRVLLLD 1131
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSA-----LHMLGlEELRDRVPH---HLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1132 EATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
971-1182 |
2.81e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.85 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 971 VVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVqWLRAQL-GIVSQ 1049
Cdd:COG1101 9 KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAKYiGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1050 EPILFDC---SIAEN--IAYGDNSRVvsqdEIVRAAKEANIHPFIET-------LPQKYETRVGdkgtQLSGGQKQRIAI 1117
Cdd:COG1101 88 DPMMGTApsmTIEENlaLAYRRGKRR----GLRRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1118 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKV 1182
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
979-1186 |
2.86e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 96.20 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 979 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeaKKLNVQwLRAQLGIVSQEPILF-DCS 1057
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIA-ARNRIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAYGDNSRVVSQDEIVRAAKEanihpFIET--LPQKYETRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:cd03269 87 VIDQLVYLAQLKGLKKEEARRRIDE-----WLERleLSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1136 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1186
Cdd:cd03269 158 GLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
346-548 |
3.68e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 346 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnvrclrefiGVVSQEPV--------LFS-TTI 416
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT----------TPPSRRPVsmlfqennLFShLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 417 AENIRYG-RGNVTMDEIKKAVKEANAY-----DFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIARALVRNPKILLLDEAT 490
Cdd:PRK10771 89 AQNIGLGlNPGLKLNAAQREKLHAIARqmgieDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 491 SALDTESEAEVQAALDKAREGR--TTIVIAHRLS-TVRNAD---VIAgfeDGVIVEQGSHSELI 548
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPrslVVA---DGRIAWDGPTDELL 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
325-551 |
3.88e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 325 EFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 404
Cdd:COG4604 3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 405 VSQEPVLFST-TIAENIRYGR-----GNVTmDEIKKAVKEANAYDFIMKLPQKF-DtlvgdrgaQLSGGQKQRIAIARAL 477
Cdd:COG4604 80 LRQENHINSRlTVRELVAFGRfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 478 VRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLstvrN-----ADVIAGFEDGVIVEQGSHSELIKK 550
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEIITP 226
|
.
gi 564345546 551 E 551
Cdd:COG4604 227 E 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
966-1187 |
4.08e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVvfNYPTRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV----LLDGQEAKKLNV 1037
Cdd:PRK13643 2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1038 QWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVRAAKE-----ANIHPFIETLPqkyetrvgdkgTQLSGG 1110
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1111 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1187
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
341-538 |
4.51e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.06 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTIsIDGqdirNFNVRCLREFIGVVSQEPVLFS-TTIAEN 419
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 420 IRYG-RGNvtmdeIKKAVKEANAydfimklpqkfdtLVG--DRG----AQLSGGQKQRIAIARALVRNPKILLLDEATSA 492
Cdd:PRK11247 102 VGLGlKGQ-----WRDAALQALA-------------AVGlaDRAnewpAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564345546 493 LDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVI 538
Cdd:PRK11247 164 LDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
324-520 |
4.63e-22 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 94.14 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVhfSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISidgqdirnfnvRCLREFIG 403
Cdd:cd03223 1 IELENL--SLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFSTTIAENIRYGRGNVtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 483
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 564345546 484 LLLDEATSALDTESEAEVqaaLDKAREGRTTIV-IAHR 520
Cdd:cd03223 113 VFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
339-543 |
4.63e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 97.03 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 339 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV--RCLRefiGVVS--QEPVLFST 414
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhrIARL---GIARtfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 415 -TIAENIRYGRGNVTMDEIKKAV--------KEANAYDFIM------KLPQKFDTLVGDrgaqLSGGQKQRIAIARALVR 479
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEellervGLADRADEPAGN----LSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 480 NPKILLLDEATSALdteSEAEVQAALD-----KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGS 543
Cdd:COG0411 170 EPKLLLLDEPAAGL---NPEETEELAElirrlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
324-547 |
5.78e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 96.83 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAN------IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ--DIRNFNV 395
Cdd:COG4167 5 LEVRNLSKTFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHklEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 396 RCLRefIGVVSQEPvlfSTTIAENIRYG-------RGNVTMDEikkavKEANAydfimklpQKFDTL--VGDRGAQ---- 462
Cdd:COG4167 85 RCKH--IRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTA-----EEREE--------RIFATLrlVGLLPEHanfy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 463 ---LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------EVQaaldkAREGRTTIVIAHRLSTVRN-ADVIA 531
Cdd:COG4167 147 phmLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqiinlmlELQ-----EKLGISYIYVSQHLGIVKHiSDKVL 221
|
250
....*....|....*.
gi 564345546 532 GFEDGVIVEQGSHSEL 547
Cdd:COG4167 222 VMHQGEVVEYGKTAEV 237
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
695-1207 |
7.96e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 102.75 E-value: 7.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 695 VLSFFTFFlqGFTFGKAGEI--------LTTRLRSMAFKAMLRQDMSWFDD-HKN-STGALSTRLATDAAQVQgatgtrl 764
Cdd:PLN03232 342 VYAFLIFF--GVTFGVLCESqyfqnvgrVGFRLRSTLVAAIFHKSLRLTHEaRKNfASGKVTNMITTDANALQ------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 765 aLIAQNTANLGTG---IIISFIYGWQL--------TLLLLSVVPFIAVAgIVEMKMLA--GNAKRDKKEmeaagKIATEA 831
Cdd:PLN03232 413 -QIAEQLHGLWSApfrIIVSMVLLYQQlgvaslfgSLILFLLIPLQTLI-VRKMRKLTkeGLQWTDKRV-----GIINEI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 832 IENIRTVVSLTQERKFESMyVEKLHGPYRNSVRKAHIygitFSISQAFMYFS---YAGCFRFGSYLIVNGHMRFKDVILV 908
Cdd:PLN03232 486 LASMDTVKCYAWEKSFESR-IQGIRNEELSWFRKAQL----LSAFNSFILNSipvVVTLVSFGVFVLLGGDLTPARAFTS 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 909 FSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLF--ERQPLIDSYSREGMWPdkfegSVTFNEVVFNYPTRANVPVLQG 986
Cdd:PLN03232 561 LSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLlsEERILAQNPPLQPGAP-----AISIKNGYFSWDSKTSKPTLSD 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 987 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLdgqeakklnvqwLRAQLGIVSQEPILFDCSIAENIAYGD 1066
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFGS 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1067 NsrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE-SEKVV 1145
Cdd:PLN03232 704 D---FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVF 780
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1146 QEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQlLAQKGIYFSMVNIQAG 1207
Cdd:PLN03232 781 DSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAG 841
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
339-551 |
1.16e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.08 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 339 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF------------------------N 394
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 395 VRCLREFIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDEiKKAVKEANAYDFIMKLPQKFDtlvgDRGA-QLSGGQKQRI 471
Cdd:PRK13651 100 IKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 472 AIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTV--RNADVIAgFEDGVIVEQGSHSELI 548
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRTIF-FKDGKIIKDGDTYDIL 253
|
...
gi 564345546 549 KKE 551
Cdd:PRK13651 254 SDN 256
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
643-900 |
1.23e-21 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 96.73 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMIaifgpgDDTVKQQKCN---MFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRL 719
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII------DSVIGGGLREllwLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 720 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFI 799
Cdd:cd18542 75 RNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 800 AVAGIVEMKMLaGNAKRDKKEMEAA-GKIATEAIENIRTVVSLTQErKFESMYVEKLHGPYRN-SVRKAHIYGITFSISQ 877
Cdd:cd18542 153 ALFSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFARE-DYEIEKFDKENEEYRDlNIKLAKLLAKYWPLMD 230
|
250 260
....*....|....*....|...
gi 564345546 878 AFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18542 231 FLSGLQIVLVLWVGGYLVINGEI 253
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
335-510 |
1.40e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.47 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 335 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGTISIDGQDIRNFNVRcLREfIGVVSQEPVL 411
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRR-IGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 412 FS-TTIAENIRYG-----RGNVTMDEIKKAVKEANAYDFimklpqkfdtlvGDRG-AQLSGGQKQRIAIARALVRNPKIL 484
Cdd:COG4136 88 FPhLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRALLAEPRAL 155
|
170 180
....*....|....*....|....*..
gi 564345546 485 LLDEATSALDTESEAEVQA-ALDKARE 510
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREfVFEQIRQ 182
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
332-528 |
1.52e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 332 SYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGqdirnfNVRclrefIGVVSQ---E 408
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------GAR-----VAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 409 PVLFSTTIAENIRYGR-------GNVTMDEiKKAVKEAnaydfIMKLpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 481
Cdd:NF040873 67 PDSLPLTVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564345546 482 KILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRNAD 528
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
972-1191 |
2.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.31 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 972 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV-----------------------LLD 1028
Cdd:PRK13651 11 IFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklVIQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1029 GQEAKKL-NVQWLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVRAAKEanihpFIET--LPQKYETRvgdK 1103
Cdd:PRK13651 91 KTRFKKIkKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIELvgLDESYLQR---S 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1104 GTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVIDNGK 1181
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
250
....*....|.
gi 564345546 1182 -VKEHGTHQQL 1191
Cdd:PRK13651 243 iIKDGDTYDIL 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
981-1181 |
2.34e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 99.23 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMA---GTVLLDGQEAKKLNVQWL-RAQLGIVSQEPILF-D 1055
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALVkE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENIAYGD---NSRVVSQDEIVRAAKE------ANIHPfietlpqkyETRVGDkgtqLSGGQKQRIAIARALIRQPR 1126
Cdd:PRK13549 97 LSVLENIFLGNeitPGGIMDYDAMYLRAQKllaqlkLDINP---------ATPVGN----LGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1127 VLLLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGK 1181
Cdd:PRK13549 164 LLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
983-1193 |
3.68e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.01 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGTVLLDGQEAKKLNVQWL---RAQLGIVSQEP---ILFDC 1056
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1057 SIAENIAYGDNsrvVSQDEIVRAAKEANIHPFIETLPQKYETRvGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:PRK15134 380 NVLQIIEEGLR---VHQPTLSAAQREQQVIAVMEEVGLDPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1137 LDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:PRK15134 456 LD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
640-1195 |
3.73e-21 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 100.76 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 640 WPYFVVGTLCAI--ANGALQPafsIILSEMIAIFGPGDDTVKQQKcnmfslVFLGLGVLSFF---TFFLQGFTFG--KAG 712
Cdd:TIGR01271 80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASYDPFNAPEREIA------YYLALGLCLLFivrTLLLHPAIFGlhHLG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 713 EILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQV-QGATGTRLALIAQNTANLGTGIIISFIYGWQLTLL 791
Cdd:TIGR01271 151 MQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFdEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 792 LLSVVPFIAVAGIVEMKMlagnAKRDKKemeaAGKIA------TEAIENIRTVVSLTQERKFESMyVEKLHGPYRNSVRK 865
Cdd:TIGR01271 229 GFLILLALFQACLGQKMM----PYRDKR----AGKISerlaitSEIIENIQSVKAYCWEEAMEKI-IKNIRQDELKLTRK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 866 AhiygitfsisqAFMYFSYAGCFRFGSYLIVNG----HMRFKDVIL--VFSA----IVL---------GAVALGHASSFA 926
Cdd:TIGR01271 300 I-----------AYLRYFYSSAFFFSGFFVVFLsvvpYALIKGIILrrIFTTisycIVLrmtvtrqfpGAIQTWYDSLGA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 927 ----PDYAKAKLSAAYLFSLFERQPLIDSYS---REGMwPDKFEGSVTFNE----------VVFNYPTRANVPVLQGLSL 989
Cdd:TIGR01271 369 itkiQDFLCKEEYKTLEYNLTTTEVEMVNVTaswDEGI-GELFEKIKQNNKarkqpngddgLFFSNFSLYVTPVLKNISF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 990 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQeakklnvqwlraqLGIVSQEPILFDCSIAENIAYGdnsr 1069
Cdd:TIGR01271 448 KLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFG---- 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1070 vVSQDEI--VRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQE 1147
Cdd:TIGR01271 511 -LSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 564345546 1148 A-LDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQK 1195
Cdd:TIGR01271 590 ScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
30-269 |
3.89e-21 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 95.19 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 30 LSMLNPG-------RILEEEMTRYAYYYSG--LGGGVL--LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIK 98
Cdd:cd18542 14 LNLLIPLlirriidSVIGGGLRELLWLLALliLGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 99 GTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLST--------AVWAKI--- 167
Cdd:cd18542 94 RTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSyvffkkvrPAFEEIreq 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 168 ---LSTFsdkelaayakagavAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYAL 244
Cdd:cd18542 174 egeLNTV--------------LQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVL 239
|
250 260
....*....|....*....|....*
gi 564345546 245 AFWYGSTLVISKEYTIGNaMTVFFS 269
Cdd:cd18542 240 VLWVGGYLVINGEITLGE-LVAFIS 263
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
335-542 |
3.97e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 335 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVL-FS 413
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 414 TTIAENIRYGRGN-----VTMDEI-KKAVKEA-NAYDFIMKLPQKFDTlvgdrgaqLSGGQKQRIAIARALVRNPKILLL 486
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTETdRAAVERAmERTGVAQFADRPVTS--------LSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 487 DEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 542
Cdd:PRK09536 164 DEPTASLDINHQVRtLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
983-1193 |
4.14e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.64 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqEAKKLNVQWLRAQLGIVSQ----EPilfDCSI 1058
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVGVVPQfdnlDP---DFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 AENIaygdnsRVVSQDEIVRAAK-EANIHPFIE--TLPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:PRK13537 98 RENL------LVFGRYFGLSAAAaRALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1136 ALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:PRK13537 168 GLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
988-1192 |
4.19e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.41 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 988 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL----RAQLGIVSQE-PILFDCSIAENI 1062
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1063 AYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYEtrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESE 1142
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1143 KVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:PRK10070 201 TEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
983-1182 |
4.75e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.97 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLL------DGQEAKKLNVQWLRaqlgivsqepILFDC 1056
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgtaplaEAREDTRLMFQDAR----------LLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1057 SIAENIAYG--DNSRvvsqdeivRAAKEAnihpfIETLpqKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1134
Cdd:PRK11247 97 KVIDNVGLGlkGQWR--------DAALQA-----LAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1135 SALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKV 1182
Cdd:PRK11247 162 GALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
980-1187 |
5.37e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.59 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPMAGTVLLDGQEAKKLNVQwLRAQLGI-VS-QEPI-- 1052
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1053 --------LfdcSIAENIAYGDNSRVV-SQDEIVRAAKEANihpfietLPQKYETR---VGdkgtqLSGGQKQRIAIARA 1120
Cdd:COG0396 90 pgvsvsnfL---RTALNARRGEELSAReFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1121 LIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIDNGKVKEHGT 1187
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
643-914 |
5.92e-21 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 94.80 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMI-AIFGPGDdtvkQQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRS 721
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLdDIFVEKD----LEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 722 MAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAV 801
Cdd:cd18552 77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 802 AgiveMKMLAGNAKRD-KKEMEAAGKIAT---EAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 877
Cdd:cd18552 155 P----IRRIGKRLRKIsRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 564345546 878 AFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVL 914
Cdd:cd18552 231 LLGAIAIALVLWYGGYQVISGELTPGEFISFITALLL 267
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
322-578 |
9.08e-21 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 99.60 E-value: 9.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 322 GNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDpTEGTISIDGQDIRNFNVRCLREF 401
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEPVLFSTTIAENIR-YGRgnVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 480
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLDpYEQ--WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 481 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL--------------STVRNADVIAGF--EDGVIVEQGSH 544
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVeallecqqflviegSSVKQYDSIQKLlnETSLFKQAMSA 1451
|
250 260 270
....*....|....*....|....*....|....*.
gi 564345546 545 SELIKKEGIYFRLVNMQTSGSQI--LSEEFEVELSD 578
Cdd:TIGR01271 1452 ADRLKLFPLHRRNSSKRKPQPKItaLREEAEEEVQN 1487
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
975-1177 |
1.07e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 975 YPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlraqlgiVSQEPILF 1054
Cdd:NF040873 2 YGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 DCSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFietlpqkyeTRVGDKG------TQLSGGQKQRIAIARALIRQPRVL 1128
Cdd:NF040873 71 PLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDAL---------ERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564345546 1129 LLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVI 1177
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
74-294 |
1.20e-20 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 93.65 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 74 RQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAI 153
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 154 SPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGI 233
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 234 AFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAA 294
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGAL 286
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
324-552 |
1.32e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 91.05 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSypsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL-----YDPTEGTISIDGQDIRNFNV--R 396
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITDLPPeeR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 397 ClREFIGVVSQEPVLFS-TTIAENIRYgrgnvtmdeikkaVKEAnaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIAR 475
Cdd:cd03217 75 A-RLGIFLAFQYPPEIPgVKNADFLRY-------------VNEG-----------------------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGSHS--ELIKK 550
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEK 197
|
..
gi 564345546 551 EG 552
Cdd:cd03217 198 KG 199
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
324-553 |
1.45e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.15 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIrNFNVR---CLRE 400
Cdd:PRK13638 2 LATSDLWFRYQDE---PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEANaydfimklpqkfdTLVGDRGAQ------LSGGQKQR 470
Cdd:PRK13638 78 QVATVFQDPeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG------ 542
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevf 224
|
250
....*....|.
gi 564345546 543 SHSELIKKEGI 553
Cdd:PRK13638 225 ACTEAMEQAGL 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
974-1195 |
1.55e-20 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 93.38 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 974 NYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQlgivsqepil 1053
Cdd:cd03291 44 NLCLVGA-PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPG---------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 fdcSIAENIAYGdnsrvVSQDE-----IVRAAK-EANIHPFietlPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRV 1127
Cdd:cd03291 113 ---TIKENIIFG-----VSYDEyryksVVKACQlEEDITKF----PEKDNTVLGEGGITLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1128 LLLDEATSALDTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQK 1195
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
339-536 |
2.10e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.54 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 339 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPT---EGTISIDGQDIRNFNVR-CLREFIGVVSQEPVLFST 414
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 415 -TIAENIRYG----RGNVtMD------EIKKAVKEanaydfiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVRNPKI 483
Cdd:PRK13549 97 lSVLENIFLGneitPGGI-MDydamylRAQKLLAQ-------LKLDINPATPVGN----LGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 484 LLLDEATSALdTESEAEVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 536
Cdd:PRK13549 165 LILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
987-1194 |
2.35e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.21 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 987 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlRAQLgI--VSQEPilfdcsiaeNIAY 1064
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKH-IrmIFQDP---------NTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1065 GDNSRVVSQ-DEIVR-------AAKEANIhpfIETLpqkyeTRVG-------DKGTQLSGGQKQRIAIARALIRQPRVLL 1129
Cdd:COG4167 101 NPRLNIGQIlEEPLRlntdltaEEREERI---FATL-----RLVGllpehanFYPHMLSSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1130 LDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:COG4167 173 ADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
324-553 |
2.39e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-I 402
Cdd:PRK15439 12 LCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVLF-STTIAENIRYG--RGNVTMDEIKKAVKEANAYdfiMKLPQKFDTL-VGDRgaqlsggqkQRIAIARALV 478
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 479 RNPKILLLDEATSALdTESEAE-----VQAALDKareGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKEG 552
Cdd:PRK15439 157 RDSRILILDEPTASL-TPAETErlfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDI 232
|
.
gi 564345546 553 I 553
Cdd:PRK15439 233 I 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-551 |
2.53e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.33 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIG 403
Cdd:PRK13537 8 IDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQ----EPvlfSTTIAENIR-YGRG-NVTMDEIKKAVkeANAYDFiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 477
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 478 VRNPKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIKKE 551
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
965-1186 |
3.05e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.94 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ-----EAKKLNVqw 1039
Cdd:PRK11000 3 SVTLRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAERGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1040 lraqlGIVSQEPILF-DCSIAENIAYGDNSRVVSQDEI---VRAAKEanihpfIETLPQKYETRVGDkgtqLSGGQKQRI 1115
Cdd:PRK11000 78 -----GMVFQSYALYpHLSVAENMSFGLKLAGAKKEEInqrVNQVAE------VLQLAHLLDRKPKA----LSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDTESEkvVQEALDKA----REGRTCIVIAH-RLSTIQNADLIVVIDNGKVKEHG 1186
Cdd:PRK11000 143 AIGRTLVAEPSVFLLDEPLSNLDAALR--VQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
324-540 |
3.37e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIdGQdirnfNVRclrefIG 403
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLF--STTIAENIRYGRGNVTmdeikkavkEANAYDFIMKL---PQKFDTLVGDrgaqLSGGQKQRIAIARALV 478
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 479 RNPKILLLDEATSALDTESEAEVQAALDkAREGrTTIVIAH-R--LSTVrnADVIAGFEDGVIVE 540
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
983-1166 |
3.66e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.03 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQW---LRAQ-LGIVSQ-EPILFDCS 1057
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAY----GDNSRVVSQDEIVRAAKEANIhpfietlpqkyETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRALEMLAAVGL-----------EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 564345546 1134 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS 1166
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
324-521 |
3.67e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 95.46 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDiRNFN-VRCLREF- 401
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFNgPKSSQEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEPVLFST-TIAENIRYGRGNVT-MDEI--KKAVKEANAYDFIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 477
Cdd:PRK10762 81 IGIIHQELNLIPQlTIAENIFLGREFVNrFGRIdwKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 478 VRNPKILLLDEATSAL-DTESEA------EVQAaldkarEGRTTIVIAHRL 521
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETESlfrvirELKS------QGRGIVYISHRL 201
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
59-280 |
3.85e-20 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 92.37 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 59 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 138
Cdd:cd18784 51 VAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 139 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 218
Cdd:cd18784 131 MFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYK 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 219 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVGQA 280
Cdd:cd18784 211 LKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILYQLELGSC 268
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
332-488 |
5.09e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.47 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 332 SYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLLQrlydPTEGTISIDGQDIRNF--NVRClREFIGVV 405
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDITHLpmHKRA-RLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 406 SQEPVLF-STTIAENIRygrgnvtmdeikkAVKEanaydfIMKLP-----QKFDTLVGD---------RGAQLSGGQKQR 470
Cdd:COG1137 84 PQEASIFrKLTVEDNIL-------------AVLE------LRKLSkkereERLEELLEEfgithlrksKAYSLSGGERRR 144
|
170
....*....|....*...
gi 564345546 471 IAIARALVRNPKILLLDE 488
Cdd:COG1137 145 VEIARALATNPKFILLDE 162
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-551 |
5.53e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIG 403
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVL-FSTTIAEN-IRYGR-GNVTMDEIKKAVkeANAYDFiMKLPQKFDTLVgdrgAQLSGGQKQRIAIARALVRN 480
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRyFGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 481 PKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIKKE 551
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
966-1179 |
6.60e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 87.98 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNypTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklnvqwlRAQLG 1045
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFDCSIAENIAYgdnsrvvsqdeivraakeanihPFietlpqkyetrvgdkGTQLSGGQKQRIAIARALIRQP 1125
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY----------------------PW---------------DDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1126 RVLLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHRLSTIQNADLIVVIDN 1179
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
341-553 |
7.16e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.82 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVL-FSTTIAEN 419
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 420 IRYGRG------NVTMDEIKKAVKEANAYDFIMKLP-QKFDTlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSA 492
Cdd:PRK10253 102 VARGRYphqplfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 493 LDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELIKKEGI 553
Cdd:PRK10253 174 LDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAELI 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
982-1194 |
7.91e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 7.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----MAGTVLLDGQEAKKLNVQWLRA----QLGIVSQEPI 1052
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1053 L-------FDCSIAENIA-YGDNSRVVSQDEIVRAAKEANIHpfietlpqKYETRVGDKGTQLSGGQKQRIAIARALIRQ 1124
Cdd:PRK15134 103 VslnplhtLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIR--------QAAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1125 PRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
324-519 |
8.24e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.53 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclRefiG 403
Cdd:PRK11248 2 LQISHLYADYGGK---PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--R---G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQ-EPVLFSTTIAENIRYGrgnVTMDEIKKAVKEANAYDFIMKlpqkfdtlVGDRGA------QLSGGQKQRIAIARA 476
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564345546 477 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 519
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
979-1194 |
8.44e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.32 E-value: 8.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 979 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNvqwlRAQLGIVSQEPILF-DCS 1057
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAY-----GdnsrvVSQDEIVRAAKEanihpFIETLpqKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDE 1132
Cdd:COG4152 88 VGEQLVYlarlkG-----LSKAEAKRRADE-----WLERL--GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1133 ATSALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:COG4152 156 PFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
336-548 |
1.08e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.10 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 336 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTIS-------IDGQDIRNFNVRCLREFIGVVSQE 408
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 409 PVLFS-TTIAENIRYGRGNVTMDEI--KKAV--------KEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARAL 477
Cdd:TIGR03269 374 YDLYPhRTVLDNLTEAIGLELPDELarMKAVitlkmvgfDEEKAEEILDKYPD-----------ELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 478 VRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELI 548
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
643-900 |
1.15e-19 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 90.96 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMIaifgpgdDTVKQQKCNMFSLVFL-GLGVLSFFTFFLQGFTFGKAGEILTTRLRS 721
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLI-------DALSAGGSSGGLLALLvALFLLQAVLSALSSYLLGRTGERVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 722 MAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQgatgtrlALIAQNTANLGTGII-------ISFIYGWQLTLLLLS 794
Cdd:cd18551 74 RLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELITSGLPQLVTGVLtvvgavvLMFLLDWVLTLVTLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 795 VVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFS 874
Cdd:cd18551 145 VVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGP 224
|
250 260
....*....|....*....|....*.
gi 564345546 875 ISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18551 225 LMGLAVQLALLVVLGVGGARVASGAL 250
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
983-1182 |
1.15e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 87.87 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNV-QWLRAQLGIVSQEP----ILFDCS 1057
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAygdnsrvvsqdeivraakeanihpfietLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1137
Cdd:cd03215 95 VAENIA----------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1138 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVIDNGKV 1182
Cdd:cd03215 136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
981-1194 |
1.24e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.82 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQ-WLRAQLGIVSQEPILF-DCSI 1058
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 AENIAYGD--NSR-VVSQDEIVRAAKEANIHPFIETLPQkyeTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:PRK11288 97 AENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1136 ALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIDNG-KVKEHG-----THQQLLAQ 1194
Cdd:PRK11288 170 SLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGrYVATFDdmaqvDRDQLVQA 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
966-1185 |
1.38e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLdGQeakklNVQwlraqLG 1045
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFDcsiaeniaygDNSRVVsqDEIVRAA---KEANIHPFIETL---PQKYETRVGDkgtqLSGGQKQRIAIAR 1119
Cdd:COG0488 382 YFDQHQEELD----------PDKTVL--DELRDGApggTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1120 ALIRQPRVLLLDEATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVIDNGKVKEH 1185
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
981-1181 |
1.48e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 93.74 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGTVLLDGQEAKKLNVQWL-RAQLGIVSQEPILF-DC 1056
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1057 SIAENIAYGD----NSRVVSQDEIVRAAKEANIHPFIETLPqkyETR-VGDKGtqlsGGQKQRIAIARALIRQPRVLLLD 1131
Cdd:TIGR02633 94 SVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1132 EATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGK 1181
Cdd:TIGR02633 167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
965-1195 |
1.54e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.22 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDG----QEAKKLNVQ 1038
Cdd:PRK13646 2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1039 WLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVRAAkeanihpFIETLPQKYETRVGDKGT-QLSGGQKQRI 1115
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-------HRLLMDLGFSRDVMSQSPfQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
...
gi 564345546 1193 AQK 1195
Cdd:PRK13646 235 KDK 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
981-1182 |
1.75e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.41 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL----RAQLGIVSQE-PILFD 1055
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENI----AYGDnsrvvsqdeIVRAAKEANIHPFIETLpqKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLD 1131
Cdd:PRK10535 101 LTAAQNVevpaVYAG---------LERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1132 EATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIDNGKV 1182
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
324-583 |
1.77e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.55 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRClrefIG 403
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR----IG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLF-STTIAENIRY-GR--GnVTMDEIKKAVKEanaydfimkLPQKFDtlVGDRGA----QLSGGQKQRIAIAR 475
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlARlkG-LSKAEAKRRADE---------WLERLG--LGDRANkkveELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 476 ALVRNPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSElIKKEG 552
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVN-VELlkDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDE-IRRQF 220
|
250 260 270
....*....|....*....|....*....|..
gi 564345546 553 IYFRL-VNMQTSGSQiLSEEFEVELSDEKAAG 583
Cdd:COG4152 221 GRNTLrLEADGDAGW-LRALPGVTVVEEDGDG 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
328-551 |
1.82e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.85 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 328 DVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL-REFIGVVS 406
Cdd:PRK10575 16 NVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 407 QEPVLFSTTIAENIRYGR-------GNVTMDEIKKaVKEANAYDFIMKLPQKfdtLVGdrgaQLSGGQKQRIAIARALVR 479
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRypwhgalGRFGAADREK-VEEAISLVGLKPLAHR---LVD----SLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 480 NPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELIKKE 551
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
962-1193 |
2.63e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 962 FEGSVTFNEVVFNYPTRAnvpvlqglslevkkgqTLALVGSSGCGKSTVVQLLERFYDPMAG-----TVLLDGQEA-KKL 1035
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1036 NVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFieTLPQKYETRVGDKGTQLSGGQKQRI 1115
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1193
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
339-538 |
2.66e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 88.26 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 339 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQD----------IRNFNVRclREFIGVVSQe 408
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqaspREILALR--RRTIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 409 pvlFSTTI----AENIrygrgnVTMDEIKKAVKEANAYDFIMKLPQKFDtlVGDRGAQL-----SGGQKQRIAIARALVR 479
Cdd:COG4778 101 ---FLRVIprvsALDV------VAEPLLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 480 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHrlstvrNADVIAGFEDGVI 538
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH------DEEVREAVADRVV 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
984-1191 |
3.89e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 87.43 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFDCSIA-ENI 1062
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1063 A-----YGDNSRVVSQ--DEIVRaakeanihpFIEtLPQKYETRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:cd03265 95 YiharlYGVPGAERREriDELLD---------FVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1136 ALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQL 1191
Cdd:cd03265 161 GLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
324-540 |
4.72e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREFI 402
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQE----PVLfstTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFD--TLVGDrgaqLSGGQKQRIAIARA 476
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 477 LVRNPKILLLDEATSALdTESEAEVQAALDKA--REGRTTIVIAHRLSTV-RNADVIAGFEDGVIVE 540
Cdd:PRK11288 155 LARNARVIAFDEPTSSL-SAREIEQLFRVIRElrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
982-1188 |
5.20e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV-LLDGQEAKKlnVQWLRAQLGIVSQepilFD----- 1055
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPAR--ARLARARIGVVPQ----FDnldle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAEN-IAYGDNSRVvSQDEIvraakEANIHPFIE--TLPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDE 1132
Cdd:PRK13536 129 FTVRENlLVFGRYFGM-STREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1133 ATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIDNG-KVKEHGTH 1188
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
324-542 |
5.58e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 86.57 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNvrclREFIG 403
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLF-STTIAENIRY-GR-GNVTMDEIKKAVKEanaydfimkLPQKFDtlVGD----RGAQLSGGQKQRIAIARA 476
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQlKGLKKEEARRRIDE---------WLERLE--LSEyankRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 477 LVRNPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 542
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVN-VELlkDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
981-1186 |
6.06e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 87.20 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQeakklnVQW-LRAQLGIVSQ----EPILFD 1055
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPEltgrENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIaeniaYGdnsrvVSQDEIvrAAKEANIHPFIEtLPQKYETRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:cd03220 109 GRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1136 ALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHG 1186
Cdd:cd03220 172 VGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
336-518 |
8.10e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 336 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGvvSQEPVLFSTT 415
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 416 IAENIR-----YGRGNVTMDEIKKAVKEANAYDfimkLPQKFdtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEAT 490
Cdd:PRK13539 90 VAENLEfwaafLGGEELDIAAALEAVGLAPLAH----LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 564345546 491 SALDTESEAEVqAALDKAREGRTTIVIA 518
Cdd:PRK13539 156 AALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
981-1184 |
8.46e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 91.39 E-value: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---MAGTVLLDGQEAKKLNvqwLRA--QLGIV--SQE--- 1050
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKD---IRDseALGIViiHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1051 -PILfdcSIAENIAYGdNSR----VVSQDEIVRAAKE------ANIHPfietlpqkyETRVGDKGTqlsgGQKQRIAIAR 1119
Cdd:NF040905 90 iPYL---SIAENIFLG-NERakrgVIDWNETNRRAREllakvgLDESP---------DTLVTDIGV----GKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1120 ALIRQPRVLLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKE 1184
Cdd:NF040905 153 ALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
339-494 |
9.18e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.76 E-value: 9.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 339 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR---CLR-EFIGVVSQEPVLFST 414
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 415 TIA-ENIRYG---RGnvtmDEIKKAVKEANAYDFIMKLPQKFDTLvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEAT 490
Cdd:PRK10584 103 LNAlENVELPallRG----ESSRQSRNGAKALLEQLGLGKRLDHL----PAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
....
gi 564345546 491 SALD 494
Cdd:PRK10584 175 GNLD 178
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
342-542 |
9.71e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 9.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-IGVVSQE-PVLFSTTIAEN 419
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 420 IRYGR------GNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 493
Cdd:PRK09700 101 LYIGRhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564345546 494 dTESEAE-VQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 542
Cdd:PRK09700 177 -TNKEVDyLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
984-1188 |
1.02e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.47 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEP-ILFDCSIA 1059
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1060 ENIAYGDNSRVVSQDEIVRAAKEAnihpfietlpqkyETRVG--DKG----TQLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAA-------------LDKVGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1134 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVIDNGKVkeHGTH 1188
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
319-578 |
1.06e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 319 SIKGNLEFSDVHFSYPSRA--NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEG-TISIDGQDIRNFN- 394
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 395 ---VRCLREFIGVVSQEP--VLFSTTIAENIRYGRGNVTMD--EIKKAVKEanaydfIMKLPQKFDTLVGDRGAQLSGGQ 467
Cdd:PRK13645 82 ikeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENkqEAYKKVPE------LLKLVQLPEDYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 468 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSH 544
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 545 SEL-----------IKKEGIYFRLVNMQTSGSQILS------EEFEVELSD 578
Cdd:PRK13645 236 FEIfsnqelltkieIDPPKLYQLMYKLKNKGIDLLNknirtiEEFAKELAK 286
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
968-1195 |
1.28e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 968 FNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQeakklnvqwlrAQLGIV 1047
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1048 SQEPILFD-CSIAENIAYGDNSRVVSQDEIVRA-AKEANIHPFIETLPQK-----------YETRVGD--KG-------- 1104
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRALEAELEELeAKLAEPDEDLERLAELqeefealggweAEARAEEilSGlgfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1105 ----TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH-R--LSTIqnADLIV 1175
Cdd:COG0488 147 drpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSHdRyfLDRV--ATRIL 220
|
250 260
....*....|....*....|.
gi 564345546 1176 VIDNGKVKEH-GTHQQLLAQK 1195
Cdd:COG0488 221 ELDRGKLTLYpGNYSAYLEQR 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-547 |
1.49e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.46 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 327 SDVHFSYPSRANIKILKGLNLKVKSGQT---------VALVGNSGCGKSTTVQLLQRLYDPTEG-----TISIDGQDIrn 392
Cdd:PRK14271 13 ADVDAAAPAMAAVNLTLGFAGKTVLDQVsmgfparavTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 393 FNVRCLREF---IGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQ 469
Cdd:PRK14271 91 FNYRDVLEFrrrVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 470 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
983-1184 |
1.87e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 85.60 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQW---LRAQ-LGIVSQEPILFDCSI 1058
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 A-ENIAY-----GDNSRvVSQDEIVRAAKEANIHPFIETLPqkyetrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDE 1132
Cdd:PRK10584 105 AlENVELpallrGESSR-QSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1133 ATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIDNGKVKE 1184
Cdd:PRK10584 173 PTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
352-542 |
1.92e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.68 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 352 GQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN---VRCLREFIGVVSQEPV-------LFSTTIAENIR 421
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasldprqTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 422 YgRGNVTMDEIKKAV---------KEANAYDFimklPQKFdtlvgdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSA 492
Cdd:PRK10261 430 V-HGLLPGKAAAARVawllervglLPEHAWRY----PHEF-----------SGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564345546 493 LDTESEAE-VQAALDKARE-GRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 542
Cdd:PRK10261 494 LDVSIRGQiINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
33-272 |
2.40e-18 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 87.08 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 33 LNPGRILEEEMTRYAYYYSGLGGGVLLAAYIQvSFWTLAAGRQI-RKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDI 111
Cdd:cd18541 29 LTAGTLTASQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 112 SKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKI-----------LSTFSDKelaaya 180
Cdd:cd18541 108 NAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKihkrfrkvqeaFSDLSDR------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 181 kagavAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTI 260
Cdd:cd18541 182 -----VQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITL 256
|
250
....*....|....
gi 564345546 261 GN--AMTVFFSILI 272
Cdd:cd18541 257 GDlvAFNSYLGMLI 270
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
986-1191 |
2.46e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.20 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 986 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLrAQLGIVS--QEPILF-DCSIAENI 1062
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1063 aygdnsrVVSQDEIV---------------RAAKEAnihpfIETLPQKYEtRVG-------DKGTqLSGGQKQRIAIARA 1120
Cdd:PRK11300 102 -------LVAQHQQLktglfsgllktpafrRAESEA-----LDRAATWLE-RVGllehanrQAGN-LAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1121 LIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1191
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
986-1191 |
2.52e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.84 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 986 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN-VQWL--RAQLGIVSQEPILF---DCSIA 1059
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLASlnpRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1060 ENIA------YGDNSRVVSQDEIVRAAKEANIHP-FIETLPQKYetrvgdkgtqlSGGQKQRIAIARALIRQPRVLLLDE 1132
Cdd:PRK15079 119 EIIAeplrtyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1133 ATSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1191
Cdd:PRK15079 188 PVSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
983-1186 |
2.86e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 84.50 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILFDcsi 1058
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 aeniayGdnsrvVSQDEIVRAAKEAnihpfietlpqkyetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1138
Cdd:cd03217 91 ------G-----VKNADFLRYVNEG-----------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1139 TESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIDNGKVKEHG 1186
Cdd:cd03217 137 IDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
984-1191 |
4.11e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.83 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLL----------ERFYDPMAGTVLLDGQEAKklNVQWLRAQLGIVSQEPIL 1053
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLAR--DIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 FD-CSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFIETLpqkyeTRVG------DKGTQLSGGQKQRIAIARALIRQPR 1126
Cdd:PRK09984 98 VNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1127 VLLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQL 1191
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
324-553 |
5.52e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF-NVRCLREFI 402
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEPVLFS-TTIAENIRYGRGNVTMDEIKKAVKEAnaYDFIMKLPQKfdtlVGDRGAQLSGGQKQRIAIARALVRNP 481
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 482 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS--TVRNADVIAGFEDGVIVEQGSHSELIKKEGI 553
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
330-542 |
6.44e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 84.12 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 330 HFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnVRCLREF-IGVvsqE 408
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSLLGLgGGF---N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 409 PVLfstTIAENIRYgRG---NVTMDEIKKavKEANAYDFiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILL 485
Cdd:cd03220 97 PEL---TGRENIYL-NGrllGLSRKEIDE--KIDEIIEF-SELGDFIDLPVK----TYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 486 LDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRN-ADVIAGFEDGVIVEQG 542
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
340-542 |
6.89e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.56 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR--NFNVRCLREfIGVVSQEPVLFST-TI 416
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRG-IGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 417 AENIrygrgnVTMDEIKKAVKEANAYDFIMKLPQKFDT--LVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 494
Cdd:PRK10895 96 YDNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564345546 495 TESEAEVQAALDKAREGRTTIVIAHRlsTVRnaDVIAGFEDGVIVEQG 542
Cdd:PRK10895 170 PISVIDIKRIIEHLRDSGLGVLITDH--NVR--ETLAVCERAYIVSQG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
316-539 |
6.95e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 84.31 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 316 KPDSIKGNLEfsdvHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV 395
Cdd:cd03267 15 KEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 396 RCLREfIGVV--SQEPVLFSTTIAENIRYGRG--NVTMDEIKKAVKEANAydfIMKLPQKFDTLVgdrgAQLSGGQKQRI 471
Cdd:cd03267 91 KFLRR-IGVVfgQKTQLWWDLPVIDSFYLLAAiyDLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQRMRA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 472 AIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIahrlsTVRNADVIAGFEDGVIV 539
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLL-----TSHYMKDIEALARRVLV 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
345-566 |
1.02e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 89.69 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 345 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIGVVSQEPVLFS-TTIAENIRYg 423
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILF- 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 424 rgnvtMDEIK-KAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQ 502
Cdd:TIGR01257 1027 -----YAQLKgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 503 AALDKAREGRTTIVIAHRLStvrNADVIAgfEDGVIVEQG----SHSELIKKE----GIYFRLV-NMQTSGSQ 566
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQGrlycSGTPLFLKNcfgtGFYLTLVrKMKNIQSQ 1169
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
962-1194 |
1.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.06 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 962 FEGSVTFNEVVFNYPTRA--NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLdGQEA-----KK 1034
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAipanlKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1035 LN-VQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVRAAKEAnihPFIETLPQKYETRvgdKGTQLSGGQ 1111
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPEL---LKLVQLPEDYVKR---SPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1112 KQRIAIARALIRQPRVLLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHG- 1186
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGs 234
|
250
....*....|...
gi 564345546 1187 -----THQQLLAQ 1194
Cdd:PRK13645 235 pfeifSNQELLTK 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
341-522 |
1.26e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.33 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF----IGVVSQ-EPVLFSTT 415
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 416 IAENirygrgnVTMDEI--KKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 493
Cdd:PRK11629 104 ALEN-------VAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 564345546 494 DTESEAEVQAALDK--AREGRTTIVIAHRLS 522
Cdd:PRK11629 177 DARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
982-1132 |
1.56e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.15 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPMAGTVLLDGQEAKKLNVqWLRAQLGI--VSQEPIL 1053
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 F-DCSIAENI-AygdnsrVVSQDEIVRAAKEANIHPFIEtlpqkyE---TRVGD-KGTQLSGGQKQRIAIARALIRQPRV 1127
Cdd:COG1137 90 FrKLTVEDNIlA------VLELRKLSKKEREERLEELLE------EfgiTHLRKsKAYSLSGGERRRVEIARALATNPKF 157
|
....*
gi 564345546 1128 LLLDE 1132
Cdd:COG1137 158 ILLDE 162
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
341-547 |
1.96e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLLQRLYDP----TEGTISIDGQDIRNFNVRCLREF----IGVVSQEPVL 411
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 412 -------FSTTIAENIRYGRGnvtMDeikkavKEANAYDFIMKLPQkfdtlVGDRGA---------QLSGGQKQRIAIAR 475
Cdd:PRK15134 104 slnplhtLEKQLYEVLSLHRG---MR------REAARGEILNCLDR-----VGIRQAakrltdyphQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
977-1162 |
2.19e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.84 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQ-EPILfd 1055
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 cSIAENIAYGDNSRVVSQDEIVRAAKEANIHPfIETLPQKYetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:PRK13539 89 -TVAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|....*..
gi 564345546 1136 ALDTESEKVVQEALdKAREGRTCIVIA 1162
Cdd:PRK13539 157 ALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
966-1197 |
2.54e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerFYDPMA--GTVLLDGQEAkklnVQW---- 1039
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDI----TDWqtak 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1040 -LRAQLGIVSQEPILFD-CSIAENIAYGD--NSRVVSQDEIVRAakeanihpfIETLPQKYETRVGDKGTqLSGGQKQRI 1115
Cdd:PRK11614 77 iMREAVAIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1116 AIARALIRQPRVLLLDEATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQ 1190
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDA 223
|
....*..
gi 564345546 1191 LLAQKGI 1197
Cdd:PRK11614 224 LLANEAV 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
324-536 |
2.72e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.80 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIdGQDIRnfnvrclrefIG 403
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVsqepvlfsttiaenirygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgAQLSGGQKQRIAIARALVRNPKI 483
Cdd:cd03221 67 YF-------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 484 LLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH-R--LSTVrnADVIAGFEDG 536
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
981-1187 |
2.83e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.82 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklNVQWLraqLGI-VSQEPILfdcSIA 1059
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSAL---LELgAGFHPEL---TGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1060 ENI-----AYGdnsrvVSQDEIVRAAKE----ANIHPFIETlPQKYetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLL 1130
Cdd:COG1134 107 ENIylngrLLG-----LSRKEIDEKFDEivefAELGDFIDQ-PVKT----------YSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1131 DEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1187
Cdd:COG1134 171 DEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
982-1206 |
3.10e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 88.15 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD-CSIAE 1060
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1061 NIAYGDNSRVVSQDEivraaKEANIHPFIETLPQKYETrvGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1140
Cdd:TIGR01257 1023 HILFYAQLKGRSWEE-----AQLEMEAMLEDTGLHHKR--NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 1141 SEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVIDNGKVKEHGTHQQL--LAQKGIYFSMV----NIQA 1206
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGTPLFLknCFGTGFYLTLVrkmkNIQS 1168
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
983-1178 |
3.79e-17 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.39 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENI 1062
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1063 AY--GDNSRvvsqDEIVRAAKEANIHPFiETLPqkyetrvgdkGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1140
Cdd:cd03231 95 RFwhADHSD----EQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 564345546 1141 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVID 1178
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELD 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
982-1182 |
5.88e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 5.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerF--YDPMAGTVLLDGQEAKKLNV-QWLRAQLGIVS----QEPILF 1054
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 DCSIAENI---AYGDNSR--VVSQDEIVRAAKEanihpFIETL---PQKYETRVGdkgtQLSGGQKQRIAIARALIRQPR 1126
Cdd:COG1129 344 DLSIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1127 VLLLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVIDNGKV 1182
Cdd:COG1129 415 VLILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
977-1191 |
7.79e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.12 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL---RAQLGIVSQEPIL 1053
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 F-DCSIAENIAYGDNSRVVSQDEIVRAakeanihpfieTLPQKYETrVGDKG------TQLSGGQKQRIAIARALIRQPR 1126
Cdd:PRK11831 96 FtDMNVFDNVAYPLREHTQLPAPLLHS-----------TVMMKLEA-VGLRGaaklmpSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1127 VLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1191
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-536 |
9.90e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 79.40 E-value: 9.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREFIGVVSQEP----VLFSTTI 416
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdAIRAGIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 417 AENIrygrgnvtmdeikkavkeanaydfimklpqkfdTLvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 496
Cdd:cd03215 96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564345546 497 SEAEVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFEDG 536
Cdd:cd03215 139 AKAEIYRLIRElADAGKAVLLISSELDELlGLCDRILVMYEG 180
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
309-550 |
1.09e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.90 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 309 SFSERGHKPDSIKGNLefsdVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGq 388
Cdd:COG1134 13 SYRLYHEPSRSLKELL----LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 389 dirnfNVRCLREFIGVVSQEpvlfsTTIAENIR-----YGrgnVTMDEIKKAVKEANAY----DFImklpqkfDTLVGdr 459
Cdd:COG1134 88 -----RVSALLELGAGFHPE-----LTGRENIYlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQPVK-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 460 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE----SEAEVQaalDKAREGRTTIVIAHRLSTVRN-ADVIAGFE 534
Cdd:COG1134 146 --TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAIWLE 220
|
250
....*....|....*.
gi 564345546 535 DGVIVEQGSHSELIKK 550
Cdd:COG1134 221 KGRLVMDGDPEEVIAA 236
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
675-900 |
1.12e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 81.97 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 675 DDTVKQQKCNMFSLVFLGLGVLSFFTFFLQG-----FTFGKAGeiLTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRL 749
Cdd:cd18784 24 DGIVIEKSQDKFSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 750 ATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIAT 829
Cdd:cd18784 100 TSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 830 EAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18784 180 ETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
973-1193 |
1.14e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.37 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 973 FNYPT----RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVS 1048
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1049 QEPilfdcsiaeniAYGDNSRV-VSQ---------DEIVRAAKEANIhpfIETLPQkyetrVG---DKGT----QLSGGQ 1111
Cdd:PRK15112 94 QDP-----------STSLNPRQrISQildfplrlnTDLEPEQREKQI---IETLRQ-----VGllpDHASyyphMLAPGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1112 KQRIAIARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTH 1188
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGST 234
|
....*
gi 564345546 1189 QQLLA 1193
Cdd:PRK15112 235 ADVLA 239
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
341-549 |
1.15e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL--YDPT----EGTISIDGQDIrnfNVRCLREFIGVVSQEPVLFST 414
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTT---LMNALafRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 415 -TIAENI------RYGRgNVTMDEIKKAVKEanaydFI--MKLPQKFDTLVGDRGAQ--LSGGQKQRIAIARALVRNPKI 483
Cdd:TIGR00955 114 lTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 484 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLST--VRNADVIAGFEDGVIVEQGSHSELIK 549
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
59-276 |
1.19e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 82.17 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 59 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 138
Cdd:cd18564 69 LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 139 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 218
Cdd:cd18564 149 MFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLR 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 219 IGIK-KAISANISMGIAfLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGAFS 276
Cdd:cd18564 229 AGLRaARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPG-DLLVFLAYLKNLYK 285
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
339-540 |
1.45e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 339 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPT---EGTISIDGQdIRNFnvRCLR--EFIGVV--SQE--- 408
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGE-VCRF--KDIRdsEALGIViiHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 409 -PVLfstTIAENIRYG-----RGNVTMDEIKKAVKEanaydfIMK---LPQKFDTLVGDRGAqlsgGQKQRIAIARALVR 479
Cdd:NF040905 90 iPYL---SIAENIFLGnerakRGVIDWNETNRRARE------LLAkvgLDESPDTLVTDIGV----GKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 480 NPKILLLDEATSAL-DTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVE 540
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
981-1182 |
1.59e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILF-DCS 1057
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYEtrVGDkgtqlsggqKQRIAIARALIRQPRVLLLDEATSAL 1137
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLE--VAD---------RQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564345546 1138 D-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVIDNGKV 1182
Cdd:PRK15439 172 TpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
983-1193 |
1.81e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.08 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGTVL----------------LDGQEAKKLNVQwlraql 1044
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVCGGT------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 gIVSQEPILFDCS------IAENIA---------YGDNSRVV----SQDEIVRAAKEAnIHPFIETLPQ-KYETRVGDKG 1104
Cdd:TIGR03269 89 -LEPEEVDFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEA-VGRAVDLIEMvQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1105 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVIDNGK 1181
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|..
gi 564345546 1182 VKEHGTHQQLLA 1193
Cdd:TIGR03269 247 IKEEGTPDEVVA 258
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
339-536 |
1.83e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.11 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 339 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPTEGTISIDGQDIRNFNVR-CLREFIGVVSQEPVLF-ST 414
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 415 TIAENIRYG-----RGNVTMDEikKAVKEANAYDFIMKLPQKFDTL-VGDRGaqlsGGQKQRIAIARALVRNPKILLLDE 488
Cdd:TIGR02633 94 SVAENIFLGneitlPGGRMAYN--AMYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 489 ATSALdTESEAEVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 536
Cdd:TIGR02633 168 PSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
978-1194 |
2.19e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 83.70 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 978 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV-------LLDGQEAKKLNVQWLRAQLGIVSQE 1050
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1051 PILF-DCSIAENIAygDNSRVVSQDEIvrAAKEANIHPFIETLPQKYETRVGDKGT-QLSGGQKQRIAIARALIRQPRVL 1128
Cdd:TIGR03269 374 YDLYpHRTVLDNLT--EAIGLELPDEL--ARMKAVITLKMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1129 LLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
324-539 |
2.58e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVhfSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-I 402
Cdd:COG3845 258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEP-----VLfSTTIAENI--------RYGRGNVtmdeIKKAVKEANAYDFImklpQKFDTLVGDRGA---QLSGG 466
Cdd:COG3845 336 AYIPEDRlgrglVP-DMSVAENLilgryrrpPFSRGGF----LDRKAIRAFAEELI----EEFDVRTPGPDTparSLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 467 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIV 539
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
345-543 |
3.37e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.46 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 345 LNLKVK-----SGQTvALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ---DIRN-FNVRCLREFIGVVSQEPVLFS-T 414
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgICLPPEKRRIGYVFQDARLFPhY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 415 TIAENIRYGrgnvtMDEikkavkeanaydfimKLPQKFDTLVG--------DR-GAQLSGGQKQRIAIARALVRNPKILL 485
Cdd:PRK11144 92 KVRGNLRYG-----MAK---------------SMVAQFDKIVAllgiepllDRyPGSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 486 LDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGS 543
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
336-543 |
3.52e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 336 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI--RNFNVRCLREF------------ 401
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGVVSQEPV-----LFST--TIAENIRYGRGnVTMDEikkAVKEANAYDFIMKLPQKfDTLVGDRGAQLSGGQKQRIAIA 474
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG-ASREE---AMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 475 RALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRT--TIVIAHRLSTVRN-ADVIAGFEDGVIVEQGS 543
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
329-524 |
3.60e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.76 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 329 VHFSYPSRANI---KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI---RNFNVRCLREFI 402
Cdd:PRK10908 2 IRFEHVSKAYLggrQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 403 GVVSQEP-VLFSTTIAENIRYGR--GNVTMDEIKKAVKEANAYDFIMKLPQKFDTlvgdrgaQLSGGQKQRIAIARALVR 479
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564345546 480 NPKILLLDEATSALDTE-SEAEVQAALDKAREGRTTIVIAHRLSTV 524
Cdd:PRK10908 155 KPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
978-1162 |
4.05e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.17 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 978 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCS 1057
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAY-----GDNSRVVSQdeivrAAKEANIHPFiETLPqkyetrvgdkGTQLSGGQKQRIAIARALIRQPRVLLLDE 1132
Cdd:TIGR01189 90 ALENLHFwaaihGGAQRTIED-----ALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|
gi 564345546 1133 ATSALDTESEKVVQEALDkAREGRTCIVIA 1162
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
983-1192 |
6.28e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.26 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDCSIAEN 1061
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1062 IAYG--------DNSRVVSQDEIVRAAKEANIhpfIETLPQKYETrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:PRK10253 102 VARGryphqplfTRWRKEDEEAVTKAMQATGI---THLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1134 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:PRK10253 171 TTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
643-900 |
8.57e-16 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 79.38 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKQQKcnMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 722
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLL--RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 723 AFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 802
Cdd:cd18541 79 LFAHLLTLSPSFY--QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 803 GIVEMKMLagnAKRDKKEMEAAGKIATEAIEN---IRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAF 879
Cdd:cd18541 157 VYRLGKKI---HKRFRKVQEAFSDLSDRVQESfsgIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLL 233
|
250 260
....*....|....*....|.
gi 564345546 880 MYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18541 234 IGLSFLIVLWYGGRLVIRGTI 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
981-1180 |
1.05e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.75 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLG--IVSQEPILFD-CS 1057
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAYGDN-SRVVSQDEIVRAAK---EANIHPFIETLPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:PRK09700 97 VLENLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564345546 1134 TSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNG 1180
Cdd:PRK09700 173 TSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
685-918 |
1.63e-15 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 78.29 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 685 MFSLVFLGLGVLSFFTFFLqgftFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 764
Cdd:cd18575 41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 765 ALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE 844
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTRE 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 845 RKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAVA 918
Cdd:cd18575 195 DAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSqfVFYAVLAAGSVG 270
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
336-548 |
1.64e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 336 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------RNFNVRCL---------- 398
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyRSQRIRMIfqdpstslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 399 REFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFImklpqkfdtlvgdrgaqLSGGQKQRIAIARALV 478
Cdd:PRK15112 103 RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM-----------------LAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 479 RNPKILLLDEATSALDTESEAE-VQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELI 548
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQlINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
978-1191 |
1.68e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 978 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLR--------------AQ 1043
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1044 LGIVSQEPI-----LFDC--SIAENIAYGDNsrvVSQDEIVRAAK----EANIhPFIETLPQKYETrvgdkgtQLSGGQK 1112
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAKrmldQVRI-PEAQTILSRYPH-------QLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1113 QRIAIARALIRQPRVLLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVIDNGKVKE 1184
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
....*..
gi 564345546 1185 HGTHQQL 1191
Cdd:PRK10261 250 TGSVEQI 256
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
976-1182 |
1.71e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 77.37 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 976 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklNVQW-----LRAQLGIV--S 1048
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1049 QEPILFDCSIAENIAYgdNSRVVSQDEivrAAKEANIHPFIETLPQkyeTRVGDKGT-QLSGGQKQRIAIARALIRQPRV 1127
Cdd:cd03267 103 KTQLWWDLPVIDSFYL--LAAIYDLPP---ARFKKRLDELSELLDL---EELLDTPVrQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1128 LLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
324-524 |
1.86e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 76.13 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLYDPT-EGTISIDGQDIRnfnvRCLRE 400
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFST-TIAENIRygrgnvtmdeikkavkeanaydFIMKLpqkfdtlvgdRGaqLSGGQKQRIAIARALVR 479
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564345546 480 NPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTV 524
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSAS 171
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
328-539 |
1.92e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.00 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 328 DVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGTISIDGQDIRNFNVRCLR----E 400
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNklraE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEP----------------VLF-------STTIAENIRygrgnvTMDEIK--KAVKEANAYdfimklPQKFdtl 455
Cdd:PRK09473 98 QISMIFQDPmtslnpymrvgeqlmeVLMlhkgmskAEAFEESVR------MLDAVKmpEARKRMKMY------PHEF--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 456 vgdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStvrnadVIAGF 533
Cdd:PRK09473 163 --------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLG------VVAGI 228
|
....*.
gi 564345546 534 EDGVIV 539
Cdd:PRK09473 229 CDKVLV 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
972-1186 |
2.15e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 972 VFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRAQLGIVS 1048
Cdd:PRK10261 329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1049 QEPIlfdCSIAENIAYGDnsrvvSQDEIVRA-------AKEANIHPFIEtlpqkyetRVGDKGT-------QLSGGQKQR 1114
Cdd:PRK10261 408 QDPY---ASLDPRQTVGD-----SIMEPLRVhgllpgkAAAARVAWLLE--------RVGLLPEhawryphEFSGGQRQR 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1115 IAIARALIRQPRVLLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1186
Cdd:PRK10261 472 ICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
966-1181 |
2.44e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.02 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklnvqwlraqlg 1045
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 ivsqepilfdcsiAENIAYgdnsrvvsqdeivraakeanihpfietlpqkYEtrvgdkgtQLSGGQKQRIAIARALIRQP 1125
Cdd:cd03221 62 -------------TVKIGY-------------------------------FE--------QLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1126 RVLLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIDNGK 1181
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
974-1182 |
2.77e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 974 NYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPMAGTVLLDGQEAKKLNV-QWLRAQLGIVSQE 1050
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1051 P-----ILfDCSIAENIAYGDNSR-------VVSQDEIVRAAKEAnihpfIEtlpqKYETRVGDKGT---QLSGGQKQRI 1115
Cdd:COG3845 342 RlgrglVP-DMSVAENLILGRYRRppfsrggFLDRKAIRAFAEEL-----IE----EFDVRTPGPDTparSLSGGNQQKV 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
628-1184 |
3.95e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 79.84 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 628 SFLKVLRlnKTEWPYFVVGTLCAIANGALqpafSIILSEMI--AIFGPGDDTVkqqkcnMFSLVFLGLGVLSFFTFFLQG 705
Cdd:COG4615 2 NLLRLLL--RESRWLLLLALLLGLLSGLA----NAGLIALInqALNATGAALA------RLLLLFAGLLVLLLLSRLASQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 706 FTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGtRLALIAQNTANlgtgIIISFIY- 784
Cdd:COG4615 70 LLLTRLGQHAVARLRLRLSRRILAAPLERLERI--GAARLLAALTEDVRTISQAFV-RLPELLQSVAL----VLGCLAYl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 785 GWQLTLLLLSVVPFIAVAGIVEMKMLagnaKRDKKEMEAAGKIATEAIENIRTVVS------LTQERKfESMYVEKLHGP 858
Cdd:COG4615 143 AWLSPPLFLLTLVLLGLGVAGYRLLV----RRARRHLRRAREAEDRLFKHFRALLEgfkelkLNRRRR-RAFFDEDLQPT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 859 ---YRNSVRKAH-IYGITFSISQAFMYFsyagcfrfgsyLIVnghmrfkdvILVFSAIVLGAVALGHASSFA-------- 926
Cdd:COG4615 218 aerYRDLRIRADtIFALANNWGNLLFFA-----------LIG---------LILFLLPALGWADPAVLSGFVlvllflrg 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 927 ---------PDYAKAKLSAAYLFSL---FERQPLIDSYSREGMWPDKFEgSVTFNEVVFNYPTRANVP--VLQGLSLEVK 992
Cdd:COG4615 278 plsqlvgalPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGDEgfTLGPIDLTIR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 993 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDcsiaeniaygdnsRVVS 1072
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-------------RLLG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1073 QDEIVRAAKeanIHPFIETLPQKYETRVGDKG---TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL 1149
Cdd:COG4615 424 LDGEADPAR---ARELLERLELDHKVSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTEL 500
|
570 580 590
....*....|....*....|....*....|....*..
gi 564345546 1150 --DKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKE 1184
Cdd:COG4615 501 lpELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
342-547 |
4.39e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREFIGVVS----QEPVLFSTTI 416
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 417 AENI------RYGRGNVtMDEiKKAVKEANAYdfIMKL---PQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLD 487
Cdd:COG1129 348 RENItlasldRLSRGGL-LDR-RRERALAEEY--IKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 488 EATSALDTESEAEVQAALDK-AREGRTTIVIahrlST-----VRNADVIAGFEDGVIVEQGSHSEL 547
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
981-1181 |
4.64e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.66 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAK----KLNVQwlrAQLGIVSQE-PILFD 1055
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQE---AGIGIIHQElNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENIAYGdnsrvvsqDEIVRA---------AKEANihPFIETLPQKY--ETRVGDkgtqLSGGQKQRIAIARALIRQ 1124
Cdd:PRK10762 94 LTIAENIFLG--------REFVNRfgridwkkmYAEAD--KLLARLNLRFssDKLVGE----LSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1125 PRVLLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIDNGK 1181
Cdd:PRK10762 160 SKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
643-898 |
7.08e-15 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 76.66 E-value: 7.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMIaifgpgDDTVKQQKCNM-----FSLVFLGLGVLSFFTFFLQGFTFGKAGEILTT 717
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAI------DDYIVPGQGDLqglllLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 718 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 797
Cdd:cd18544 75 DLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 798 FIAVAgIVEMKMLAGNAKRDKKEMEAA--GKIAtEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKA-HIYGITFS 874
Cdd:cd18544 153 LLLLA-TYLFRKKSRKAYREVREKLSRlnAFLQ-ESISGMSVIQLFNREKREFEEF-DEINQEYRKANLKSiKLFALFRP 229
|
250 260
....*....|....*....|....
gi 564345546 875 ISQAFMYFSYAGCFRFGSYLIVNG 898
Cdd:cd18544 230 LVELLSSLALALVLWYGGGQVLSG 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
340-579 |
8.00e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.69 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRL--YDPTEGTIsidgqdIRNFNV--RCLR----EFIG-------- 403
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRI------IYHVALceKCGYverpSKVGepcpvcgg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLF---STTIAENIR-------------YGRGNV------TMDEIKKAVKEA--NAYDFI--MKLPQKFDTLVG 457
Cdd:TIGR03269 88 TLEPEEVDFwnlSDKLRRRIRkriaimlqrtfalYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSHRITHIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 458 DrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA--REGRTTIVIAHRLSTVRN-ADVIAGFE 534
Cdd:TIGR03269 168 D----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 564345546 535 DGVIVEQGSHSELIKKegiYFRLVNMqtsgsqiLSEEFEVELSDE 579
Cdd:TIGR03269 244 NGEIKEEGTPDEVVAV---FMEGVSE-------VEKECEVEVGEP 278
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
968-1194 |
9.18e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.86 E-value: 9.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 968 FNEVVFNYPTR--ANVPVlqglSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1045
Cdd:PRK10522 325 LRNVTFAYQDNgfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFDcsiaeniaygdnsRVVSQDEivRAAKEANIHPFIETLPQKYETRVGD---KGTQLSGGQKQRIAIARALI 1122
Cdd:PRK10522 401 AVFTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1123 RQPRVLLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVIDNGKVKE-HGTHQQLLAQ 1194
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
984-1192 |
1.20e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL---------RAQLGIVSQEP--- 1051
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1052 ILFDCSIAENIA----------YGdNSRVVSQDEIVRAAKEANihpfietlpqkyetRVGDKGTQLSGGQKQRIAIARAL 1121
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYG-DIRATAGDWLERVEIDAA--------------RIDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1122 IRQPRVLLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
49-262 |
1.55e-14 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 75.45 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 49 YYSG-----LGGGVLLAAYIQVSFW--------TLAAG-----------RQIRKIRQKFFHAILRQEMGWFDIKGTTELN 104
Cdd:cd18590 17 YYTGrvidiLGGEYQHNAFTSAIGLmclfslgsSLSAGlrgglfmctlsRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 105 TRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGA 184
Cdd:cd18590 97 SRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 185 VAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 262
Cdd:cd18590 177 LAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGS 254
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
335-505 |
1.66e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 73.68 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 335 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFST 414
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 415 TIAENIRYGRGNVTMDEIKKAVKEANAydfimklpqkfdTLVGDRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSAL 493
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGL------------NGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170
....*....|..
gi 564345546 494 DTESEAEVQAAL 505
Cdd:cd03231 157 DKAGVARFAEAM 168
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
980-1187 |
1.67e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.73 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEP-ILFDCSI 1058
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENhINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 AENIAYG----DNSRVVSQD-EIVRAAkeanIHPF-IETLPQKYETrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDE 1132
Cdd:COG4604 93 RELVAFGrfpySKGRLTAEDrEIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1133 ATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVIDNGKVKEHGT 1187
Cdd:COG4604 162 PLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
33-261 |
1.74e-14 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 75.50 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 33 LNPGRILEEEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDIS 112
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 113 KISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGA 192
Cdd:cd18544 110 ALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 193 IRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 261
Cdd:cd18544 190 MSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG 258
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
963-1192 |
1.89e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 963 EGSVTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN------ 1036
Cdd:PRK10575 9 DTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSskafar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1037 -VQWLRAQL----GIVSQEPIlfdcSIAENIAYGDNSRVVSQD--EIVRAAKEANIHPFIEtlpqkyetRVGDkgtQLSG 1109
Cdd:PRK10575 86 kVAYLPQQLpaaeGMTVRELV----AIGRYPWHGALGRFGAADreKVEEAISLVGLKPLAH--------RLVD---SLSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1110 GQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVIDNGKVKEH 1185
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQ 229
|
....*..
gi 564345546 1186 GTHQQLL 1192
Cdd:PRK10575 230 GTPAELM 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
984-1192 |
2.15e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.78 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----MAGTVLLDGqeaKKLNVQWLRAQLGIVSQEPILFDCSIA 1059
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1060 -ENIAYgdNSRVVSQDEIVRAAKEANIHPFIETLPQK--YETRVGDKGTQ--LSGGQKQRIAIARALIRQPRVLLLDEAT 1134
Cdd:TIGR00955 117 rEHLMF--QAHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1135 SALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:TIGR00955 195 SGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
52-275 |
2.45e-14 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 75.13 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 52 GLGGGVL---LAAYIQVSFwtlaagrqIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQA 128
Cdd:cd18548 52 GLIAGILagyFAAKASQGF--------GRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 129 IATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELER 208
Cdd:cd18548 124 PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEER 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 209 YQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-------AMTVFFSILIGAF 275
Cdd:cd18548 204 FDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDlvafinyLMQILMSLMMLSM 277
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
344-542 |
2.47e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.26 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 344 GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI--------------RNF-NVRCLREFigvvsqe 408
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREM------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 409 pvlfstTIAENI-----RYGRGNVTMDEIKKAV---KEANAYDFIMKLPQKFDTL-VGDRGA-QLSGGQKQRIAIARALV 478
Cdd:PRK11300 96 ------TVIENLlvaqhQQLKTGLFSGLLKTPAfrrAESEALDRAATWLERVGLLeHANRQAgNLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 479 RNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIagfedgVIVEQG 542
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRI------YVVNQG 230
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
41-488 |
2.69e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 77.15 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 41 EEMTRYAYYYSGLGGGVLLAAYI-QVSFWTLAAgRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEgig 119
Cdd:COG4615 45 AALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQ-HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQ--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 120 dkvgmFFQAIATFFAGFIVGFirgwkLTLVIMA-ISPILGLSTAVWAKILSTF---SDKELAAYAKAGAVAEEAL-GAIR 194
Cdd:COG4615 121 -----AFVRLPELLQSVALVL-----GCLAYLAwLSPPLFLLTLVLLGLGVAGyrlLVRRARRHLRRAREAEDRLfKHFR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 195 TVIafGGqNKEL------------ERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLV-ISKEYTIG 261
Cdd:COG4615 191 ALL--EG-FKELklnrrrrraffdEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGwADPAVLSG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 262 NAMTVFFsiLIGAfsVGQAAPCIDAFANARGAAyvifdiidnnPKIDSFSERGHKPDSIKGN------------LEFSDV 329
Cdd:COG4615 268 FVLVLLF--LRGP--LSQLVGALPTLSRANVAL----------RKIEELELALAAAEPAAADaaappapadfqtLELRGV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 330 HFSYPSRANIK--ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQ 407
Cdd:COG4615 334 TYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 408 EPVLFSTTiaenirYGRGNVTMDEikkavkEANAYDFIMKLPQK-------FDTLvgdrgaQLSGGQKQRIAIARALVRN 480
Cdd:COG4615 414 DFHLFDRL------LGLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALLVALLED 475
|
....*...
gi 564345546 481 PKILLLDE 488
Cdd:COG4615 476 RPILVFDE 483
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
698-900 |
3.14e-14 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 74.89 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 698 FFTFFLQG-FTF------GKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDaaqVQGATGTRLALIAQN 770
Cdd:cd18574 49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFDTHR--TGELVNRLTAD---VQEFKSSFKQCVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 771 TANLG--TGIIISFIY-GWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF 847
Cdd:cd18574 124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 848 ESMYVEKLhgpyrNSVRKAHIY-GITFSISQAFMYFSYAG----CFRFGSYLIVNGHM 900
Cdd:cd18574 204 LELYEEEV-----EKAAKLNEKlGLGIGIFQGLSNLALNGivlgVLYYGGSLVSRGEL 256
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
340-524 |
3.32e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnvrcLRefIGVVSQEPVLFST---TI 416
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQKLYLDTTlplTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 417 AENIRYgRGNVTMDEIKKAVKEANAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 496
Cdd:PRK09544 87 NRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190
....*....|....*....|....*....|
gi 564345546 497 SEAEVQAALDKARE--GRTTIVIAHRLSTV 524
Cdd:PRK09544 155 GQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
341-547 |
3.34e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.97 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP----TEGTISIDGQDIRNFNVRCLRefIGVVSQ------EPV 410
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRK--IATIMQnprsafNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 411 LFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFdtlvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEAT 490
Cdd:PRK10418 96 HTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLY-------PFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 491 SALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK10418 169 TDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
56-265 |
3.64e-14 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 74.50 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 56 GVLLAAYIqvSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISK--------ISEGIgdkvgmffQ 127
Cdd:cd18574 56 SLLTFAYI--SLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------R 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 128 AIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 207
Cdd:cd18574 126 SVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 208 RYQKHLENAKK--------IGIKKAISaNISMGIAFLLIYasyalafWYGSTLVISKEYTIGNAMT 265
Cdd:cd18574 206 LYEEEVEKAAKlneklglgIGIFQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGDLMS 263
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
987-1186 |
4.16e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.30 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 987 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-DC 1056
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdAEKGICLPPEKRRIGYVFQDARLFpHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1057 SIAENIAYGDNSRVVSQ-DEIVRAAKeanihpfIETLPQKYETRvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:PRK11144 92 KVRGNLRYGMAKSMVAQfDKIVALLG-------IEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1136 ALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVIDNGKVKEHG 1186
Cdd:PRK11144 158 SLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
979-1186 |
7.90e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.81 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 979 ANVPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGTVLLDGQ--EAKKLN---------------- 1036
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvAPCALRgrkiatimqnprsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1037 -VQWLRA-------QLGIVSQEPILFDCsiAENIAYGDNSRVVSqdeivraakeanIHPFietlpqkyetrvgdkgtQLS 1108
Cdd:PRK10418 94 pLHTMHTharetclALGKPADDATLTAA--LEAVGLENAARVLK------------LYPF-----------------EMS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1109 GGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEH 1185
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
.
gi 564345546 1186 G 1186
Cdd:PRK10418 223 G 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
334-518 |
8.97e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 71.52 E-value: 8.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 334 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL------YDPTEGTISIDGQDIRNFNVRCLREFIgVVSQ 407
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYPGEII-YVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 408 EPVLFST-TIAEnirygrgnvTMDeikkAVKEANAYDFImklpqkfdtlvgdRGaqLSGGQKQRIAIARALVRNPKILLL 486
Cdd:cd03233 91 EDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190
....*....|....*....|....*....|...
gi 564345546 487 DEATSALDTESEAE-VQAALDKAREGRTTIVIA 518
Cdd:cd03233 143 DNSTRGLDSSTALEiLKCIRTMADVLKTTTFVS 175
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
330-553 |
9.93e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 330 HFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ-RLYDPTE-------GTISIDGQDIRNFNVR---CL 398
Cdd:PRK13547 6 HLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPrlaRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 399 REFIGVVSQEPVLFSttIAENIRYGR----------GNVTMDEIKKAVKEANAydfimklpqkfDTLVGDRGAQLSGGQK 468
Cdd:PRK13547 85 RAVLPQAAQPAFAFS--AREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 469 QRIAIARAL---------VRNPKILLLDEATSALDTESEAEVQAAL-DKARE---GRTTIVIAHRLSTvRNADVIAGFED 535
Cdd:PRK13547 152 ARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrRLARDwnlGVLAIVHDPNLAA-RHADRIAMLAD 230
|
250
....*....|....*...
gi 564345546 536 GVIVEQGSHSELIKKEGI 553
Cdd:PRK13547 231 GAIVAHGAPADVLTPAHI 248
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
330-520 |
1.13e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 330 HFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPTEGTISIDGQDIrnfnvrclrefigvvS 406
Cdd:COG2401 33 AFGVELRVVERyVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------G 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 407 QEpvlfsTTIAENIrYGRGNV-TMDEIKKAVKEANAYDFImklpQKFDtlvgdrgaQLSGGQKQRIAIARALVRNPKILL 485
Cdd:COG2401 98 RE-----ASLIDAI-GRKGDFkDAVELLNAVGLSDAVLWL----RRFK--------ELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 564345546 486 LDEATSALDTESEAEVQAALDK-AREGRTTIVIA-HR 520
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKlARRAGITLVVAtHH 196
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
323-549 |
1.21e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 73.62 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 323 NLEFSDVHF---SYPSRANIKIlkglNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-P---TEGTISIDGQDIRNFNV 395
Cdd:PRK11022 5 NVDKLSVHFgdeSAPFRAVDRI----SYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 396 RCLREFIG----VVSQEPVlfsTTIaeNIRYGRGNVTMDEIK------KAVKEANAYDFImklpqkfdTLVG--DRGA-- 461
Cdd:PRK11022 81 KERRNLVGaevaMIFQDPM---TSL--NPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLL--------NQVGipDPASrl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 462 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGF 533
Cdd:PRK11022 148 dvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLelQQKENMALVLITHDLALVaEAAHKIIVM 227
|
250
....*....|....*.
gi 564345546 534 EDGVIVEQGSHSELIK 549
Cdd:PRK11022 228 YAGQVVETGKAHDIFR 243
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
982-1184 |
1.25e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERfydpmagtVLLDGQEAKKLNVQWLraqlgivsqePILFDCSIAEN 1061
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------ALKGTPVAGCVDVPDN----------QFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1062 IA-YGDNSRVVsqdEIVRAAKEANihpfietlPQKYETRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1140
Cdd:COG2401 106 IGrKGDFKDAV---ELLNAVGLSD--------AVLWLRRF----KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564345546 1141 SEKVVQEALDKA--REGRTCIVIAHR---LSTIQnADLIVVIDNGKVKE 1184
Cdd:COG2401 171 TAKRVARNLQKLarRAGITLVVATHHydvIDDLQ-PDLLIFVGYGGVPE 218
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
688-902 |
1.66e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 72.98 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 688 LVFLGLGVLSFFTFfLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALI 767
Cdd:cd18565 59 LTVAAFLLESLFQY-LSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGANSI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 768 AQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVVSLTQE 844
Cdd:cd18565 136 IRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRI---EPRYRAVREAVGDLNArleNNLSGIAVIKAFTAE 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 845 RkFESMYVEKLHGPYRNSVRKAHIYGITFsisQAFMYF----SYAGCFRFGSYLIVNGHMRF 902
Cdd:cd18565 213 D-FERERVADASEEYRDANWRAIRLRAAF---FPVIRLvagaGFVATFVVGGYWVLDGPPLF 270
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
643-900 |
1.70e-13 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 72.44 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMI-AIFGPGDDTVKQQKCNMFSLVF--LGLGVLSFFTFFLQGFTFGKAGEILTTRL 719
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIdLIIEGLGGGGGVDFSGLLRILLllLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 720 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFI 799
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 800 AVAgiveMKMLAGNAKRD-KKEMEAAGKI---ATEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKAHIY-GITFS 874
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREEEAIEEF-DEINEELYKASFKAQFYsGLLMP 233
|
250 260
....*....|....*....|....*.
gi 564345546 875 ISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18547 234 IMNFINNLGYVLVAVVGGLLVINGAL 259
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
335-518 |
2.38e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 70.08 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 335 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE--FIGVVSQ-EPVL 411
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilYLGHLPGlKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 412 fstTIAENIRYGR--GNVTMDEIKKAVKEANAYDFImklpqkfDTLVgdrgAQLSGGQKQRIAIARALVRNPKILLLDEA 489
Cdd:TIGR01189 89 ---SALENLHFWAaiHGGAQRTIEDALAAVGLTGFE-------DLPA----AQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180
....*....|....*....|....*....
gi 564345546 490 TSALDTESEAEVQAALDkAREGRTTIVIA 518
Cdd:TIGR01189 155 TTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
352-542 |
2.40e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.50 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 352 GQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL----REFI-----GVVSQEPvlfsttiAENIRY 422
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHP-------RDGLRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 423 G---RGNVTmdEIKKAVKE-------ANAYDFIMKL---PQKFDtlvgDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 489
Cdd:PRK11701 105 QvsaGGNIG--ERLMAVGArhygdirATAGDWLERVeidAARID----DLPTTFSGGMQQRLQIARNLVTHPRLVFMDEP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 490 TSALDTeseaEVQAA-LDKARE-----GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 542
Cdd:PRK11701 179 TGGLDV----SVQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
351-539 |
3.01e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 68.55 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 351 SGQTVALVGNSGCGKSTTVQLLQRLYDPTEGT-ISIDGQDIRNFNVRCLREFIgvvsqepvlfsttiaenirygrgnvtm 429
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 430 deikkavkeanaydfimklpqkfdtlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--- 506
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 564345546 507 ---KAREGRTTIVIAHRLSTVRNADVIAGFEDGVIV 539
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
342-524 |
3.68e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRnfnvRCLRE-FIGVVSQEPVL---FSTTIA 417
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSEEVdwsFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 418 ENIRYGR-GNVTMDEIKKA-----VKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 491
Cdd:PRK15056 99 DVVMMGRyGHMGWLRRAKKrdrqiVTAALARVDMVEFRHR-------QIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|....
gi 564345546 492 ALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTV 524
Cdd:PRK15056 172 GVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
643-900 |
4.49e-13 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 71.36 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMI--AIFGPGDDTVKqqkcnMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLR 720
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdgPIAHGDRSALW-----PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 721 SMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGtRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIA 800
Cdd:cd18543 76 TDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 801 VAGIVEMKMLAGNAKRDKkemEAAGKIATEAIEN---IRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 877
Cdd:cd18543 153 LVARRFRRRYFPASRRAQ---DQAGDLATVVEESvtgIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLE 229
|
250 260
....*....|....*....|...
gi 564345546 878 AFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18543 230 ALPELGLAAVLALGGWLVANGSL 252
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
340-543 |
6.41e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 6.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPTEG--------TISIDGQDIRNfnVRCLREFIGVVSQEP 409
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiellgrTVQREGRLARD--IRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 410 VLFST-TIAENIRYGRGNVT------MDEIKKAVKEaNAYDFIMKLPQKFdtLVGDRGAQLSGGQKQRIAIARALVRNPK 482
Cdd:PRK09984 96 NLVNRlSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRVGMVH--FAHQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 483 ILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGS 543
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
324-550 |
6.94e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.82 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGTISIDGQDIRNFNVRCLR-E 400
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAgE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPV--------LFSTTIAENIRYGRGNVTMDEIKKAvkeanayDFI------MKLPQkfDTLVGDRGAQLSGG 466
Cdd:PRK09580 79 GIFMAFQYPVeipgvsnqFFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGFSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 467 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREG-RTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGS 543
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGD 229
|
....*..
gi 564345546 544 HSeLIKK 550
Cdd:PRK09580 230 FT-LVKQ 235
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
56-261 |
7.37e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 70.62 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 56 GVLLAAYIQVSFWTLAAGRQIRK--------IRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQ 127
Cdd:cd18563 47 LGLAGAYVLSALLGILRGRLLARlgeritadLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 128 AIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 207
Cdd:cd18563 127 NILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIK 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 208 RYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 261
Cdd:cd18563 207 RFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG 260
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
327-521 |
7.74e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.45 E-value: 7.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 327 SDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIrNFNV--RCLREFIGV 404
Cdd:PRK10982 2 SNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSskEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 405 VSQE-PVLFSTTIAENI---RYGRGNVTMDEiKKAVKEANAYdfimklpqkFDTL-----VGDRGAQLSGGQKQRIAIAR 475
Cdd:PRK10982 78 VHQElNLVLQRSVMDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564345546 476 ALVRNPKILLLDEATSALdteSEAEVQ---AALDKARE-GRTTIVIAHRL 521
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSL---TEKEVNhlfTIIRKLKErGCGIVYISHKM 194
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
59-262 |
8.28e-13 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 70.51 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 59 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 138
Cdd:cd18547 60 LFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIM 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 139 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 218
Cdd:cd18547 140 MLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYK 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564345546 219 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 262
Cdd:cd18547 220 ASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGV 263
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
982-1182 |
9.98e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGTVLLDG---QEAKKLNVQWL-----RAQLGIVsqepil 1053
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgriIYEQDLIVARLqqdppRNVEGTV------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 FDcSIAENIA--------YGDNSRVVSQDEIVRAAKE-ANIHPFIETLPQ-KYETRVGD-----------KGTQLSGGQK 1112
Cdd:PRK11147 84 YD-FVAEGIEeqaeylkrYHDISHLVETDPSEKNLNElAKLQEQLDHHNLwQLENRINEvlaqlgldpdaALSSLSGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1113 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
966-1165 |
1.05e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQeakklnvqwLRaqLG 1045
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEpILFDCSIAENIaygdnSRV------VSQDEIVRAAKEANIHPFIETLPQKyetrvgdkgtqLSGGQKQRIAIAR 1119
Cdd:PRK09544 71 YVPQK-LYLDTTLPLTV-----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564345546 1120 ALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV--IAHRL 1165
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
983-1197 |
1.79e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILFD-CSIA 1059
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1060 ENIA-----YGDNSRVVSQDEIVRAAKEANIHPFIETLpqkyetrvgdkGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1134
Cdd:PRK10895 97 DNLMavlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1135 SALDTESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVIDNGKVKEHGTHQQLLAQKGI 1197
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-516 |
2.01e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 339 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREfIGVV----SQ----EPV 410
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR-IGVVfgqrSQlwwdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 411 LFSTTIAENIrYGrgnVTMDEIKKAVKEanaYDFIMKLPQKFDTLVgdRgaQLSGGQKQRIAIARALVRNPKILLLDEAT 490
Cdd:COG4586 114 IDSFRLLKAI-YR---IPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180
....*....|....*....|....*..
gi 564345546 491 SALDTESEAEVQAALDK-AREGRTTIV 516
Cdd:COG4586 183 IGLDVVSKEAIREFLKEyNRERGTTIL 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
344-519 |
2.09e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 344 GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRnfnvRCLREFI----------GVvsqEPVLfs 413
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEYHqdllylghqpGI---KTEL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 414 tTIAENIRY---GRGNVTMDEIKKAvkeanaydfimkLPQkfdtlVGDRG------AQLSGGQKQRIAIARALVRNPKIL 484
Cdd:PRK13538 90 -TALENLRFyqrLHGPGDDEALWEA------------LAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 564345546 485 LLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH 519
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
977-1182 |
2.28e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.91 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN-----------VQWLRAQLG 1045
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVSQEPILFDCSIAENIAYGDNSRVVSQDEIvraakEANIHPFIETLPQK---YETRVGdkgtQLSGGQKQRIAIARALI 1122
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1123 RQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
345-559 |
2.57e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.04 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 345 LNLKVKSGQTVALVGNSGCGKSTtvqLLQRLYD--PTEGTISIDGQDIRNFNVRCLREFIGVVSQE-PVLFSTTIAENI- 420
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 421 RYGRGNVTMDEIKKAVKE-ANAYDFIMKLPqkfdTLVGdrgaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSA 492
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 493 LDTESeaevQAALDK-----AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELIKKE------GIYFRLVN 559
Cdd:PRK03695 164 LDVAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEnlaqvfGVNFRRLD 238
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
980-1187 |
2.84e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.13 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 980 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGTVLLDGQEAKKLNVQwLRAQLGI----------- 1046
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1047 -VSQEPILfdcsiaeNIAYgdNSRVVSQDEivraaKEANIHPFIETLPQKYETrVGDKGTQL--------SGGQKQRIAI 1117
Cdd:CHL00131 98 gVSNADFL-------RLAY--NSKRKFQGL-----PELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1118 ARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVIDNGKVKEHGT 1187
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
337-522 |
3.43e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 70.93 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 337 ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDgQDIRNFNVRcLREFIGVVS-QEPVLFSTT 415
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP-AKGKLFYVP-QRPYMTLGTlRDQIIYPDS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 416 IAENIRYGRGNVTMDEIKKAVKeanaYDFIMKLPQKFDTlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 495
Cdd:TIGR00954 541 SEDMKRRGLSDKDLEQILDNVQ----LTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|....*...
gi 564345546 496 ESEaevQAALDKARE-GRTTIVIAHRLS 522
Cdd:TIGR00954 616 DVE---GYMYRLCREfGITLFSVSHRKS 640
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
341-534 |
3.80e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLydpTEGTISidgQDIRNFNVRCLRE-F---IGVVSQEPV-LFST 414
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERV---TTGVIT---GGDRLVNGRPLDSsFqrsIGYVQQQDLhLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 415 TIAENIRYGRGNVTMDEIKKavKEANAY-DFIMKL---PQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILL-LDEA 489
Cdd:TIGR00956 852 TVRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564345546 490 TSALDTESEAEVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFE 534
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFD 971
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
293-488 |
3.90e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 293 AAYVIFDIIdNNPKIDSFSERGHKPDSIKG--NLEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGKSTTVQ 370
Cdd:PRK10522 291 SAQVAFNKL-NKLALAPYKAEFPRPQAFPDwqTLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 371 LLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTtiaenirygrgnvTMDEIKKAVKEANAYDFI--MKL 448
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQ-------------LLGPEGKPANPALVEKWLerLKM 434
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564345546 449 PQKFdTLVGDRGA--QLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:PRK10522 435 AHKL-ELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
643-906 |
4.01e-12 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 68.25 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMIaifgpgDDTVKQQKCNMFSLVFLGLGVLSFFTFFLQgFTFGKAGEILTTR---- 718
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYII------DDLLPSKNLRLILIIGAILLALYILRTLLN-YFVTYWGHVMGARietd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 719 LRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVqgatgTRLA-------LIAqnTANLGTGIIISFIYGWQLTLL 791
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDNNK--TGQLMSRITNDLFDI-----SELAhhgpedlFIS--IITIIGSFIILLTINVPLTLI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 792 LLSVVPFIAVAGIVEMKMLAGNAKRDKKEMeaaGKI---ATEAIENIRTVVSLTQE----RKFESMYVEklhgpYRNSVR 864
Cdd:cd18549 148 VFALLPLMIIFTIYFNKKMKKAFRRVREKI---GEInaqLEDSLSGIRVVKAFANEeyeiEKFDEGNDR-----FLESKK 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564345546 865 KAHIY-GITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 906
Cdd:cd18549 220 KAYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLV 262
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
324-547 |
5.54e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSypsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL---RE 400
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFS-TTIAENIRYG-RGNVTMDE--IKKAVkeanaydfIMKLPQkfdtlVGDRGA------QLSGGQKQR 470
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKLEA-----VGLRGAaklmpsELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEA-------EVQAALdkareGRTTIVIAHR----LSTVRNADVIAgfeDGVIV 539
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGvlvklisELNSAL-----GVTCVVVSHDvpevLSIADHAYIVA---DKKIV 223
|
....*...
gi 564345546 540 EQGSHSEL 547
Cdd:PRK11831 224 AHGSAQAL 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
993-1178 |
6.41e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 64.70 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 993 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVlldgqeakklnvqwlraqlgivsqepILFDCSIAeniaygdnsrvvs 1072
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDI------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1073 qdeivraakeanihpFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD-- 1150
Cdd:smart00382 42 ---------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180 190
....*....|....*....|....*....|...
gi 564345546 1151 -----KAREGRTCIVIAHRLSTIQNADLIVVID 1178
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
688-849 |
7.01e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 67.92 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 688 LVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALI 767
Cdd:cd18564 58 AALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRR--TGDLLSRLTGDVGAIQDLLVSGVLPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 768 AQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIV---EMKMLAGNAKRDKKEMEAagkIATEAIENIRTVVSLTQE 844
Cdd:cd18564 136 LTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRfsrRIKEASREQRRREGALAS---VAQESLSAIRVVQAFGRE 212
|
....*
gi 564345546 845 RKFES 849
Cdd:cd18564 213 EHEER 217
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
73-265 |
7.26e-12 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 67.50 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 73 GRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLV-IM 151
Cdd:cd18589 65 SRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLtAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 152 AISPILGLSTAV--WAKILSTFSDKELAAYAKAGAvaeEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANI 229
Cdd:cd18589 145 GLPLLLLVPKFVgkFQQSLAVQVQKSLARANQVAV---ETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAV 221
|
170 180 190
....*....|....*....|....*....|....*....
gi 564345546 230 SM---GIAFLLIYASyalAFWYGSTLVISKEYTIGNAMT 265
Cdd:cd18589 222 SMwtsSFSGLALKVG---ILYYGGQLVTAGTVSSGDLVT 257
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
985-1163 |
1.06e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 985 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKL------NVQWLRAQLGIVS----QEPILF 1054
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKTeltaLENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 DCSIAeniaygdnsRVVSQDEIVRAAKEANIHPFiETLPQKyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEAT 1134
Cdd:PRK13538 98 YQRLH---------GPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 564345546 1135 SALDTESEKVVQEALDK-AREGRTCIVIAH 1163
Cdd:PRK13538 158 TAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
966-1166 |
1.08e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 69.01 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVF-NYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklnvqwlRA 1042
Cdd:TIGR00954 447 YQDNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQEPILFDCSIAENIAYGDNSrvvsQDEIVRAAKEANIHPFIETLPQKY--ETRVG-----DKGTQLSGGQKQRI 1115
Cdd:TIGR00954 516 KLFYVPQRPYMTLGTLRDQIIYPDSS----EDMKRRGLSDKDLEQILDNVQLTHilEREGGwsavqDWMDVLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAreGRTCIVIAHRLS 1166
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
324-550 |
1.10e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGTISIDGQDIRNFNVRcLREF 401
Cdd:CHL00131 8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 402 IGV--VSQEPVlfstTIA--ENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDtLVGDRGAQL--------SGGQKQ 469
Cdd:CHL00131 84 LGIflAFQYPI----EIPgvSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 470 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGShSE 546
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AE 237
|
....
gi 564345546 547 LIKK 550
Cdd:CHL00131 238 LAKE 241
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-522 |
1.16e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 66.24 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 349 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTIS--IDGQDIrnfnvrcLREFIGVVSQEpvLFSTTIAENIRYGRGN 426
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdpPDWDEI-------LDEFRGSELQN--YFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 427 VTMDEIKKAVKeANAYDFIMKLPQ--KFDTLVG--------DRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 495
Cdd:cd03236 94 QYVDLIPKAVK-GKVGELLKKKDErgKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 564345546 496 ESEAEVQAALDK-AREGRTTIVIAHRLS 522
Cdd:cd03236 173 KQRLNAARLIRElAEDDNYVLVVEHDLA 200
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
77-268 |
1.42e-11 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 66.70 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 77 RKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPI 156
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 157 LGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFL 236
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
170 180 190
....*....|....*....|....*....|....*..
gi 564345546 237 LIYASYALAFWYGSTLVISKEYTIG-----NAMTVFF 268
Cdd:cd18570 234 ISLIGSLLILWIGSYLVIKGQLSLGqliafNALLGYF 270
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
976-1182 |
1.72e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.03 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 976 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRaQLGIV----SQep 1051
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1052 ILFDCSIAENIA-----YGdnsrvVSQDEIvraakEANIHPFIETLpqkyetRVGDKGT----QLSGGQKQRIAIARALI 1122
Cdd:COG4586 107 LWWDLPAIDSFRllkaiYR-----IPDAEY-----KKRLDELVELL------DLGELLDtpvrQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1123 RQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1182
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
684-900 |
2.23e-11 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 66.21 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 684 NMFSLVFLGLGVLSFFTFFLQG-----FTFgkAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG 758
Cdd:cd18590 33 NAFTSAIGLMCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLMSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 759 ATGTRLALIAQNTANlgTGIIISFIYG--WQLTLLLLSVVPFIAVAgiveMKMLAGNAKRDKKEME----AAGKIATEAI 832
Cdd:cd18590 109 SVALNANVLLRSLVK--TLGMLGFMLSlsWQLTLLTLIEMPLTAIA----QKVYNTYHQKLSQAVQdsiaKAGELAREAV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 833 ENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18590 183 SSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
983-1205 |
2.42e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPMAGTVLLDGqeaKKLNVQWLRaQLGIVSQEPILF-DCSIA 1059
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---RKPTKQILK-RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1060 ENIAYGDNSRV---VSQDEIVRAAkEANIHPFieTLPQKYETRVGDKGTQ-LSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:PLN03211 159 ETLVFCSLLRLpksLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1136 ALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIDNGKVKEHGTHQQLLAqkgiYFSMVNIQ 1205
Cdd:PLN03211 236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
971-1194 |
3.97e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 971 VVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--MAGTVLLDGQE-----AKKLNVqwLRA 1042
Cdd:PRK09473 20 VTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREilnlpEKELNK--LRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 -QLGIVSQEP-----------------ILFDCSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFietlpqkyetrvgdkg 1104
Cdd:PRK09473 97 eQISMIFQDPmtslnpymrvgeqlmevLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPH---------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1105 tQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVIDNGK 1181
Cdd:PRK09473 161 -EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMYAGR 239
|
250
....*....|...
gi 564345546 1182 VKEHGTHQQLLAQ 1194
Cdd:PRK09473 240 TMEYGNARDVFYQ 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
987-1193 |
4.19e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.77 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 987 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PMAGTVLLDGQEAKKLN-VQWLRAQLGIVSQEP----ILFDCSIAE 1060
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1061 NIAYGDNSRVVSQDEIVRAAKEANIHPFIETLpqKYETRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1139
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1140 ESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVK----EHG-THQQLLA 1193
Cdd:TIGR02633 437 GAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
965-1187 |
4.97e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 65.53 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVvfNYPTRAnvpvLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL 1040
Cdd:PRK11022 10 SVHFGDE--SAPFRA----VDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1041 R----AQLGIVSQEPI--LFDC-----SIAENIAY--GDNSRVVSQdeivRAakeanihpfIETLPQ----KYETRVGDK 1103
Cdd:PRK11022 84 RnlvgAEVAMIFQDPMtsLNPCytvgfQIMEAIKVhqGGNKKTRRQ----RA---------IDLLNQvgipDPASRLDVY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1104 GTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIDNG 1180
Cdd:PRK11022 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAG 230
|
....*..
gi 564345546 1181 KVKEHGT 1187
Cdd:PRK11022 231 QVVETGK 237
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
978-1187 |
5.93e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 978 RANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPMA-------GTVLLDGQEAKKLNVQWL---RAQLGI 1046
Cdd:PRK13547 12 RHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1047 VSQEPILFdcSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFIETlpqKYETRVGDKGTQLSGGQKQRIAIARAL----- 1121
Cdd:PRK13547 91 AAQPAFAF--SAREIVLLGRYPHARRAGALTHRDGEIAWQALALA---GATALVGRDVTTLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1122 ----IRQPRVLLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVIDNGKVKEHGT 1187
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
688-906 |
7.83e-11 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 64.34 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 688 LVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA--TGTRLA 765
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFvmMLLRML 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 766 LIAqnTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE- 844
Cdd:cd18548 121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 845 ---RKFESMyVEKLhgpYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 906
Cdd:cd18548 199 yeeERFDKA-NDDL---TDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLV 259
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
970-1172 |
1.26e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 970 EVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlRAQLGIVSQ 1049
Cdd:PRK13540 6 ELDFDYHDQ---PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1050 EP-ILFDCSIAENIAYG--DNSRVVSQDEIVRAAKEANIHPFIETLpqkyetrvgdkgtqLSGGQKQRIAIARALIRQPR 1126
Cdd:PRK13540 82 RSgINPYLTLRENCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564345546 1127 VLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1172
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
333-546 |
1.36e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.20 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 333 YPSRANIKILKGLNLKVKSG-----QTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDirnfnvrclrefigvVSQ 407
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 408 EPVLFSTTIAENIRYgrgnvTMDEIKKAVKEANAYDF-IMKlPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 486
Cdd:cd03237 66 KPQYIKADYEGTVRD-----LLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 487 DEATSALDTESEAEVQAALDKAREG--RTTIVIAHrlsTVRNADVIAgfeDGVIVEQGSHSE 546
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH---DIIMIDYLA---DRLIVFEGEPSV 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
964-1180 |
1.72e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.49 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 964 GSVTFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-ERFYD-PMAGTVLLDGQEAKKLnvqwL 1040
Cdd:cd03232 2 SVLTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDKN----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1041 RAQLGIVSQEPILFDCSiaeniaygdnsrvvsqdeIVRAAKE--ANIhpfietlpqkyetrvgdKGtqLSGGQKQRIAIA 1118
Cdd:cd03232 78 QRSTGYVEQQDVHSPNL------------------TVREALRfsALL-----------------RG--LSVEQRKRLTIG 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1119 RALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVIDNG 1180
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
970-1193 |
2.54e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 970 EVVF---NY----PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM-AGTVLLDGQEAKKLN-VQWL 1040
Cdd:PRK13549 257 EVILevrNLtawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNpQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1041 RAQLGIVSQEP----ILFDCSIAENIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKY---ETRVGdkgtQLSGGQKQ 1113
Cdd:PRK13549 337 AQGIAMVPEDRkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTaspELAIA----RLSGGNQQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1114 RIAIARALIRQPRVLLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVK----- 1183
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdlin 489
|
250
....*....|
gi 564345546 1184 EHGTHQQLLA 1193
Cdd:PRK13549 490 HNLTQEQVME 499
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
982-1194 |
2.64e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.12 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPI----- 1052
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1053 ----LFDCSIAENIAYGDnsrvvsQDEIVRAAKEANIHPFIETL--PQKYETRVGDKGtqLSGGQKQRIAIARALIRQPR 1126
Cdd:PRK09580 94 snqfFLQTALNAVRSYRG------QEPLDRFDFQDLMEEKIALLkmPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1127 VLLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVIDNGKVKEHGTH---QQLLAQ 1194
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
987-1192 |
2.74e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 987 LSLEVKKGQTLALVGSSGCGKSTvvqLLERfydpMAGT------VLLDGQ-----EAKKLNVQwlRAQLgiVSQEPILF- 1054
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLAR----MAGLlpgsgsIQFAGQpleawSAAELARH--RAYL--SQQQTPPFa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 -------DCSIAENIAYGDNSRVVsqDEIVRAAKeanihpfietLPQKYETRVGdkgtQLSGGQKQRIAIArALIRQ--- 1124
Cdd:PRK03695 84 mpvfqylTLHQPDKTRTEAVASAL--NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLA-AVVLQvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1125 ---P--RVLLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLL 1192
Cdd:PRK03695 147 dinPagQLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
684-900 |
2.91e-10 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 62.85 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 684 NMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLaTDAAQVQGA-TGT 762
Cdd:cd18570 42 NIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRK--TGEIISRF-NDANKIREAiSST 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 763 RLALIAQNTANLGTGIIIsFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVV 839
Cdd:cd18570 119 TISLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYILIILLFNKPF---KKKNREVMESNAELNSyliESLKGIETIK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 840 SLTQERKFesmyVEKLHGPYRNSVRKAHIYGITFSISQAFM----YFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18570 195 SLNAEEQF----LKKIEKKFSKLLKKSFKLGKLSNLQSSIKglisLIGSLLILWIGSYLVIKGQL 255
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
965-1168 |
3.84e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.21 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 965 SVTFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQL 1044
Cdd:PRK15056 6 GIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 GiVSQE-----PILFDcSIAENIAYGDNS---RVVSQD-EIVRAAKEAnihpfIETLPQKYEtRVGdkgtQLSGGQKQRI 1115
Cdd:PRK15056 84 P-QSEEvdwsfPVLVE-DVVMMGRYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1116 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1168
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
59-276 |
4.09e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 62.50 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 59 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 138
Cdd:cd18550 54 LLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 139 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGA--IRTVIAFGGQNKELERYQKHLENA 216
Cdd:cd18550 134 MLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSREL 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 217 KKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAFS 276
Cdd:cd18550 214 RDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTlvAFTALLGRLYGPLT 275
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
685-900 |
7.45e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 61.37 E-value: 7.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 685 MFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG-ATGTR 763
Cdd:cd18563 44 LLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDfLSDGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 764 LALIAQNTANLGTGIIIsFIYGWQLTLLLLSVVPFIAVAGIVEMKML-AGNAKRDKKEMEAAGKIAtEAIENIRTVVSLT 842
Cdd:cd18563 122 PDFLTNILMIIGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIrRLFHRQWRRWSRLNSVLN-DTLPGIRVVKAFG 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 843 QErKFESMYVEKLHGPYRNSVRKAH--------IYGITFSISQAFMYFsyagcfrFGSYLIVNGHM 900
Cdd:cd18563 200 QE-KREIKRFDEANQELLDANIRAEklwatffpLLTFLTSLGTLIVWY-------FGGRQVLSGTM 257
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
981-1181 |
7.76e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 981 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAK-KLNVQWLRAQLGIVSQE-PILFDCSI 1058
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 AENIAYGDNSR---VVSQDEIVRAAKEANIHPFIETLPQkyetrvgDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:PRK10982 91 MDNMWLGRYPTkgmFVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1136 ALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVIDNGK 1181
Cdd:PRK10982 164 SL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
324-528 |
1.01e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 403
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPVLFSTTIAEN----IRYGRGNVTMDEIKKAVKEANAYDFIMKLpqkfdtlvgdrgaqLSGGQKQRIAIARALVR 479
Cdd:PRK13540 79 VGHRSGINPYLTLRENclydIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564345546 480 NPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRNAD 528
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
55-275 |
1.10e-09 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 60.93 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 55 GGVLLAAYI-------QVSFWTLAAGRQI-RKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISE----GIGDkv 122
Cdd:cd18549 45 GAILLALYIlrtllnyFVTYWGHVMGARIeTDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 123 gmFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLST--------AVWAKILSTFSDkelaayakAGAVAEEALGAIR 194
Cdd:cd18549 123 --LFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTiyfnkkmkKAFRRVREKIGE--------INAQLEDSLSGIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 195 TVIAFGGQNKELERYQK---HLENAKKIGIKkaISANISMGIAFL--LIYASyALAFwyGSTLVISKEYTIGNAMTvfFS 269
Cdd:cd18549 193 VVKAFANEEYEIEKFDEgndRFLESKKKAYK--AMAYFFSGMNFFtnLLNLV-VLVA--GGYFIIKGEITLGDLVA--FL 265
|
....*.
gi 564345546 270 ILIGAF 275
Cdd:cd18549 266 LYVNVF 271
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
43-261 |
1.10e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 60.94 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 43 MTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKV 122
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 123 GMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQ 202
Cdd:cd18545 119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFARE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 203 NKELERYQKHLENAKKIGIkKAISANISMGIAFLLIYA-SYALAFWYGSTLVISKEYTIG 261
Cdd:cd18545 199 DENEEIFDELNRENRKANM-RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG 257
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
340-519 |
1.38e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDgQDIRnfnvrclrefIGVVSQEPVLFST-TIAE 418
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK----------VGYLPQEPQLDPTkTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 419 NIRYGrgnvtMDEIKKAVKE-------------------------------ANAYDFIMKLPQKFDTL---VGD-RGAQL 463
Cdd:TIGR03719 88 NVEEG-----VAEIKDALDRfneisakyaepdadfdklaaeqaelqeiidaADAWDLDSQLEIAMDALrcpPWDaDVTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564345546 464 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH 519
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
687-900 |
1.64e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 60.58 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 687 SLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLAL 766
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERET--SGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 767 IAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKmLAGNAKRDKKEmEAAGKIAT--EAIENIRTVVSLTQE 844
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR-RSSRAYRRARE-RIAAVNADlqETLAGIRVVQAFRRE 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 845 RKFESMYVEkLHGPYRNSVRKAHIYgitFSISQAFMYF----SYAGCFRFGSYLIVNGHM 900
Cdd:cd18546 198 RRNAERFAE-LSDDYRDARLRAQRL---VAIYFPGVELlgnlATAAVLLVGAWRVAAGTL 253
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
693-898 |
1.69e-09 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 60.56 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 693 LGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTA 772
Cdd:cd18589 45 LTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 773 NLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYV 852
Cdd:cd18589 123 RGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYR 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564345546 853 EKLHGPYRNSVRKAHIYGI---TFSISQAFMyfsYAGCFRFGSYLIVNG 898
Cdd:cd18589 203 QRLQKTYRLNKKEAAAYAVsmwTSSFSGLAL---KVGILYYGGQLVTAG 248
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
315-539 |
1.88e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.76 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 315 HKPDSIKGN-LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPT-EGTISIDGQ--DI 390
Cdd:TIGR02633 248 HEPHEIGDViLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 391 RNfnvrCL-------------REFIGVVSQEPVLFSTTIAENIRY-GRGNVT----MDEIKKAVKEANAYDFIMKLPQkf 452
Cdd:TIGR02633 328 RN----PAqairagiamvpedRKRHGIVPILGVGKNITLSVLKSFcFKMRIDaaaeLQIIGSAIQRLKVKTASPFLPI-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 453 dtlvgdrgAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVrnadviA 531
Cdd:TIGR02633 402 --------GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEV------L 467
|
....*...
gi 564345546 532 GFEDGVIV 539
Cdd:TIGR02633 468 GLSDRVLV 475
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
324-502 |
1.93e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTIsidgqdIRNFNVRclrefIG 403
Cdd:PLN03073 509 ISFSDASFGYP--GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPV----LFSTTIaenirygrgnVTMDEIKKAVKEanaydfimklpQKFDTLVGDRGAQ----------LSGGQKQ 469
Cdd:PLN03073 576 VFSQHHVdgldLSSNPL----------LYMMRCFPGVPE-----------QKLRAHLGSFGVTgnlalqpmytLSGGQKS 634
|
170 180 190
....*....|....*....|....*....|....
gi 564345546 470 RIAIARALVRNPKILLLDEATSALDTES-EAEVQ 502
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
982-1197 |
2.20e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVlldgqeakklnvQWL-RAQLGIVSQEP--------I 1052
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeNANIGYYAQDHaydfendlT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1053 LFDCsIAENIAYGDNSRVV---------SQDEIVRAAKeanihpfietlpqkyetrvgdkgtQLSGGQKQRIAIARALIR 1123
Cdd:PRK15064 401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVK------------------------VLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1124 QPRVLLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVIDNGKVKEHGTHQQLLAQKGI 1197
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
643-866 |
2.52e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 59.86 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 643 FVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVkqQKCNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSM 722
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL--GLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 723 AFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQgatgtRLAL--IAQNTANLGTGIIIS---FIYGWQLTLLLLSVVP 797
Cdd:cd18778 79 LYDKLQRLSLRYFDDR--QTGDLMSRVINDVANVE-----RLIAdgIPQGITNVLTLVGVAiilFSINPKLALLTLIPIP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 798 FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKfESMYVEKLHGPYRNSVRKA 866
Cdd:cd18778 152 FLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEE-EAKRFEALSRRYRKAQLRA 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
334-524 |
2.57e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 334 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-PTEGTISIDGQ--DIRNfnvrCL------------ 398
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRN----PQqaiaqgiamvpe 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 399 -REFIGVVSQEPVLFSTTIAENIRYGRGNVtmdeIKKAVKEANAYDFIMKLPQKFDTLVGdRGAQLSGGQKQRIAIARAL 477
Cdd:PRK13549 346 dRKRDGIVPVMGVGKNITLAALDRFTGGSR----IDDAAELKTILESIQRLKVKTASPEL-AIARLSGGNQQKAVLAKCL 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564345546 478 VRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTV 524
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEV 468
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
969-1166 |
3.53e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 969 NEVVFNYPtrANVPVLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDPMAGTVLLD---GQEAKKLNV 1037
Cdd:cd03236 4 DEPVHRYG--PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1038 QWLRAQLGI------VSQEPILFDCSIAENIAYGDNSRVvsQDEIVraaKEANIHPFIETlpqkyetrvgdKGTQLSGGQ 1111
Cdd:cd03236 81 KLLEGDVKVivkpqyVDLIPKAVKGKVGELLKKKDERGK--LDELV---DQLELRHVLDR-----------NIDQLSGGE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1112 KQRIAIARALIRQPRVLLLDEATSALDTESE----KVVQEAldkAREGRTCIVIAHRLS 1166
Cdd:cd03236 145 LQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaRLIREL---AEDDNYVLVVEHDLA 200
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
314-523 |
4.28e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 314 GHKPDSikgnlefSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ-RLYDPT-EGTISIDGqdiR 391
Cdd:PLN03211 66 GHKPKI-------SDETRQIQERT---ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---R 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 392 NFNVRCLREfIGVVSQEPVLFS-TTIAENIRYGRGNVTMDEIKKAVKEANAYDFI--MKLPQKFDTLVGD---RGaqLSG 465
Cdd:PLN03211 133 KPTKQILKR-TGFVTQDDILYPhLTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISG 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 466 GQKQRIAIARALVRNPKILLLDEATSALD-TESEAEVQAALDKAREGRTTIVIAHRLST 523
Cdd:PLN03211 210 GERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
975-1187 |
7.06e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 57.80 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 975 YPTRANVPVLQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLerfydpmAGTVLLDGQEAKKLNVQwlraqlgiVSQ 1049
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT--------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1050 EPilfdcsiaENIAYGDNSRVvsQDEIVRAAKEANIHPFIET-------LPQKYETRVgdkgTQLSGGQKQRIAIARALI 1122
Cdd:cd03237 66 KP--------QYIKADYEGTV--RDLLSSITKDFYTHPYFKTeiakplqIEQILDREV----PELSGGELQRVAIAACLS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1123 RQPRVLLLDEATSALDTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVIDnGKVKEHGT 1187
Cdd:cd03237 132 KDADIYLLDEPSAYLDVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
984-1174 |
1.41e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 984 LQGLSLEV-----KKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLldgqeaKKLNV----QWLRA-QLGIVSQepil 1053
Cdd:PRK13409 350 LGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELKIsykpQYIKPdYDGTVED---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1054 FDCSIAENIaygDNSRVvsQDEIVRaakeanihPFieTLPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:PRK13409 420 LLRSITDDL---GSSYY--KSEIIK--------PL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564345546 1134 TSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIqnaDLI 1174
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
988-1192 |
1.67e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 988 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeaKKLNV----QWLRAqlGIV------SQEPILFDCS 1057
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIrsprDAIRA--GIMlcpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1058 IAENIAYGDNSRVVSQDEIVRAAKEA-NIHPFIETLPQKyeTRVGD-KGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1135
Cdd:PRK11288 348 VADNINISARRHHLRAGCLINNRWEAeNADRFIRSLNIK--TPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 1136 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV-----KEHGTHQQLL 1192
Cdd:PRK11288 426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
349-521 |
2.71e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 349 VKSGQTVALVGNSGCGKSTTVQLLQrlydptegtisidGQDIRNFnvrclrefiGVVSQEPvlfstTIAENIRYGRGNVT 428
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------------GELIPNL---------GDYEEEP-----SWDEVLKRFRGTEL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 429 MD--------EIKKAVKeaNAYdfIMKLPQKFDTLVGD-------RGA-------------------QLSGGQKQRIAIA 474
Cdd:PRK13409 149 QNyfkklyngEIKVVHK--PQY--VDLIPKVFKGKVREllkkvdeRGKldevverlglenildrdisELSGGELQRVAIA 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564345546 475 RALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 521
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
335-543 |
4.78e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 55.70 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 335 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVqlLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG---VVSQEPV- 410
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 411 ------------LFsTTIAE----------------NIRYgRGNVTMDEIKKAVKEAnaYDFIMKLPQ---KFDTLV--- 456
Cdd:cd03271 82 rtprsnpatytgVF-DEIRElfcevckgkrynretlEVRY-KGKSIADVLDMTVEEA--LEFFENIPKiarKLQTLCdvg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 457 ------GDRGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN 526
Cdd:cd03271 158 lgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKC 237
|
250 260
....*....|....*....|...
gi 564345546 527 ADVI------AGFEDGVIVEQGS 543
Cdd:cd03271 238 ADWIidlgpeGGDGGGQVVASGT 260
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
309-519 |
5.07e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 309 SFSERGHKPDSikgnleFSDVHFSYPSRanIKILKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLLQRLYDPTEGTI 383
Cdd:PRK13409 325 EFEERPPRDES------ERETLVEYPDL--TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 384 SID------GQDIRNfnvrclrEFIGVVSQepVLFSttIAENIRygrGNVTMDEIKKAvkeanaydfiMKLPQKFDTLVG 457
Cdd:PRK13409 397 DPElkisykPQYIKP-------DYDGTVED--LLRS--ITDDLG---SSYYKSEIIKP----------LQLERLLDKNVK 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 458 DrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAH 519
Cdd:PRK13409 453 D----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
346-546 |
6.21e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 346 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRnfnVRCLREFI--GVV------SQEPVLFSTTIA 417
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRSPRDAIraGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 418 ENI------RYGRGNVTMDEIKKAvkeANAYDFIMKLPQKF---DTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:PRK11288 350 DNInisarrHHLRAGCLINNRWEA---ENADRFIRSLNIKTpsrEQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 489 ATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSE 546
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
339-544 |
7.13e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 339 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGTISIDG-----QDIRNFNVRCLREFI---GVVSQE 408
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqETFARISGYCEQNDIhspQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 409 PVLFSTTIAENIRYGRGNVTM--DEIKKAVKEANAYDFIMKLPqkfdtlvGDRGaqLSGGQKQRIAIARALVRNPKILLL 486
Cdd:PLN03140 973 SLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 487 DEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTvrnaDVIAGFEDGVIVEQGSH 544
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1099-1175 |
7.62e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.93 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1099 RVGDKGTQLSGGQKQRIAIARALIRQPR---VLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLI 1174
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
|
.
gi 564345546 1175 V 1175
Cdd:cd03271 242 I 242
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
53-273 |
1.10e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 54.91 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 53 LGGGVLLAAYIQVSF-------WTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLtDDISKISEGIGDkvgmf 125
Cdd:cd18782 44 IGVVMLVAALLEAVLtalrtylFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTG----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 126 fQAIATFF-AGFIVGFIR-----GWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAf 199
Cdd:cd18782 118 -TALTTLLdVLFSVIYIAvlfsySPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 200 ggQNKEL-------ERYQKHLENAKKIGIKKAISANISMGIAFLliyaSYALAFWYGSTLVISKEYTIGNAMTvfFSILI 272
Cdd:cd18782 196 --QNAELkarwrwqNRYARSLGEGFKLTVLGTTSGSLSQFLNKL----SSLLVLWVGAYLVLRGELTLGQLIA--FRILS 267
|
.
gi 564345546 273 G 273
Cdd:cd18782 268 G 268
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
55-275 |
1.21e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 54.85 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 55 GGVLLAAYIQVSFWT--------LAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFF 126
Cdd:cd18778 43 ALLLLGAYLLRALLNflriylnhVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 127 QAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKEL 206
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 207 ERYQKHLENAKkigiKKAISANISMGIAFLLIY----ASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAF 275
Cdd:cd18778 203 KRFEALSRRYR----KAQLRAMKLWAIFHPLMEfltsLGTVLVLGFGGRLVLAGELTIGD--LVAFLLYLGLF 269
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
359-494 |
1.23e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 359 GNSGCGKSTTVQLLQRLYDPTEGTISIDGQ--DIRNFNVRcLRefIGVVSQEpvlFST----TIAENIR-----YGrgnV 427
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIATR-RR--VGYMSQA---FSLygelTVRQNLElharlFH---L 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 428 TMDEIKKAVKEanaydfimkLPQKFD--TLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 494
Cdd:NF033858 370 PAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
350-523 |
1.24e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 350 KSGQTVALVGNSGCGKSTTVQLLQrlydptegtisidGQDIRNFnvrclrefiGVVSQEPvlfstTIAENIRYGRGNVTM 429
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------------GELKPNL---------GDYDEEP-----SWDEVLKRFRGTELQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 430 D--------EIKKAVKEanayDFIMKLPQKFDTLVGD-------RGA-------------------QLSGGQKQRIAIAR 475
Cdd:COG1245 150 DyfkklangEIKVAHKP----QYVDLIPKVFKGTVREllekvdeRGKldelaeklglenildrdisELSGGELQRVAIAA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLST 523
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIYQRLNVARLIrELAEEGKYVLVVEHDLAI 274
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
59-277 |
1.25e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 54.88 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 59 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 138
Cdd:cd18565 69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 139 GFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKk 218
Cdd:cd18565 149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYR- 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 219 igiKKAISAnISMGIAF-----LLIYASYALAFWYGSTLVISKEYTIGNAMTVffsiliGAFSV 277
Cdd:cd18565 228 ---DANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
81-275 |
1.32e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 54.82 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 81 QKFFHAILRQEMGWFDIKGTTELNTRLtDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLS 160
Cdd:cd18555 79 SDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 161 TAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYA 240
Cdd:cd18555 158 LLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFI 237
|
170 180 190
....*....|....*....|....*....|....*
gi 564345546 241 SYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF 275
Cdd:cd18555 238 APLLILWIGAYLVINGELTLG--ELIAFSSLAGSF 270
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
325-496 |
1.39e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 325 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ-DIRNFNVRclREFIg 403
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQH--RAEL- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 vvsqEPvlfSTTIAENIRYGRGNVTMDEIKKAVKeanAY--DFIMKlPQKFDTLVgdrgAQLSGGQKQRIAIARALVRNP 481
Cdd:PRK11147 395 ----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLKPS 459
|
170
....*....|....*
gi 564345546 482 KILLLDEATSALDTE 496
Cdd:PRK11147 460 NLLILDEPTNDLDVE 474
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
84-273 |
1.41e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 54.51 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 84 FHAILRQEMGWFDIKGTTELNTRLTDdISKISEgigdkvgmFF--QAIATF----FAG--FIVGFIRGWKLTLVIMAISP 155
Cdd:cd18566 82 FEHLLSLPLSFFEREPSGAHLERLNS-LEQIRE--------FLtgQALLALldlpFVLifLGLIWYLGGKLVLVPLVLLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 156 ILglstAVWAKILSTFSDKELAAYAKAGAVAE----EALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISM 231
Cdd:cd18566 153 LF----VLVAILLGPILRRALKERSRADERRQnfliETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQ 228
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564345546 232 GIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIG 273
Cdd:cd18566 229 TLGQLFSQVSMVAVVAFGALLVINGDLTVG--ALIACTMLSG 268
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
349-534 |
1.55e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.57 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 349 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGqdirnfnvrclrefigvvsqepvlfsttiaenirygrgnvt 428
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 429 mdeIKKAVKeanaydfimklPQKFDtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA 508
Cdd:cd03222 61 ---ITPVYK-----------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 564345546 509 RE--GRTTIVIAHRLSTVRN-ADVIAGFE 534
Cdd:cd03222 118 SEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
988-1194 |
1.60e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 988 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG--------TVLLDGQEAKKL-NVQWLRAQLGIVSQEPILFDCSI 1058
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshITRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1059 AENIAYG--DNSRVVsqdeivRAAKEANIHPFIETlPQKYetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:PRK10938 103 AEIIQDEvkDPARCE------QLAQQFGITALLDR-RFKY----------LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1137 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1194
Cdd:PRK10938 166 LDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
990-1187 |
1.79e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 990 EVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGTVLLDGQEA-KKLNV----QWLRAQLGIVSQEpILFDcSIAENIay 1064
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVdEDLKIsykpQYISPDYDGTVEE-FLRS-ANTDDF-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1065 gDNSRVvsQDEIVRaakeanihPF-IETLpqkYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEK 1143
Cdd:COG1245 431 -GSSYY--KTEIIK--------PLgLEKL---LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564345546 1144 VVQEALDKAREGR--TCIVIAHRLSTIqnaDLI---VVIDNGKVKEHGT 1187
Cdd:COG1245 493 AVAKAIRRFAENRgkTAMVVDHDIYLI---DYIsdrLMVFEGEPGVHGH 538
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
341-518 |
1.96e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 341 ILKGLNLKVKSGQTVALVGNSGCGKST-----TVQLLQRLYDpTEGTISIDG---QDIRNFnvrcLREFIGVVSQEPVLF 412
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGitpEEIKKH----YRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 413 -STTIAENIRYG--------RGNvTMDEIKKAVKEANAYDFIMKLPQKFDTLVGD---RGaqLSGGQKQRIAIARALVRN 480
Cdd:TIGR00956 151 pHLTVGETLDFAarcktpqnRPD-GVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGG 227
|
170 180 190
....*....|....*....|....*....|....*....
gi 564345546 481 PKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA 518
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALkTSANILDTTPLVA 266
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
648-845 |
2.02e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 54.03 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 648 LCAIANGALQPAFSIILSEMI--AIFGPGDDTVkqqkcNMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFK 725
Cdd:cd18550 6 LLILLSALLGLLPPLLLREIIddALPQGDLGLL-----VLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 726 AMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP-FIAVAGI 804
Cdd:cd18550 81 HLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPlFVLPTRR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564345546 805 VemkmlaGNAKRdkkemeaagKIATEAIENIRTVVSLTQER 845
Cdd:cd18550 159 V------GRRRR---------KLTREQQEKLAELNSIMQET 184
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
420-548 |
2.03e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 55.40 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 420 IRYgRGNVTMDEIKKAVKEAnaYDFIMKLP---QKFDTLVgDRGAQ----------LSGGQKQRIAIARALVR---NPKI 483
Cdd:TIGR00630 778 VKY-KGKNIADVLDMTVEEA--YEFFEAVPsisRKLQTLC-DVGLGyirlgqpattLSGGEAQRIKLAKELSKrstGRTL 853
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 484 LLLDEATSALDTESEAE----VQAALDKareGRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQGSHSELI 548
Cdd:TIGR00630 854 YILDEPTTGLHFDDIKKllevLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEVA 925
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
324-553 |
2.52e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTIsidgQDIRNFNvrclrefIG 403
Cdd:PRK15064 320 LEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSENAN-------IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQEPV--------LFS-----TTIAEN---IR--YGRGNVTMDEIKKAVKeanaydfimklpqkfdtlvgdrgaQLSG 465
Cdd:PRK15064 386 YYAQDHAydfendltLFDwmsqwRQEGDDeqaVRgtLGRLLFSQDDIKKSVK------------------------VLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 466 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKArEGrTTIVIAH------RLSTvrnaDVIAGFEDGVIV 539
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
|
250
....*....|....
gi 564345546 540 EQGSHSELIKKEGI 553
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
685-900 |
2.53e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 53.64 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 685 MFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 764
Cdd:cd18540 43 GFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 765 ALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIA-VAGIVEMKMLAGNAKRDKKEMEAAGKIaTEAIENIRTVVSLTQ 843
Cdd:cd18540 121 VDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAvVSIYFQKKILKAYRKVRKINSRITGAF-NEGITGAKTTKTLVR 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 844 ERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18540 200 EEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAI 256
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
461-615 |
2.82e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 461 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdKAREGrTTIVIAHRLSTVRN-ADVIAGFEDGVIV 539
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKLV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 540 E-QGSHSE-LIKKEGiYFRLVNMQtsgsqilSEEFEVELSDEKAaggvapngW-----KARIFRNSTK-KSLKSSR-AHQ 610
Cdd:PRK11147 233 SyPGNYDQyLLEKEE-ALRVEELQ-------NAEFDRKLAQEEV--------WirqgiKARRTRNEGRvRALKALRrERS 296
|
....*
gi 564345546 611 NRLDV 615
Cdd:PRK11147 297 ERREV 301
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
991-1163 |
2.93e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 991 VKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklnvQWlraQLGIVSQEPILFDCSIAENIAYGDnsRV 1070
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------NW---QLAWVNQETPALPQPALEYVIDGD--RE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1071 VSQDEI-VRAAKEANIHPFIETLPQKYET---------------RVGDKGTQL-------SGGQKQRIAIARALIRQPRV 1127
Cdd:PRK10636 91 YRQLEAqLHDANERNDGHAIATIHGKLDAidawtirsraasllhGLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSDL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 564345546 1128 LLLDEATSALDTESEKVVQEALdKAREGrTCIVIAH 1163
Cdd:PRK10636 171 LLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISH 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
982-1193 |
3.18e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQlGIV------SQEPILFD 1055
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1056 CSIAENI---AYGDNSRVVSQdeIVRAAKEANIHPFIETLPQKYETR---VGDkgtqLSGGQKQRIAIARALIRQPRVLL 1129
Cdd:PRK10762 345 MSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMeqaIGL----LSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 1130 LDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIDNGKV-----KEHGTHQQLLA 1193
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
314-521 |
3.68e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.02 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 314 GHKPDSIKGNlEFSDVHFSYPSRANIKILKGlnlkVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNf 393
Cdd:TIGR01257 1932 GNKTDILRLN-ELTKVYSGTSSPAVDRLCVG----VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 394 NVRCLREFIGVVSQ-EPVLFSTTIAENIR-YGR-GNVTMDEIKKAvkeANAYDFIMKLPQKFDTLVGdrgaQLSGGQKQR 470
Cdd:TIGR01257 2006 NISDVHQNMGYCPQfDAIDDLLTGREHLYlYARlRGVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRK 2078
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564345546 471 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRL 521
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
340-519 |
4.17e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLLQRLYDPTEG------TISIDGQDIRNFNVRCLREFIGVVSQE 408
Cdd:COG1245 349 KSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlKISYKPQYISPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 409 PvlFSTTIAENirygrgnvtmdEIKKAvkeanaydfiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:COG1245 429 D--FGSSYYKT-----------EIIKP----------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190
....*....|....*....|....*....|...
gi 564345546 489 ATSALDTESEAEVQAALDKAREGR--TTIVIAH 519
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDH 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
340-497 |
4.50e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 340 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDgQDIRnfnvrclrefIGVVSQEPVLFST-TIAE 418
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK----------VGYLPQEPQLDPEkTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 419 NIRYGrgnvtMDEIKKAVKEANAYDFIMKLPQ-KFDTLVGDRG----------------------------------AQL 463
Cdd:PRK11819 90 NVEEG-----VAEVKAALDRFNEIYAAYAEPDaDFDALAAEQGelqeiidaadawdldsqleiamdalrcppwdakvTKL 164
|
170 180 190
....*....|....*....|....*....|....
gi 564345546 464 SGGQKQRIAIARALVRNPKILLLDEATSALDTES 497
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1080-1180 |
5.81e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.86 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1080 AKEANIHPFIETLPQ---KYeTRVGDKGTQLSGGQKQRIAIARALIRQ---PRVLLLDEATSALDTESEK----VVQEAL 1149
Cdd:TIGR00630 801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
|
90 100 110
....*....|....*....|....*....|.
gi 564345546 1150 DKareGRTCIVIAHRLSTIQNADLIvvIDNG 1180
Cdd:TIGR00630 880 DK---GNTVVVIEHNLDVIKTADYI--IDLG 905
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
988-1150 |
5.88e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 988 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVlldgQEAKKLNVQWL---RAQLgivsqEPilfDCSIAENIAY 1064
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFdqhRAEL-----DP---EKTVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1065 GD-----NSR---VVS--QDEIvraakeanIHPFIETLPQKyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEAT 1134
Cdd:PRK11147 407 GKqevmvNGRprhVLGylQDFL--------FHPKRAMTPVK----------ALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
170
....*....|....*.
gi 564345546 1135 SALDTESEKVVQEALD 1150
Cdd:PRK11147 469 NDLDVETLELLEELLD 484
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
968-1196 |
5.91e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.25 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 968 FNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIV 1047
Cdd:TIGR01257 1940 LNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1048 SQEPILFDCSIA-ENIAYGDNSRVVSQDEIVRAAKEAnihpfIETLPQK-YETRVGdkGTqLSGGQKQRIAIARALIRQP 1125
Cdd:TIGR01257 2018 PQFDAIDDLLTGrEHLYLYARLRGVPAEEIEKVANWS-----IQSLGLSlYADRLA--GT-YSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1126 RVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQKG 1196
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
982-1141 |
5.92e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 982 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLlerfydpMAGtvlLDGQ---EAkklnvqwlRAQLGI----VSQEPILf 1054
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRI-------MAG---VDKDfngEA--------RPQPGIkvgyLPQEPQL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1055 DCS--IAENIAYGDNSRVVSQDEI---------------VRAAKEANIHPFIET-----LPQKYETRV-------GD-KG 1104
Cdd:TIGR03719 80 DPTktVRENVEEGVAEIKDALDRFneisakyaepdadfdKLAAEQAELQEIIDAadawdLDSQLEIAMdalrcppWDaDV 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 564345546 1105 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1141
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1105-1141 |
6.23e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 6.23e-07
10 20 30
....*....|....*....|....*....|....*..
gi 564345546 1105 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1141
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
983-1149 |
6.37e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLdgqeAKKLnvqwlraQLGIVSQEpilfdcsiaeni 1062
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGI-------KLGYFAQH------------ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1063 aygdnsrvvsQDEIVRAaKEANIHPFIETLPQKYETRV----------GDKGT----QLSGGQKQRIAIARALIRQPRVL 1128
Cdd:PRK10636 384 ----------QLEFLRA-DESPLQHLARLAPQELEQKLrdylggfgfqGDKVTeetrRFSGGEKARLVLALIVWQRPNLL 452
|
170 180
....*....|....*....|.
gi 564345546 1129 LLDEATSALDTESEKVVQEAL 1149
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
53-271 |
6.84e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 52.48 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 53 LGGGVLLAAYIQ-VSFWT-------LAAGRQIRkIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGdKVGM 124
Cdd:cd18543 41 LVLLLLALGVAEaVLSFLrrylagrLSLGVEHD-LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 125 FFQAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNK 204
Cdd:cd18543 119 LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERR 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 205 ELERYQKHLENAKKIGIKKA-ISANISMGIAfLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSIL 271
Cdd:cd18543 199 ELDRFEAAARRLRATRLRAArLRARFWPLLE-ALPELGLAAVLALGGWLVANGSLTLG-TLVAFSAYL 264
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
684-900 |
6.88e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 52.59 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 684 NMFSLVFLGLGVLSFFTFFLQGF---TFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQGAT 760
Cdd:cd18566 39 PTLQVLVIGVVIAILLESLLRLLrsyILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 761 GTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVS 840
Cdd:cd18566 116 TGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 841 LTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18566 196 MAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDL 255
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
991-1177 |
8.06e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 991 VKKGQTLALVGSSGCGKSTVVQLL---------------------ERFydpmAGTVLLDgqEAKKLNVQWLRAQLGI--V 1047
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTELQN--YFKKLYNGEIKVVHKPqyV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1048 SQEPILFDCSIAENIAYGDNSRVVsqDEIVraaKEANIHPFIetlpqkyetrvgDKG-TQLSGGQKQRIAIARALIRQPR 1126
Cdd:PRK13409 170 DLIPKVFKGKVRELLKKVDERGKL--DEVV---ERLGLENIL------------DRDiSELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1127 VLLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVVI 1177
Cdd:PRK13409 233 FYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
966-1189 |
9.87e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 966 VTFNEVVFNYPtraNVPVL-QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLldgQEAKklnvqwlrAQL 1044
Cdd:PLN03073 509 ISFSDASFGYP---GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAK--------VRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 GIVSQEPIlfdcsiaeniaygDNSRVVSQDEIVRAakeaniHPFIETLPQKYETRVGDKGTQ----------LSGGQKQR 1114
Cdd:PLN03073 575 AVFSQHHV-------------DGLDLSSNPLLYMM------RCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSR 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1115 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVIDNGKVKE-HGTHQ 1189
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
324-546 |
1.85e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 324 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIdGQDIRnfnvrclrefIG 403
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 404 VVSQ--EPVLFSTTIAENIRYGrgnvtMDEIKKAVKEAN--AY----DFIMKLPQKfdtLVGdrgaQLSGGQKQRIAIAR 475
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGG-----LDIIKLGKREIPsrAYvgrfNFKGSDQQK---KVG----QLSGGERNRVHLAK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 476 ALVRNPKILLLDEATSALDTESEAEVQAALDKAreGRTTIVIAH-RLSTVRNADVIAGFEDGVIVE--QGSHSE 546
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdRWFLDRIATHILAFEGDSHVEwfEGNFSE 528
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
684-900 |
2.21e-06 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 50.93 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 684 NMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA-TGT 762
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLlSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 763 RLALIAqNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAgiveMKMLAGNAKRdkKEMEAAGKIAT------EAIENIR 836
Cdd:cd18545 118 LINLIP-DLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLV----VFLLRRRARK--AWQRVRKKISNlnaylhESISGIR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 837 TVVSLTQE----RKFESMYVEKLHGpYRNSVRKAHIYG----ITFSISQAFMYFsyagcfrFGSYLIVNGHM 900
Cdd:cd18545 191 VIQSFAREdeneEIFDELNRENRKA-NMRAVRLNALFWplveLISALGTALVYW-------YGGKLVLGGAI 254
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
675-900 |
2.87e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 50.59 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 675 DDTVKQQKCNMFSLVFLGLGVLSFFTF---FLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRlAT 751
Cdd:cd18555 30 DNVIVPGNLNLLNVLGIGILILFLLYGlfsFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE--NRSSGDLLFR-AN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 752 DAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAgnaKRDKKEMEAAGK---IA 828
Cdd:cd18555 107 SNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIK---KLNQEEIVAQTKvqsYL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 829 TEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18555 184 TETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1106-1177 |
3.31e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 3.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1106 QLSGGQKQRIAIARALIRQPRVLLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVI 1177
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
335-542 |
3.58e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 335 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQllQRLYDPTEgtisidgqdirnfnvRCLREFIGVVSQEPVLF-- 412
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGK---------------ARLISFLPKFSRNKLIFid 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 413 --STTIAENIRYgrgnvtmdeikkavkeanaydfiMKLPQKFDTLvgdrgaqlSGGQKQRIAIARALVRNPK--ILLLDE 488
Cdd:cd03238 67 qlQFLIDVGLGY-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 489 ATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQG 542
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
983-1167 |
6.04e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 983 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLdGQEAKklnvqwlraqLGIVSQ--EPILFDCSIAE 1060
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNKTVWE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1061 NIAYGdnsrvvsQDEIVRAAKEANihpfietlPQKYETRVGDKGT-------QLSGGQKQRIAIARALIRQPRVLLLDEA 1133
Cdd:TIGR03719 406 EISGG-------LDIIKLGKREIP--------SRAYVGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564345546 1134 TSALDTESEKVVQEALDKAreGRTCIVIAH------RLST 1167
Cdd:TIGR03719 471 TNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
51-261 |
6.67e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 49.41 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 51 SGLGGGVLLAAYIQVSFWTLAAGRQ----IRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFF 126
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTgerlLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 127 QAIATFFAGFIVGFIRGWKLTLVIMAISPILGLSTAVW---------------AKILSTFSdkelaayakagavaeEALG 191
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFrrrssrayrrareriAAVNADLQ---------------ETLA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564345546 192 AIRTVIAFGGQNKELERYQKHLENAKKIGIKkaisANISMGIAF----LLIYASYALAFWYGSTLVISKEYTIG 261
Cdd:cd18546 187 GIRVVQAFRRERRNAERFAELSDDYRDARLR----AQRLVAIYFpgveLLGNLATAAVLLVGAWRVAAGTLTVG 256
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
342-518 |
7.83e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN-----------VRCLREFIGVVSQEPV 410
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 411 LFSTTIAeNIRYGRGNVTMDEIKKAVKEANAYDFIM--KLPQKfDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDE 488
Cdd:PRK10982 344 GFNSLIS-NIRNYKNKVGLLDNSRMKSDTQWVIDSMrvKTPGH-RTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190
....*....|....*....|....*....|.
gi 564345546 489 ATSALDTESEAEV-QAALDKAREGRTTIVIA 518
Cdd:PRK10982 418 PTRGIDVGAKFEIyQLIAELAKKDKGIIIIS 448
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
57-275 |
9.27e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 49.10 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 57 VLLAAYIQVSFWTLAAG--RQI------RKIR----QKFFHAILRQEMGWFDikgttelnTRLTDDI-SKISEGigDKVG 123
Cdd:cd18568 43 LILIGLLIVGIFQILLSavRQYlldyfaNRIDlsllSDFYKHLLSLPLSFFA--------SRKVGDIiTRFQEN--QKIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 124 MFF--QAIATF------FAGFIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRT 195
Cdd:cd18568 113 RFLtrSALTTIldllmvFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIAT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 196 VIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIG 273
Cdd:cd18568 193 IKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQlvAFNMLFGSVIN 272
|
..
gi 564345546 274 AF 275
Cdd:cd18568 273 PL 274
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
979-1181 |
1.14e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.32 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 979 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ-------------LLERFYDPMagTVLLDgqeakklnvqwlraQLG 1045
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeglyasgkarlisFLPKFSRNK--LIFID--------------QLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1046 IVsqepilfdcsIAENIAYgdnsrvvsqdeivraakeanihpfiETLPQKYETrvgdkgtqLSGGQKQRIAIARALIRQP 1125
Cdd:cd03238 70 FL----------IDVGLGY-------------------------LTLGQKLST--------LSGGELQRVKLASELFSEP 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 1126 R--VLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIvvIDNGK 1181
Cdd:cd03238 107 PgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWI--IDFGP 163
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1067-1181 |
1.17e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1067 NSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGD---KGtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESek 1143
Cdd:TIGR00956 169 QNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT-- 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 564345546 1144 vvqeALDKAREGRTCIVIAHRLSTI------QNA----DLIVVIDNGK 1181
Cdd:TIGR00956 245 ----ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
976-1138 |
1.24e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 47.64 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 976 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPmAGTVLLDGQEAKKLNVQWLRaqlgivsqep 1051
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKYPG---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1052 ilfdcsiaeNIAYgdnsrvVSQDEIvraakeaniHPFIETLPQKYETRVGDKGTQ----LSGGQKQRIAIARALIRQPRV 1127
Cdd:cd03233 84 ---------EIIY------VSEEDV---------HFPTLTVRETLDFALRCKGNEfvrgISGGERKRVSIAEALVSRASV 139
|
170
....*....|.
gi 564345546 1128 LLLDEATSALD 1138
Cdd:cd03233 140 LCWDNSTRGLD 150
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
342-580 |
1.24e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.27 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnVRCLREFIGVVSQepvlfsTTIAENIR 421
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------VSVIAISAGLSGQ------LTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 422 YGR--GNVTMDEIKKAVKEANAY----DFIMKLPQKFdtlvgdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDt 495
Cdd:PRK13546 108 FKMlcMGFKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 496 esEAEVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKegiYFRLVNMQTSGSQILSE 570
Cdd:PRK13546 176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAFLNDFKKKSKAEQK 250
|
250
....*....|
gi 564345546 571 EFEVELSDEK 580
Cdd:PRK13546 251 EFRNKLDESR 260
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1101-1196 |
1.36e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1101 GDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVID 1178
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|....*...
gi 564345546 1179 NGKVKEHGTHQQLLAQKG 1196
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
57-275 |
1.70e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 48.24 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 57 VLLAAYIQVSFWtlaagrqiRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISE----GIGDkvgmFFQAIATF 132
Cdd:cd18540 63 IRLAGKIEMGVS--------YDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEiiswGLVD----LVWGITYM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 133 FAGFIVGFIRGWKLTLVIMAISPILGLsTAVW----------------AKILSTFSdkelaayakagavaeEALGAIRTV 196
Cdd:cd18540 131 IGILIVMLILNWKLALIVLAVVPVLAV-VSIYfqkkilkayrkvrkinSRITGAFN---------------EGITGAKTT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 197 IAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGAF 275
Cdd:cd18540 195 KTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIG-TLVAFISYATQFF 272
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
136-276 |
2.05e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 47.88 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 136 FIVGFIRGWKLTLVIMAISPILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLEN 215
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 216 AKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAFS 276
Cdd:cd18588 213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIG--QLIAFNMLAGQVS 271
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
342-501 |
2.42e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 342 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREFIGVVSQEP-----VL---- 411
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdglVLgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 412 ---FSTTIAENIRYGRGNVTMDEIKKAVKeanayDFIM----KLPQKfDTLVGDrgaqLSGGQKQRIAIARALVRNPKIL 484
Cdd:PRK10762 348 kenMSLTALRYFSRAGGSLKHADEQQAVS-----DFIRlfniKTPSM-EQAIGL----LSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|....*..
gi 564345546 485 LLDEATSALDTESEAEV 501
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEI 434
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
977-1196 |
2.53e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGtvlldgqeAKKL---NVQWL---------RAQL 1044
Cdd:NF033858 14 TVA----LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AG--------ARKIqqgRVEVLggdmadarhRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1045 GivsqeP-ILF-----------DCSIAENIAY-GdnsRVVSQDeivRAAKEANI---------HPFIETLPQKyetrvgd 1102
Cdd:NF033858 75 C-----PrIAYmpqglgknlypTLSVFENLDFfG---RLFGQD---AAERRRRIdellratglAPFADRPAGK------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1103 kgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKvvQ-----EALDKAREGRTCIViahrlST--IQNA---D 1172
Cdd:NF033858 137 ----LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLV-----ATayMEEAerfD 205
|
250 260
....*....|....*....|....
gi 564345546 1173 LIVVIDNGKVKEHGTHQQLLAQKG 1196
Cdd:NF033858 206 WLVAMDAGRVLATGTPAELLARTG 229
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
684-906 |
2.62e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 47.59 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 684 NMFSLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQG-ATGT 762
Cdd:cd18782 42 YVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPVGELSTRIS-ELDTIRGfLTGT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 763 RLALIAqNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVV 839
Cdd:cd18782 119 ALTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPIL---RRQIRRRAEASAKTQSylvESLTGIQTVK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 840 SLTQERKFESMYvEKLHGPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 906
Cdd:cd18782 195 AQNAELKARWRW-QNRYARSLGEGFKLTVLGTTSGsLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLI 261
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1099-1180 |
2.64e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1099 RVGDKGTQLSGGQKQRIAIARALIRQP--RVL-LLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1171
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
....*....
gi 564345546 1172 DLIvvIDNG 1180
Cdd:PRK00349 900 DWI--IDLG 906
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
778-900 |
3.65e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 47.11 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 778 IIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagNAKRDKKEMEAAGKIA--TEAIENIRTVVSLTQERKFESMYVEKL 855
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPIL--RRRLEEKFQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEELL 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 564345546 856 HGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18588 211 ARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGEL 255
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
969-1172 |
3.70e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 969 NEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE----RFYdpmAGTVLLDGQEAKKLNVQW-LRAQ 1043
Cdd:PRK10938 264 NNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGY---SNDLTLFGRRRGSGETIWdIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1044 LGIVS-------------QEPIL---FDcSIAENIAYGDNSRVVSQDEIVR---AAKEANiHPFietlpqkyetrvgdkg 1104
Cdd:PRK10938 338 IGYVSsslhldyrvstsvRNVILsgfFD-SIGIYQAVSDRQQKLAQQWLDIlgiDKRTAD-APF---------------- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1105 TQLSGGQkQRIA-IARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRT--------------CivIAHRLSTI 1168
Cdd:PRK10938 400 HSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLEFV 476
|
....
gi 564345546 1169 QNAD 1172
Cdd:PRK10938 477 PDGD 480
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1001-1174 |
3.82e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1001 GSSGCGKSTVVQLLERFYDPMAGTVL---LDGQEAKKLNVQWLRAQLGIVSqepilfDCSIAENIAYGdnSRVVSQDEIV 1077
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYyknCNINNIAKPYCTYIGHNLGLKL------EMTVFENLKFW--SEIYNSAETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1078 RAAkeanIHPFietlpqKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD-KAREGR 1156
Cdd:PRK13541 105 YAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGG 174
|
170
....*....|....*...
gi 564345546 1157 TCIVIAHRLSTIQNADLI 1174
Cdd:PRK13541 175 IVLLSSHLESSIKSAQIL 192
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
46-163 |
3.83e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 47.11 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 46 YAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDikgTTE----LNtRLTDDISKISEGIGDK 121
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFD---TTPsgriLN-RFSKDIGLIDEELPLA 116
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 564345546 122 VGMFFQAIATFFAGFIvgfirgwkltlVIMAISPILGLSTAV 163
Cdd:cd18580 117 LLDFLQSLFSVLGSLI-----------VIAIVSPYFLIVLPP 147
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
337-542 |
4.21e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 337 ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVqllqrlYDptegTISIDGQ-----DIRNFnvrcLREFIGVVSQEPVL 411
Cdd:cd03270 6 AREHNLKNVDVDIPRNKLVVITGVSGSGKSSLA------FD----TIYAEGQrryveSLSAY----ARQFLGQMDKPDVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 412 F----STTIAENIRYGRGNV-----TMDEIkkavkeanaYDFI------MKLPQKFDTLVG--------DRGAQ-LSGGQ 467
Cdd:cd03270 72 SieglSPAIAIDQKTTSRNPrstvgTVTEI---------YDYLrllfarVGIRERLGFLVDvglgyltlSRSAPtLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 468 KQRIAIARALVRNPK--ILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVI------AGFEDGVI 538
Cdd:cd03270 143 AQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVidigpgAGVHGGEI 222
|
....
gi 564345546 539 VEQG 542
Cdd:cd03270 223 VAQG 226
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
359-530 |
4.52e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 359 GNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnvrCLREFIGVVSQEPVL-FSTTIAENIRYgrgnvtMDEIKKAVK 437
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN----IAKPYCTYIGHNLGLkLEMTVFENLKF------WSEIYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 438 EANAYDFIMKLpqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD-KAREGRTTIV 516
Cdd:PRK13541 103 TLYAAIHYFKL----HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLL 178
|
170
....*....|....
gi 564345546 517 IAHRLSTVRNADVI 530
Cdd:PRK13541 179 SSHLESSIKSAQIL 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
977-1184 |
4.60e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 977 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPMA-GTVLLDGQEAK-KLNVQWLRAQLGIVSQ--- 1049
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISpRSPLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1050 EPILF-DCSIAENIAygdnsrvvsqdeIVRAAKEANIHPFIETLPQKYETRVGDKG---------------TQLSGGQKQ 1113
Cdd:PRK09700 349 DNGFFpNFSIAQNMA------------ISRSLKDGGYKGAMGLFHEVDEQRTAENQrellalkchsvnqniTELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564345546 1114 RIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIDNGKVKE 1184
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
346-547 |
5.60e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 346 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG---------VVSQEPVLFSTTI 416
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSdewqrnntdMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 417 AENIRygrgnvtmDEIKKAVKeanaydfIMKLPQKF--DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 494
Cdd:PRK10938 103 AEIIQ--------DEVKDPAR-------CEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 495 TESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 547
Cdd:PRK10938 168 VASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEI 222
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1094-1163 |
7.14e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 7.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1094 QKYETRvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARegRTCIVIAH 1163
Cdd:PLN03073 338 QVKATK------TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
462-553 |
8.04e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 462 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFEDGVIV 539
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
|
90
....*....|....
gi 564345546 540 EQGSHSELIKKEGI 553
Cdd:PRK09700 489 QILTNRDDMSEEEI 502
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1106-1193 |
8.56e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.33 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1106 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIDNGKV 1182
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 564345546 1183 KEHGTHQQLLA 1193
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
305-528 |
1.01e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 305 PKIDSFSERGHKPDSIKgNLEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ----------- 373
Cdd:PRK10938 243 PEPDEPSARHALPANEP-RIVLNNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndl 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 374 RLYDPTEGTisidGQDIRNfnvrcLREFIGVVSQEPVL---FSTTIAENIRYGrgnvTMDEIK--KAVKEANaydfiMKL 448
Cdd:PRK10938 319 TLFGRRRGS----GETIWD-----IKKHIGYVSSSLHLdyrVSTSVRNVILSG----FFDSIGiyQAVSDRQ-----QKL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 449 PQKFDTLVG--DRGAQ-----LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV--- 516
Cdd:PRK10938 381 AQQWLDILGidKRTADapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvs 459
|
250 260
....*....|....*....|.
gi 564345546 517 ---------IAHRLSTVRNAD 528
Cdd:PRK10938 460 hhaedapacITHRLEFVPDGD 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
462-519 |
1.23e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 462 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARegRTTIVIAH 519
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1107-1178 |
1.45e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.10 E-value: 1.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1107 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVID 1178
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
991-1136 |
1.48e-04 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 45.28 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 991 VKKGQTLaLVGSSGCGKSTVVQLLER-FYDPMAGtvllDGQEakklnvqwlraqlGIVSqepilfdcsiaeniaygDNSR 1069
Cdd:pfam09818 77 IPKGITL-IVGGGFHGKSTLLEALERgVYNHIPG----DGRE-------------FVVT-----------------DPDA 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1070 VVSQDEIVRAAKEANIHPFIETLPQkyetrvGDKGTQL-----SGGQKQRIAIARALIRQPRVLLLDEATSA 1136
Cdd:pfam09818 122 VKIRAEDGRSVHGVDISPFINNLPP------GKDTTDFstedaSGSTSQAANIMEALEAGASLLLIDEDTSA 187
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
684-855 |
1.49e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 45.21 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 684 NMFSLVFLGLGVL-SFFTFFlQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGT 762
Cdd:cd18605 42 NFFLTVYGFLAGLnSLFTLL-RAFLFAYGGLRAARRLHNKLLSSILFAKMSFFD--KTPVGRILNRFSSDVYTIDDSLPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 763 RL-ALIAQNTANLGTGIIISFIYGWqltlLLLSVVPFIAVAGIVEMKMLAGNakRDKKEMEAA--GKIAT---EAIENIR 836
Cdd:cd18605 119 ILnILLAQLFGLLGYLVVICYQLPW----LLLLLLPLAFIYYRIQRYYRATS--RELKRLNSVnlSPLYThfsETLKGLV 192
|
170
....*....|....*....
gi 564345546 837 TVVSLTQERKFESMYVEKL 855
Cdd:cd18605 193 TIRAFRKQERFLKEYLEKL 211
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1106-1175 |
1.82e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 1.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564345546 1106 QLSGGQKQRIAIARALI---RQPRVL-LLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1175
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
462-533 |
1.89e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 462 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTEseaEVQAALDKARE----GRTTIVIAHRLSTVRNADVIAGF 533
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR---DGQALAEAILEhlvkGAQVIVITHLPELAELADKLIHI 153
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
457-540 |
1.97e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 457 GDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIV----------IAHRLSTVR 525
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLttqymeeaeqLAHELTVID 218
|
90
....*....|....*
gi 564345546 526 NADVIAgfeDGVIVE 540
Cdd:NF000106 219 RGRVIA---DGKVDE 230
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
335-550 |
2.13e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 335 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTV---------QLLQRLYDPT----EGTI----------------SI 385
Cdd:PRK00635 604 SKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLIndtlvpaveEFIEQGFCSNlsiqWGAIsrlvhitrdlpgrsqrSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 386 DGQDIRNFN---------VRCLR------EF-----IGVVSQEPVLFSTTIAEN--------------------IRYGRG 425
Cdd:PRK00635 684 PLTYIKAFDdlrelfaeqPRSKRlgltksHFsfntpLGACAECQGLGSITTTDNrtsipcpsclgkrflpqvleVRYKGK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 426 NVTmdeikkAVKEANAYD---FIMKLP---QKFDTL---------VGDRGAQLSGGQKQRIAIARAL---VRNPKILLLD 487
Cdd:PRK00635 764 NIA------DILEMTAYEaekFFLDEPsihEKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLD 837
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 488 EATSALDTES-EAEVQAALDKAREGRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQGSHSELIKK 550
Cdd:PRK00635 838 EPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVlelgpeGGNLGGYLLASCSPEELIHL 907
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
334-517 |
3.02e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 334 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLLQRLYDP-TEGTISIDGQDIRNFNVRCL-----------RE 400
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 401 FIGVVSQEPVLFSTTIAENIRYGRGNVtMDEIKKaVKEANAY--DFIMKLPQKFDTLVgdrgaQLSGGQKQRIAIARALV 478
Cdd:NF040905 348 GYGLNLIDDIKRNITLANLGKVSRRGV-IDENEE-IKVAEEYrkKMNIKTPSVFQKVG-----NLSGGNQQKVVLSKWLF 420
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564345546 479 RNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVI 517
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVI 460
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
345-553 |
4.26e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.27 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 345 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREfiGVV-----SQEPVLF------ 412
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLAR--GLVylpedRQSSGLYldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 413 ----STTIAEN---IRYGRGNVTMDEIKKAvkeanaydfimkLPQKFDTLvgDRGAQ-LSGGQKQRIAIARALVRNPKIL 484
Cdd:PRK15439 360 wnvcALTHNRRgfwIKPARENAVLERYRRA------------LNIKFNHA--EQAARtLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564345546 485 LLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLstvrnaDVIAGFEDGVIV-EQGSHSELIKKEGI 553
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIyQLIRSIAAQNVAVLFISSDL------EEIEQMADRVLVmHQGEISGALTGAAI 490
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
462-548 |
6.71e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 462 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVI 538
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 564345546 539 VEQGSHSELI 548
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
687-900 |
8.26e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 42.83 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 687 SLVFLGLGVLSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFddHKNSTGALSTRL-ATDAAQ---VQGATGT 762
Cdd:cd18567 45 AIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYF--EKRHLGDIVSRFgSLDEIQqtlTTGFVEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 763 RL-ALIAqntanLGTGIIIsFIYGWQLTLLllsVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSL 841
Cdd:cd18567 123 LLdGLMA-----ILTLVMM-FLYSPKLALI---VLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 842 -------TQERKFESMYVEKLhgpyrNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18567 194 klfgreaEREARWLNLLVDAI-----NADIRLQRLQILFSaANGLLFGLENILVIYLGALLVLDGEF 255
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1105-1178 |
9.69e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 9.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564345546 1105 TQLSGGQKQRIAIARALIR--QPRVL-LLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIvvID 1178
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWI--ID 900
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
434-530 |
1.25e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 434 KAVKEANAYDFIMKLPQ-KFDTLVGDRGAQLSGGQKQ------RIAIARALVRNPKILLLDEATSALDTESEAEVQAALD 506
Cdd:cd03240 86 TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEII 165
|
90 100
....*....|....*....|....*..
gi 564345546 507 KAREG---RTTIVIAHRLSTVRNADVI 530
Cdd:cd03240 166 EERKSqknFQLIVITHDEELVDAADHI 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1094-1150 |
1.31e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1094 QKyetRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD 1150
Cdd:PRK11819 440 QK---KVG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
778-900 |
1.65e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 41.78 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 778 IIISFIYGWQLTLLLLSVVP-FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIaTEAIENIRTVVSLTQERKFESmYVEKLH 856
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPlYVLLTLLSSPKLKRNSREIFQANAEQQSFL-VEALTGIATIKALAAERPIRW-RWENKF 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 564345546 857 GPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHM 900
Cdd:cd18568 211 AKALNTRFRGQKLSIVLQlISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
47-213 |
1.84e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 41.68 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 47 AYY---YSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDikgTT---ELNTRLTDDISKISEGIGD 120
Cdd:cd18604 43 LYYlgiYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLD---TTpvgRILNRFSKDIETIDSELAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 121 KVGMFFQAIATFFAGFIVGFIRGWKL---TLVIMAISPILG---LSTAVWAK---------ILSTFSdkelaayakagav 185
Cdd:cd18604 120 SLSSLLESTLSLLVILIAIVVVSPAFllpAVVLAALYVYIGrlyLRASRELKrlesvarspILSHFG------------- 186
|
170 180
....*....|....*....|....*...
gi 564345546 186 aeEALGAIRTVIAFGGQnkelERYQKHL 213
Cdd:cd18604 187 --ETLAGLVTIRAFGAE----ERFIEEM 208
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1100-1186 |
3.85e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1100 VGDKGTQLSGGQKQRIAIARALI---RQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1175
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
90
....*....|.
gi 564345546 1176 VIDNGKVKEHG 1186
Cdd:PRK00635 1773 EMGPGSGKTGG 1783
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
984-1014 |
4.00e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 4.00e-03
10 20 30
....*....|....*....|....*....|..
gi 564345546 984 LQGLSLEVKKGQTLALVGSSGCGKSTVV-QLL 1014
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
441-554 |
4.42e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 441 AYDF---IMKLPQKFDTLV---------GDRGAQLSGGQKQRIAIARALVRNP--KIL-LLDEATSALDTESEA---EV- 501
Cdd:PRK00349 797 ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRkllEVl 876
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 564345546 502 QAALDKareGRTTIVIAHRLSTVRNADVIA--GFEDGV----IVEQGSHSELIKKEGIY 554
Cdd:PRK00349 877 HRLVDK---GNTVVVIEHNLDVIKTADWIIdlGPEGGDgggeIVATGTPEEVAKVEASY 932
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1107-1175 |
7.82e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.16 E-value: 7.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564345546 1107 LSGGQKQRIAIARALIRQPRVLL--LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1175
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
331-497 |
7.89e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.60 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 331 FSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPT---EGTISIDGQDIRNFNVRCLREFIgvvSQ 407
Cdd:PLN03140 170 INLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSAYI---SQ 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 408 EPV-LFSTTIAENIRY-------GRGNVTMDEIKKAVKEANAY-----DFIMK---------------------LPQKFD 453
Cdd:PLN03140 247 NDVhVGVMTVKETLDFsarcqgvGTRYDLLSELARREKDAGIFpeaevDLFMKatamegvksslitdytlkilgLDICKD 326
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564345546 454 TLVGD---RGaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 497
Cdd:PLN03140 327 TIVGDemiRG--ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSST 371
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1105-1175 |
8.10e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 8.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564345546 1105 TQLSGGQKQRIAIarALI-----RQPRVL-LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIV 1175
Cdd:pfam02463 1076 DLLSGGEKTLVAL--ALIfaiqkYKPAPFyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
976-1161 |
8.27e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 976 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-MAGTVLLDGQEAKKLNVQWL-----------RA 1042
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564345546 1043 QLGIVSQEPILFDCSIA--ENIAygdNSRVVSQDEIVRAAKEanihpFIETLPQKYETrVGDKGTQLSGGQKQRIAIARA 1120
Cdd:NF040905 348 GYGLNLIDDIKRNITLAnlGKVS---RRGVIDENEEIKVAEE-----YRKKMNIKTPS-VFQKVGNLSGGNQQKVVLSKW 418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564345546 1121 LIRQPRVLLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1161
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
|
|
| |
