|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
42-632 |
3.61e-176 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 533.20 E-value: 3.61e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 42 LFRYSdWQDKLFMLLGTAMAIAHGSGLPLMMIVFGEMTDKFVdNAGNFSLpvnfslsmlnpgrileeeMTRYAYYYSGLG 121
Cdd:COG1132 12 LLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDLSA------------------LLLLLLLLLGLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 122 GGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFA 201
Cdd:COG1132 72 LLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 202 GFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLE 281
Cdd:COG1132 152 ALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 282 NAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFPNARGAA 361
Cdd:COG1132 232 ELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 362 YVIFDIIDNNPKIDSfSERGHKPDSIKGNLEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQR 441
Cdd:COG1132 312 ERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPG--DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 442 LYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDT 521
Cdd:COG1132 389 FYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 522 LVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFE 601
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLD 548
|
570 580 590
....*....|....*....|....*....|.
gi 6981354 602 DGVIVEQGSHSELIKKEGIYFRLVNMQTSGS 632
Cdd:COG1132 549 DGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
29-1271 |
2.76e-172 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 550.40 E-value: 2.76e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 29 EKKKKVNLIGPLTLFRYSDWQDKLFML------------LGTAMAIAHGSG--LPLMMIVFGEMTDKFvdNAGNFSLPVN 94
Cdd:PTZ00265 23 EVEKELNKKGTFELYKKIKTQKIPFFLpfkclpashrklLGVSFVCATISGgtLPFFVSVFGVIMKNM--NLGENVNDII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 95 FSLSMLnpgrileeemtryayyysGLGGGVLlaAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRL 174
Cdd:PTZ00265 101 FSLVLI------------------GIFQFIL--SFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 175 TDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAE 254
Cdd:PTZ00265 161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 255 EALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVIS--------KEYT 326
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 327 IGNAMTVFFSILIGAFSVGQAAPCIDAFPNARGAAYVIFDIIDNNPKIDSfSERGHKPDSIKgNLEFSDVHFSYPSRANI 406
Cdd:PTZ00265 321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISI-DGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAE 485
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 486 NIRYG----------------RGNVTMD-----------------------------------------EIKKAVKEANA 508
Cdd:PTZ00265 479 NIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLI 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 509 YDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAH 586
Cdd:PTZ00265 559 HDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAH 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 587 RLSTVRNADVI-----------------------------------------------AGFEDGVIVEQGSHSELIK-KE 618
Cdd:PTZ00265 639 RLSTIRYANTIfvlsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKnKN 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 619 GIYFRLVNMQTSGSQILSEEFEVELSDEKAAG-GVAPNGWKARIFRNSTKKSLKSSRAHQNRLDVETNELDANV-PPVSF 696
Cdd:PTZ00265 719 GIYYTMINNQKVSSKKSSNNDNDKDSDMKSSAyKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENASENNAgGKLPF 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 697 LKVLRLNKTEWPY---------------FVVGTLCAIANGALQPAFSIILSEMIA-IFgpgDDTVKQQKCNMFSLVFLGL 760
Cdd:PTZ00265 799 LRNLFKRKPKAPNnlrivyreifsykkdVTIIALSILVAGGLYPVFALLYAKYVStLF---DFANLEANSNKYSLYILVI 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 761 GVHSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTAN 840
Cdd:PTZ00265 876 AIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVL 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 841 LGTGIIISFiYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKI----------------ATEAIENIRT 904
Cdd:PTZ00265 956 FLVSMVMSF-YFCPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNT 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 905 VVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI-LVFSAIVLGA 983
Cdd:PTZ00265 1035 VIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMkSLFTFLFTGS 1114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 984 VAlGHASSFAPDYAKAKLSAAYLFSLFERQPLIDSYSREGMW---PDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKK 1060
Cdd:PTZ00265 1115 YA-GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDS 1193
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1061 GQTLALVGSSGCGKSTVVQLLERFYD------------------------------------------------------ 1086
Cdd:PTZ00265 1194 KKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvf 1273
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1087 PMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETR 1166
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTN 1351
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1167 VGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIV 1242
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIV 1429
|
1450 1460 1470
....*....|....*....|....*....|....*
gi 6981354 1243 VIDNGK-----VKEHGTHQQLL-AQKGIYFSMVNI 1271
Cdd:PTZ00265 1430 VFNNPDrtgsfVQAHGTHEELLsVQDGVYKKYVKL 1464
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
695-1276 |
1.00e-165 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 505.85 E-value: 1.00e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 695 SFLKVLRLNKTEWPYFVVGTLCAIANGALQPAFSIILSEMI-AIFGPGDdtvkQQKCNMFSLVFLGLGVHSFFTFFLQGF 773
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGD----LSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 774 TFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGW 853
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 854 QLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKA 933
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 934 HIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQ 1013
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1014 PLIDSYSREGMwPDKFEGSVTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVL 1093
Cdd:COG1132 322 PEIPDPPGAVP-LPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1094 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQ 1173
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1174 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHG 1253
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|...
gi 6981354 1254 THQQLLAQKGIYFSMVNIQAGTQ 1276
Cdd:COG1132 557 THEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
392-628 |
2.64e-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: 454.69 E-value: 2.64e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 392 EFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 471
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 472 VSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 552 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 628
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1033-1272 |
3.71e-149 |
|
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: 448.91 E-value: 3.71e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1112
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFDCSIAKNIAYGDNSRvvSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQP 1192
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1193 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQ 1272
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
120-629 |
2.93e-141 |
|
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: 446.20 E-value: 2.93e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 120 LGGGVLLAAYIQV------SFWTLAAGRQI-RKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdISKISEGIGDKVGMF 192
Cdd:COG2274 198 LAIGLLLALLFEGllrllrSYLLLRLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 193 FQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 272
Cdd:COG2274 277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 273 LERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF--SVGQAAPC 350
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLG--QLIAFNILSGRFlaPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 351 IDAFPNARGAAYVIFDIIDNNPKIDSFSERGHKPDsIKGNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGC 430
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 431 GKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYD 510
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 511 FIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLST 590
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
490 500 510
....*....|....*....|....*....|....*....
gi 6981354 591 VRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQT 629
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; ... |
700-1016 |
1.79e-138 |
|
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: 424.17 E-value: 1.79e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 700 LRLNKTEWPYFVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKQQKCNMFSLVFLGLGVHSFFTFFLQGFTFGKAG 779
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 780 EILTTRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLL 859
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 860 LSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGIT 939
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 940 FSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLI 1016
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
54-364 |
2.46e-132 |
|
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: 407.82 E-value: 2.46e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 54 MLLGTAMAIAHGSGLPLMMIVFGEMTDKFVdNAGNFSLPVNFS--LSMLNPGRILEEEMTRYAYYYSGLGGGVLLAAYIQ 131
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFT-NGGMTNITGNSSglNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 132 VSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGW 211
Cdd:cd18558 80 GSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 212 KLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA 291
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 292 ISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFPNARGAAYVI 364
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-625 |
2.01e-130 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 417.59 E-value: 2.01e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 29 EKKKKVNLIgpLTLFRYSDWQDKLFMLLGTAMAIahgSGLPLMMIVF--GEMTDKFVDNAGNFSLPVN-FSLSMLNPGRI 105
Cdd:TIGR00958 141 GQSETADLL--FRLLGLSGRDWPWLISAFVFLTL---SSLGEMFIPFytGRVIDTLGGDKGPPALASAiFFMCLLSIASS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 106 LEEemtryayyysGLGGGVLLAAYiqvsfwtlaaGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGI 185
Cdd:TIGR00958 216 VSA----------GLRGGSFNYTM----------ARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 186 GDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIA 265
Cdd:TIGR00958 276 SLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 266 FGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVG 345
Cdd:TIGR00958 356 FAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGN----LVSFLLYQEQLG 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 346 QAAPCIDAFPN----ARGAAYVIFDIIDNNPKIDSfsERGHKPDSIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQT 421
Cdd:TIGR00958 432 EAVRVLSYVYSgmmqAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEV 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 422 VALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKK 501
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMA 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 502 AVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAalDKAREGRTT 581
Cdd:TIGR00958 590 AAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTV 667
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 6981354 582 IVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLV 625
Cdd:TIGR00958 668 LLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
692-1273 |
5.69e-128 |
|
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: 410.76 E-value: 5.69e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 692 PPVSFLKVLRLNKTEWPYFVVGTLCAIANGALQPAFSIILseMIAIfgpgdDTVKQQKcNMFSLVFLGLGVHSFFTF--- 768
Cdd:COG2274 140 KPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFT--QVVI-----DRVLPNQ-DLSTLWVLAIGLLLALLFegl 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 769 --FLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLaTDAAQVQGATGTRLALIAQNTANLGTGII 846
Cdd:COG2274 212 lrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 847 ISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAgnaKRDKKEMEAAGKIAT---EAIENIRTVVSLTQERKFESMYVEKLH 923
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLR---RLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWENLLA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 924 GPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFkDVILVFSAIVLGAVA-LGHASSFAPDYAKAKLS 1002
Cdd:COG2274 366 KYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQLIGLLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1003 AAYLFSLFERQPLIDSySREGMWPDKFEGSVTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE 1082
Cdd:COG2274 445 LERLDDILDLPPEREE-GRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1083 RFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQK 1162
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLAGLHDFIEALPMG 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1163 YETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIV 1242
Cdd:COG2274 601 YDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRII 680
|
570 580 590
....*....|....*....|....*....|.
gi 6981354 1243 VIDNGKVKEHGTHQQLLAQKGIYFSMVNIQA 1273
Cdd:COG2274 681 VLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
116-628 |
1.10e-123 |
|
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: 394.84 E-value: 1.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 116 YYSGLGGGVL---LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMF 192
Cdd:TIGR02204 60 YFAFLLVVALvlaLGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 193 FQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 272
Cdd:TIGR02204 140 LRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 273 LERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIGAfSVGQAAPCI 351
Cdd:TIGR02204 220 RSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTlGQFVFYAVMVAG-SIGTLSEVW 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 352 DAFPNARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCG 431
Cdd:TIGR02204 299 GELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 432 KSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDF 511
Cdd:TIGR02204 379 KSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 512 IMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV 591
Cdd:TIGR02204 459 ISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538
|
490 500 510
....*....|....*....|....*....|....*..
gi 6981354 592 RNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 628
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
683-1269 |
1.31e-119 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 388.31 E-value: 1.31e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 683 ETNELDANVPPVSFlKVLRLNKTEWPYFVVGTL---CAIANGALQPAFSiilSEMIAIFGpGDDTVKQQKCNMFSLVFLG 759
Cdd:TIGR00958 137 EAEQGQSETADLLF-RLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYT---GRVIDTLG-GDKGPPALASAIFFMCLLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 760 LGvhSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTA 839
Cdd:TIGR00958 212 IA--SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENK--TGELTSRLSSDTQTMSRSLSLNVNVLLRNLV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 840 NLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYV 919
Cdd:TIGR00958 288 MLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 920 EKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRfKDVILVFsaiVLGAVALGHA----SSFAPD 995
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVS-SGNLVSF---LLYQEQLGEAvrvlSYVYSG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 996 YAKAKLSAAYLFSLFERQPLIdsySREGMW-PDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPNI---PLTGTLaPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGK 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1075 STVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHP 1154
Cdd:TIGR00958 521 STVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAAKAANAHD 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1155 FIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEalDKAREGRTCIVIAHRLST 1234
Cdd:TIGR00958 599 FIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLST 676
|
570 580 590
....*....|....*....|....*....|....*
gi 6981354 1235 IQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMV 1269
Cdd:TIGR00958 677 VERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
54-364 |
1.78e-116 |
|
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: 364.87 E-value: 1.78e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 54 MLLGTAMAIAHGSGLPLMMIVFGEMTDKFVDNAGNFSLPVNFslsmlnpgrilEEEMTRYAYYYSGLGGGVLLAAYIQVS 133
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEF-----------LDDVNKYALYFVYLGIGSFVLSYIQTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 134 FWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKL 213
Cdd:cd18577 70 CWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 214 TLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAIS 293
Cdd:cd18577 150 TLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 294 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFPNARGAAYVI 364
Cdd:cd18577 230 SGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
752-1272 |
1.54e-113 |
|
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: 367.49 E-value: 1.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 752 MFSLVFLGLGVHSFFTFFLqgftFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 831
Cdd:TIGR02204 63 FLLVVALVLALGTAARFYL----VTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSSL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 832 ALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE 911
Cdd:TIGR02204 137 SMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 912 RKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDV-ILVFSAIVLGAvALGHAS 990
Cdd:TIGR02204 217 DAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgQFVFYAVMVAG-SIGTLS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 991 SFAPDYAKAKLSAAYLFSLFERQPLIDSYSREGMWPDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSS 1070
Cdd:TIGR02204 296 EVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1071 GCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGdnsRV-VSQDEIVRAAKE 1149
Cdd:TIGR02204 376 GAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG---RPdATDEEVEAAARA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1150 ANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIA 1229
Cdd:TIGR02204 453 AHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIA 532
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 6981354 1230 HRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQ 1272
Cdd:TIGR02204 533 HRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
391-624 |
3.80e-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: 3.80e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 551 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRL 624
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
126-628 |
4.55e-112 |
|
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: 363.27 E-value: 4.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 126 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 206 GFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNaMTVFFSILIGAFS-VGQAAPCIDAFPNARGAAYVI 364
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFITAMIALIRpLKSLTNVNAPMQRGLAAAESL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 365 FDIIDNNPKIDsfsERGHKPDSIKGNLEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD 444
Cdd:TIGR02203 308 FTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 445 PTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGR-GNVTMDEIKKAVKEANAYDFIMKLPQKFDTLV 523
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPI 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 524 GDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDG 603
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543
|
490 500
....*....|....*....|....*
gi 6981354 604 VIVEQGSHSELIKKEGIYFRLVNMQ 628
Cdd:TIGR02203 544 RIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
262-633 |
1.08e-111 |
|
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: 1.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 262 TVIAFGGQNKELERYQKHLENAKKIGIKKAISAN---------ISMGIAFLLIYASYAlafwygstlVISKEYTIGNamt 332
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAllnfgqaliIALGLTAMMLMAAQG---------VVAGTMTVGD--- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 333 vfFsILIGAFSVGQAAPCidafpNARGAAY-----------VIFDIIDNNPKIDSfserghKPDSI-----KGNLEFSDV 396
Cdd:COG5265 298 --F-VLVNAYLIQLYIPL-----NFLGFVYreirqaladmeRMFDLLDQPPEVAD------APDAPplvvgGGEVRFENV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 397 HFSY-PSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQE 475
Cdd:COG5265 364 SFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 476 PVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:COG5265 441 TVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 556 ATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQTSGSQ 633
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEE 598
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
695-1275 |
1.08e-105 |
|
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: 345.93 E-value: 1.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 695 SFLKVLRLNKTEWPYFVVGTLCAIANGALQPAFSIILSEMI-AIFGPGDDTVKQQKCNMFSLVFLGLGVHSFFTFFLQGF 773
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 774 TFGKageiLTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGW 853
Cdd:TIGR02203 81 VSNK----VVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 854 QLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE----RKFESMYVEKLhgpyRNS 929
Cdd:TIGR02203 155 QLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQayetRRFDAVSNRNR----RLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 930 VRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSL 1009
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1010 FERQPLIDSYSREgmwPDKFEGSVTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA 1089
Cdd:TIGR02203 311 LDSPPEKDTGTRA---IERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1090 GTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSRVVSQdEIVRAAKEANIHPFIETLPQKYETRVGD 1169
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRA-EIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1170 KGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKV 1249
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570 580
....*....|....*....|....*.
gi 6981354 1250 KEHGTHQQLLAQKGIYFSMVNIQAGT 1275
Cdd:TIGR02203 546 VERGTHNELLARNGLYAQLHNMQFRE 571
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
139-628 |
1.23e-105 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 346.24 E-value: 1.23e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 139 AGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDD------------ISKISEGigdkvgmffqaiATFFAGFIVG 206
Cdd:PRK11176 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREG------------ASIIGLFIMM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 207 FIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKI 286
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 287 GIKKAISANISMGIAFLLiyASYALAF--WYGSTLVISKEYTIGnAMTVFFSILIGAFSVGQAAPCIDA-FPNARGAAYV 363
Cdd:PRK11176 241 GMKMVSASSISDPIIQLI--ASLALAFvlYAASFPSVMDTLTAG-TITVVFSSMIALMRPLKSLTNVNAqFQRGMAACQT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 364 IFDIIDNNPKIDsfsERGHKPDSIKGNLEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY 443
Cdd:PRK11176 318 LFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 444 DPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNV-TMDEIKKAVKEANAYDFIMKLPQKFDTL 522
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 523 VGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFED 602
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
490 500
....*....|....*....|....*.
gi 6981354 603 GVIVEQGSHSELIKKEGIYFRLVNMQ 628
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1033-1265 |
3.09e-105 |
|
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: 331.89 E-value: 3.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1112
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFDCSIAKNIAYGDnsRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQP 1192
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1193 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIY 1265
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
391-628 |
3.45e-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: 3.45e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSY-PSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFI 469
Cdd:cd03253 1 IEFENVTFAYdPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPK 549
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 550 ILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 628
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
710-1006 |
8.45e-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: 331.55 E-value: 8.45e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVK-----------------QQKCNMFSLVFLGLGVHSFFTFFLQG 772
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNItgnssglnssagpfeklEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 773 FTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYG 852
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 853 WQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRK 932
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 933 AHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMR-FKDVILVFSAIVLGAVALGHASSFAPdYAKAKLSAAYL 1006
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSiGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1006-1273 |
3.41e-103 |
|
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: 340.26 E-value: 3.41e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1006 LFSLFERQPLIdsYSREGMWPDKF-EGSVTFNEVVFNY-PTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLER 1083
Cdd:COG5265 332 MFDLLDQPPEV--ADAPDAPPLVVgGGEVRFENVSFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1084 FYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKY 1163
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDFIESLPDGY 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1164 ETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVV 1243
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
250 260 270
....*....|....*....|....*....|
gi 6981354 1244 IDNGKVKEHGTHQQLLAQKGIYFSMVNIQA 1273
Cdd:COG5265 565 LEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1033-1272 |
2.27e-100 |
|
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: 318.79 E-value: 2.27e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1112
Cdd:cd03253 1 IEFENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQP 1192
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1193 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQ 1272
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
389-619 |
6.67e-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: 314.55 E-value: 6.67e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 389 GNLEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF 468
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 548
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 549 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEG 619
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
292-628 |
1.47e-96 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 321.53 E-value: 1.47e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 292 ISANISMGIAFLLiyasyalafwyGSTLVISKEYTIGN--AMTVFFSILIG------AF--SVGQAAPCIDAFpnargaa 361
Cdd:PRK13657 248 AASTITMLAILVL-----------GAALVQKGQLRVGEvvAFVGFATLLIGrldqvvAFinQVFMAAPKLEEF------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 362 yviFDIIDNNPKIDsfsERGHKPD--SIKGNLEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL 439
Cdd:PRK13657 310 ---FEVEDAVPDVR---DPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 440 QRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKF 519
Cdd:PRK13657 382 QRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 520 DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAG 599
Cdd:PRK13657 462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541
|
330 340
....*....|....*....|....*....
gi 6981354 600 FEDGVIVEQGSHSELIKKEGIYFRLVNMQ 628
Cdd:PRK13657 542 FDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1031-1263 |
1.53e-95 |
|
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: 305.30 E-value: 1.53e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1031 GSVTFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQ 1110
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1111 LGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIR 1190
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1191 QPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKG 1263
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
356-619 |
3.65e-94 |
|
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: 314.00 E-value: 3.65e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 356 NARGAAYVIFDIIDNNPKIdsfSERGHKPDSIKGN--LEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGKS 433
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPA---APAGTAPLPAAGPpsIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKS 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 434 TTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIM 513
Cdd:COG4988 378 TLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVA 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 514 KLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN 593
Cdd:COG4988 458 ALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ 537
|
250 260
....*....|....*....|....*.
gi 6981354 594 ADVIAGFEDGVIVEQGSHSELIKKEG 619
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
786-1274 |
5.00e-93 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 311.57 E-value: 5.00e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 786 LRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPF 865
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 866 IAVAgiveMKMLAGNAKRDKKEMEAA-GKIATEAIENIR--TVVSLTQERKFESMYVEKLHGPYR-NSVRKAHIYGITFS 941
Cdd:PRK11176 178 VSIA----IRVVSKRFRNISKNMQNTmGQVTTSAEQMLKghKEVLIFGGQEVETKRFDKVSNRMRqQGMKMVSASSISDP 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 942 ISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQPLIDSYSR 1021
Cdd:PRK11176 254 IIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKR 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1022 EgmwPDKFEGSVTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKK 1101
Cdd:PRK11176 334 V---IERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1102 LNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSRVvSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQR 1181
Cdd:PRK11176 410 YTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQY-SREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQR 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1182 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
490
....*....|...
gi 6981354 1262 KGIYFSMVNIQAG 1274
Cdd:PRK11176 569 NGVYAQLHKMQFG 581
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
135-624 |
1.48e-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: 307.08 E-value: 1.48e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 135 WTLaagRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDIskisegigDKVGMFF---------QAIATFFAGFIV 205
Cdd:COG4987 82 ATL---RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlrvllpllvALLVILAAVAFL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 206 GFIrGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKA-GAVAEEALGAIRTVIAFGGQNKELERYQKHLENAK 284
Cdd:COG4987 151 AFF-SPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAAlRARLTDLLQGAAELAAYGALDRALARLDAAEARLA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 285 KIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVFFSILIGAFSVgqAAPCIDAF---PNARGAA 361
Cdd:COG4987 230 AAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALALFEA--LAPLPAAAqhlGRVRAAA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 362 YVIFDIIDNNPKIDSFSERGHKPDSikGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQR 441
Cdd:COG4987 307 RRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 442 LYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDT 521
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDT 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 522 LVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFE 601
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
490 500
....*....|....*....|...
gi 6981354 602 DGVIVEQGSHSELIKKEGIYFRL 624
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1026-1249 |
5.32e-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: 281.67 E-value: 5.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1026 PDKFEGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQ 1105
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1106 WLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIA 1185
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1186 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKV 1249
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
988-1263 |
2.75e-86 |
|
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: 292.05 E-value: 2.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 988 HASsfapdyAKAKLSAAYLFSLFErQPLIDSYSREGMWPDKFEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALV 1067
Cdd:COG4988 299 HAR------ANGIAAAEKIFALLD-APEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1068 GSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDnsRVVSQDEIVRAA 1147
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAAL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1148 KEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV 1227
Cdd:COG4988 448 EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVIL 527
|
250 260 270
....*....|....*....|....*....|....*.
gi 6981354 1228 IAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKG 1263
Cdd:COG4988 528 ITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
198-629 |
2.20e-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: 290.88 E-value: 2.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 198 TFFAgfiVGFIRGWKLT-LVIMAITAILGLSTAVwAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERY 276
Cdd:TIGR01846 268 VFLA---VMFFYSPTLTgVVIGSLVCYALLSVFV-GPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 277 QKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAFS--VGQAAPCIDAF 354
Cdd:TIGR01846 344 DRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQ--LVAFNMLAGRVTqpVLRLAQLWQDF 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 355 PNARGAAYVIFDIIdNNPKIDSFSERGHKPDsIKGNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKST 434
Cdd:TIGR01846 422 QQTGIALERLGDIL-NSPTEPRSAGLAALPE-LRGAITFENIRFRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKST 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 435 TVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMK 514
Cdd:TIGR01846 499 LTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 515 LPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNA 594
Cdd:TIGR01846 579 LPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRAC 658
|
410 420 430
....*....|....*....|....*....|....*
gi 6981354 595 DVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQT 629
Cdd:TIGR01846 659 DRIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
384-605 |
1.04e-82 |
|
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: 1.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 384 PDSIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR 463
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 464 CLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARA 543
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 544 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVI 605
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
391-603 |
1.40e-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: 1.40e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFSTTIAENIrygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6981354 551 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDG 603
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
391-628 |
5.77e-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: 5.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 551 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 628
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
782-1271 |
3.76e-81 |
|
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: 277.80 E-value: 3.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 782 LTTRLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATgtrLALIAQNTANLGTGIIISFIYGWQLTLLLLS 861
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGL--ARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 862 VVPFIAVAGIVeMKMLAG--NAKRDKKEMEAAGKIATEAIENIRTVVSLT----QERKFESmyVEKLHGPYRNSVRKAHI 935
Cdd:COG4987 161 LALGLLLAGLL-LPLLAArlGRRAGRRLAAARAALRARLTDLLQGAAELAaygaLDRALAR--LDAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 936 Y-GITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDV-ILVFSAIVLGAVALGHASSFApDYAKAKLSAAYLFSLFERQ 1013
Cdd:COG4987 238 LsALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLaLLVLAALALFEALAPLPAAAQ-HLGRVRAAARRLNELLDAP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1014 PLIdSYSREGMWPDKFeGSVTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVL 1093
Cdd:COG4987 317 PAV-TEPAEPAPAPGG-PSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1094 LDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQ 1173
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1174 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHG 1253
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
490
....*....|....*...
gi 6981354 1254 THQQLLAQKGIYFSMVNI 1271
Cdd:COG4987 552 THEELLAQNGRYRQLYQR 569
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
710-1006 |
1.86e-80 |
|
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: 266.26 E-value: 1.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIAIF-----GPGDDTVKQQKCNMFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTT 784
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 785 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 864
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 865 FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 944
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 945 AFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYL 1006
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1033-1272 |
3.55e-80 |
|
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: 263.19 E-value: 3.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQL 1111
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 GIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQ 1191
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1192 PRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNI 1271
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 6981354 1272 Q 1272
Cdd:cd03252 237 Q 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
847-1263 |
1.56e-78 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 271.06 E-value: 1.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 847 ISFIYGWQLTLLLLS-VVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKiATEAIENIRTVVSLTQERKfesmYVEKLHGp 925
Cdd:PRK13657 150 LALFMNWRLSLVLVVlGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAH-VSDAIGNVSVVQSYNRIEA----ETQALRD- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 926 YRNSVRKAHI-----YGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFApdyAKAK 1000
Cdd:PRK13657 224 IADNLLAAQMpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFI---NQVF 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1001 LSAAYLFSLF----------ERQPLIDsysregmwPDKFEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSS 1070
Cdd:PRK13657 301 MAAPKLEEFFevedavpdvrDPPGAID--------LGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1071 GCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEA 1150
Cdd:PRK13657 371 GAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1151 NIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1230
Cdd:PRK13657 449 QAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAH 528
|
410 420 430
....*....|....*....|....*....|...
gi 6981354 1231 RLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKG 1263
Cdd:PRK13657 529 RLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
708-1265 |
3.78e-78 |
|
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: 273.36 E-value: 3.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 708 PYFVVGTLCAIANGALQPAFSIILSEMIAIfgpgddtvkQQKCNMFSLVFLGLGVHSFFTFFLQGFTfgkagEILTTRLR 787
Cdd:TIGR03796 157 LYLLLAGLLLVLPGLVIPAFSQIFVDEILV---------QGRQDWLRPLLLGMGLTALLQGVLTWLQ-----LYYLRRLE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 788 ---SMAFKA-----MLRQDMSWFDdhKNSTGALSTRLATdAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLL 859
Cdd:TIGR03796 223 iklAVGMSArflwhILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 860 lsvvpfIAVAGIVEMKMLAGNAKR---DKKEMEAAGKIATEAIENIRTVVSLtQERKFESMYVEKLHGPYRNSVRKAHIY 936
Cdd:TIGR03796 300 ------IAFAAINVLALQLVSRRRvdaNRRLQQDAGKLTGVAISGLQSIETL-KASGLESDFFSRWAGYQAKLLNAQQEL 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 937 GITFSI----SQAFMYFSYAGCFRFGSYLIVNGHMR------FKDVILVFSAIVLGAVALGHA-SSFAPDYAKAKLSAAY 1005
Cdd:TIGR03796 373 GVLTQIlgvlPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGTlQELEGDLNRLDDVLRN 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1006 -LFSLFERQPLIDSYSREgmwPDKFEGSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF 1084
Cdd:TIGR03796 453 pVDPLLEEPEGSAATSEP---PRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1085 YDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLPQKYE 1164
Cdd:TIGR03796 529 YQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSRPGGYD 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1165 TRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALdkAREGRTCIVIAHRLSTIQNADLIVVI 1244
Cdd:TIGR03796 607 AELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVL 684
|
570 580
....*....|....*....|.
gi 6981354 1245 DNGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR03796 685 ERGKVVQRGTHEELWAVGGAY 705
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1033-1248 |
1.30e-77 |
|
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: 253.07 E-value: 1.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1112
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFDCSIAKNIaygdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkgtqLSGGQKQRIAIARALIRQP 1192
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1193 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGK 1248
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
54-342 |
9.29e-75 |
|
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: 249.48 E-value: 9.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 54 MLLGTAMAIAHGSGLPLMMIVFGEMTDKFVDNagnfslpvnfslsmlnpGRILEEEMTRYAYYYSGLGGGVLLAAYIQVS 133
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPD-----------------GDPETQALNVYSLALLLLGLAQFILSFLQSY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 134 FWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKL 213
Cdd:pfam00664 64 LLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 214 TLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAIS 293
Cdd:pfam00664 144 TLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 294 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAF 342
Cdd:pfam00664 224 NGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
849-1274 |
1.19e-74 |
|
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: 262.76 E-value: 1.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 849 FIYGWQLTLLLLSVVPF-----IAVAGIVEMKMlagnakRDKKEMEAAGK-IATEAIENIRTVVSLTQERKFESMYVEKL 922
Cdd:TIGR01846 274 FFYSPTLTGVVIGSLVCyallsVFVGPILRKRV------EDKFERSAAATsFLVESVTGIETIKATATEPQFQNRWDRQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 923 HGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVIL--VFSAIVLGAVAlgHASSFAPDYAKAK 1000
Cdd:TIGR01846 348 AAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAfnMLAGRVTQPVL--RLAQLWQDFQQTG 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1001 LSAAYLFSLFErQPlIDSYSREGMWPDKFEGSVTFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL 1080
Cdd:TIGR01846 426 IALERLGDILN-SP-TEPRSAGLAALPELRGAITFENIRFRYAPDS-PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1081 LERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAKEANIHPFIETLP 1160
Cdd:TIGR01846 503 LQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELP 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1161 QKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADL 1240
Cdd:TIGR01846 581 QGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDR 660
|
410 420 430
....*....|....*....|....*....|....
gi 6981354 1241 IVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQAG 1274
Cdd:TIGR01846 661 IIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
712-1277 |
1.61e-73 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 269.59 E-value: 1.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 712 VGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKQqkcnMFSLVFLGLgvHSFFTFFLQGFTFgkagEILTTR----LR 787
Cdd:PTZ00265 64 VSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDI----IFSLVLIGI--FQFILSFISSFCM----DVVTTKilktLK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 788 SMAFKAMLRQDMSWFDDHKNSTgaLSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIA 867
Cdd:PTZ00265 134 LEFLKSVFYQDGQFHDNNPGSK--LTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 868 VAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMY--VEKLHGPY---RNSVRKAHIYGItfsi 942
Cdd:PTZ00265 212 ICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFnlSEKLYSKYilkANFMESLHIGMI---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 943 sQAFMYFSYAGCFRFGSYLIV--------NGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLFERQP 1014
Cdd:PTZ00265 288 -NGFILASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1015 LIDSYSREGMWPDKfeGSVTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLL 1094
Cdd:PTZ00265 367 LVENNDDGKKLKDI--KKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1095 -DGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAY------------------------GDNSR------------- 1136
Cdd:PTZ00265 445 nDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRnscrakcagdlnd 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1137 ------------------VVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:PTZ00265 525 msnttdsneliemrknyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILD 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1199 EATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQNADLIVVIDNGK---------------------------- 1248
Cdd:PTZ00265 605 EATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkd 684
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 6981354 1249 -------------------VKEHGTHQQLLAQK-GIYFSMVNIQAGTQN 1277
Cdd:PTZ00265 685 dnnnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYYTMINNQKVSSK 733
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
137-638 |
3.71e-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: 3.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 137 LAAGRQIrKIRQKFFHAILRQEMGWFDIKGTTE-LNT--RLTDDISKISegigdkVGMFFQAIATFFAGFI---VGFIRG 210
Cdd:TIGR01192 83 LAHGRRA-TLLTEAFGRIISMPLSWHQQRGTSNaLHTllRATETLFGLW------LEFMRQHLATFVALFLlipTAFAMD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 211 WKLTLVIMAItAILGLSTAVWakILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQN------KELERYQKHLENAK 284
Cdd:TIGR01192 156 WRLSIVLMVL-GILYILIAKL--VMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNrieaetSALKQFTNNLLSAQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 285 ---------KIGIKKaISANISMGIAFLLiyasyalafwyGSTLVISKEYTIGNAMTV--FFSILIGAFSvgQAAPCIDA 353
Cdd:TIGR01192 233 ypvldwwalASGLNR-MASTISMMCILVI-----------GTVLVIKGELSVGEVIAFigFANLLIGRLD--QMSGFITQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 354 FPNARGAAYVIFDIIDNNPKIDSFSERGHKPDsIKGNLEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKS 433
Cdd:TIGR01192 299 IFEARAKLEDFFDLEDSVFQREEPADAPELPN-VKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTGAGKT 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 434 TTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIM 513
Cdd:TIGR01192 376 TLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFIL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 514 KLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN 593
Cdd:TIGR01192 456 KRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRN 535
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 6981354 594 ADVIAGFEDGVIVEQGSHSELIKKEGIYFRLvnMQTSGsqILSEE 638
Cdd:TIGR01192 536 ADLVLFLDQGRLIEKGSFQELIQKDGRFYKL--LRRSG--LLTNQ 576
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
48-374 |
1.24e-72 |
|
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: 245.05 E-value: 1.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 48 WQDKLFMLLGTAMAIAHGSGLPLMMIVFGEMTDkfvdnagNFSLPvnfslsmlnPGRILEEEMTRYAYYYSGLGGGVLLA 127
Cdd:cd18578 5 KPEWPLLLLGLIGAIIAGAVFPVFAILFSKLIS-------VFSLP---------DDDELRSEANFWALMFLVLAIVAGIA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 128 AYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKG--TTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18578 69 YFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 206 GFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:cd18578 149 AFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFPNARGAAYVIF 365
Cdd:cd18578 229 KGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIF 308
|
....*....
gi 6981354 366 DIIDNNPKI 374
Cdd:cd18578 309 RLLDRKPEI 317
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
710-984 |
1.66e-68 |
|
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: 231.76 E-value: 1.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKQqKCNMFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSM 789
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ-ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 790 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 869
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 870 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYF 949
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 6981354 950 SYAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAV 984
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVafLSLFAQLFGPL 274
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
389-609 |
7.36e-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: 227.47 E-value: 7.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 389 GNLEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF 468
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 548
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 549 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 609
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
849-1272 |
1.09e-67 |
|
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: 242.55 E-value: 1.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 849 FIYGWQLTL----LLLSVVPFIAVAGIVEMKMLagnakrdKKEMEAAGKIATEAIENIRTVVSL----TQERKFesMYVE 920
Cdd:TIGR03797 271 FYYSWKLALvavaLALVAIAVTLVLGLLQVRKE-------RRLLELSGKISGLTVQLINGISKLrvagAENRAF--ARWA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 921 KLHGPYRNSVRKAH-IYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDvILVFSAivlgavALGHASSFAPDYAKA 999
Cdd:TIGR03797 342 KLFSRQRKLELSAQrIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGS-FLAFNT------AFGSFSGAVTQLSNT 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1000 KLSAAYLFSLFER-QPLIDS---YSREGMWPDKFEGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:TIGR03797 415 LISILAVIPLWERaKPILEAlpeVDEAKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1075 STVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDnsrVVSQDEIVRAAKEANIHP 1154
Cdd:TIGR03797 493 STLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1155 FIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLST 1234
Cdd:TIGR03797 570 DIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLST 647
|
410 420 430
....*....|....*....|....*....|....*...
gi 6981354 1235 IQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQ 1272
Cdd:TIGR03797 648 IRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
356-597 |
2.03e-66 |
|
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: 234.49 E-value: 2.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 356 NARGAAYVIFDIIDNNPKIdsFSERGHKPDSIKGNLEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGKSTT 435
Cdd:TIGR02857 289 DGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 436 VQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKL 515
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 516 PQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNAD 595
Cdd:TIGR02857 445 PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
|
..
gi 6981354 596 VI 597
Cdd:TIGR02857 525 RI 526
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1031-1249 |
1.84e-65 |
|
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: 220.92 E-value: 1.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1031 GSVTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQ 1110
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1111 LGIVSQEPILFDCSIAKNIAYGDnsRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIR 1190
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1191 QPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKV 1249
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
389-610 |
1.90e-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: 220.83 E-value: 1.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 389 GNLEFSDVHFSYpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 467
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFSTTIAENI----RYgrgnvTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARA 543
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 544 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 610
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
155-628 |
2.28e-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: 235.62 E-value: 2.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 155 LRQEMGWFDIKGTTELNTRlTDDISKISEGIGDKvgMFFQAIATFFAGFIVG--FIRGWKLTLVIMAITAILGLSTAVWA 232
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASR-AMGISQIRRILSGS--TLTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLVLG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 233 KILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANI-SMGIAFLLIYASYAL 311
Cdd:TIGR03797 297 LLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLlTVFNAVLPVLTSAAL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 312 aFWYGSTLVISKEYTIGN-------------AMTVFFSILIGAFSV----GQAAPCIDAFPNARGAayvifdiidnnpKI 374
Cdd:TIGR03797 377 -FAAAISLLGGAGLSLGSflafntafgsfsgAVTQLSNTLISILAViplwERAKPILEALPEVDEA------------KT 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 375 DsfserghkPDSIKGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDG 454
Cdd:TIGR03797 444 D--------PGKLSGAIEVDRVTFRYRPDGPL-ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDG 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 455 QDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIrYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQ 534
Cdd:TIGR03797 515 QDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQ 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 535 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRttIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:TIGR03797 594 RQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDEL 671
|
490
....*....|....
gi 6981354 615 IKKEGIYFRLVNMQ 628
Cdd:TIGR03797 672 MAREGLFAQLARRQ 685
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
129-626 |
2.35e-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: 233.09 E-value: 2.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 129 YIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdISKISEGIGDKVGMFFQAIATFFagfIVGFI 208
Cdd:TIGR01193 214 YIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLDMWILV---IVGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 209 RGWK-LTLVIMAITAILGLSTAVWA--KILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGqnkELERYQK------- 278
Cdd:TIGR01193 290 LVRQnMLLFLLSLLSIPVYAVIIILfkRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS---EAERYSKidsefgd 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 279 HLENAKKIGIKKAISANISMGIAFLLIyasyALAFWYGSTLVISKEYTIGNAMTvfFSILIGAFsVGQAAPCIDAFPNAR 358
Cdd:TIGR01193 367 YLNKSFKYQKADQGQQAIKAVTKLILN----VVILWTGAYLVMRGKLTLGQLIT--FNALLSYF-LTPLENIINLQPKLQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 359 gAAYVIFDIIDNNPKIDSFSERGHKPDS---IKGNLEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGKSTT 435
Cdd:TIGR01193 440 -AARVANNRLNEVYLVDSEFINKKKRTElnnLNGDIVINDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 436 VQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYG-RGNVTMDEIKKAVKEANAYDFIMK 514
Cdd:TIGR01193 517 AKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIEN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 515 LPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREgRTTIVIAHRLSTVRNA 594
Cdd:TIGR01193 597 MPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQS 675
|
490 500 510
....*....|....*....|....*....|..
gi 6981354 595 DVIAGFEDGVIVEQGSHSELIKKEGIYFRLVN 626
Cdd:TIGR01193 676 DKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
782-1272 |
6.69e-64 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 228.44 E-value: 6.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 782 LTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR-LALIAQNTANLGTGIIISFIYGWQLTLLLL 860
Cdd:PRK10789 67 LAVELREDFYRQLSRQHPEFYLRHR--TGDLMARATNDVDRVVFAAGEGvLTLVDSLVMGCAVLIVMSTQISWQLTLLAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 861 SVVPFIAVAgivemkmlagnAKRDKKEMEAAGKIATEAIE--NIRTVVSLTQERKFESMYVEKLHGPY---------RNS 929
Cdd:PRK10789 145 LPMPVMAIM-----------IKRYGDQLHERFKLAQAAFSslNDRTQESLTSIRMIKAFGLEDRQSALfaadaedtgKKN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 930 VRKAHI---YGITFSISQAFMYFSYAGCfrfGSYLIVNGHMrfkdvilvfsaivlgavALGHASSFA--------PDYAK 998
Cdd:PRK10789 214 MRVARIdarFDPTIYIAIGMANLLAIGG---GSWMVVNGSL-----------------TLGQLTSFVmylglmiwPMLAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 999 AKL-------SAAY--LFSLFERQPLIDsysrEGMWP-DKFEGSVTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVG 1068
Cdd:PRK10789 274 AWMfnivergSAAYsrIRAMLAEAPVVK----DGSEPvPEGRGELDVNIRQFTYPQ-TDHPALENVNFTLKPGQMLGICG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1069 SSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSrvVSQDEIVRAAK 1148
Cdd:PRK10789 349 PTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD--ATQQEIEHVAR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1149 EANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVI 1228
Cdd:PRK10789 427 LASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIIS 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 6981354 1229 AHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQ 1272
Cdd:PRK10789 507 AHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
397-1277 |
7.21e-64 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 239.11 E-value: 7.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 397 HFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEgTISIDgqdirnfnvrcLREFIGVVSQEP 476
Cdd:PLN03232 621 YFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV-----------IRGSVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 477 VLFSTTIAENIRYGrGNVTMDEIKKAVK-EANAYDFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PLN03232 689 WIFNATVRENILFG-SDFESERYWRAIDvTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 556 ATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLvnMQTSGSqi 634
Cdd:PLN03232 767 PLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL--MENAGK-- 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 635 LSEEFEVELSDEKaaggVAPNGWKARIfrNSTKKSLKSSRAHQNRLDVETNELDANVPPVSFLKVLRLNKTEWPYFVVGT 714
Cdd:PLN03232 843 MDATQEVNTNDEN----ILKLGPTVTI--DVSERNLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMI 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 715 L--CAIANGALQPAFSIILSemiaiFGPGDDTVKQQKCNMFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSMAFK 792
Cdd:PLN03232 917 LlvCYLTTEVLRVSSSTWLS-----IWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLN 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 793 AMLRQDMSWFddHKNSTGALSTRLATDAAQvqgatgtrlalIAQNTANLGTGIIISFiygWQL--TLLLLSVVPFIAVAG 870
Cdd:PLN03232 992 SILRAPMLFF--HTNPTGRVINRFSKDIGD-----------IDRNVANLMNMFMNQL---WQLlsTFALIGTVSTISLWA 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 871 IVEMKML-------AGNAKRDKKEMEAAGKIATEAI--ENIRTVVSLTQERKFESMyvEKLHGPYRN------------- 928
Cdd:PLN03232 1056 IMPLLILfyaaylyYQSTSREVRRLDSVTRSPIYAQfgEALNGLSSIRAYKAYDRM--AKINGKSMDnnirftlantssn 1133
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 929 ---SVRKAHIYGITFSISQAFMYFSYAGcfrfgsyliVNGHMRFKDVILVFSAIVLGAVALghASSFAPDYAKAKLS--- 1002
Cdd:PLN03232 1134 rwlTIRLETLGGVMIWLTATFAVLRNGN---------AENQAGFASTMGLLLSYTLNITTL--LSGVLRQASKAENSlns 1202
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1003 ---AAYLFSLFERQPLIDSYSRE-GMWPDKfeGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTV 1077
Cdd:PLN03232 1203 verVGNYIDLPSEATAIIENNRPvSGWPSR--GSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSM 1278
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1078 VQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIaygDNSRVVSQDEIVRAAKEANIHPFIE 1157
Cdd:PLN03232 1279 LNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVID 1355
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1158 TLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN 1237
Cdd:PLN03232 1356 RNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID 1435
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 6981354 1238 ADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQAGTQN 1277
Cdd:PLN03232 1436 CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
995-1244 |
7.53e-63 |
|
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: 224.09 E-value: 7.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 995 DYAKAKLSAAYLFSLFERQPLIDSYSREGMWPDkfEGSVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAPVTAAP--ASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1075 STVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGDnsRVVSQDEIVRAAKEANIHP 1154
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1155 FIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1234
Cdd:TIGR02857 440 FVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLAL 519
|
250
....*....|
gi 6981354 1235 IQNADLIVVI 1244
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
999-1261 |
1.68e-62 |
|
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: 223.86 E-value: 1.68e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 999 AKLSAAYLFSLFERQPLidsySREGMWPDKFEGSVTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVV 1078
Cdd:COG4618 301 ARQAYRRLNELLAAVPA----EPERMPLPRPKGRLSVENLTVVPP-GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1079 QLLERFYDPMAGTVLLDGQEAKklnvQWLRAQLG--I--VSQEPILFDCSIAKNIA-YGDnsrvVSQDEIVRAAKEANIH 1153
Cdd:COG4618 376 RLLVGVWPPTAGSVRLDGADLS----QWDREELGrhIgyLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVH 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1154 PFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRL 1232
Cdd:COG4618 448 EMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRP 527
|
250 260
....*....|....*....|....*....
gi 6981354 1233 STIQNADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:COG4618 528 SLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
409-1268 |
3.25e-61 |
|
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: 230.99 E-value: 3.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnvrclrefIGVVSQEPVLFSTTIAENIR 488
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 489 YGRGnvTMDEIKKAVKEANAY--DFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 566
Cdd:TIGR00957 721 FGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 567 EVqaaLDKA------REGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQTSGSQILSEEfe 640
Cdd:TIGR00957 798 HI---FEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLE-- 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 641 velsdEKAAGGVAPNGWKARIFRNST----------KKSLKSSRAH---QNRLDVETNELDANVPPVSFLKVLRLNKTE- 706
Cdd:TIGR00957 873 -----DSWTALVSGEGKEAKLIENGMlvtdvvgkqlQRQLSASSSDsgdQSRHHGSSAELQKAEAKEETWKLMEADKAQt 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 707 --------WPYFVVGTLCA--------IANGALQPAFSIILSEMIaifgpgDDTV---KQQKCNMFSLVFLGLGVHSFFT 767
Cdd:TIGR00957 948 gqvelsvyWDYMKAIGLFItflsiflfVCNHVSALASNYWLSLWT------DDPMvngTQNNTSLRLSVYGALGILQGFA 1021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 768 FFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTAN-LGTGII 846
Cdd:TIGR00957 1022 VFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvIGALIV 1099
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 847 ISFIygwqlTLLLLSVVPFIAVAGIVEMKMLAGNAkRDKKEMEAAGKIATEAIENiRTVVSLTQERKFEsmyveklhgpy 926
Cdd:TIGR00957 1100 ILLA-----TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLESVSRSPVYSHFN-ETLLGVSVIRAFE----------- 1161
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 927 rNSVRKAHIYGITFSISQAFMYfsyagcfrfgSYLIVNGHMRFKdVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYL 1006
Cdd:TIGR00957 1162 -EQERFIHQSDLKVDENQKAYY----------PSIVANRWLAVR-LECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYS 1229
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1007 FSL--------------------FERQPLIDSYSREGMW-------PDKF--EGSVTFNEVVFNYPTRANVpVLQGLSLE 1057
Cdd:TIGR00957 1230 LQVtfylnwlvrmssemetnivaVERLKEYSETEKEAPWqiqetapPSGWppRGRVEFRNYCLRYREDLDL-VLRHINVT 1308
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1058 VKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIaygDNSRV 1137
Cdd:TIGR00957 1309 IHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPFSQ 1385
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1138 VSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD 1217
Cdd:TIGR00957 1386 YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR 1465
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1218 KAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSM 1268
Cdd:TIGR00957 1466 TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1031-1254 |
5.93e-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: 208.12 E-value: 5.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1031 GSVTFNEVVFNYptRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRA 1109
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQEPILFDCSIAKNIaygDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALI 1189
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1190 RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGT 1254
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
388-617 |
8.67e-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: 218.85 E-value: 8.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 388 KGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 467
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFSTTIAENI-RYGrgNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVR 546
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 547 NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKK 617
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
330-624 |
1.04e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 218.93 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 330 AMTVF-----FSILI---GAFS-VGQaapCIdafpnarGAAYVIFDIIDNNPKIdSFSERgHKPDSIKGNLEFSDVHFSY 400
Cdd:PRK11160 281 ALFVFaalaaFEALMpvaGAFQhLGQ---VI-------ASARRINEITEQKPEV-TFPTT-STAAADQVSLTLNNVSFTY 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 401 PSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFS 480
Cdd:PRK11160 349 PDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 481 TTIAENIRYGRGNVTmDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK11160 428 ATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 561 DTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRL 624
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
122-656 |
1.74e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 218.43 E-value: 1.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 122 GGVLLAA---YIQVSFWTL----AAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQ 194
Cdd:PRK10789 40 GTMVLIAvvvYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 195 AIATFFAGFIVGFIR-GWKLTLV------IMAItAILGLSTAVWAKI------LSTFSDKelaayakagavAEEALGAIR 261
Cdd:PRK10789 120 SLVMGCAVLIVMSTQiSWQLTLLallpmpVMAI-MIKRYGDQLHERFklaqaaFSSLNDR-----------TQESLTSIR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 262 TVIAFGgqnkeLERYQKHL--ENAKKIGIKKA----ISANISMGIaFLLIYASYALAFWYGSTLVISKEYTIGN------ 329
Cdd:PRK10789 188 MIKAFG-----LEDRQSALfaADAEDTGKKNMrvarIDARFDPTI-YIAIGMANLLAIGGGSWMVVNGSLTLGQltsfvm 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 330 ----------AMTVFFSILigafsvgqaapcidafpnARG-AAYV-IFDIIDNNPKIDSfserGHKP-DSIKGNLEFSDV 396
Cdd:PRK10789 262 ylglmiwpmlALAWMFNIV------------------ERGsAAYSrIRAMLAEAPVVKD----GSEPvPEGRGELDVNIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 397 HFSYPsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEP 476
Cdd:PRK10789 320 QFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 477 VLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 557 TSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQtsgsqils 636
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ-------- 550
|
570 580
....*....|....*....|
gi 6981354 637 eEFEVELSDEKAAGGVAPNG 656
Cdd:PRK10789 551 -QLEAALDDAPEIREEAVDA 569
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
395-1269 |
2.20e-58 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 221.92 E-value: 2.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 395 DVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LLQRLYDPTEGTISIDGQdirnfnvrclrefIGVVS 473
Cdd:PLN03130 619 NGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 474 QEPVLFSTTIAENIRYGrGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PLN03130 686 QVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 554 DEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLvnMQTSGS 632
Cdd:PLN03130 765 DDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL--MENAGK 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 633 QILSEEFEVELSDEKAAGGVAPNGWKARIFRNStkkSLKSSRAHQNRLDVETNELDANVppVSFLKVLRLNKTEWPYFVV 712
Cdd:PLN03130 843 MEEYVEENGEEEDDQTSSKPVANGNANNLKKDS---SSKKKSKEGKSVLIKQEERETGV--VSWKVLERYKNALGGAWVV 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 713 GTL--CAIANGALQPAFSIILSEMIaifgpgDDTVKQQKCNMFSLvflglGVHSFFTFFLQGFTFGKAGEILTT------ 784
Cdd:PLN03130 918 MILflCYVLTEVFRVSSSTWLSEWT------DQGTPKTHGPLFYN-----LIYALLSFGQVLVTLLNSYWLIMSslyaak 986
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 785 RLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDaaqvqgatgtrLALIAQNTANLGTGIIISFiygWQL--TLLLLSV 862
Cdd:PLN03130 987 RLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKD-----------LGDIDRNVAVFVNMFLGQI---FQLlsTFVLIGI 1050
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 863 VPFIAVAGIveMKMLAG---------NAKRDKKEMEaagkiateaienirtvvSLTQERKFeSMYVEKLHG-----PYRN 928
Cdd:PLN03130 1051 VSTISLWAI--MPLLVLfygaylyyqSTAREVKRLD-----------------SITRSPVY-AQFGEALNGlstirAYKA 1110
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 929 SVRKAHIYGITFSISQAFMYFSYAGCFRFGSYL-IVNGHMrfkdVILVFSAIVLGAVALGHASSFAP------DYA---- 997
Cdd:PLN03130 1111 YDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLeTLGGLM----IWLTASFAVMQNGRAENQAAFAStmglllSYAlnit 1186
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 998 ---KAKLSAAYL----FSLFER-----------QPLIDSYSREGMWPDKfeGSVTFNEVVFNYptRANVP-VLQGLSLEV 1058
Cdd:PLN03130 1187 sllTAVLRLASLaensLNAVERvgtyidlpseaPLVIENNRPPPGWPSS--GSIKFEDVVLRY--RPELPpVLHGLSFEI 1262
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1059 KKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIaygDNSRVV 1138
Cdd:PLN03130 1263 SPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---DPFNEH 1339
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1139 SQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK 1218
Cdd:PLN03130 1340 NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE 1419
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1219 arEGRTC--IVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFS-MV 1269
Cdd:PLN03130 1420 --EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkMV 1471
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
723-1270 |
2.90e-58 |
|
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: 214.99 E-value: 2.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 723 LQPAFSIILSEMIAIFGPgddtvkQQKCNMFSLVFLGLGV----HSFFTFFlQGFTFGKAGEILTTRLRSMAFKAMLRQD 798
Cdd:TIGR01193 171 ISIAGSYYLQKIIDTYIP------HKMMGTLGIISIGLIIayiiQQILSYI-QIFLLNVLGQRLSIDIILSYIKHLFELP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 799 MSWFDDHKnsTGALSTRLaTDAAQVQGATG-TRLALIAqntaNLGTGIIISFIYGWQ---LTLLLLSVVPFIAVAGIVEM 874
Cdd:TIGR01193 244 MSFFSTRR--TGEIVSRF-TDASSIIDALAsTILSLFL----DMWILVIVGLFLVRQnmlLFLLSLLSIPVYAVIIILFK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 875 KMLAgnaKRDKKEMEAAGKIATEAIEN---IRTVVSLTQE----RKFESMYVEKLHGPYRNS----VRKAHIYGITFSIS 943
Cdd:TIGR01193 317 RTFN---KLNHDAMQANAVLNSSIIEDlngIETIKSLTSEaerySKIDSEFGDYLNKSFKYQkadqGQQAIKAVTKLILN 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 944 QAFMYFsyagcfrfGSYLIVNGHMRFKDVIlVFSAIV-LGAVALGHASSFAPDYAKAKLSAAYLFSLFerqpLIDSYSRE 1022
Cdd:TIGR01193 394 VVILWT--------GAYLVMRGKLTLGQLI-TFNALLsYFLTPLENIINLQPKLQAARVANNRLNEVY----LVDSEFIN 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1023 GMWPDKFE---GSVTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEA 1099
Cdd:TIGR01193 461 KKKRTELNnlnGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1100 KKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGdNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQK 1179
Cdd:TIGR01193 539 KDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1180 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREgRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
570
....*....|.
gi 6981354 1260 AQKGIYFSMVN 1270
Cdd:TIGR01193 697 DRNGFYASLIH 707
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
757-1278 |
3.82e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 211.89 E-value: 3.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 757 FLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQ 836
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 837 NTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF-E 915
Cdd:PRK10790 149 SAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFgE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 916 SMyveklhgpyrNSVRKAHiygitfsisqafmYFSYAGCFRFGSYLIvnghmrfKDVILVFSAIVL------------GA 983
Cdd:PRK10790 229 RM----------GEASRSH-------------YMARMQTLRLDGFLL-------RPLLSLFSALILcgllmlfgfsasGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 984 VALGHASSFApdyakaklsaAYLFSLFErqPLIDSYSREGMWPDK-------FE------------------GSVTFNEV 1038
Cdd:PRK10790 279 IEVGVLYAFI----------SYLGRLNE--PLIELTTQQSMLQQAvvagervFElmdgprqqygnddrplqsGRIDIDNV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1039 VFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEP 1118
Cdd:PRK10790 347 SFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1119 ILFDCSIAKNIAYGdnsRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:PRK10790 425 VVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1199 EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSMVNIQAGTQNL 1278
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEEL 581
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1002-1268 |
9.17e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 204.67 E-value: 9.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1002 SAAYLFSLFERQPLIdSYSREGMWPDKfEGSVTFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1081
Cdd:PRK11160 310 SARRINEITEQKPEV-TFPTTSTAAAD-QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1082 ERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYgdnsrvvsqdeivrAAKEANIHPFIETL-- 1159
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL--------------AAPNASDEALIEVLqq 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1160 ---------PQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1230
Cdd:PRK11160 453 vgleklledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH 532
|
250 260 270
....*....|....*....|....*....|....*...
gi 6981354 1231 RLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSM 1268
Cdd:PRK11160 533 RLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
255-588 |
1.08e-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: 200.28 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 255 EALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVF 334
Cdd:TIGR02868 198 DALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 335 FSILIGAFSVGQAAP-CIDAFPNARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKG-NLEFSDVHFSYPSRAniKILKGL 412
Cdd:TIGR02868 277 VLLPLAAFEAFAALPaAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PVLDGV 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRG 492
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARP 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 493 NVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL 572
Cdd:TIGR02868 435 DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL 514
|
330
....*....|....*.
gi 6981354 573 DKAREGRTTIVIAHRL 588
Cdd:TIGR02868 515 LAALSGRTVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
389-644 |
9.35e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 199.17 E-value: 9.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 389 GNLEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF 468
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGVVSQEPVLFSTTIAENIRYGRgNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 549 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRLVNMQ 628
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
250
....*....|....*.
gi 6981354 629 TSGSQILSEEFEVELS 644
Cdd:PRK10790 576 LAGEELAASVREEESL 591
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
255-617 |
1.36e-53 |
|
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: 197.19 E-value: 1.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 255 EALGAIRTViafggQNKELERYQKHLENAKKIGIKKAISANISMgiAFLLIYASYALAFwyGSTLVISKEYTIGnaMTVF 334
Cdd:TIGR01842 194 EAMGMMGNL-----TKRWGRFHSKYLSAQSAASDRAGMLSNLSK--YFRIVLQSLVLGL--GAYLAIDGEITPG--MMIA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 335 FSILigafsVGQAAPCID-------AFPNARGAAYVIFDIIDNNPkidsFSERGHKPDSIKGNLEFSDVHFSYPSrANIK 407
Cdd:TIGR01842 263 GSIL-----VGRALAPIDgaiggwkQFSGARQAYKRLNELLANYP----SRDPAMPLPEPEGHLSVENVTIVPPG-GKKP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENI 487
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 488 -RYGRgNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 566
Cdd:TIGR01842 413 aRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 6981354 567 EVQAALDKAR-EGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKK 617
Cdd:TIGR01842 492 ALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
391-618 |
1.78e-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: 1.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPV--LFSTTIAENIRYG---RGnVTMDEIKKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIA 541
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenLG-LPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIKKE 618
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
391-614 |
1.92e-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: 1.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGTISIDGQDIR--NFNVR 463
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYdlDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 464 CLREFIGVVSQEPVLFSTTIAENIRYG---RGNVTMDEIKKAVKEANAydfIMKLPQKfdtlVGDR--GAQLSGGQKQRI 538
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlHGIKLKEELDERVEEALR---KAALWDE----VKDRlhALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 539 AIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
357-624 |
2.77e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 194.68 E-value: 2.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 357 ARGAAYVIFDIIDNNpkiDSFSERGHKPDSIKGNLEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTV 436
Cdd:PRK11174 317 AVGAAESLVTFLETP---LAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 437 QLLqrL-YDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKL 515
Cdd:PRK11174 394 NAL--LgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLL 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 516 PQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNAD 595
Cdd:PRK11174 472 PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWD 551
|
250 260
....*....|....*....|....*....
gi 6981354 596 VIAGFEDGVIVEQGSHSELIKKEGIYFRL 624
Cdd:PRK11174 552 QIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
391-615 |
3.72e-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: 3.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAN--IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF 468
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 ---IGVVSQEPV--LF-STTIAENIRYG---RGNVTMDEIKKAVKEAnaydfiMK---LPQKFdtlvGDR-GAQLSGGQK 535
Cdd:COG1123 341 rrrVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAEL------LErvgLPPDL----ADRyPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 536 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 612
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
...
gi 6981354 613 ELI 615
Cdd:COG1123 491 EVF 493
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1054-1268 |
4.17e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 190.83 E-value: 4.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1054 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIAYGD 1133
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1134 NSrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQ 1213
Cdd:PRK11174 448 PD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1214 EALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFSM 1268
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
842-1261 |
5.60e-51 |
|
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: 189.48 E-value: 5.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 842 GTGIIISFIYGWQLTLLLLSVV--PFIAVAGIVEMKMLAG----NAKRDKKEME-------AAGKIATEAIENIRTVVSL 908
Cdd:TIGR01842 117 GPGLFAFFDAPWMPIYLLVCFLlhPWIGILALGGAVVLVGlallNNRATKKPLKeateasiRANNLADSALRNAEVIEAM 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 909 TQERKFESMYvEKLHGPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILvfSAIVLGAvALG 987
Cdd:TIGR01842 197 GMMGNLTKRW-GRFHSKYLSAQSAASDRAGMLSnLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIA--GSILVGR-ALA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 988 ---HASSFAPDYAKAKLSAAYLFSLFERQPLidsySREGMWPDKFEGSVTFNEVVFnYPTRANVPVLQGLSLEVKKGQTL 1064
Cdd:TIGR01842 273 pidGAIGGWKQFSGARQAYKRLNELLANYPS----RDPAMPLPEPEGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEAL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1065 ALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKklnvQWLRAQLG----IVSQEPILFDCSIAKNIA-YGDNsrvVS 1139
Cdd:TIGR01842 348 AIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK----QWDRETFGkhigYLPQDVELFPGTVAENIArFGEN---AD 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1140 QDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA 1219
Cdd:TIGR01842 421 PEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL 500
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 6981354 1220 R-EGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:TIGR01842 501 KaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
392-603 |
6.24e-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: 6.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 392 EFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 471
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 472 VSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEANAydfimklpqkfdtLVGDRG------AQLSGGQKQRIAIA 541
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlgLPEEEIEERVEEALE-------------LVGLEGlrdrspFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDG 603
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
391-605 |
3.18e-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: 3.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFSTTIAENIrygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 551 LLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVI 605
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
391-617 |
5.46e-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: 5.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF- 468
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 --IGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIKKAVKEanaydfimklpqkFDTLVG--DRG----AQLSGGQKQR 537
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPLeiAGVPKAEIEERVLE-------------LLELVGleDKAdaypAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 6981354 615 IKK 617
Cdd:cd03258 229 FAN 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
409-558 |
8.77e-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: 167.44 E-value: 8.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFS-TTIAENI 487
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 488 RYGRgnvTMDEIKKAVKEANAYDFIMKLPQKF--DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
391-610 |
9.84e-48 |
|
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: 9.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF- 468
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 --IGVVSQEPVLFST-TIAENIRY-----GrgnVTMDEIKKAVKE----------ANAYdfimklPqkfdtlvgdrgAQL 530
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALpleiaG---VPKAEIRKRVAEllelvglsdkADAY------P-----------SQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVE 607
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 6981354 608 QGS 610
Cdd:COG1135 222 QGP 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1033-1262 |
9.97e-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: 170.21 E-value: 9.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1112
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPI--LFDCSIAKNIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIAR 1186
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1187 ALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLAQK 1262
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
391-609 |
2.06e-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: 2.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF- 468
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 --IGVVSQEPV-----LFS--TTIAENIRYGRGNVTMDEIKKAVKEA-----NAYDFIMKLPqkfdtlvgdrgAQLSGGQ 534
Cdd:cd03257 82 keIQMVFQDPMsslnpRMTigEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYP-----------HELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 535 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 609
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
391-609 |
2.09e-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: 2.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNvRCLREFIG 470
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFSTTIAENIrygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 551 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 609
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1050-1258 |
2.35e-47 |
|
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: 169.28 E-value: 2.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFD 1122
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNIAYGDNSRVVSQ----DEIVRAA-KEANIHPfietlpqkyetRVGDK--GTQLSGGQKQRIAIARALIRQPRVL 1195
Cdd:cd03260 95 GSIYDNVAYGLRLHGIKLkeelDERVEEAlRKAALWD-----------EVKDRlhALGLSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1196 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1258
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1033-1261 |
5.16e-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: 177.02 E-value: 5.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRAN--VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWL 1107
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1108 RAQLGIVSQEPIL-FDC--SIAKNIAYG-DNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRvgdKGTQLSGGQKQR 1181
Cdd:COG1123 341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-----LERvgLPPDLADR---YPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1182 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1258
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
...
gi 6981354 1259 LAQ 1261
Cdd:COG1123 493 FAN 495
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
391-586 |
6.43e-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: 6.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:COG4619 1 LELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFSTTIAENI----RYGRGNVTMDEIKKAVKEANaydfimkLPQKF-DTLVgdrgAQLSGGQKQRIAIARALV 545
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPV----ERLSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6981354 546 RNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 586
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1025-1254 |
1.69e-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: 1.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1025 WPDkfEGSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN 1103
Cdd:cd03369 1 WPE--HGEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1104 VQWLRAQLGIVSQEPILFDCSIAKNI-AYGDNSrvvsqDEIVRAAkeanihpfietlpqkyeTRVGDKGTQLSGGQKQRI 1182
Cdd:cd03369 77 LEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEYS-----DEEIYGA-----------------LRVSEGGLNLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGT 1254
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1038-1249 |
1.89e-46 |
|
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: 164.31 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1038 VVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1117
Cdd:cd03246 6 VSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1118 PILFDCSIAKNIaygdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLL 1197
Cdd:cd03246 85 DELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1198 DEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIDNGKV 1249
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
391-615 |
4.25e-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: 165.94 E-value: 4.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI--RNFNVRCLREF 468
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGVVSQEPVLFS-TTIAENIRYG----RGnvtMDEiKKAVKEAnaydfiMKLPQKfdtlVG--DRG----AQLSGGQKQR 537
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvKK---MSK-AEAEERA------MELLER----VGlaDKAdaypAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELI 615
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFF 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
391-608 |
4.52e-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: 4.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL---- 465
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 466 REFIGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIKKAVKEANAY----DFIMKLPqkfdtlvgdrgAQLSGGQKQRI 538
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLllAGVSRKERRERARELLERvglgDRLDHRP-----------SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 539 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIA-HRLSTVRNADVIAGFEDGVIVEQ 608
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
391-626 |
5.29e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 165.62 E-value: 5.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRcLREFIG 470
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFST-TIAENIRYGRG--NVTMDEIKKAVKEANAydfIMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRN 547
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 548 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFEDGVIVEQGSHSELIKK--EGIYFR 623
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARllEDVFLE 229
|
...
gi 6981354 624 LVN 626
Cdd:COG1131 230 LTG 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1035-1248 |
9.54e-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: 163.79 E-value: 9.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1035 FNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIV 1114
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1115 SQEP--ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARAL 1188
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1189 IRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGK 1248
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1049-1249 |
1.44e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.45 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKN 1128
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1129 IA--YGDNSRVVSQDEIVRAAKEANIHPFIetlpqkYETRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1206
Cdd:COG4619 94 LPfpFQLRERKFDRERALELLERLGLPPDI------LDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6981354 1207 ESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:COG4619 164 ENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
391-605 |
3.92e-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: 162.27 E-value: 3.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF- 468
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 ---IGVVSQEPVLFST-TIAENIRYGrgnVTMDEIKKAVKEANAYDFI--MKLPQKFDTLVgdrgAQLSGGQKQRIAIAR 542
Cdd:cd03255 81 rrhIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTVRNADVIAGFEDGVI 605
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1033-1253 |
7.19e-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: 160.17 E-value: 7.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLG 1112
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFDCSIAKNIaygdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkGTQLSGGQKQRIAIARALIRQP 1192
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1193 RVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHG 1253
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
391-603 |
8.64e-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: 8.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR--NFNVRCLREF 468
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGVVSQEPVLFST-TIAENIRYGrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRN 547
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 548 PKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 603
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
391-615 |
1.57e-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: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPT---EGTISIDGQDIRNFNVRCLRE 467
Cdd:COG1123 5 LEVRDLSVRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEP--VLFSTTIAENIRYG--RGNVTMDEIKKAVKEANAYDFImklpqkfDTLVGDRGAQLSGGQKQRIAIARA 543
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGL-------ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 544 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELI 615
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
389-610 |
1.95e-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: 159.89 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 389 GNLEFSDVHFSYpsRANI-KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 467
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFSTTIAENI-RYGRgnVTMDEIKKAVKeanaydfimklpqkfdtlVGDRGAQLSGGQKQRIAIARALVR 546
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 547 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 610
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
391-620 |
2.28e-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: 2.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF-NVRCLREFI 469
Cdd:TIGR04520 1 IEVENVSFSYPE-SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIA 541
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 542 RALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG------SHSE 613
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228
|
....*..
gi 6981354 614 LIKKEGI 620
Cdd:TIGR04520 229 LLKEIGL 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
391-609 |
3.38e-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: 159.61 E-value: 3.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclREFIG 470
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFST-TIAENIRYG--RGNVTMDEIKKAVKEANAydfimklpqkfdtLVGDRG------AQLSGGQKQRIAIA 541
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLE-------------LVGLEGllnrypHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 609
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
391-616 |
9.56e-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: 159.37 E-value: 9.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-- 468
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 -IGVVSQEPVLFST-TIAENIRYG---RGNVTMDEIKKAVkeanaydfIMKLpqkfdTLVGDRGA------QLSGGQKQR 537
Cdd:COG1127 83 rIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 6981354 615 IK 616
Cdd:COG1127 230 LA 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
391-614 |
2.27e-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: 161.80 E-value: 2.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------RNfnvr 463
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 464 clrefIGVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIKKAVKEANAydfIMKLPQkfdtlVGDRG-AQLSGGQKQRI 538
Cdd:COG3842 79 -----VGMVFQDYALFPhLTVAENVAFGlrmRG-VPKAEIRARVAELLE---LVGLEG-----LADRYpHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 539 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSE 613
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222
|
.
gi 6981354 614 L 614
Cdd:COG3842 223 I 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1032-1232 |
3.24e-43 |
|
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: 166.38 E-value: 3.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQL 1111
Cdd:TIGR02868 334 TLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 GIVSQEPILFDCSIAKN--IAYGDnsrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALI 1189
Cdd:TIGR02868 412 SVCAQDAHLFDTTVRENlrLARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6981354 1190 RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRL 1232
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
391-615 |
4.79e-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: 4.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFS-TTIAENIrygrGNV-TMDEIKKAVKEANAYDfIMKL----PQKFdtlvGDR-GAQLSGGQKQRIAIARA 543
Cdd:cd03295 79 YVIQQIGLFPhMTVEENI----ALVpKLLKWPKEKIRERADE-LLALvgldPAEF----ADRyPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 544 LVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRL-STVRNADVIAGFEDGVIVEQGSHSELI 615
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1042-1253 |
5.45e-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: 156.51 E-value: 5.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1042 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL---RAQLGIVSQE 1117
Cdd:cd03257 11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1118 PI-----LFdcSIAKNIAygdnsrvvsqdEIVRAAKEANIHPFIETLPQKYETRVGDKGT-------QLSGGQKQRIAIA 1185
Cdd:cd03257 91 PMsslnpRM--TIGEQIA-----------EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryphELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1186 RALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1253
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
392-603 |
5.81e-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: 153.94 E-value: 5.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 392 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 471
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 472 VSQepvlfsttiaenirygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 552 LLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFEDG 603
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
391-614 |
9.27e-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: 156.89 E-value: 9.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRA-NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFI 469
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVL-----FS--TTIAENIR-YGRGNVtMDEIKKAVKEANaydfimkLPqkfDTLVGDRGAQLSGGQKQRIAIA 541
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRiHGLPDR-EERIAELLEQVG-------LP---PSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 542 RALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADL 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
391-618 |
1.74e-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: 155.97 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVL-FSTTIAENIRYGR-------GNVT---MDEIKKAVKEANAYDFIMKLpqkFDTlvgdrgaqLSGGQKQRIA 539
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfGRPSaedREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 540 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELIK 616
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
..
gi 6981354 617 KE 618
Cdd:COG1120 228 PE 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1044-1253 |
2.75e-42 |
|
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: 154.21 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILFD- 1122
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPqkyetrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1199 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHG 1253
Cdd:cd03259 156 EPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
391-586 |
6.25e-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: 154.86 E-value: 6.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclrefI 469
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVLFS-TTIAENIRYGrgnVTMDEIKKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIAIAR 542
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALG---LELRGVPKAERRERARELL--------ELVGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 586
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 ... |
391-586 |
8.35e-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: 8.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPS-RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclrefI 469
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIKKAVKEANA----YDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIA 541
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelQG-VPKAEARERAEELLElvglSGFENAYP-----------HQLSGGMRQRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6981354 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 586
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1033-1251 |
1.34e-41 |
|
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: 152.24 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEakklnVQWLRAQL 1111
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 GIVSQEPILFD-CSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpfIEtlpqkyetRVGDKGT------QLSGGQKQRIAI 1184
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-----LE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1185 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDN--GKVKE 1251
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
113-626 |
1.48e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 167.46 E-value: 1.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 113 YAYYYSGLGGGVLLAAYIQvSFWTLAAG-RQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGM 191
Cdd:PLN03232 952 YIVVYALLGFGQVAVTFTN-SFWLISSSlHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 192 F----FQAIATFFAGFIVGFIRGWKLT--LVIMAITAILGLSTAVWAKILSTFSDKELAAYAKagavaeEALGAIRTVIA 265
Cdd:PLN03232 1031 FmnqlWQLLSTFALIGTVSTISLWAIMplLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFG------EALNGLSSIRA 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 266 FGGQNKELERYQKHLENAKKIGIKkAISAN-------ISMGIAFLLIYASYALAFW--------YGSTLVISKEYTIgNA 330
Cdd:PLN03232 1105 YKAYDRMAKINGKSMDNNIRFTLA-NTSSNrwltirlETLGGVMIWLTATFAVLRNgnaenqagFASTMGLLLSYTL-NI 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 331 MTVFFSILIGAFSVGQAAPCIDAFPNARGAAYVIFDIIDNNPKIDSFSERGhkpdSIKgnleFSDVHFSYpsRANIK-IL 409
Cdd:PLN03232 1183 TTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG----SIK----FEDVHLRY--RPGLPpVL 1252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 410 KGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIR- 488
Cdd:PLN03232 1253 HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDp 1332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 489 YGRGNVTmdEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV 568
Cdd:PLN03232 1333 FSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 569 QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEG-IYFRLVN 626
Cdd:PLN03232 1411 QRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVH 1469
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
391-605 |
1.68e-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: 151.91 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRN--FNVRCLREF 468
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGVVSQEPVLFS-TTIAENIRYGRgnVTMDEIKKAVKEANAYDFIMK--LPQKFDtlvgDRGAQLSGGQKQRIAIARALV 545
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 546 RNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVI 605
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1047-1261 |
2.16e-41 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 152.46 E-value: 2.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF 1121
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1122 -DCSIAKNIAYGdnSRVV---SQDEIVRAAKEAnihpfietLpqkyeTRVG--DKG----TQLSGGQKQRIAIARALIRQ 1191
Cdd:COG1126 90 pHLTVLENVTLA--PIKVkkmSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1192 PRVLLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:COG1126 155 PKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1051-1202 |
4.20e-41 |
|
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: 148.18 E-value: 4.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILF-DCSIAKNI 1129
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1130 AYGDNSRvvsqdEIVRAAKEANIHPFIETLPQKY--ETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1202
Cdd:pfam00005 81 RLGLLLK-----GLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1045-1260 |
5.43e-41 |
|
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: 151.49 E-value: 5.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1045 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEP------ 1118
Cdd:COG1124 15 GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPyaslhp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1119 ------ILFDCSIAKNIAYgdnsrvvSQDEIVRAAKEANihpfietLPQKYETRVGDkgtQLSGGQKQRIAIARALIRQP 1192
Cdd:COG1124 95 rhtvdrILAEPLRIHGLPD-------REERIAELLEQVG-------LPPSFLDRYPH---QLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1193 RVLLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:COG1124 158 ELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
391-616 |
1.02e-40 |
|
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: 150.34 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-- 468
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 -IGVVSQEPVLF-STTIAENIRYG---RGNVTMDEIKKAVKeanaydfiMKLpqkfdTLVGDRG------AQLSGGQKQR 537
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlreHTRLSEEEIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEVQA-ALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDlIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 6981354 615 IK 616
Cdd:cd03261 225 RA 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1033-1261 |
2.51e-40 |
|
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: 157.37 E-value: 2.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGTVLLDGQEAKKLNVQWLRA 1109
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQEPI--LFDCSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETrvgdkgtQLSGGQKQRIAIARA 1187
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1188 LIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1032-1254 |
3.02e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 152.94 E-value: 3.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQL 1111
Cdd:COG3842 5 ALELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 GIVSQEPILF-DCSIAKNIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPqkyetrvgdkgTQLSGGQKQRIAIAR 1186
Cdd:COG3842 80 GMVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYP-----------HQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1187 ALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVIDNGKVKEHGT 1254
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
391-616 |
7.21e-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: 7.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGTISIDGQDIRNFNVRCLR 466
Cdd:COG0444 2 LEVRNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 467 EF----IGVVSQEPvlFS---------TTIAENIRYGRGnVTMDEIKKAVKEA-------NAYDFIMKLPQkfdtlvgdr 526
Cdd:COG0444 82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRIHGG-LSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 527 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIA- 598
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAv 223
|
250 260
....*....|....*....|
gi 6981354 599 --GfedGVIVEQGSHSELIK 616
Cdd:COG0444 224 myA---GRIVEEGPVEELFE 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
391-619 |
7.98e-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: 7.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREfIG 470
Cdd:COG4555 2 IEVENLSKKYGKV---PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFST-TIAENIRY-GRGNvtmdEIKKAVKEANAYDFI--MKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVR 546
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfAELY----GLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 547 NPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKEG 619
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
391-614 |
1.16e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 150.99 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------RNfnvr 463
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdRN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 464 clrefIGVVSQEPVLF-STTIAENIRYG---RGnVTMDEIKKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIA 539
Cdd:COG3839 77 -----IAMVFQSYALYpHMTVYENIAFPlklRK-VPKAEIDRRVREAAE---LLGL----EDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 540 IARALVRNPKILLLDEATSALD------TESE-AEVQAALdkareGRTTIVIAH------RLstvrnADVIAGFEDGVIV 606
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHdqveamTL-----ADRIAVMNDGRIQ 213
|
....*...
gi 6981354 607 EQGSHSEL 614
Cdd:COG3839 214 QVGTPEEL 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1033-1261 |
1.87e-39 |
|
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: 146.57 E-value: 1.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGTVLLDGQEAKKLN---VQ 1105
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1106 WLRAQLGIVSQEPILFDC-SIAKNIAYGDNSRVVSQDEIVRAAKEanihpfieTLPQkyetrVG--DKG----TQLSGGQ 1178
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLE--------LLEL-----VGleDKAdaypAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1179 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTH 1255
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*.
gi 6981354 1256 QQLLAQ 1261
Cdd:cd03258 226 EEVFAN 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
392-620 |
2.83e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.44 E-value: 2.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 392 EFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 471
Cdd:PRK13632 9 KVENVSFSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 472 VSQEP--VLFSTTIAENIRYGRGN--VTMDEIKK----AVKEANAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIARA 543
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGLENkkVPPKKMKDiiddLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 544 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGI 620
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1033-1251 |
3.91e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.57 E-value: 3.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGTVLLDGQEAKKLN----V 1104
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1105 QWLRAQLGIVSQEPILFDC-SIAKNIA----YGDNSRVVSQDEIVRAAKEANIHPFIETLPqkyetrvgdkgTQLSGGQK 1179
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1180 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIDNGKVKE 1251
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
392-613 |
4.53e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 149.18 E-value: 4.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 392 EFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-- 468
Cdd:PRK11153 3 ELKNISKVFPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 -IGVVSQE-PVLFSTTIAENIRYGR--GNVTMDEIKKAVKE----------ANAYdfimklPqkfdtlvgdrgAQLSGGQ 534
Cdd:PRK11153 83 qIGMIFQHfNLLSSRTVFDNVALPLelAGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 535 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIV-IAHRLSTVRN-ADVIAGFEDGVIVEQGSH 611
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQGTV 225
|
..
gi 6981354 612 SE 613
Cdd:PRK11153 226 SE 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1047-1261 |
7.04e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 145.21 E-value: 7.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlRAQLGIVSQEPILF-DCSI 1125
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGYVPQEPALYpDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 AKNIAYGDNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1203
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDEL-----LELfgLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1204 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:COG1131 162 LDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
391-605 |
1.02e-38 |
|
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: 142.15 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIG 470
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFST-TIAENIRYgrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqlSGGQKQRIAIARALVRNPK 549
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 550 ILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVI 605
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1033-1262 |
1.70e-38 |
|
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: 145.27 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAK-KLNVQWLRAQL 1111
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 GIVSQEPilfD----CSIAKN-IAYGDNSRVVSQDEIVR----AAKEANIHPFIETLPQKyetrvgdkgtqLSGGQKQRI 1182
Cdd:TIGR04520 80 GMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHL-----------LSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 6981354 1261 QK 1262
Cdd:TIGR04520 226 QV 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1033-1251 |
2.22e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 144.46 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEakklnVQWLRAQL 1111
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 GIVSQEPILFD-CSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpfIEtlpqkyetRVGDKG------TQLSGGQKQRIAI 1184
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERAREL-----LE--------LVGLAGfedaypHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1185 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVIDN--GKVKE 1251
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
82-364 |
2.81e-38 |
|
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: 145.01 E-value: 2.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 82 FVDNAGNFSLPVNFslsmlnpGRILE--------EEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHA 153
Cdd:cd18557 6 LISSAAQLLLPYLI-------GRLIDtiikggdlDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 154 ILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAK 233
Cdd:cd18557 79 LLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 234 ILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAF 313
Cdd:cd18557 159 YIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 6981354 314 WYGSTLVISKEYTIGNAMT-VFFSILIgAFSVGQAAPCIDAFPNARGAAYVI 364
Cdd:cd18557 239 WYGGYLVLSGQLTVGELTSfILYTIMV-ASSVGGLSSLLADIMKALGASERV 289
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
391-607 |
3.39e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.50 E-value: 3.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQD---IRNFNVRCLRE 467
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQE-PVLFSTTIAENIRY-----GRgnvTMDEIKKAVKEAnaydfIMK--LPQKFDTLVgdrgAQLSGGQKQRIA 539
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGK---SRKEIRRRVREV-----LDLvgLSDKAKALP----HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 540 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRNAD--VIAgFEDGVIVE 607
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
391-609 |
3.66e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 143.64 E-value: 3.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD--P---TEGTISIDGQDI--RNFNVR 463
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 464 CLREFIGVVSQEPVLFSTTIAENIRYG------RGNVTMDEI-KKAVKEANAYDfimklpqkfdtLVGDR----GAQLSG 532
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWD-----------EVKDRlkksALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREgRTTIVI-------AHRLStvrnaDVIAGFEDGVI 605
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGEL 231
|
....
gi 6981354 606 VEQG 609
Cdd:COG1117 232 VEFG 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
391-614 |
4.93e-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: 4.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-- 468
Cdd:COG3638 3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 -IGVVSQEPVLFS-TTIAENI-----------RYGRGNVTMDEIKKAvkeanaydfimklpqkFDTL--VG------DRG 527
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVlagrlgrtstwRSLLGLFPPEDRERA----------------LEALerVGladkayQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 528 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGV 604
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
250
....*....|
gi 6981354 605 IVEQGSHSEL 614
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1038-1259 |
4.94e-38 |
|
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: 143.26 E-value: 4.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1038 VVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1117
Cdd:COG1120 7 LSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1118 PIL-FDCSIAKNIAYG------DNSRVVSQD-EIVRAA-KEANIHPFIEtlpQKYetrvgdkgTQLSGGQKQRIAIARAL 1188
Cdd:COG1120 84 PPApFGLTVRELVALGryphlgLFGRPSAEDrEAVEEAlERTGLEHLAD---RPV--------DELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1189 IRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
398-1265 |
5.94e-38 |
|
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: 155.45 E-value: 5.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 398 FSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnvrclrefIGVVSQEPV 477
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 478 LFSTTIAENIRYGrgnVTMDEIK--KAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:TIGR01271 498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 556 ATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL-------------------- 614
Cdd:TIGR01271 575 PFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELqakrpdfsslllgleafdnf 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 615 -----------------IKKEGIYFR------------------------------------LVNMQTSGSQILSEEFEV 641
Cdd:TIGR01271 655 saerrnsiltetlrrvsIDGDSTVFSgpetikqsfkqpppefaekrkqsiilnpiasarkfsFVQMGPQKAQATTIEDAV 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 642 -ELSDEKAA--------------GGVAPNGW----------------------KARIFRNSTKKSLKSSRAHQ--NRLDV 682
Cdd:TIGR01271 735 rEPSERKFSlvpedeqgeeslprGNQYHHGLqhqaqrrqsvlqlmthsnrgenRREQLQTSFRKKSSITQQNElaSELDI 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 683 ---------------ETNELD---------ANVPPV-SFLKVLRLNKTEWPYFVVGTLCAIANGAlQPAFSIILSEMIAI 737
Cdd:TIGR01271 815 ysrrlskdsvyeiseEINEEDlkecfaderENVFETtTWNTYLRYITTNRNLVFVLIFCLVIFLA-EVAASLLGLWLITD 893
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 738 FGPGDDTVKQQKCNMFSL-----VFLGLGVHSFFTF-------------FLQGFTFGKAGEILTTRLRSMAFKAMLRQDM 799
Cdd:TIGR01271 894 NPSAPNYVDQQHANASSPdvqkpVIITPTSAYYIFYiyvgtadsvlalgFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPM 973
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 800 SWFDDHKnsTGALSTRLATDAAQVQGATG-TRLALIAQNTANLGTGIIISFIYGWqltlLLLSVVPFIAVAGIVEMKMLA 878
Cdd:TIGR01271 974 AVLNTMK--AGRILNRFTKDMAIIDDMLPlTLFDFIQLTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIMLRAYFLR 1047
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 879 GNAKRDKKEMEAAGKIATEAIENIR---TVVSLTQERKFESMYVEKLHGPYRN-SVRKAHIYGITFSISQAFMYFSYAGC 954
Cdd:TIGR01271 1048 TSQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHTANwFLYLSTLRWFQMRIDIIFVFFFIAVT 1127
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 955 F-RFGSYLIVNGHMrfkDVILVFSAIVLGAVALGHASSFAPDYAKAKLSAAYLF-SLFERQP---------------LID 1017
Cdd:TIGR01271 1128 FiAIGTNQDGEGEV---GIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFiDLPQEEPrpsggggkyqlstvlVIE 1204
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1018 SYSREGMWPDkfEGSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGTVLLDGQ 1097
Cdd:TIGR01271 1205 NPHAQKCWPS--GGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGV 1280
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1098 EAKKLNVQWLRAQLGIVSQEPILFDCSIAKNIaygDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGG 1177
Cdd:TIGR01271 1281 SWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNG 1357
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1178 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQ 1257
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQK 1437
|
....*...
gi 6981354 1258 LLAQKGIY 1265
Cdd:TIGR01271 1438 LLNETSLF 1445
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1036-1261 |
8.37e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 143.62 E-value: 8.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1036 NEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVS 1115
Cdd:PRK13635 9 EHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1116 QEPilfD-----CSIAKNIAYGDNSRVVSQDEIVR----AAKEANIHPFIETLPQKyetrvgdkgtqLSGGQKQRIAIAR 1186
Cdd:PRK13635 88 QNP---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1187 ALIRQPRVLLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1042-1254 |
1.16e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.84 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1042 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGTVLLDGQEAKKLNVQWLRA---QLGIV 1114
Cdd:COG1135 11 FPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELRAarrKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1115 SQEPILFD-CSIAKNIAY-----GdnsrvVSQDEIvraakEANIHPFIEtlpqkyetRVG--DKG----TQLSGGQKQRI 1182
Cdd:COG1135 88 FQHFNLLSsRTVAENVALpleiaG-----VPKAEI-----RKRVAELLE--------LVGlsDKAdaypSQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1254
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1033-1248 |
2.08e-37 |
|
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: 139.53 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRANV--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPMAGTVLLDGQEAkklnvqwlr 1108
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGSIA--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1109 aqlgIVSQEPILFDCSIAKNIAYG---DNSRVvsqDEIVRAAKeanIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIA 1185
Cdd:cd03250 70 ----YVSQEPWIQNGTIRENILFGkpfDEERY---EKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1186 RALIRQPRVLLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVIDNGK 1248
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1034-1248 |
3.07e-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: 3.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1034 TFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGI 1113
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1114 VSQepilfdcsiakniaygdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkgtqLSGGQKQRIAIARALIRQPR 1193
Cdd:cd00267 78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1194 VLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIDNGK 1248
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
388-624 |
6.51e-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: 6.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 388 KGNLEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 467
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFSTTIAENIRyGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 547
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 548 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYFRL 624
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
391-614 |
6.82e-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: 139.63 E-value: 6.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-- 468
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 -IGVVSQEPVLFS-TTIAENIRYGR-----------GNVTMDEIKKAVKEANAYDFIMKLPQkfdtlvgdRGAQLSGGQK 535
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAALERVGLLDKAYQ--------RADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 536 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTVR-NADVIAGFEDGVIVEQGSHS 612
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 6981354 613 EL 614
Cdd:cd03256 231 EL 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1050-1258 |
9.58e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 139.79 E-value: 9.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--P---MAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFD 1122
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDiyDPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNIAYG-----DNSRVVsQDEIVRAA-KEANihpfietLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLL 1196
Cdd:COG1117 106 KSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1197 LDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVIDNGKVKEHGTHQQL 1258
Cdd:COG1117 178 MDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1034-1263 |
1.14e-36 |
|
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: 138.84 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1034 TFNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNvQWLRAQLGI 1113
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1114 VSQEPILFD-CSIAKNI-----AYGDNSRVVSQ--DEIVRAAKeanihpfietLPQKYETRVGDkgtqLSGGQKQRIAIA 1185
Cdd:COG4555 79 LPDERGLYDrLTVRENIryfaeLYGLFDEELKKriEELIELLG----------LEEFLDRRVGE----LSTGMKKKVALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1186 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQKG 1263
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
407-1270 |
1.26e-36 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 151.47 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGtisidgqdirnfnvRCLRE-FIGVVSQEPVLFSTTIAE 485
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG--------------RVWAErSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 486 NIRYgrgnvtMDE-----IKKAVK----EANaydfIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:PTZ00243 740 NILF------FDEedaarLADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 557 TSALDTE-SEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEgIYFRL-----VNMQTS 630
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLaaelkENKDSK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 631 GSQILSEEFEVELSDEkaaGGVAPNGWKARIFRNSTKKSLKSSRAHQNRLDVETNELDANVPPVSFLKVLRL--NKTEWP 708
Cdd:PTZ00243 889 EGDADAEVAEVDAAPG---GAVDHEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFcgGLHAAG 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 709 Y----FVVGTLCAIANGalqpafsIILSEMIA-IFGPGDDTvkqqkcnmFSLVFLGLGVHSFFTFFLQGFTFGKAGEILT 783
Cdd:PTZ00243 966 FvlatFAVTELVTVSSG-------VWLSMWSTrSFKLSAAT--------YLYVYLGIVLLGTFSVPLRFFLSYEAMRRGS 1030
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 784 TRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAqvqgatgtrlalIAQNTANLGTGIIISFIYGWQLTLLLLSVV 863
Cdd:PTZ00243 1031 RNMHRDLLRSVSRGTMSFFD--TTPLGRILNRFSRDID------------ILDNTLPMSYLYLLQCLFSICSSILVTSAS 1096
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 864 -PFIAVA----GIVEMK-MLAGNAkrdkkemeaagkiateAIENIRTVVSLTQERKFeSMYVEKLHGpyrnsvrKAHI-- 935
Cdd:PTZ00243 1097 qPFVLVAlvpcGYLYYRlMQFYNS----------------ANREIRRIKSVAKSPVF-TLLEEALQG-------SATIta 1152
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 936 YGITFSISQ-AFMYFSYAgcfrFGSYLIVNGHMRFKDVILVF-SAIVLGAVAL-------GHASSfaPDYAKAKLSAAYL 1006
Cdd:PTZ00243 1153 YGKAHLVMQeALRRLDVV----YSCSYLENVANRWLGVRVEFlSNIVVTVIALigvigtmLRATS--QEIGLVSLSLTMA 1226
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1007 FSLFE------RQ--------------------------PLIDSY-----SREGMWPDKF-------------------E 1030
Cdd:PTZ00243 1227 MQTTAtlnwlvRQvatveadmnsverllyytdevphedmPELDEEvdaleRRTGMAADVTgtvviepasptsaaphpvqA 1306
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1031 GSVTFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRA 1109
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQEPILFDCSIAKNIaygDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALI 1189
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1190 -RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQL-LAQKGIYFS 1267
Cdd:PTZ00243 1462 kKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHS 1541
|
...
gi 6981354 1268 MVN 1270
Cdd:PTZ00243 1542 MVE 1544
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1044-1248 |
1.61e-36 |
|
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: 136.16 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN--VQWLRAQLGIVSQEPILF 1121
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1122 -DCSIAKNIAYGdnsrvvsqdeivraakeanihpfietlpqkyetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1200
Cdd:cd03229 89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1201 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGK 1248
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
391-603 |
2.13e-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: 136.83 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL---YDPTEGTISIDGQdirnfnvrcl 465
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 466 refIGVVSQEPVLFSTTIAENIRYGRgnvTMDEIK-KAVKEANA--YDFIMkLPQKFDTLVGDRGAQLSGGQKQRIAIAR 542
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGK---PFDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEV--QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDG 603
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1049-1269 |
2.52e-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: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKN 1128
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1129 IaygDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1208
Cdd:cd03288 115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1209 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQK-GIYFSMV 1269
Cdd:cd03288 192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
403-614 |
2.77e-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: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF---IGVVSQEPvlF 479
Cdd:COG4608 28 VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 480 S---------TTIAENIRYgRGNVTMDEIKKAVKEanaydfIMklpqkfdTLVG------DRGA-QLSGGQKQRIAIARA 543
Cdd:COG4608 106 AslnprmtvgDIIAEPLRI-HGLASKAERRERVAE------LL-------ELVGlrpehaDRYPhEFSGGQRQRIGIARA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 544 LVRNPKILLLDEATSALDTESEAEV-------QAALdkareGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG4608 172 LALNPKLIVCDEPVSALDVSIQAQVlnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
391-605 |
3.52e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.53 E-value: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnvrcLREFIG 470
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVL---FSTTIAENI---RYGRGNVTM---DEIKKAVKEA----NAYDFImklpqkfDTLVGdrgaQLSGGQKQR 537
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsRADREAVDEAlervGLEDLA-------DRPIG----ELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVR-NADVIAGFEDGVI 605
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLV 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
413-615 |
3.63e-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: 138.55 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF----IGVVSQEPVLF-STTIAENI 487
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 488 RYG---RGNVTMDEIKKAVKEANAY---DFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:cd03294 124 AFGlevQGVPRAEREERAAEALELVgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 562 TESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELI 615
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1035-1264 |
3.68e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.59 E-value: 3.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1035 FNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIV 1114
Cdd:PRK13632 10 VENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1115 SQEPilfD-----CSIAKNIAYGDNSRVVSQDE----IVRAAKEANIHPFIETLPQKyetrvgdkgtqLSGGQKQRIAIA 1185
Cdd:PRK13632 89 FQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1186 RALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKG 1263
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
.
gi 6981354 1264 I 1264
Cdd:PRK13632 235 I 235
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
713-1005 |
4.87e-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: 4.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 713 GTLCAIANGALQPAFSIILSEMIAIFGPGDDtvkQQKCNMFSLVFLGLGV-HSFFTFFlQGFTFGKAGEILTTRLRSMAF 791
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGD---LDVLNELALILLAIYLlQSVFTFV-RYYLFNIAGERIVARLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 792 KAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGI 871
Cdd:cd18557 77 SSLLRQEIAFFDKHK--TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 872 VEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSY 951
Cdd:cd18557 155 IYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 952 AGCFRFGSYLIVNGHMRFKDVI--LVFSAIVlgAVALGHASSFAPDYAKAkLSAAY 1005
Cdd:cd18557 235 LLVLWYGGYLVLSGQLTVGELTsfILYTIMV--ASSVGGLSSLLADIMKA-LGASE 287
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1050-1249 |
7.56e-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: 135.74 E-value: 7.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF-DCSIA 1126
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltDDKKNINELRQKVGMVFQQFNLFpHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1127 KNIAYGD-NSRVVSQDEIVRAAKEanihpfietlpqkYETRVG--DKGT----QLSGGQKQRIAIARALIRQPRVLLLDE 1199
Cdd:cd03262 95 ENITLAPiKVKGMSKAEAEERALE-------------LLEKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1200 ATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:cd03262 162 PTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
391-585 |
1.75e-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: 134.46 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRC---LRE 467
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFST-TIAENIRYGR--GNVTMDEIKKAVKEANAydfIMKLPQKFDTLvgdrGAQLSGGQKQRIAIARAL 544
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALevTGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6981354 545 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA 585
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1049-1260 |
1.78e-35 |
|
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: 135.49 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNV---QWLRAQLGIVSQEPILFDC-S 1124
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAYG-DNSRVVSQDEIVRAAKEAnihpfIEtlpqkyetRVGDKGT------QLSGGQKQRIAIARALIRQPRVLLL 1197
Cdd:COG1127 99 VFENVAFPlREHTDLSEAEIRELVLEK-----LE--------LVGLPGAadkmpsELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1198 DEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
105-343 |
3.82e-35 |
|
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: 136.14 E-value: 3.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 105 ILEEEMTRYAYYYSGLGGGVLLAA---YIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKI 181
Cdd:cd07346 30 IPAGDLSLLLWIALLLLLLALLRAllsYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 182 SEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIR 261
Cdd:cd07346 110 QNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 262 TVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGA 341
Cdd:cd07346 190 VVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG-ELVAFLAYLGML 268
|
..
gi 6981354 342 FS 343
Cdd:cd07346 269 FG 270
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
392-594 |
4.04e-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: 133.43 E-value: 4.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 392 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclrefIGV 471
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 472 VSQEPVL---FSTTIAENI---RYGRGNVTMdEIKKAVKEA--NAYDFimklpqkfdtlVG-----DRG-AQLSGGQKQR 537
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmgLYGHKGLFR-RLSKADKAKvdEALER-----------VGlselaDRQiGELSGGQQQR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA 594
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEY 198
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1032-1261 |
4.52e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.59 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGTVLLDGQEAK-KLNVQwl 1107
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1108 RAQLGIVSQEPILF-DCSIAKNIAYGDNSRVVSQDEIVRAAKE----ANIHPFIETLPqkyetrvgdkgTQLSGGQKQRI 1182
Cdd:COG1118 74 ERRVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVIDNGKVKEH 1252
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQV 215
|
....*....
gi 6981354 1253 GTHQQLLAQ 1261
Cdd:COG1118 216 GTPDEVYDR 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1033-1260 |
5.92e-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: 133.97 E-value: 5.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1112
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILF-DCSIAKNIAYgdnsrVVSQDEIVRAAKEANIHPFIETL---PQKYETRVGDkgtQLSGGQKQRIAIARAL 1188
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIAL-----VPKLLKWPKEKIRERADELLALVgldPAEFADRYPH---ELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1189 IRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1033-1260 |
6.11e-35 |
|
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: 133.78 E-value: 6.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNV---QWLRA 1109
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQEPILFDC-SIAKNIAYG--DNSRvVSQDEIVRAAKE----ANIHPFIETLPqkyetrvgdkgTQLSGGQKQRI 1182
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlrEHTR-LSEEEIREIVLEkleaVGLRGAEDLYP-----------AELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1183 AIARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELR 225
|
.
gi 6981354 1260 A 1260
Cdd:cd03261 226 A 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
710-1003 |
6.15e-35 |
|
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: 135.76 E-value: 6.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDtvkQQKCNMFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSM 789
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD---LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 790 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 869
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 870 GIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYF 949
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 950 SYAGCFRFGSYLIVNGHMRFKDVILVFSAIVLGAVALGHASSFAPDYAKAKLSA 1003
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
395-586 |
6.38e-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: 6.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 395 DVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGqdiRNFNVRCLREFIGVVSQ 474
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 475 EP--VLFSTTIAENIRYGRGNVTMD--EIKKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 6981354 551 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH 586
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1033-1249 |
6.91e-35 |
|
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: 133.00 E-value: 6.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL---- 1107
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1108 RAQLGIVSQE----PILfdcSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRVGdkgtQLSGGQKQR 1181
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1182 IAIARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVIDNGKV 1249
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
391-614 |
7.19e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.20 E-value: 7.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIrNFNVRCLREFIG 470
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLF-STTIAENIRYG--RGNVTMDEIKKAVKE----------ANAYdfimklPqkfdtlvgdrgAQLSGGQKQR 537
Cdd:COG1118 79 FVFQHYALFpHMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------P-----------SQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhDELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
389-625 |
7.97e-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: 7.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 389 GNLEFSDVHFSYPSraNIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 467
Cdd:cd03288 18 GEIKIHDLCVRYEN--NLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFSTTIAENIRYGRgNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 548 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELI-KKEGIYFRLV 625
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1031-1258 |
9.61e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 136.74 E-value: 9.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1031 GSVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQeakklNVQWLRAQ 1110
Cdd:COG3839 2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-----DVTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1111 ---LGIVSQEPILFD-CSIAKNIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPqkyetrvgdkgTQLSGGQKQRI 1182
Cdd:COG3839 74 drnIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKP-----------KQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1183 AIARALIRQPRVLLLDEATSALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVIDNGKVKEH 1252
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQV 215
|
....*.
gi 6981354 1253 GTHQQL 1258
Cdd:COG3839 216 GTPEEL 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
113-686 |
9.86e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 145.27 E-value: 9.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 113 YAYYYSGLGGGVLLAAYIQvSFW----TLAAGRqirKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDK 188
Cdd:PLN03130 955 YNLIYALLSFGQVLVTLLN-SYWlimsSLYAAK---RLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVF 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 189 VGMF----FQAIATFFAGFIVGFIRGWK-LTLVIMAITAILGL-STAVWAKILSTFSDKELAAYAKagavaeEALGAIRT 262
Cdd:PLN03130 1031 VNMFlgqiFQLLSTFVLIGIVSTISLWAiMPLLVLFYGAYLYYqSTAREVKRLDSITRSPVYAQFG------EALNGLST 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 263 VIAFGGQNKELERYQKHLENAKKIGIKKaISANISMGIAF-----LLIY--ASYAL----------AFWYGSTLVISKEY 325
Cdd:PLN03130 1105 IRAYKAYDRMAEINGRSMDNNIRFTLVN-MSSNRWLAIRLetlggLMIWltASFAVmqngraenqaAFASTMGLLLSYAL 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 326 TIGNAMTVFF---SILIGAF-SVGQAAPCIDAFPNARGaayvifdIIDNNPKIDSFserghkPDSikGNLEFSDVHFSYp 401
Cdd:PLN03130 1184 NITSLLTAVLrlaSLAENSLnAVERVGTYIDLPSEAPL-------VIENNRPPPGW------PSS--GSIKFEDVVLRY- 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 402 sRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFS 480
Cdd:PLN03130 1248 -RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFS 1326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 481 TTIAENIR-YGRGNVTmdEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PLN03130 1327 GTVRFNLDpFNEHNDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 560 LDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGIYF-RLVnmQTSGS------ 632
Cdd:PLN03130 1405 VDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFsKMV--QSTGAanaqyl 1482
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 633 -QILSEEFEVELSDEKAAG------GVAPNGWkARIFRNSTKKSLKSSRAHQNRLDVETNE 686
Cdd:PLN03130 1483 rSLVFGGDEDRLAREESKAldgqrkWLASSRW-AAAAQFALAVSLTSSQNDLQSLEIEDEN 1542
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
392-609 |
1.21e-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: 131.02 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 392 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 471
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 472 VSQepvlfsttiaenirygrgnvtmdeikkAVKEANAYDFIMKLpqkFDTlvgdrgaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 552 LLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 609
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1033-1249 |
2.64e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.49 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRA 1109
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQEPILFD-CSIAKNI---AYGDNS------RVVSQDEIVRAAkEAnihpfIET--LPQKYETRVGdkgtQLSGG 1177
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERAL-EA-----LERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1178 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1047-1258 |
4.42e-34 |
|
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: 131.21 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAkkLNVQWLRAQLGIVSQEPILF-DCSI 1125
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 AKNIAYGDNSRVVSQDEIVRAAKEAnihpfietLPQ----KYETRvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1201
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEA--------LDLvqleGYANR---KPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1202 SALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQL 1258
Cdd:cd03300 159 GALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
108-329 |
6.81e-34 |
|
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: 132.28 E-value: 6.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 108 EEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGD 187
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 188 KVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFG 267
Cdd:cd18572 113 NLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 268 GQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 329
Cdd:cd18572 193 TEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
409-617 |
1.29e-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: 129.76 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclREFIGVVSQEPVLF-STTIAENI 487
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 488 RYGRGNVTMD--EIKKAVKEanaydfIMKLpQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 565
Cdd:cd03299 93 AYGLKKRKVDkkEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 566 AEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKK 617
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
391-609 |
1.34e-33 |
|
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: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------RNfnvr 463
Cdd:cd03301 1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlppkdRD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 464 clrefIGVVSQEPVLF-STTIAENIRYG--RGNVTMDEIKKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIAI 540
Cdd:cd03301 74 -----IAMVFQNYALYpHMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQI----EHLLDRKPKQLSGGQRQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 541 ARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQG 609
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
391-610 |
2.36e-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: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANI--------KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLyDPTEGTISIDGQDIRNFN- 461
Cdd:COG4172 276 LEARDLKVWFPIKRGLfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 462 --VRCLREFIGVVSQEPvlFST-----TIAENIRYG----RGNVTMDEIKKAVKEAnaydfimkLPQkfdtlVG-DRGA- 528
Cdd:COG4172 355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEA--------LEE-----VGlDPAAr 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 529 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADV 596
Cdd:COG4172 420 hryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVVRAlAHR 495
|
250
....*....|....
gi 6981354 597 IAGFEDGVIVEQGS 610
Cdd:COG4172 496 VMVMKDGKVVEQGP 509
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
391-616 |
2.80e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.52 E-value: 2.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:PRK13635 6 IRVEHISFRYPD-AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEP--VLFSTTIAENIRYGRGN--VTMDE----IKKAVKEANAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 542
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIK 616
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
107-347 |
2.84e-33 |
|
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: 130.83 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 107 EEEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIG 186
Cdd:cd18780 38 LRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 187 DKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAF 266
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 267 GGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFfsiLIGAFSVGQ 346
Cdd:cd18780 198 AKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTG-LLTSF---LLYTLTVAM 273
|
.
gi 6981354 347 A 347
Cdd:cd18780 274 S 274
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
391-614 |
3.06e-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: 128.32 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV-RCLREFI 469
Cdd:cd03224 1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVLFST-TIAENIRYGRGNVTMDEIKKAVKEAnaYDFIMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNP 548
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 549 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVI----AHRLSTVrnADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1033-1253 |
5.25e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.86 E-value: 5.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRA 1109
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQE-PILFDCSIAKNIAY-----GdnsrvVSQDEIVRAAKEAnihpfietLpqkyeTRVG--DKG----TQLSGG 1177
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREV--------L-----DLVGlsDKAkalpHELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1178 QKQRIAIARALIRQPRVLLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVIDNGKVKEHG 1253
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
391-615 |
5.52e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 128.29 E-value: 5.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDV--HFsypsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR--NFNVRCLR 466
Cdd:PRK09493 2 IEFKNVskHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 467 EFIGVVSQEPVLFSTTIA-ENIRYG----RGnvtmdeIKKAVKEANAYDFIMKlpqkfdtlVG--DRG----AQLSGGQK 535
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFGplrvRG------ASKEEAEKQARELLAK--------VGlaERAhhypSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 536 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSE 613
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222
|
..
gi 6981354 614 LI 615
Cdd:PRK09493 223 LI 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
408-614 |
5.76e-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: 5.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnVRCLREFIGVVSQEPVLFS-TTIAEN 486
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTVFQNYALFPhLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 487 IRYG--RGNVTMDEIKKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:cd03300 93 IAFGlrLKKLPKAEIKERVAEA------LDLVQ-LEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 565 EAEVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03300 166 RKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1050-1259 |
1.04e-32 |
|
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: 127.45 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAKN 1128
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1129 IAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETRvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1208
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1209 EKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:cd03299 165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1036-1249 |
1.28e-32 |
|
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: 124.82 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1036 NEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGIVS 1115
Cdd:cd03230 4 RNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1116 QEPILFDcsiakniaygdnsrvvsqDEIVRaakeanihpfiETLpqkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVL 1195
Cdd:cd03230 80 EEPSLYE------------------NLTVR-----------ENL-------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1196 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
391-627 |
1.71e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 130.84 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnVRCLREFIG 470
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--VPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFS-TTIAENIRYG--RGNVTMDEIKKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRN 547
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMVQ-LEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 548 PKILLLDEATSALDTESEAEVQAALdKA--RE-GRTTIVIAH----RLSTvrnADVIAGFEDGVIVEQGSHSElikkegI 620
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPRE------I 232
|
....*..
gi 6981354 621 YFRLVNM 627
Cdd:PRK09452 233 YEEPKNL 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
391-614 |
2.35e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.83 E-value: 2.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-I 469
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVLFST-TIAENI---RYGRGNVTMDEiKKAVKEANAydfIMK---LPQKFDTLVGDrgaqLSGGQKQRIAIAR 542
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIflgREPRRGGLIDW-RAMRRRARE---LLArlgLDIDPDTPVGD----LSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 543 ALVRNPKILLLDEATSALdteSEAEVQAALD-----KAReGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG1129 154 ALSRDARVLILDEPTASL---TEREVERLFRiirrlKAQ-GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
407-609 |
2.43e-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: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVK---SGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ---DIR-NFNVRCLREFIGVVSQEPVLF 479
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 480 S-TTIAENIRYGRGNVTMDEIKKAVKEANAYdfiMKLpqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:cd03297 88 PhLNVRENLAFGLKRKRNREDRISVDELLDL---LGL----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 559 ALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 609
Cdd:cd03297 161 ALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
408-614 |
4.07e-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: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTI-----SIDGQdiRNFN-----VRCLREFIGVVSQEPV 477
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSqqkglIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 478 LFS-TTIAENIRygRGNVTMDEIKKAVKEANAYDFIMKLpqkfdTLVGDRGA---QLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK11264 96 LFPhRTVLENII--EGPVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 554 DEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
407-616 |
7.27e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.70 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI--RNFNVRCLREFIGVVSQEP--VLFSTT 482
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 483 IAENIRYGRGNVTM--DEIKKAVKEANAydfIMKLPqkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK13637 101 IEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 561 DTESEAEVQAALDKARE--GRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIK 616
Cdd:PRK13637 176 DPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1033-1261 |
1.13e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLnvqwlRAQLG 1112
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQE-------PIL-FDCsiaknIAYGDNSRV-------VSQDEIVRAA-KEANIHPFIETlpqkyetRVGdkgtQLSG 1176
Cdd:COG1121 79 YVPQRaevdwdfPITvRDV-----VLMGRYGRRglfrrpsRADREAVDEAlERVGLEDLADR-------PIG----ELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1177 GQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIdNGKVKEHGT 1254
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGP 221
|
....*..
gi 6981354 1255 HQQLLAQ 1261
Cdd:COG1121 222 PEEVLTP 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1044-1258 |
1.27e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.16 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEPil 1120
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 FDC-----SIAKNIAYG-DNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRVGDkgtQLSGGQKQRIAIARALIRQP 1192
Cdd:COG4608 105 YASlnprmTVGDIIAEPlRIHGLASKAERRERVAEL-----LELvgLRPEHADRYPH---EFSGGQRQRIGIARALALNP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1193 RVLLLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1258
Cdd:COG4608 177 KLIVCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1047-1258 |
1.51e-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: 123.99 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSI 1125
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 AKNIAYG----DNSRVVSQDEIVRAAKEANIHPFIETLPQKYETrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEAT 1201
Cdd:cd03296 92 FDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1202 SALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQL 1258
Cdd:cd03296 165 GALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1038-1253 |
2.70e-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: 121.39 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1038 VVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNvqwlRAQLgivsqe 1117
Cdd:cd03214 5 LSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----PKEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1118 pilfdcsiAKNIAYgdnsrvVSQdeivrAAKEANIHPFIEtlpQKYetrvgdkgTQLSGGQKQRIAIARALIRQPRVLLL 1197
Cdd:cd03214 72 --------ARKIAY------VPQ-----ALELLGLAHLAD---RPF--------NELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1198 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHG 1253
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1048-1249 |
2.83e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.75 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQ-LGI--VSQEPILF-DC 1123
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPR--DAQaAGIaiIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNIAYGD---NSRVVSQDEIVRAAKEA------NIHPfietlpqkyETRVGDkgtqLSGGQKQRIAIARALIRQPRV 1194
Cdd:COG1129 95 SVAENIFLGReprRGGLIDWRAMRRRARELlarlglDIDP---------DTPVGD----LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1195 LLLDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:COG1129 162 LILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
391-614 |
2.96e-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: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREfIG 470
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS-LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFST-TIAENIRY-----GRGNVTMDEIKKAVKEanaydfIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 544
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRART----LSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 545 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
391-614 |
3.30e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 124.42 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL--REF 468
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGVVSQEP--VLFSTTIAENIRYGRGNV--TMDEIKKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAI 540
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 541 ARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1048-1261 |
3.52e-31 |
|
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: 123.91 E-value: 3.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRA----QLGIVSQEPILF-D 1122
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1199 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
391-614 |
3.67e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.35 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGTISIDGQDI---RNFNV 462
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 463 RcLREFIGVVSQEPVLFSTTIAENIRYG------RGNVTMDE-IKKAVKEANAYDFIMklpqkfDTLvGDRGAQLSGGQK 535
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVK------DRL-HDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 536 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1049-1254 |
3.95e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 126.60 E-value: 3.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAK 1127
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1128 NIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKyetrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1207
Cdd:PRK09452 106 NVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQR-------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1208 SEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVIDNGKVKEHGT 1254
Cdd:PRK09452 179 LRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1048-1260 |
4.54e-31 |
|
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: 122.16 E-value: 4.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILF-DCS 1124
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAYGDNSRVvsqdeivRAAKEANIHPFIETLPQKYEtRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1204
Cdd:cd03224 92 VEENLLLGAYARR-------RAKRKARLERVYELFPRLKE-RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1205 dteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVIDNGKVKEHGTHQQLLA 1260
Cdd:cd03224 164 ---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1044-1261 |
4.63e-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: 129.80 E-value: 4.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPMAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEPil 1120
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 fdcsiakniaYGD-NSR-----------VVSQDEIVRAAKEANIhpfIETLpqkyeTRVG-DKGT------QLSGGQKQR 1181
Cdd:COG4172 372 ----------FGSlSPRmtvgqiiaeglRVHGPGLSAAERRARV---AEAL-----EEVGlDPAArhryphEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1182 IAIARALIRQPRVLLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1254
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
....*..
gi 6981354 1255 HQQLLAQ 1261
Cdd:COG4172 510 TEQVFDA 516
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1042-1254 |
5.47e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 125.68 E-value: 5.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1042 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPMAGTVLLDGQEAKKLNVQWLRA---QLGIV 1114
Cdd:PRK11153 11 FPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1115 SQE-PILFDCSIAKNIAY-----GdnsrvVSQDEIvraakEANIHPFIEtlpqkyetRVG--DKG----TQLSGGQKQRI 1182
Cdd:PRK11153 88 FQHfNLLSSRTVFDNVALplelaG-----TPKAEI-----KARVTELLE--------LVGlsDKAdrypAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGT 1254
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1034-1249 |
6.23e-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: 122.29 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1034 TFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE---AKKLNVQWLRAQ 1110
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1111 LGIVSQEPILFD-CSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQ-----KYETRVGdkgtQLSGGQKQRIAI 1184
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERvglldKAYQRAD----QLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1185 ARALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVIDNGKV 1249
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
409-614 |
6.80e-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: 122.06 E-value: 6.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclREFIGVVSQEPVLFS-TTIAENI 487
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 488 RYG------RGNVTMDEIKKAVKEanaydfIMKLPQkFDTLvGDR-GAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:cd03296 96 AFGlrvkprSERPPEAEIRAKVHE------LLKLVQ-LDWL-ADRyPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 561 DTESEAEVQAALDKARE--GRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03296 168 DAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
391-597 |
7.45e-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: 7.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRcLREFIG 470
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFST-TIAENIR-----YGRgNVTMDEIKKAVKEanaydfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARAL 544
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 545 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRNADVI 597
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1042-1261 |
1.52e-30 |
|
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: 123.62 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1042 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GTVLLDGQEAKKLNVQWLRA----QLGI 1113
Cdd:COG0444 11 FPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1114 VSQEPI-----LFdcSIAKNIA-----YGDNSRVVSQDEIVRAAKEANIHPfietlPqkyETRVGDKGTQLSGGQKQRIA 1183
Cdd:COG0444 91 IFQDPMtslnpVM--TVGDQIAeplriHGGLSKAEARERAIELLERVGLPD-----P---ERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1184 IARALIRQPRVLLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQ 1256
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPVE 236
|
....*
gi 6981354 1257 QLLAQ 1261
Cdd:COG0444 237 ELFEN 241
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
391-614 |
1.93e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.15 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 542
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1055-1261 |
1.94e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.63 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVqwlrAQ--LGIVSQEPILFD-CSIAKNIAY 1131
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErpVSMLFQENNLFPhLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1132 GDNSR----VVSQDEIVRAAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD-- 1205
Cdd:COG3840 95 GLRPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1206 --TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:COG3840 164 lrQEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1033-1261 |
2.09e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.15 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1112
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEP--ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpfIETLP-QKYETRvgdKGTQLSGGQKQRIAIARALI 1189
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEA-----LELVGmQDFKER---EPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1190 RQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
391-606 |
2.26e-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: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPsraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREFI 469
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQepvlfsttiaenirygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPK 549
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 550 ILLLDEATSALdteSEAEVQAALD----KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIV 606
Cdd:cd03216 103 LLILDEPTAAL---TPAEVERLFKvirrLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
751-967 |
2.61e-30 |
|
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: 122.24 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 751 NMFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR 830
Cdd:cd18573 41 KTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNK--TGELVSRLSSDTSVVGKSLTQN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 831 LALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQ 910
Cdd:cd18573 119 LSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 911 ERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18573 199 ERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGEL 255
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1033-1259 |
2.85e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.58 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAK--KLNVQWLRAQ 1110
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1111 LGIVSQEPILFDCSIA-KNIAYGDNSrvvsqdeiVRAAKEANIHPFIETLPQK--YETRVGDKGTQLSGGQKQRIAIARA 1187
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGPLR--------VRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1188 LIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1044-1243 |
6.20e-30 |
|
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: 118.35 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlRAQLGIVSQEPILF-D 1122
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNIA-----YGdnsRVVSQDEIVRAAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLL 1197
Cdd:COG4133 90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6981354 1198 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1243
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
391-618 |
6.71e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 120.24 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANIKiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 542
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKE 618
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
391-614 |
7.76e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 120.20 E-value: 7.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIAR 542
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1051-1249 |
7.89e-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: 118.17 E-value: 7.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-D 1122
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNIAYG-----DNSRVVSQDEIVRAAkeaNIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLL 1197
Cdd:cd03297 90 LNVRENLAFGlkrkrNREDRISVDELLDLL---GLDHLLNRYPA-----------QLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1198 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1047-1249 |
1.44e-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: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQ-LGIvsqepilfdcsi 1125
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARrAGI------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 akniaygdnsrvvsqdeivraakeANIHpfietlpqkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL- 1204
Cdd:cd03216 78 ------------------------AMVY-------------------QLSVGERQMVEIARALARNARLLILDEPTAALt 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6981354 1205 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
391-618 |
1.55e-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: 118.65 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEG-TISIDGQDIRNFNVRCLREFI 469
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVS---------QEPVL-------FSTTiaeniryGRGNVTMDEIKKAVKEANAYdfiMKLPQKFDTLVGdrgaQLSGG 533
Cdd:COG1119 81 GLVSpalqlrfprDETVLdvvlsgfFDSI-------GLYREPTDEQRERARELLEL---LGLAHLADRPFG----TLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStvrnaDVIAGF------EDGVI 605
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIthvlllKDGRV 221
|
250
....*....|...
gi 6981354 606 VEQGSHSELIKKE 618
Cdd:COG1119 222 VAAGPKEEVLTSE 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
391-618 |
1.88e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.07 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 542
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKE 618
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1050-1250 |
1.98e-29 |
|
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: 116.97 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeaKKLNVQWLRAQLGIVSQEP--ILFDCSIAK 1127
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDVdyQLFTDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1128 NIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1207
Cdd:cd03226 92 ELLLGLKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6981354 1208 SEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVK 1250
Cdd:cd03226 161 NMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1051-1254 |
2.13e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.38 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEP--ILFDCSIA 1126
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1127 KNIAYGDNSRVVSQDEIVRAAKEAnihpfIETLPQKYETrVGDKGT-QLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1205
Cdd:PRK13637 103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1206 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1254
Cdd:PRK13637 177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
391-607 |
2.86e-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: 117.15 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAN-IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN------VR 463
Cdd:COG4181 9 IELRGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 464 clREFIGVVSQ-EPVLFSTTIAENI-----RYGRGNVTmdeiKKAVKEANAYDfimklpqkfdtlVGDRG----AQLSGG 533
Cdd:COG4181 89 --ARHVGFVFQsFQLLPTLTALENVmlpleLAGRRDAR----ARARALLERVG------------LGHRLdhypAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTVRNADVIAGFEDGVIVE 607
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1035-1253 |
3.12e-29 |
|
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: 116.48 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1035 FNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLnvqwlRAQLGIV 1114
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1115 SQEPIL---FDCSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpFIETLpqkyeTRVGDKG------TQLSGGQKQRIAIA 1185
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK----VDEAL-----ERVGLSEladrqiGELSGGQQQRVLLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1186 RALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIdNGKVKEHG 1253
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1047-1253 |
3.86e-29 |
|
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: 116.20 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ-----EAKKLNVqwlraqlGIVSQEPILF 1121
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlPPKDRDI-------AMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1122 -DCSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEA 1200
Cdd:cd03301 85 pHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPK-------QLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1201 TSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVIDNGKVKEHG 1253
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
403-607 |
4.62e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.87 E-value: 4.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF---IGVVSQEP--- 476
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrdIQMVFQDSisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 477 VLFSTTIAENIRYG-RGNVTMDEikkAVKEANAYDFI--MKLPqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK10419 102 VNPRKTVREIIREPlRHLLSLDK---AERLARASEMLraVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 554 DEATSALDTESEAEVQAALDKAREGRTT--IVIAHRLSTV-RNADVIAGFEDGVIVE 607
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1033-1249 |
5.24e-29 |
|
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: 115.97 E-value: 5.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRA 1109
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQE-PILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpfIETLPQKYETRvgDKGTQLSGGQKQRIAIARAL 1188
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAA-----LELVGLSHKHR--ALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1189 IRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNA--DLIVVIDNGKV 1249
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
764-967 |
5.34e-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: 118.51 E-value: 5.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 764 SFFTFfLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGT 843
Cdd:cd18780 56 SIATF-LRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 844 GIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLH 923
Cdd:cd18780 133 GLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKIN 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6981354 924 GPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18780 213 ESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGEL 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1040-1269 |
8.15e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.14 E-value: 8.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1040 FNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1117
Cdd:PRK13647 12 FRYKdgTKA----LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1118 P--ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEA----NIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQ 1191
Cdd:PRK13647 88 PddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1192 PRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHG-----THQQLLAQKGI 1264
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGL 236
|
....*
gi 6981354 1265 YFSMV 1269
Cdd:PRK13647 237 RLPLV 241
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
391-608 |
8.59e-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: 8.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPS------RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN--- 461
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 462 VRCLREFIGVVSQE-PVLFS--TTIAENIRYGRGNVT-MDEIKKAVKEANAYDfIMKLPqkfDTLVGDRGAQLSGGQKQR 537
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNprMTVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQ 608
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1033-1260 |
1.09e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 117.01 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN-VQWLRAQL 1111
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 GIVSQEP--ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpFIETLPQKYETRvgdKGTQLSGGQKQRIAIARALI 1189
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1190 RQPRVLLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
390-618 |
1.22e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 115.24 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 390 NLEFSDVHFSYPSRAnikilKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV--RClre 467
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaeRP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 fIGVVSQEPVLFS-TTIAENIRYG---RGNVTMDEiKKAVKEANA----YDFIMKLPqkfdtlvgdrgAQLSGGQKQRIA 539
Cdd:COG3840 73 -VSMLFQENNLFPhLTVAQNIGLGlrpGLKLTAEQ-RAQVEQALErvglAGLLDRLP-----------GQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 540 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIK 616
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
..
gi 6981354 617 KE 618
Cdd:COG3840 220 GE 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
391-614 |
1.23e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.22 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR------------ 458
Cdd:PRK10619 6 LNVIDLHKRYGEH---EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 459 -NFNVRCLREFIGVVSQEPVLFS-TTIAENIRygRGNVTMDEIKKAVKEANAYDFIMKLPQKfDTLVGDRGAQLSGGQKQ 536
Cdd:PRK10619 83 dKNQLRLLRTRLTMVFQHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNADVIAGF-EDGVIVEQGSHSEL 614
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1258 |
1.28e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.39 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1112
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPI-LFDCSIAK-NIAYGDNSRVVSQDEIVR----AAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIAR 1186
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRrvseALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1187 ALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQL 1258
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1050-1254 |
1.58e-28 |
|
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: 115.23 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGIVS--QEPILF-DCSIA 1126
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1127 KNI----------AYGDNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRV 1194
Cdd:cd03219 94 ENVmvaaqartgsGLLLARARREEREARERAEEL-----LERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1195 LLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1254
Cdd:cd03219 165 LLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
391-617 |
2.11e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.42 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRA--NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI----RNFNVRC 464
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 465 LREFIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDeIKKAvkEANAYDFIMKLPQKFDTLvGDRGAQLSGGQKQRIAIAR 542
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIKK 617
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
710-967 |
2.30e-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: 116.49 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALqPAFsiiLSEMI--AIFGPGDDTVKQqkcNMFSLVFLGLGvHSFFTFfLQGFTFGKAGEILTTRLR 787
Cdd:cd18572 2 FVFLVVAALSELAI-PHY---TGAVIdaVVADGSREAFYR---AVLLLLLLSVL-SGLFSG-LRGGCFSYAGTRLVRRLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 788 SMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIA 867
Cdd:cd18572 73 RDLFRSLLRQDIAFFDATK--TGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 868 VAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFM 947
Cdd:cd18572 151 LITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQ 230
|
250 260
....*....|....*....|
gi 6981354 948 YFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18572 231 NGTQVLVLFYGGHLVLSGRM 250
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
412-617 |
2.32e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.90 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 412 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclREFIGVVSQEPVLFS-TTIAENIRYG 490
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPhMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 491 RG--NVTMDEIKKAVKEANAydfimklpqkfdtLV-----GDRGA-QLSGGQKQRIAIARALVRNPKILLLDEATSALDt 562
Cdd:PRK11432 103 LKmlGVPKEERKQRVKEALE-------------LVdlagfEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLD- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 563 eseAEVQAAL-DKARE-----GRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSELIKK 617
Cdd:PRK11432 169 ---ANLRRSMrEKIRElqqqfNITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
391-618 |
2.78e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.05 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGTISIDGQDIRNFNVRCLRE 467
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEANA----YDFIMKLPQkfdtlvgdrgaQLSGGQKQRIA 539
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 540 IARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKK 617
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 6981354 618 E 618
Cdd:PRK13640 234 V 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
391-617 |
2.94e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.27 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI----RNFNVRC 464
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 465 LREFIGVVSQ--EPVLFSTTIAENIRYGRGN--VTMDEIKKAVKEANAydfIMKLPQKfdtlVGDRGA-QLSGGQKQRIA 539
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPEE----LLARSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 540 IARALVRNPKILLLDEATSALDTESEAEVQ---AALDKaREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELI 615
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIF 234
|
..
gi 6981354 616 KK 617
Cdd:PRK13634 235 AD 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
391-620 |
3.01e-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: 114.31 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPsraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV-RCLREFI 469
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVLFST-TIAENIR---YGRGNVtmDEIKKAVKEAnaYDFIMKLPQKFDTlvgdRGAQLSGGQKQRIAIARALV 545
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLlgaYARRDR--AEVRADLERV--YELFPRLKERRRQ----RAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 546 RNPKILLLDEATSALdteseA-----EVQAALDKAREGRTTIVI----AHRLSTVrnADVIAGFEDGVIVEQGSHSELIK 616
Cdd:COG0410 153 SRPKLLLLDEPSLGL-----ApliveEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
....
gi 6981354 617 KEGI 620
Cdd:COG0410 226 DPEV 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1050-1261 |
3.35e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.51 E-value: 3.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAKN 1128
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1129 IAYGDNSRVVSQDEIVRAAKEAnihpfIETLP-QKYETRVGDkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1207
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEA-----LELVDlAGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1208 SEKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:PRK11432 171 LRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
713-985 |
3.47e-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: 115.66 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 713 GTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKqqkCNMFSLVFLG-LGVHSFFTFFlQGFTFGKAGEILTTRLRSMAF 791
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTAS---LNQIALLLLGlFLLQAVFSFF-RIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 792 KAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGI 871
Cdd:cd18576 77 RHLQRLPLSFFHERR--VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 872 VEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERkFESM-YVEKLHGPYRNSVRKAHIYGITFSISQAFMYFS 950
Cdd:cd18576 155 LFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLLFGA 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 6981354 951 YAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAVA 985
Cdd:cd18576 234 IVAVLWYGGRLVLAGELTAGDLVafLLYTLFIAGSIG 270
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
391-636 |
4.07e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 121.75 E-value: 4.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPS-RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL---- 465
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 466 REFIGVVSQEPVLFSTTIAENirygrgNVTMDEI----KKAVKEANAYDFIMKLpqKFDTLVGDRGAQLSGGQKQRIAIA 541
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQ------NVEVPAVyaglERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 542 RALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKKEGI 620
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGG 236
|
250
....*....|....*.
gi 6981354 621 YFRLVNMQTSGSQILS 636
Cdd:PRK10535 237 TEPVVNTASGWRQFVS 252
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
384-628 |
4.26e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 115.33 E-value: 4.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 384 PDSIkgnLEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ--DIRNFN 461
Cdd:PRK13636 2 EDYI---LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 462 VRCLREFIGVVSQEP--VLFSTTIAENIRYGRGNVTM--DEIKKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQR 537
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIA-HRLSTVR-NADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEImKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
250
....*....|....*
gi 6981354 615 I-KKEGIyfRLVNMQ 628
Cdd:PRK13636 230 FaEKEML--RKVNLR 242
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
108-328 |
4.72e-28 |
|
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: 115.69 E-value: 4.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 108 EEMTRYAYYYSGLGGGVLL----AAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISE 183
Cdd:cd18573 34 EIFGLSLKTFALALLGVFVvgaaANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 184 GIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTV 263
Cdd:cd18573 114 SLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTV 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 264 IAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 328
Cdd:cd18573 194 RAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVG 258
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
264-587 |
4.90e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 120.68 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 264 IAF-GGQNKELERYQKHLENAKKIgIKKAISANISMGiAFLLIYASYALAFWY--GSTLVISKEYTIGNAMTV--FFSIL 338
Cdd:COG4178 234 IALyRGEAAERRRLRRRFDAVIAN-WRRLIRRQRNLT-FFTTGYGQLAVIFPIlvAAPRYFAGEITLGGLMQAasAFGQV 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 339 IGAFSVgqaapCIDAFPN-ARGAAYVI-----FDIIDNNPKIDSFSERGHKPDSikGNLEFSDVHFSYPSRAniKILKGL 412
Cdd:COG4178 312 QGALSW-----FVDNYQSlAEWRATVDrlagfEEALEAADALPEAASRIETSED--GALALEDLTLRTPDGR--PLLEDL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISI-DGQDIrnfnvrcLrefigVVSQEPVLFSTTIAENIRY-- 489
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------L-----FLPQRPYLPLGTLREALLYpa 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 490 GRGNVTMDEIKKAVKEANaydfIMKLPQKFDTlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQ 569
Cdd:COG4178 451 TAEAFSDAELREALEAVG----LGHLAERLDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
330
....*....|....*...
gi 6981354 570 AALDKAREGRTTIVIAHR 587
Cdd:COG4178 526 QLLREELPGTTVISVGHR 543
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1020-1277 |
5.88e-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: 123.13 E-value: 5.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1020 SREGMWPDKFE---------GSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG 1090
Cdd:TIGR00957 615 SHEELEPDSIErrtikpgegNSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1091 TVLLDGQEAkklnvqwlraqlgIVSQEPILFDCSIAKNIAYGDNSrvvsQDEIVRAAKEA-NIHPFIETLPQKYETRVGD 1169
Cdd:TIGR00957 694 HVHMKGSVA-------------YVPQQAWIQNDSLRENILFGKAL----NEKYYQQVLEAcALLPDLEILPSGDRTEIGE 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1170 KGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL---DKAREGRTCIVIAHRLSTIQNADLIVVIDN 1246
Cdd:TIGR00957 757 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSG 836
|
250 260 270
....*....|....*....|....*....|.
gi 6981354 1247 GKVKEHGTHQQLLAQKGIYFSMVNIQAGTQN 1277
Cdd:TIGR00957 837 GKISEMGSYQELLQRDGAFAEFLRTYAPDEQ 867
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
391-601 |
6.89e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.36 E-value: 6.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGTISIDGQDI--RNFNVR 463
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 464 CLREFIGVVSQEPVLFSTTIAENIRYG------RGNVTMDEI-KKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQ 536
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFE 601
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFK 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1044-1246 |
1.18e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.80 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPIL 1120
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 FD-CSIAKNIAYG---DNSRVVSQDEIVRAAKEANIHPFIETLPqkyetrvgdkgTQLSGGQKQRIAIARALIRQPRVLL 1196
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1197 LDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIDN 1246
Cdd:COG4136 157 LDEPFSKLDAAlRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
390-612 |
1.26e-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: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 390 NLEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIrNFN-------V 462
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSqkpsekaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 463 RCLREFIGVVSQE----PVLfstTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLvgdrGAQLSGGQKQRI 538
Cdd:COG4161 78 RLLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 539 AIARALVRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 612
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQvVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
391-609 |
1.50e-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: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHF---SYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGTISIDGQDIRNFNVRCL 465
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 466 refIGVVSQEPVLFST-TIAENIrygrgnvtmdeikkavkeanayDFIMKLpqkfdtlvgdRGaqLSGGQKQRIAIARAL 544
Cdd:cd03213 84 ---IGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 545 VRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTvrnaDVIAGFEDGVIVEQG 609
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQG 188
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1031-1265 |
2.03e-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: 113.41 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1031 GSVTFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGTVLLDGQEAKKLNVQWLRAQ 1110
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1111 LGIVSQEPILFDCSIAKNI-AYGDNSrvvsQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALI 1189
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1190 RQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIY 1265
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1054-1262 |
2.39e-27 |
|
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: 115.21 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1054 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-DCSIAKN 1128
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1129 IAYG-----DNSRVVSQDEIVRAAkeaNIHPFIETLPQKyetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSA 1203
Cdd:TIGR02142 96 LRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1204 LDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQK 1262
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
391-616 |
2.44e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 113.39 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYP--SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR----NFNVRC 464
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 465 LREFIGVVSQ--EPVLFSTTIAENIRYGRGN--VTMDEIK-KAVKeanaydFIMKLPQKfDTLVGDRGAQLSGGQKQRIA 539
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKeKALK------WLKKVGLS-EDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 540 IARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHrlstvrNADVIAGFEDGVIVEQgsHSELIK 616
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVLE--HGKLIK 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1049-1267 |
2.86e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 115.32 E-value: 2.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKklNVQWLRAQLGIVSQEPILF-DCSIAK 1127
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1128 NIAYGdnsrvVSQDEIVRAAKEANIHPFIETLP-QKYETRvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1206
Cdd:PRK11607 111 NIAFG-----LKQDKLPKAEIASRVNEMLGLVHmQEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1207 ESEKVVQ-EALD-KAREGRTCIVIAH-RLSTIQNADLIVVIDNGKVKEHGTHQQLLAQKGIYFS 1267
Cdd:PRK11607 183 KLRDRMQlEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
391-623 |
3.59e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.91 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSR-------ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN-- 461
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 462 -VRCLREFIGVVSQ-----------------EPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYdfimklPQKFdtlv 523
Cdd:PRK11308 86 aQKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY------PHMF---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 524 gdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIV-IAHRLSTVRN-ADVIAGF 600
Cdd:PRK11308 156 -------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQELGLSYVfISHDLSVVEHiADEVMVM 228
|
250 260
....*....|....*....|...
gi 6981354 601 EDGVIVEQGShselikKEGIYFR 623
Cdd:PRK11308 229 YLGRCVEKGT------KEQIFNN 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1260 |
4.62e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.81 E-value: 4.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYptRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLL------DGQEAKKL 1102
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1103 NVqwLRAQLGIVSQ--EPILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRvgdKGTQLSGGQ 1178
Cdd:PRK13634 81 KP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IELvgLPEELLAR---SPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1179 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1254
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....*.
gi 6981354 1255 HQQLLA 1260
Cdd:PRK13634 230 PREIFA 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1038-1260 |
5.04e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.11 E-value: 5.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1038 VVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQE 1117
Cdd:PRK13642 10 LVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1118 P--ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpFIETLPQKYETRvgdKGTQLSGGQKQRIAIARALIRQPRVL 1195
Cdd:PRK13642 90 PdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEA----LLAVNMLDFKTR---EPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1196 LLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
391-614 |
5.99e-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: 5.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLLQRLYDPTEGTISIDGQDIRNFNVRCL 465
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVeAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 466 REF----IGVVSQEPV-----LFS--TTIAENIRYGRGnVTMDEIKKAVKEAnaydfimkLpqkfdTLVGDRGA------ 528
Cdd:COG4172 87 RRIrgnrIAMIFQEPMtslnpLHTigKQIAEVLRLHRG-LSGAAARARALEL--------L-----ERVGIPDPerrlda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 529 ---QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFED 602
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKdlQRELGMALLLITHDLGVVRRfADRVAVMRQ 232
|
250
....*....|..
gi 6981354 603 GVIVEQGSHSEL 614
Cdd:COG4172 233 GEIVEQGPTAEL 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
391-614 |
6.87e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 113.26 E-value: 6.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSD--VHFSYPSR--------ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF 460
Cdd:PRK15079 9 LEVADlkVHFDIKDGkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 461 N---VRCLREFIGVVSQEPvLFSTT--------IAENIRYGRGNVTMDEIKKAVKEanaydFIMK---LPQkfdtLVGDR 526
Cdd:PRK15079 89 KddeWRAVRSDIQMIFQDP-LASLNprmtigeiIAEPLRTYHPKLSRQEVKDRVKA-----MMLKvglLPN----LINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 527 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLSTVRN-ADVIAGFEDG 603
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlQREmGLSLIFIAHDLAVVKHiSDRVLVMYLG 238
|
250
....*....|.
gi 6981354 604 VIVEQGSHSEL 614
Cdd:PRK15079 239 HAVELGTYDEV 249
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1051-1232 |
7.55e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.41 E-value: 7.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA-----GTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFDC 1123
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNIAYGD--NSRVVSQDEIV-RAAKEAnihpfieTLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1200
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVeRSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 6981354 1201 TSALDTESEKVVQEALDKAREGRTCIVIAHRL 1232
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-614 |
7.61e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.77 E-value: 7.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 405 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLF 479
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 480 ST-TIAENIRYG----RGNVTMDEIKKAVKEAnaydfiMKLPQKFDTlVGDR----GAQLSGGQKQRIAIARALVRNPKI 550
Cdd:PRK14247 95 PNlSIFENVALGlklnRLVKSKKELQERVRWA------LEKAQLWDE-VKDRldapAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 551 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1051-1261 |
7.71e-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: 113.66 E-value: 7.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPMAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEP 1118
Cdd:COG4148 11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1119 ILFD-CSIAKNIAYG-----DNSRVVSQDEIVRAakeANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQP 1192
Cdd:COG4148 87 RLFPhLSVRGNLLYGrkrapRAERRISFDEVVEL---LGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1193 RVLLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:COG4148 153 RLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1045-1262 |
1.02e-26 |
|
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: 111.05 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1045 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRA---QLGIVSQepilf 1121
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1122 DCSIAKNI------AYGDNSR-VVSQDEIVRAAKEANIHPFIETLPQKYETRvgdkGTQLSGGQKQRIAIARALIRQPRV 1194
Cdd:TIGR02769 96 DSPSAVNPrmtvrqIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKL----PRQLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1195 LLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQK 1262
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
395-617 |
1.09e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 111.33 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 395 DVHFSYPSRANIK---ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF-NVRCLREFIG 470
Cdd:PRK13633 9 NVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEA----NAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 542
Cdd:PRK13633 89 MVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELIKK 617
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1048-1261 |
1.29e-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: 115.94 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRA----QLGIVSQEPI 1119
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1120 -----LFdcSIAKNIAygdnsrvvsqdEIVR---------AAKEAnihpfIETL-----PQKyETRVGDKGTQLSGGQKQ 1180
Cdd:COG4172 103 tslnpLH--TIGKQIA-----------EVLRlhrglsgaaARARA-----LELLervgiPDP-ERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1181 RIAIARALIRQPRVLLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1253
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQG 239
|
....*...
gi 6981354 1254 THQQLLAQ 1261
Cdd:COG4172 240 PTAELFAA 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
404-618 |
1.38e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.10 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 404 ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVL-FSTT 482
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 483 IAENIRYGR-------GNVTMDEiKKAVKEAnaydfiMKLPQkFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK11231 93 VRELVAYGRspwlslwGRLSAED-NARVNQA------MEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 556 ATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIKKE 618
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1033-1254 |
1.70e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 110.66 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GTVLLDGQEAKKLNVQWLRA 1109
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQEP--ILFDCSIAKNIAYGDNSRVVSQDEIVR----AAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIA 1183
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1184 IARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGT 1254
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1050-1260 |
2.46e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.45 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV-----LLDGQE---AKKLNVQWLRAQLGIVSQEPILF 1121
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARslsQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1122 DC-SIAKNIAYGDnsrVVSQDEiVRAAKEAnihpfietLPQKYETRVGDKGTQ------LSGGQKQRIAIARALIRQPRV 1194
Cdd:PRK11264 98 PHrTVLENIIEGP---VIVKGE-PKEEATA--------RARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1195 LLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:PRK11264 166 ILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1046-1261 |
2.88e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.21 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1046 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEPilfd 1122
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 csiakniaYGD-NSR-VVSQ---------DEIVRAAKEANIHPFIEtlpqkyetRVGDKGTQ-------LSGGQKQRIAI 1184
Cdd:PRK11308 102 --------YGSlNPRkKVGQileepllinTSLSAAERREKALAMMA--------KVGLRPEHydryphmFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1185 ARALIRQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1033-1261 |
3.46e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNY---PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQW-LR 1108
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1109 AQLGIVSQEPilfDCSIAKNI-----AYGDNSRVVSQDEIVR----AAKEANIHPFietlpQKYETRVgdkgtqLSGGQK 1179
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVATIveedvAFGPENLGIPPEEIRErvdeSLKKVGMYEY-----RRHAPHL------LSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1180 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQ 1257
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
....
gi 6981354 1258 LLAQ 1261
Cdd:PRK13633 231 IFKE 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
391-617 |
3.62e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.83 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPS------RAnikiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR----NF 460
Cdd:PRK13649 3 INLQNVSYTYQAgtpfegRA----LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 461 NVRCLREFIGVVSQ--EPVLFSTTIAENIRYGRGN--VTMDEIKKAVKEanaydfimKLpqkfdTLVG------DRGA-Q 529
Cdd:PRK13649 79 DIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALARE--------KL-----ALVGiseslfEKNPfE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFEDGVIVE 607
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVL 225
|
250
....*....|
gi 6981354 608 QGSHSELIKK 617
Cdd:PRK13649 226 SGKPKDIFQD 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1047-1260 |
3.66e-26 |
|
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: 108.53 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVqWLRAQLGI--VSQEPILF-DC 1123
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNIAYGdnSRVVSQDEIVRAAKEAnIHpfiETLPQKYEtRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1203
Cdd:COG0410 94 TVEENLLLG--AYARRDRAEVRADLER-VY---ELFPRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1204 LdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:COG0410 167 L---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
409-600 |
4.24e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.10 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD--PT---EGTISIDGQDIRNFNVRC--LREFIGVVSQEPVLFST 481
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDPveVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 482 TIAENIRYG------RGNvtMDE-IKKAVKEANAYDFIM-KLPQKfdtlvgdrGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK14243 106 SIYDNIAYGaringyKGD--MDElVERSLRQAALWDEVKdKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6981354 554 DEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGF 600
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFF 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
391-618 |
5.09e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.12 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEP--VLFSTTIAENIRYGRGNVTMDE------IKKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIAR 542
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKE 618
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
52-361 |
5.11e-26 |
|
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: 109.50 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 52 LFMLLGTAMAIAhgsgLPLMMivfGEMTDKFVDNAGNFSLpvnfslsmlnpgrileeemtryaYYYSGLGGGVLLA---- 127
Cdd:cd18576 3 ILLLLSSAIGLV----FPLLA---GQLIDAALGGGDTASL-----------------------NQIALLLLGLFLLqavf 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 128 AYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGF 207
Cdd:cd18576 53 SFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 208 IRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIG 287
Cdd:cd18576 133 FISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLA 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 288 IKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMT-VFFSILIGAfSVGQAAPCIDAFPNARGAA 361
Cdd:cd18576 213 LKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQKALGAS 286
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1054-1253 |
5.35e-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: 107.19 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1054 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAKNIAYG 1132
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1133 DNSRV----VSQDEIVRAAKEANIHPFIETLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1208
Cdd:cd03298 95 LSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6981354 1209 EKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1253
Cdd:cd03298 164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
391-592 |
5.70e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.58 E-value: 5.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPS-RANikilKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ--DIRNFNVrCLRE 467
Cdd:COG3845 6 LELRGITKRFGGvVAN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRD-AIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFST-TIAENIRYGR-----GNVTMDEIKKAVKE-ANAYDFIMKLpqkfDTLVGDrgaqLSGGQKQRIAI 540
Cdd:COG3845 81 GIGMVHQHFMLVPNlTVAENIVLGLeptkgGRLDRKAARARIRElSERYGLDVDP----DAKVED----LSVGEQQRVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 541 ARALVRNPKILLLDEATSALdTESEA-EVQAALDK-AREGRTTIVIAHRLSTVR 592
Cdd:COG3845 153 LKALYRGARILILDEPTAVL-TPQEAdELFEILRRlAAEGKSIIFITHKLREVM 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
391-609 |
5.81e-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: 106.89 E-value: 5.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTvALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIG 470
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFST-TIAENIRY-GR-GNVTMDEIKKAVKEA----NAYDFimklpqkfdtlVGDRGAQLSGGQKQRIAIARA 543
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiAWlKGIPSKEVKARVDEVlelvNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 544 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 609
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
391-612 |
7.29e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.79 E-value: 7.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirNFN--------- 461
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDfsktpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 462 VRCLREFIGVVSQEPVLFS-TTIAENIRYGRGNVT-MDEiKKAVKEAnaydfiMKLPQKFD-TLVGDR-GAQLSGGQKQR 537
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPhLTVQQNLIEAPCRVLgLSK-DQALARA------EKLLERLRlKPYADRfPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 612
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1050-1253 |
7.39e-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: 106.89 E-value: 7.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD------- 1122
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPnftvref 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 ---CSIAKNIAYGDNSRvvsqdEIVRAAKEANIHPFietlpqkYETRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDE 1199
Cdd:cd03264 93 ldyIAWLKGIPSKEVKA-----RVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1200 ATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1253
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
405-609 |
7.54e-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: 106.53 E-value: 7.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 405 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREfIGVVSQEPVLFST-TI 483
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRR-IGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 484 AENIR-----YGRGNVTMDEIKKAVKEANAYDfimklpqkfdtlvgDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:cd03268 90 RENLRllarlLGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6981354 559 ALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 609
Cdd:cd03268 156 GLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1032-1254 |
8.04e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 108.68 E-value: 8.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE----AKKLNVQ 1105
Cdd:PRK13649 2 GINLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1106 WLRAQLGIVSQ--EPILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpfiETLPQKYETRVGDKGTQLSGGQKQRIA 1183
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1184 IARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1254
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
391-597 |
8.60e-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: 107.14 E-value: 8.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF--NVRCLRef 468
Cdd:cd03219 1 LEVRGLTKRF---GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLppHEIARL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 iGVVS--QEPVLFST-TIAENIRYG-----RGNVTMDEIKKAVKEANAYDF----IMKLPQKFDTLVGDrgaqLSGGQKQ 536
Cdd:cd03219 76 -GIGRtfQIPRLFPElTVLENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 537 RIAIARALVRNPKILLLDEATSALdteSEAEVQAALDK----AREGRTTIVIAHRLSTVRN-ADVI 597
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGL---NPEETEELAELirelRERGITVLLVEHDMDVVMSlADRV 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1032-1235 |
9.01e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.20 E-value: 9.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGTVLLDGQ--------EAKKLN 1103
Cdd:PRK14258 7 AIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1104 VQWLRAQLGIVSQEPILFDCSIAKNIAYGDN----SRVVSQDEIVRAA-KEANihpfietLPQKYETRVGDKGTQLSGGQ 1178
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESAlKDAD-------LWDEIKHKIHKSALDLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1179 KQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTI 1235
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
409-614 |
9.78e-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: 106.69 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIGVVSQEPvlfsttIAENIR 488
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL------SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 489 YGRGNVTM---------DEIKKAVKEANAYdfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:cd03265 89 TGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 560 LDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03265 162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1037-1262 |
1.15e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.40 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1037 EVVFNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ--EAKKLNVQWLRAQLG 1112
Cdd:PRK13636 10 ELNYNYSdgTHA----LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEP--ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPqkyetrvgDKGTQ-LSGGQKQRIAIARALI 1189
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK--------DKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1190 RQPRVLLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVIDNGKVKEHGTHQQLLAQK 1262
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
423-614 |
1.31e-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: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 423 ALVGNSGCGKSTTVQLLQRLYDPTEGTISIDG---QDI-RNFNVRCLREFIGVVSQEPVLFST-TIAENIRYGRgnvtmd 497
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSaRGIFLPPHRRRIGYVFQEARLFPHlSVRGNLLYGR------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 498 eiKKAVKEANAYDFimklpqkfDTLVG--------DRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV 568
Cdd:COG4148 103 --KRAPRAERRISF--------DEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981354 569 QAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG4148 173 LPYLERlRDELDIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPLAEV 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1049-1247 |
1.63e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.98 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLL-DGQEAkklnvqwlraqLgIVSQEPILFDCSIAK 1127
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------L-FLPQRPYLPLGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1128 NIAYGDNSRVVSQDEIVRAAKEANIHPFIETLpqkyeTRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1207
Cdd:COG4178 445 ALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6981354 1208 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNG 1247
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
390-561 |
1.92e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.55 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 390 NLEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------RNfnv 462
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelepadRD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 463 rclrefIGVVSQEPVLFS-TTIAENIRYG---RGnVTMDEIKKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRI 538
Cdd:PRK11650 78 ------IAMVFQNYALYPhMSVRENMAYGlkiRG-MPKAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRV 143
|
170 180
....*....|....*....|...
gi 6981354 539 AIARALVRNPKILLLDEATSALD 561
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
407-588 |
2.47e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.71 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnvrcLRE-----FIGVVSQEPVL--- 478
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-----LPEykrakYIGRVFQDPMMgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 479 FSTTIAEN--IRYGRGN-------VT---MDEIKKAVKEANaydfiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVR 546
Cdd:COG1101 95 PSMTIEENlaLAYRRGKrrglrrgLTkkrRELFRELLATLG-----LGLENRLDTKVG----LLSGGQRQALSLLMATLT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6981354 547 NPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRL 588
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
391-561 |
3.10e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.57 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFSTTIAENIRYGRgnvtmdEIKKAVKEANAY-DFIMK--LPqkfDTLVGDRGAQLSGGQKQRIAIARALVRN 547
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170
....*....|....
gi 6981354 548 PKILLLDEATSALD 561
Cdd:PRK10247 156 PKVLLLDEITSALD 169
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1034-1230 |
3.20e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.48 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1034 TFNEVVFNYP-TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEakklnVQWLRAQLG 1112
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFD-CSIAKNIAYGDNSRVVSQDEIVRAAKEanihpfietlpqkYETRVGDKGT------QLSGGQKQRIAIA 1185
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEE-------------LLALVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6981354 1186 RALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1230
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
405-577 |
3.23e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 405 NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRefIGVVSQEPVLFS-TTI 483
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 484 AENIRYG------RGNVTMDEIKKAVkeanaydfiMKLPQ--KFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK10851 92 FDNIAFGltvlprRERPNAAAIKAKV---------TQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180
....*....|....*....|..
gi 6981354 556 ATSALDTESEAEVQAALDKARE 577
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHE 184
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
391-609 |
3.38e-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: 104.88 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAnikilKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclREFIG 470
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFS-TTIAENIRYGRG------NVTMDEIKKAVKEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARA 543
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 544 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 609
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1047-1253 |
4.75e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 4.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEP-IL 1120
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 FDCSIAKNIAYGD--NSRVVSQDEIVRAAKEAnihpfIET--LPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLL 1196
Cdd:PRK14247 95 PNLSIFENVALGLklNRLVKSKKELQERVRWA-----LEKaqLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1197 LDEATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVIDNGKVKEHG 1253
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1039-1265 |
4.83e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.63 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1039 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV---------------LLDGQEAKKL- 1102
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnheLITNPYSKKIk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1103 NVQWLRAQLGIVSQEP--ILFDCSIAKNIAYGDNSRVVSQDEivrAAKEANIH--------PFIETLPqkyetrvgdkgT 1172
Cdd:PRK13631 110 NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYlnkmglddSYLERSP-----------F 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1173 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVK 1250
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKIL 255
|
250
....*....|....*
gi 6981354 1251 EHGTHQQLLAQKGIY 1265
Cdd:PRK13631 256 KTGTPYEIFTDQHII 270
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-614 |
6.16e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.51 E-value: 6.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ------DIRNFNVRCLREFIGVVSQEPVLFS- 480
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 481 TTIAENIRY---GRGNVTMDEIKKAVKEANAYDFIMKlpQKFDTLvGDRGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK14246 105 LSIYDNIAYplkSHGIKEKREIKKIVEECLRKVGLWK--EVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 558 SALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1046-1247 |
7.39e-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: 103.95 E-value: 7.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1046 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVL----LDGQEAKKLNVQWLRAQLGIVSQEPILF 1121
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1122 DCSIAKNIAYGDNSRVVSQDEIVRAAkeaNIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1201
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981354 1202 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIDNG 1247
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
391-586 |
8.46e-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: 8.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYP-SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclRefi 469
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVLFS-TTIAENIRYG---RGnvtmdeIKKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIA 539
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGlrlRG------VPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981354 540 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 586
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
406-621 |
9.79e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.47 E-value: 9.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISID----GQD--------------IRNFnvRCLRE 467
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKknnhelitnpyskkIKNF--KELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEP--VLFSTTIAENIRYGrgNVTMDEIKKAVKEANAYdFIMKLPQKFDTLvgDRGA-QLSGGQKQRIAIARAL 544
Cdd:PRK13631 117 RVSMVFQFPeyQLFKDTIEKDIMFG--PVALGVKKSEAKKLAKF-YLNKMGLDDSYL--ERSPfGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 545 VRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKEGIY 621
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1044-1259 |
1.06e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.39 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FD 1122
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNIAYGDN---SRVVSQDEIVRAAKEanihpfiETLPQKYETRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:PRK09536 92 FDVRQVVEMGRTphrSRFDTWTETDRAAVE-------RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1199 EATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:PRK09536 165 EPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
407-609 |
1.26e-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: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLYDP--TEGTISIDGQDIRNFNVRclrEFIGVVSQEPVLFST-T 482
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRKPDQFQ---KCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 483 IAENIRYGRGNVTMDEIKKAVKEANAYDFIMKlpQKFDTLVGD-RGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKKRVEDVLLR--DLALTRIGGnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 562 TESEAEVQAAL-DKAREGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQG 609
Cdd:cd03234 176 SFTALNLVSTLsQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
389-626 |
1.51e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 111.79 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 389 GNLEFSDVHFSYpsRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE 467
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFSTTIAENIRyGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALV-R 546
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkK 1463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 547 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELI-KKEGIYFRLV 625
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVmNRQSIFHSMV 1543
|
.
gi 6981354 626 N 626
Cdd:PTZ00243 1544 E 1544
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1051-1241 |
1.64e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.09 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILFDC 1123
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNIAYGDNSRVVSQDEIVRAAKEANIHPfiETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1203
Cdd:PRK14239 101 SIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 6981354 1204 LDTESEKVVQEALDKAREGRTCIVIAHrlsTIQNADLI 1241
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
391-614 |
1.90e-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: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------Rnfnvr 463
Cdd:TIGR03410 1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklppheR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 464 cLREFIGVVSQEPVLFST-TIAENIRYGrgnvtMDEIKKAVKEANayDFIMKL-PQKFDTLvGDRGAQLSGGQKQRIAIA 541
Cdd:TIGR03410 73 -ARAGIAYVPQGREIFPRlTVEENLLTG-----LAALPRRSRKIP--DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 542 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1036-1262 |
2.20e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.39 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1036 NEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL--RAQLGI 1113
Cdd:PRK13639 5 RDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1114 VSQEP--ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpfietlpqkyETRVGDKGTQ------LSGGQKQRIAIA 1185
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEA-------------LKAVGMEGFEnkpphhLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1186 RALIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVIDNGKVKEHGTHQQLLAQK 1262
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-609 |
2.41e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 103.77 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-----PTEGTISIDGQDIRNFNVRCL--REFIGVVSQEPVLFS 480
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 481 -TTIAENIRYG-------RGNVTMDE-IKKAVKEANAYDfimklpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK14267 99 hLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWD-------EVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 552 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHR-LSTVRNADVIAGFEDGVIVEQG 609
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
391-610 |
4.12e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.25 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANIK--------ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPTEGTISIDGQDIRNFNV 462
Cdd:PRK15134 276 LDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 463 RCL---REFIGVVSQEP---------VLfsTTIAENIRYGRGNVTMDEIKKAVKEAnaydfiMKlPQKFDTLVGDR-GAQ 529
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------ME-EVGLDPETRHRyPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNA--DVIAgFEDGVI 605
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALchQVIV-LRQGEV 504
|
....*
gi 6981354 606 VEQGS 610
Cdd:PRK15134 505 VEQGD 509
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1051-1247 |
4.30e-24 |
|
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: 102.16 E-value: 4.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLraqlgIVSQEPILFD-CSIAKNI 1129
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1130 AYGDNS-----RVVSQDEIVRaakeanihpfiETLPQKYETRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1203
Cdd:TIGR01184 76 ALAVDRvlpdlSKSERRAIVE-----------EHIALVGLTEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6981354 1204 LDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIDNG 1247
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1048-1249 |
5.23e-24 |
|
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: 102.81 E-value: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVqWLRAQLGIVS--QEPILF-DCS 1124
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFpELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIA----YGDNSRVVSQ-----------DEIVRAAKEAnihpfIET--LPQKYETRVGDkgtqLSGGQKQRIAIARA 1187
Cdd:COG0411 96 VLENVLvaahARLGRGLLAAllrlprarreeREARERAEEL-----LERvgLADRADEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1188 LIRQPRVLLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:COG0411 167 LATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
401-609 |
6.28e-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: 101.29 E-value: 6.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 401 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIrNFNVRCLREFIGVVSQEPVLFS 480
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 481 -TTIAENIRY--GRGNVTMDEIKKAVKEanaydfimkLPQKFDT--LVGDRGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:cd03266 92 rLTARENLEYfaGLYGLKGDELTARLEE---------LADRLGMeeLLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 556 ATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFEDGVIVEQG 609
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1042-1258 |
6.47e-24 |
|
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: 101.43 E-value: 6.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1042 YPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILF 1121
Cdd:cd03263 10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1122 D----------CSIAKNIAYGDNSRVVSQDEIVRAakeanihpfietLPQKYETRVGDkgtqLSGGQKQRIAIARALIRQ 1191
Cdd:cd03263 88 DeltvrehlrfYARLKGLPKSEIKEEVELLLRVLG------------LTDKANKRART----LSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1192 PRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1258
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
412-614 |
7.68e-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: 7.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 412 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGqdirnfnvRCL------------REFIGVVSQEPVLF 479
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG--------RTLfdsrkgiflppeKRRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 480 S-TTIAENIRYGRGNVTMDEikKAVKEANAYDFImklpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:TIGR02142 88 PhLSVRGNLRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 559 ALDTESEAEVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:TIGR02142 161 ALDDPRKYEILPYLERlHAEFGIPILyVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1050-1261 |
1.14e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.97 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE-------------AKKLNVQWLRAQLGIVSQ 1116
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1117 EPILFD-CSIAKNIAYGDN-----SRVVSQDEIVRAAKEANIHpfiETLPQKYETrvgdkgtQLSGGQKQRIAIARALIR 1190
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPIqvlglSKQEARERAVKYLAKVGID---ERAQGKYPV-------HLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1191 QPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1032-1255 |
1.41e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE---AKKLN---VQ 1105
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSekaIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1106 WLRAQLGIVSQE----PIL--FDCSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQkyetrvgdkgtQLSGGQK 1179
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHLtvMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPL-----------HLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1180 QRIAIARALIRQPRVLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTH 1255
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
409-636 |
1.44e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.73 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF----IGVVSQEPVLFS-TTI 483
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 484 AENIRYGrgnVTMDEIKKAVKEANAYDFIMKLpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:PRK10070 124 LDNTAFG---MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 564 SEAEVQAALDK--AREGRTTIVIAHRL-STVRNADVIAGFEDGVIVEQGSHSELIKKEG-----IYFRLVNMqtsgSQIL 635
Cdd:PRK10070 199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyvrTFFRGVDI----SQVF 274
|
.
gi 6981354 636 S 636
Cdd:PRK10070 275 S 275
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1043-1253 |
1.50e-23 |
|
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: 99.55 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1043 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGTVLLDGqeaKKLNVQWLRAQLGIVSQEPIL 1120
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 FDC-SIAKNIAYgdnsrvvsqdeivrAAKeanihpfietLpqkyetrvgdKGtqLSGGQKQRIAIARALIRQPRVLLLDE 1199
Cdd:cd03213 94 HPTlTVRETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1200 ATSALDTESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVIDNGKVKEHG 1253
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1033-1253 |
1.60e-23 |
|
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: 99.98 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlrAQLG 1112
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFDcsiakNIAYGDNSRVVSQDEIVRaakEANIHPFIETLPQKYETRvgDKGTQLSGGQKQRIAIARALIRQP 1192
Cdd:cd03268 76 ALIEAPGFYP-----NLTARENLRLLARLLGIR---KKRIDEVLDVVGLKDSAK--KKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1193 RVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1253
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
409-586 |
1.74e-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: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLrefigVVSQEPVLFS-TTIAENI 487
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 488 RYGRGNVtMDEIKKAVKEANAYDFImklpqkfdTLVGDRGA------QLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:TIGR01184 76 ALAVDRV-LPDLSKSERRAIVEEHI--------ALVGLTEAadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*..
gi 6981354 562 TESEAEVQAALDKARE--GRTTIVIAH 586
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEehRVTVLMVTH 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
393-586 |
1.99e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.92 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 393 FSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGqdirnfNVRclrefIGVV 472
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 473 SQEPVLFST-TIAENIRYGRGNV--TMDEIKKAVK--------------------EANAYDF------IMK---LPQK-F 519
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELraLEAELEELEAklaepdedlerlaelqeefeALGGWEAearaeeILSglgFPEEdL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 520 DTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAEVqaaldKAREGrTTIVIAH 586
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
391-603 |
2.24e-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: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKST----TVQLLQRLYDPTEGTISIDGQDIRNFNVRCLR 466
Cdd:cd03290 1 VQVTNGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSlllaILGEMQTLEGKVHWSNKNESEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 467 EFIGVVSQEPVLFSTTIAENIRYGrgNVTMDEIKKAVKEANAYD-FIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALV 545
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 546 RNPKILLLDEATSALDTE-SEAEVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFEDG 603
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1043-1253 |
2.72e-23 |
|
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: 99.75 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1043 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD 1122
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 -CSIAKNIAYGDNSRVVSQDEIVRAAKE-ANIHPFIETLpqkyETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1200
Cdd:cd03266 92 rLTARENLEYFAGLYGLKGDELTARLEElADRLGMEELL----DRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1201 TSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIDNGKVKEHG 1253
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
391-618 |
2.79e-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: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV-RCLREFI 469
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVLF-STTIAENIRygrgnVTMDEIKKAVKEANaydfimklpQKFDTLVGD---------RGAQLSGGQKQRIA 539
Cdd:cd03218 78 GYLPQEASIFrKLTVEENIL-----AVLEIRGLSKKERE---------EKLEELLEEfhithlrksKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 540 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HR----LSTVRNADVIAgfeDGVIVEQGSHSEL 614
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRAYIIY---EGKVLAEGTPEEI 220
|
....
gi 6981354 615 IKKE 618
Cdd:cd03218 221 AANE 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1051-1262 |
2.95e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.44 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQ--EPILFDCS 1124
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAYGDNSRVVSQDEivraAKEANIhpfietlpqKYETRVG------DKGT-QLSGGQKQRIAIARALIRQPRVLLL 1197
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1198 DEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLAQK 1262
Cdd:PRK13641 170 DEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1048-1230 |
2.96e-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: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQE-----AKKLNVQWL---RAQLGIVSQ--- 1116
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQASPREILalrRRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1117 ------------EPILfdcsiakniaygdnSRVVSQDEIVRAAKEA----NIHPFIETLPQkyetrvgdkgTQLSGGQKQ 1180
Cdd:COG4778 104 viprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLPERLWDLPP----------ATFSGGEQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1181 RIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH 1230
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
391-618 |
2.98e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVL-FSTTIAENIRYGRGnvTMDEIKKAVKEanaydfimkLPQKFDTLVG-----DRG-AQLSGGQKQRIAIARA 543
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRA--PHGLSRAEDDA---------LVAAALAQVDlahlaGRDyPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 544 LVR------NPKILLLDEATSALDTESEAEV-QAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVlRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEV 228
|
....
gi 6981354 615 IKKE 618
Cdd:PRK13548 229 LTPE 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1055-1262 |
3.02e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILFD-CSIAKNIAYGD 1133
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1134 NSRV---VSQDEIVRA-AKEANIHPFIETLPqkyetrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD---- 1205
Cdd:PRK10771 97 NPGLklnAAQREKLHAiARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1206 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLLAQK 1262
Cdd:PRK10771 166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
389-647 |
3.41e-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: 101.08 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 389 GNLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDpTEGTISIDGQDIRNFNVRCLREF 468
Cdd:cd03289 1 GQMTVKDLTAKYTEGGN-AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGVVSQEPVLFSTTIAENIR-YGRGNvtMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 548 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL--------------STVRNADVIAGF--EDGVIVEQGSH 611
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIeamlecqrflvieeNKVRQYDSIQKLlnEKSHFKQAISP 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 6981354 612 SELIKKEGIYFRLVNMQTSGSQI--LSEEFEVELSDEK 647
Cdd:cd03289 237 SDRLKLFPRRNSSKSKRKPRPQIqaLQEETEEEVQDTR 274
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1048-1251 |
3.42e-23 |
|
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: 99.82 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGTVLLDGQEAKKLN----VQWLRAQLGIVSQE--- 1117
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfql 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1118 -PILfdcSIAKNIAY-----GDNsrvvsqDEIVRAAKEanihpfietLpqkyeTRVGDKG------TQLSGGQKQRIAIA 1185
Cdd:COG4181 102 lPTL---TALENVMLplelaGRR------DARARARAL---------L-----ERVGLGHrldhypAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1186 RALIRQPRVLLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVIDNGKVKE 1251
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
391-610 |
4.20e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.83 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSraNIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN-VRCLREFI 469
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEP--VLFSTTIAENIRYGRGNVTMD--EIKKAVKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQRIAIARALV 545
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 546 RNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 610
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
391-617 |
4.69e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.96 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRANI--KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDgqDI------RNFNV 462
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 463 RCLREFIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKE-----ANAYDFIMKLPqkfdtlvgdrgAQLSGG 533
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSH 611
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*.
gi 6981354 612 SELIKK 617
Cdd:PRK13643 229 SDVFQE 234
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
126-344 |
5.07e-23 |
|
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: 100.96 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 126 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18552 54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 206 GFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:cd18552 134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSV 344
Cdd:cd18552 214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1050-1249 |
5.98e-23 |
|
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: 98.88 E-value: 5.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GTVLLDGQEAKKlnVQWLRaQLGIVSQEPILFDC-SI 1125
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 AKNIAYGDNSRV-VSQDEIVRAAKEAnihpfIETLPQKYETRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1203
Cdd:cd03234 99 RETLTYTAILRLpRKSSDAIRKKRVE-----DVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981354 1204 LDTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVIDNGKV 1249
Cdd:cd03234 174 LDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1050-1259 |
6.11e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 99.74 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---MAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILF-D 1122
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFieTLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1202
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1203 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1050-1251 |
6.12e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.15 E-value: 6.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN----------VQWL----------RA 1109
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsisavnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQEPI--LFDCSIAKNIAygdnsRVvsqDEIVRAAKEANIHpfIETLPQkyetrvgdkgtQLSGGQKQRIAIARA 1187
Cdd:PRK10419 107 TVREIIREPLrhLLSLDKAERLA-----RA---SEMLRAVDLDDSV--LDKRPP-----------QLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1188 LIRQPRVLLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKE 1251
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1032-1205 |
6.56e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.84 E-value: 6.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpMAGTVLLDGQeakklnvqwlr 1108
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGR----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1109 aqlgIVSQ-EPILFDC-------------SIAKNIAYGDNSRVVSQDEIVR----AAKEANIHPFIETLPQkyetrvgdk 1170
Cdd:PRK11650 67 ----VVNElEPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIEErvaeAARILELEPLLDRKPR--------- 133
|
170 180 190
....*....|....*....|....*....|....*
gi 6981354 1171 gtQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1205
Cdd:PRK11650 134 --ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1049-1230 |
7.95e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 99.39 E-value: 7.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEakklnVQWLRAQLGIVSQ-EPILFDCSIAK 1127
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQnEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1128 NIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYETrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1207
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*
gi 6981354 1208 SEKVVQEALDK--AREGRTCIVIAH 1230
Cdd:PRK11248 163 TREQMQTLLLKlwQETGKQVLLITH 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1049-1260 |
8.88e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 99.70 E-value: 8.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ--EAKKLNVQWLRAQLGIVSQEP--ILFDCS 1124
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAYGDNSRVVSQDEIVRAAKEAnihpfiETLPQKYETRvgDKGTQ-LSGGQKQRIAIARALIRQPRVLLLDEATSA 1203
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEA------LTLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1204 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:PRK13638 167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
391-617 |
1.33e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.22 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGTISIDGQDIRNFNV--RClR 466
Cdd:COG0396 1 LEIKNLHVSVEGK---EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPdeRA-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 467 EFIGVVSQEPV--------LFSTTIAENIRygRGNVTMDEIKKAVKEANAydfIMKLPQKFdtlvGDRG--AQLSGGQKQ 536
Cdd:COG0396 77 AGIFLAFQYPVeipgvsvsNFLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGShSE 613
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KE 226
|
....
gi 6981354 614 LIKK 617
Cdd:COG0396 227 LALE 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1045-1259 |
1.39e-22 |
|
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: 98.23 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1045 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-TVLLDGQEAKKLNVQWLRAQLGIVS---QEPIL 1120
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLVSpalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 FDCSiAKNI----AYG--DNSRVVSQDEIVRAA---KEANIHPFIEtlpQKYETrvgdkgtqLSGGQKQRIAIARALIRQ 1191
Cdd:COG1119 93 RDET-VLDVvlsgFFDsiGLYREPTDEQRERARellELLGLAHLAD---RPFGT--------LSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1192 PRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVIDNGKVKEHGTHQQLL 1259
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAGPKEEVL 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
400-614 |
1.48e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 101.26 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 400 YPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdiRNFNVRCLREFIGVVSQEPVLF 479
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 480 S-TTIAENIRYGR--GNVTMDEIKKAVKEANAydfIMKLpqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:PRK11000 88 PhLSVAENMSFGLklAGAKKEEINQRVNQVAE---VLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 557 TSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1033-1254 |
1.51e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.42 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVvfNYPTRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV----LLDGQEAKKLNV 1104
Cdd:PRK13643 2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1105 QWLRAQLGIVSQEP--ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKE-----ANIHPFIETLPqkyetrvgdkgTQLSGG 1177
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1178 QKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1254
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1045-1259 |
1.53e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.69 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1045 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDC 1123
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNIAYG--DNSRVVSQD-EIVRAA-KEANIHPFIEtlpQKYetrvgdkgTQLSGGQKQRIAIARALIR------QPR 1193
Cdd:PRK13548 92 TVEEVVAMGraPHGLSRAEDdALVAAAlAQVDLAHLAG---RDY--------PQLSGGEQQRVQLARVLAQlwepdgPPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1194 VLLLDEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:PRK13548 161 WLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
412-586 |
1.71e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.07 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 412 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnVRCLREFIGVVSQEPVLFS-TTIAENIRYG 490
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFPhMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 491 --RGNVTMDEIKKAVKE----ANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE- 563
Cdd:PRK11607 116 lkQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKl 184
|
170 180
....*....|....*....|....*.
gi 6981354 564 ---SEAEVQAALDkaREGRTTIVIAH 586
Cdd:PRK11607 185 rdrMQLEVVDILE--RVGVTCVMVTH 208
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
396-614 |
2.16e-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: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 396 VHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnvrclrefIGVVSQE 475
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 476 PVLFSTTIAENIRYGrgnVTMDEI--KKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:cd03291 107 SWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 554 DEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1046-1262 |
2.40e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1046 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDCS 1124
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAYGDN------SRVVSQDE-IVRAAKEANihpFIETLPQKyetRVgdkgTQLSGGQKQRIAIARALIRQPRVLLL 1197
Cdd:PRK11231 93 VRELVAYGRSpwlslwGRLSAEDNaRVNQAMEQT---RINHLADR---RL----TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1198 DEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLLAQK 1262
Cdd:PRK11231 163 DEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1050-1253 |
2.47e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.99 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGTVLLDGQE--AKKLNVQWLRAQLGIVSQEPILF- 1121
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1122 DCSIAKNIAYGD--NSRVVSQ---DEIVR-AAKEAnihpfieTLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVL 1195
Cdd:PRK14267 99 HLTIYDNVAIGVklNGLVKSKkelDERVEwALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1196 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlSTIQNA---DLIVVIDNGKVKEHG 1253
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1049-1242 |
3.09e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKN 1128
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1129 IAYGDNSRVVSQDEivrAAKEANIHPFieTLPqkyETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1208
Cdd:PRK10247 101 LIFPWQIRNQQPDP---AIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 6981354 1209 EKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIV 1242
Cdd:PRK10247 173 KHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVI 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
413-615 |
3.91e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnvrclrefiGVVSQEPV--------LFS-TTI 483
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT----------TPPSRRPVsmlfqennLFShLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 484 AENIRYG-RGNVTMDEIKKAVKEANAY-----DFIMKLPqkfdtlvgdrgAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK10771 89 AQNIGLGlNPGLKLNAAQREKLHAIARqmgieDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 558 SALDTESEAEVQAALDKAREGR--TTIVIAHRLS-TVRNAD---VIAgfeDGVIVEQGSHSELI 615
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPrslVVA---DGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1042-1261 |
4.31e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1042 YPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEP--I 1119
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1120 LFDCSIAKNIAYGDNSRVVSQDEIVRAAKEAnihpfIETLP-QKYETRVGDkgtQLSGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSA-----LHMLGlEELRDRVPH---HLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1199 EATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
408-605 |
4.80e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.06 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTIsIDGqdirNFNVRCLREFIGVVSQEPVLFS-TTIAEN 486
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 487 IRYG-RGNvtmdeIKKAVKEANAydfimklpqkfdtLVG--DRG----AQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PRK11247 102 VGLGlKGQ-----WRDAALQALA-------------AVGlaDRAnewpAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981354 560 LDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVI 605
Cdd:PRK11247 164 LDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
391-587 |
4.91e-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: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVhfSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISidgqdirnfnvRCLREFIG 470
Cdd:cd03223 1 IELENL--SLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFSTTIAENIRYGRGNVtmdeikkavkeanaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 6981354 551 LLLDEATSALDTESEAEVqaaLDKAREGRTTIV-IAHR 587
Cdd:cd03223 113 VFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
392-618 |
5.39e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 96.69 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 392 EFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGV 471
Cdd:COG4604 3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 472 VSQEPVLFST-TIAENIRYGR-----GNVTmDEIKKAVKEANAYDFIMKLPQKF-DtlvgdrgaQLSGGQKQRIAIARAL 544
Cdd:COG4604 80 LRQENHINSRlTVRELVAFGRfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 545 VRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLstvrN-----ADVIAGFEDGVIVEQGSHSELIKK 617
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEIITP 226
|
.
gi 6981354 618 E 618
Cdd:COG4604 227 E 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
406-610 |
5.80e-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: 96.65 E-value: 5.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV--RCLRefiGVVS--QEPVLFST 481
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhrIARL---GIARtfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 482 -TIAENIRYGRGNVTMDEIKKAV--------KEANAYDFIM------KLPQKFDTLVGDrgaqLSGGQKQRIAIARALVR 546
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEellervGLADRADEPAGN----LSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 547 NPKILLLDEATSALdteSEAEVQAALD-----KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGS 610
Cdd:COG0411 170 EPKLLLLDEPAAGL---NPEETEELAElirrlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
391-614 |
6.78e-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: 6.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAN------IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ--DIRNFNV 462
Cdd:COG4167 5 LEVRNLSKTFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHklEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 463 RCLRefIGVVSQEPvlfSTTIAENIRYG-------RGNVTMDEikkavKEANAydfimklpQKFDTL--VGDRGAQ---- 529
Cdd:COG4167 85 RCKH--IRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTA-----EEREE--------RIFATLrlVGLLPEHanfy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 530 ---LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------EVQaaldkAREGRTTIVIAHRLSTVRN-ADVIA 598
Cdd:COG4167 147 phmLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqiinlmlELQ-----EKLGISYIYVSQHLGIVKHiSDKVL 221
|
250
....*....|....*.
gi 6981354 599 GFEDGVIVEQGSHSEL 614
Cdd:COG4167 222 VMHQGEVVEYGKTAEV 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1050-1258 |
7.08e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.00 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSIAKN 1128
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1129 IAYG---------DNSRVVSQD-----EIVRAAKEANIHPfietlpqkyetrvgdkgTQLSGGQKQRIAIARALIRQPRV 1194
Cdd:PRK10851 95 IAFGltvlprrerPNAAAIKAKvtqllEMVQLAHLADRYP-----------------AQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1195 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVIDNGKVKEHGTHQQL 1258
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1050-1256 |
7.37e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 7.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDG------QEAKKLNVQWLRAQLGIVSQE----PI 1119
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1120 LfdcSIAKNIAYGDnSRV--VSQDEIVRAAKEanihpFIETLpqkyetRVGDKGT----QLSGGQKQRIAIARALIRQPR 1193
Cdd:PRK11124 97 L---TVQQNLIEAP-CRVlgLSKDQALARAEK-----LLERL------RLKPYADrfplHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1194 VLLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQ 1256
Cdd:PRK11124 162 VLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
108-345 |
7.62e-22 |
|
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: 97.17 E-value: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 108 EEMTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGD 187
Cdd:cd18575 33 ALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 188 KVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFG 267
Cdd:cd18575 113 SLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFT 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 268 GQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIgAFSVG 345
Cdd:cd18575 193 REDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGElSQFVFYAVLA-AGSVG 270
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1050-1254 |
8.39e-22 |
|
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: 95.67 E-value: 8.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlRAQLGI--VSQEPILF-DCSIA 1126
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1127 KNIAYGDNsrvvsqdeiVRAAKEANIHPFIETL-PQKYETRvGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1205
Cdd:TIGR03410 94 ENLLTGLA---------ALPRRSRKIPDEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1206 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGT 1254
Cdd:TIGR03410 164 PSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1039-1258 |
9.83e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.46 E-value: 9.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1039 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV-----------------------LLD 1095
Cdd:PRK13651 11 IFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklVIQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1096 GQEAKKL-NVQWLRAQLGIVSQ--EPILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEanihpFIET--LPQKYETRvgdK 1170
Cdd:PRK13651 91 KTRFKKIkKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIELvgLDESYLQR---S 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1171 GTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVIDNGK 1248
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
250
....*....|.
gi 6981354 1249 -VKEHGTHQQL 1258
Cdd:PRK13651 243 iIKDGDTYDIL 253
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
762-1274 |
1.36e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 102.36 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 762 VHSFFTFFlqGFTFGKAGEI--------LTTRLRSMAFKAMLRQDMSWFDD-HKN-STGALSTRLATDAAQVQgatgtrl 831
Cdd:PLN03232 342 VYAFLIFF--GVTFGVLCESqyfqnvgrVGFRLRSTLVAAIFHKSLRLTHEaRKNfASGKVTNMITTDANALQ------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 832 aLIAQNTANLGTG---IIISFIYGWQL--------TLLLLSVVPFIAVAgIVEMKMLA--GNAKRDKKEmeaagKIATEA 898
Cdd:PLN03232 413 -QIAEQLHGLWSApfrIIVSMVLLYQQlgvaslfgSLILFLLIPLQTLI-VRKMRKLTkeGLQWTDKRV-----GIINEI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 899 IENIRTVVSLTQERKFESMyVEKLHGPYRNSVRKAHIygitFSISQAFMYFS---YAGCFRFGSYLIVNGHMRFKDVILV 975
Cdd:PLN03232 486 LASMDTVKCYAWEKSFESR-IQGIRNEELSWFRKAQL----LSAFNSFILNSipvVVTLVSFGVFVLLGGDLTPARAFTS 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 976 FSAIVLGAVALGHASSFAPDYAKAKLSAAYLFSLF--ERQPLIDSYSREGMWPdkfegSVTFNEVVFNYPTRANVPVLQG 1053
Cdd:PLN03232 561 LSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLlsEERILAQNPPLQPGAP-----AISIKNGYFSWDSKTSKPTLSD 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1054 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLdgqeakklnvqwLRAQLGIVSQEPILFDCSIAKNIAYGD 1133
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFGS 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1134 NsrvVSQDEIVRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE-SEKVV 1212
Cdd:PLN03232 704 D---FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVF 780
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1213 QEALDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQlLAQKGIYFSMVNIQAG 1274
Cdd:PLN03232 781 DSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAG 841
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1051-1249 |
1.37e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEakklnVQW------LRAQLGIVSQEPILFDC- 1123
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP-----VRIrsprdaIALGIGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNIAYG-DNSRVVSQDeIVRAAKEanihpfIETLPQKY------ETRVGDkgtqLSGGQKQRIAIARALIRQPRVLL 1196
Cdd:COG3845 96 TVAENIVLGlEPTKGGRLD-RKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1197 LDEATSAL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIDNGKV 1249
Cdd:COG3845 165 LDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
406-618 |
1.50e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.69 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF------------------------N 461
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 462 VRCLREFIGVVSQ--EPVLFSTTIAENIRYGRGNVTMDEiKKAVKEANAYDFIMKLPQKFDtlvgDRGA-QLSGGQKQRI 538
Cdd:PRK13651 100 IKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 539 AIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTV--RNADVIAgFEDGVIVEQGSHSELI 615
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRTIF-FKDGKIIKDGDTYDIL 253
|
...
gi 6981354 616 KKE 618
Cdd:PRK13651 254 SDN 256
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
402-577 |
1.86e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.09 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGTISIDGQDIRNFNVRcLREfIGVVSQEPVL 478
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRR-IGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 479 FS-TTIAENIRYG-----RGNVTMDEIKKAVKEANAYDFimklpqkfdtlvGDRG-AQLSGGQKQRIAIARALVRNPKIL 551
Cdd:COG4136 88 FPhLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRALLAEPRAL 155
|
170 180
....*....|....*....|....*..
gi 6981354 552 LLDEATSALDTESEAEVQA-ALDKARE 577
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREfVFEQIRQ 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1049-1260 |
2.19e-21 |
|
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: 94.53 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVqWLRAQLGI--VSQEPILF-DCSI 1125
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 AKNIAYGDNSRVVSQDEIVRAAkEANIHPF-IETLPQKyetrvgdKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1204
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1205 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
399-595 |
2.20e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.07 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 399 SYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGqdirnfNVRclrefIGVVSQ---E 475
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------GAR-----VAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 476 PVLFSTTIAENIRYGR-------GNVTMDEiKKAVKEAnaydfIMKLpqKFDTLVGDRGAQLSGGQKQRIAIARALVRNP 548
Cdd:NF040873 67 PDSLPLTVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6981354 549 KILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRNAD 595
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1046-1253 |
2.46e-21 |
|
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: 93.50 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1046 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeaKKLNVQwLRAQLGIVSQEPILF-DCS 1124
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIA-ARNRIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAYGDNSRVVSQDEIVRAAKEanihpFIET--LPQKYETRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1202
Cdd:cd03269 87 VIDQLVYLAQLKGLKKEEARRRIDE-----WLERleLSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1203 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1253
Cdd:cd03269 158 GLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
355-645 |
3.42e-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: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 355 PNARGAAYVIFD--IIDNNPKIDSFSERGHkpdsikgnLEFSDVHFSYPSRANiKILKGLNLKVKSGQTVALVGNSGCGK 432
Cdd:TIGR01271 1188 PSGGGGKYQLSTvlVIENPHAQKCWPSGGQ--------MDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGK 1258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 433 STTVQLLQRLYDpTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTTIAENIR-YGRgnVTMDEIKKAVKEANAYDF 511
Cdd:TIGR01271 1259 STLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQ--WSDEEIWKVAEEVGLKSV 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 512 IMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL--- 588
Cdd:TIGR01271 1336 IEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVeal 1415
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 589 -----------STVRNADVIAGF--EDGVIVEQGSHSELIKKEGIYFRLVNMQTSGSQI--LSEEFEVELSD 645
Cdd:TIGR01271 1416 lecqqflviegSSVKQYDSIQKLlnETSLFKQAMSAADRLKLFPLHRRNSSKRKPQPKItaLREEAEEEVQN 1487
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1047-1254 |
4.13e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.98 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPMAGTVLLDGQEAKKLNVQwLRAQLGI-VS-QEPI-- 1119
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1120 --------LfdcSIAKNIAYGDNSRVV-SQDEIVRAAKEANihpfietLPQKYETR---VGdkgtqLSGGQKQRIAIARA 1187
Cdd:COG0396 90 pgvsvsnfL---RTALNARRGEELSAReFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1188 LIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIDNGKVKEHGT 1254
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
402-609 |
4.26e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVL-FS 480
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 481 TTIAENIRYGRGN-----VTMDEI-KKAVKEA-NAYDFIMKLPQKFDTlvgdrgaqLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTETdRAAVERAmERTGVAQFADRPVTS--------LSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 554 DEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 609
Cdd:PRK09536 164 DEPTASLDINHQVRtLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1050-1260 |
5.82e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGTVLLDGQEAKKLNVQWL---RAQLGIVSQEP---ILFDC 1123
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNIAYGDNsrvVSQDEIVRAAKEANIHPFIETLPQKYETRvGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSA 1203
Cdd:PRK15134 380 NVLQIIEEGLR---VHQPTLSAAQREQQVIAVMEEVGLDPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1204 LDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:PRK15134 456 LD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1050-1260 |
5.85e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.26 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqEAKKLNVQWLRAQLGIVSQepilFDcSIAKNI 1129
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVGVVPQ----FD-NLDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1130 AYGDNSRVVSQDEIVRAAK-EANIHPFIE--TLPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1206
Cdd:PRK13537 96 TVRENLLVFGRYFGLSAAAaRALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1207 ESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:PRK13537 172 QARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1055-1259 |
1.01e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.26 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL----RAQLGIVSQE-PILFDCSIAKNI 1129
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1130 AYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYEtrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESE 1209
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1210 KVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:PRK10070 201 TEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1038-1249 |
1.04e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.23 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1038 VVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVqWLRAQL-GIVSQ 1116
Cdd:COG1101 9 KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAKYiGRVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1117 EPILFDC---SIAKN--IAYGDNSRVvsqdEIVRAAKEANIHPFIET-------LPQKYETRVGdkgtQLSGGQKQRIAI 1184
Cdd:COG1101 88 DPMMGTApsmTIEENlaLAYRRGKRR----GLRRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1185 ARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKV 1249
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1050-1249 |
1.05e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.20 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLL------DGQEAKKLNVQWLRaqlgivsqepILFDC 1123
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgtaplaEAREDTRLMFQDAR----------LLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNIAYG--DNSRvvsqdeivRAAKEAnihpfIETLpqKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEAT 1201
Cdd:PRK11247 97 KVIDNVGLGlkGQWR--------DAALQA-----LAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1202 SALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKV 1249
Cdd:PRK11247 162 GALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
707-1262 |
1.30e-20 |
|
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: 99.21 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 707 WPYFVVGTLCAI--ANGALQPafsIILSEMIAIFGPGDDTVKQQKcnmfslVFLGLGVHSFF---TFFLQGFTFG--KAG 779
Cdd:TIGR01271 80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASYDPFNAPEREIA------YYLALGLCLLFivrTLLLHPAIFGlhHLG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 780 EILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQV-QGATGTRLALIAQNTANLGTGIIISFIYGWQLTLL 858
Cdd:TIGR01271 151 MQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFdEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 859 LLSVVPFIAVAGIVEMKMlagnAKRDKKemeaAGKIA------TEAIENIRTVVSLTQERKFESMyVEKLHGPYRNSVRK 932
Cdd:TIGR01271 229 GFLILLALFQACLGQKMM----PYRDKR----AGKISerlaitSEIIENIQSVKAYCWEEAMEKI-IKNIRQDELKLTRK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 933 AhiygitfsisqAFMYFSYAGCFRFGSYLIVNG----HMRFKDVIL--VFSA----IVL---------GAVALGHASSFA 993
Cdd:TIGR01271 300 I-----------AYLRYFYSSAFFFSGFFVVFLsvvpYALIKGIILrrIFTTisycIVLrmtvtrqfpGAIQTWYDSLGA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 994 ----PDYAKAKLSAAYLFSLFERQPLIDSYS---REGMwPDKFEGSVTFNE----------VVFNYPTRANVPVLQGLSL 1056
Cdd:TIGR01271 369 itkiQDFLCKEEYKTLEYNLTTTEVEMVNVTaswDEGI-GELFEKIKQNNKarkqpngddgLFFSNFSLYVTPVLKNISF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1057 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQeakklnvqwlraqLGIVSQEPILFDCSIAKNIAYGdnsr 1136
Cdd:TIGR01271 448 KLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFG---- 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1137 vVSQDEI--VRAAKEANIHPFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQE 1214
Cdd:TIGR01271 511 -LSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 6981354 1215 A-LDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQK 1262
Cdd:TIGR01271 590 ScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
391-620 |
1.54e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.15 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIrNFNVR---CLRE 467
Cdd:PRK13638 2 LATSDLWFRYQDE---PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEP--VLFSTTIAENIRYGRGN--VTMDEIKKAVKEANaydfimklpqkfdTLVGDRGAQ------LSGGQKQR 537
Cdd:PRK13638 78 QVATVFQDPeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG------ 609
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevf 224
|
250
....*....|.
gi 6981354 610 SHSELIKKEGI 620
Cdd:PRK13638 225 ACTEAMEQAGL 235
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
710-967 |
1.90e-20 |
|
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: 93.26 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIaifgpgDDTVKQQKCN---MFSLVFLGLGV-HSFFTFfLQGFTFGKAGEILTTR 785
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII------DSVIGGGLREllwLLALLILGVALlRGVFRY-LQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 786 LRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPF 865
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 866 IAVAGIVEMKMLaGNAKRDKKEMEAA-GKIATEAIENIRTVVSLTQErKFESMYVEKLHGPYRN-SVRKAHIYGITFSIS 943
Cdd:cd18542 152 IALFSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFARE-DYEIEKFDKENEEYRDlNIKLAKLLAKYWPLM 229
|
250 260
....*....|....*....|....
gi 6981354 944 QAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18542 230 DFLSGLQIVLVLWVGGYLVINGEI 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
391-619 |
1.91e-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: 90.66 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSypsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL-----YDPTEGTISIDGQDIRNFNV--R 463
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITDLPPeeR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 464 ClREFIGVVSQEPVLFS-TTIAENIRYgrgnvtmdeikkaVKEAnaydfimklpqkfdtlvgdrgaqLSGGQKQRIAIAR 542
Cdd:cd03217 75 A-RLGIFLAFQYPPEIPgVKNADFLRY-------------VNEG-----------------------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGSHS--ELIKK 617
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEK 197
|
..
gi 6981354 618 EG 619
Cdd:cd03217 198 KG 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1048-1248 |
2.23e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.54 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMA---GTVLLDGQEAKKLNVQWL-RAQLGIVSQEPILF-D 1122
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALVkE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNIAYGD---NSRVVSQDEIVRAAKE------ANIHPfietlpqkyETRVGDkgtqLSGGQKQRIAIARALIRQPR 1193
Cdd:PRK13549 97 LSVLENIFLGNeitPGGIMDYDAMYLRAQKllaqlkLDINP---------ATPVGN----LGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1194 VLLLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGK 1248
Cdd:PRK13549 164 LLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
406-603 |
2.33e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.15 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPT---EGTISIDGQDIRNFNVR-CLREFIGVVSQEPVLFST 481
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 482 -TIAENIRYG----RGNVtMD------EIKKAVKEanaydfiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVRNPKI 550
Cdd:PRK13549 97 lSVLENIFLGneitPGGI-MDydamylRAQKLLAQ-------LKLDINPATPVGN----LGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 551 LLLDEATSALdTESEAEVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 603
Cdd:PRK13549 165 LILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
391-620 |
2.55e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-I 469
Cdd:PRK15439 12 LCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVLF-STTIAENIRYG--RGNVTMDEIKKAVKEANAYdfiMKLPQKFDTL-VGDRgaqlsggqkQRIAIARALV 545
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 546 RNPKILLLDEATSALdTESEAE-----VQAALDKareGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKEG 619
Cdd:PRK15439 157 RDSRILILDEPTASL-TPAETErlfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDI 232
|
.
gi 6981354 620 I 620
Cdd:PRK15439 233 I 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
391-618 |
2.70e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.33 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIG 470
Cdd:PRK13537 8 IDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQ----EPvlfSTTIAENIR-YGRG-NVTMDEIKKAVkeANAYDFiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 544
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 545 VRNPKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIKKE 618
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
97-336 |
2.83e-20 |
|
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: 92.88 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 97 LSMLNPG-------RILEEEMTRYAYYYSG--LGGGVL--LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIK 165
Cdd:cd18542 14 LNLLIPLlirriidSVIGGGLRELLWLLALliLGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 166 GTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLST--------AVWAKI--- 234
Cdd:cd18542 94 RTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSyvffkkvrPAFEEIreq 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 235 ---LSTFsdkelaayakagavAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYAL 311
Cdd:cd18542 174 egeLNTV--------------LQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVL 239
|
250 260
....*....|....*....|....*
gi 6981354 312 AFWYGSTLVISKEYTIGNaMTVFFS 336
Cdd:cd18542 240 VLWVGGYLVINGEITLGE-LVAFIS 263
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1054-1261 |
2.86e-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: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1054 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlRAQLgI--VSQEPilfdcsiakNIAY 1131
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKH-IrmIFQDP---------NTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1132 GDNSRVVSQ-DEIVR-------AAKEANIhpfIETLpqkyeTRVG-------DKGTQLSGGQKQRIAIARALIRQPRVLL 1196
Cdd:COG4167 101 NPRLNIGQIlEEPLRlntdltaEEREERI---FATL-----RLVGllpehanFYPHMLSSGQKQRVALARALILQPKIII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1197 LDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:COG4167 173 ADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
391-588 |
4.28e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 95.46 E-value: 4.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDiRNFN-VRCLREF- 468
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFNgPKSSQEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGVVSQEPVLFST-TIAENIRYGRGNVT-MDEI--KKAVKEANAYDFIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARAL 544
Cdd:PRK10762 81 IGIIHQELNLIPQlTIAENIFLGREFVNrFGRIdwKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 545 VRNPKILLLDEATSAL-DTESEA------EVQAaldkarEGRTTIVIAHRL 588
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETESlfrvirELKS------QGRGIVYISHRL 201
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
391-607 |
4.49e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIdGQdirnfNVRclrefIG 470
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLF--STTIAENIRYGRGNVTmdeikkavkEANAYDFIMKL---PQKFDTLVGDrgaqLSGGQKQRIAIARALV 545
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 546 RNPKILLLDEATSALDTESEAEVQAALDkAREGrTTIVIAH-R--LSTVrnADVIAGFEDGVIVE 607
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
399-555 |
5.68e-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: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 399 SYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLLQrlydPTEGTISIDGQDIRNF--NVRClREFIGVV 472
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDITHLpmHKRA-RLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 473 SQEPVLF-STTIAENIRygrgnvtmdeikkAVKEanaydfIMKLP-----QKFDTLVGD---------RGAQLSGGQKQR 537
Cdd:COG1137 84 PQEASIFrKLTVEDNIL-------------AVLE------LRKLSkkereERLEELLEEfgithlrksKAYSLSGGERRR 144
|
170
....*....|....*...
gi 6981354 538 IAIARALVRNPKILLLDE 555
Cdd:COG1137 145 VEIARALATNPKFILLDE 162
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
391-618 |
5.91e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIG 470
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVL-FSTTIAEN-IRYGR-GNVTMDEIKKAVkeANAYDFiMKLPQKFDTLVgdrgAQLSGGQKQRIAIARALVRN 547
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRyFGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 548 PKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELIKKE 618
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
141-343 |
6.40e-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: 91.73 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 141 RQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAI 220
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 221 TAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGI 300
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6981354 301 AFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAFS 343
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTlvAFLLYLFQLITPLS 270
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1032-1262 |
6.84e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDG----QEAKKLNVQ 1105
Cdd:PRK13646 2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1106 WLRAQLGIVSQ--EPILFDCSIAKNIAYGDNSRVVSQDEIVRAAkeanihpFIETLPQKYETRVGDKGT-QLSGGQKQRI 1182
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-------HRLLMDLGFSRDVMSQSPfQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
...
gi 6981354 1260 AQK 1262
Cdd:PRK13646 235 KDK 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1049-1261 |
7.34e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----MAGTVLLDGQEAKKLNVQWLRA----QLGIVSQEPI 1119
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1120 -----LFdcSIAKNIA-----YGDNSRVVSQDEIVRAAKEANIHpfietlpqKYETRVGDKGTQLSGGQKQRIAIARALI 1189
Cdd:PRK15134 103 vslnpLH--TLEKQLYevlslHRGMRREAARGEILNCLDRVGIR--------QAAKRLTDYPHQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1190 RQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
408-620 |
7.63e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.82 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVL-FSTTIAEN 486
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 487 IRYGRG------NVTMDEIKKAVKEANAYDFIMKLP-QKFDTlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PRK10253 102 VARGRYphqplfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 560 LDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELIKKEGI 620
Cdd:PRK10253 174 LDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAELI 237
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1042-1244 |
7.92e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.83 E-value: 7.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1042 YPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwlraqlgiVSQEPILF 1121
Cdd:NF040873 2 YGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1122 DCSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFietlpqkyeTRVGDKG------TQLSGGQKQRIAIARALIRQPRVL 1195
Cdd:NF040873 71 PLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDAL---------ERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6981354 1196 LLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVI 1244
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1041-1262 |
7.98e-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: 91.07 E-value: 7.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1041 NYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQlgivsqepil 1120
Cdd:cd03291 44 NLCLVGA-PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPG---------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 fdcSIAKNIAYGdnsrvVSQDE-----IVRAAK-EANIHPFietlPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRV 1194
Cdd:cd03291 113 ---TIKENIIFG-----VSYDEyryksVVKACQlEEDITKF----PEKDNTVLGEGGITLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1195 LLLDEATSALDTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKEHGTHQQLLAQK 1262
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
391-586 |
8.78e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.53 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRclRefiG 470
Cdd:PRK11248 2 LQISHLYADYGGK---PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--R---G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQ-EPVLFSTTIAENIRYGrgnVTMDEIKKAVKEANAYDFIMKlpqkfdtlVGDRGA------QLSGGQKQRIAIARA 543
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6981354 544 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 586
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
403-615 |
1.17e-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: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTIS-------IDGQDIRNFNVRCLREFIGVVSQE 475
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 476 PVLFS-TTIAENIRYGRGNVTMDEI--KKAV--------KEANAYDFIMKLPQkfdtlvgdrgaQLSGGQKQRIAIARAL 544
Cdd:TIGR03269 374 YDLYPhRTVLDNLTEAIGLELPDELarMKAVitlkmvgfDEEKAEEILDKYPD-----------ELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 545 VRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELI 615
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
710-981 |
1.19e-19 |
|
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: 90.94 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIaifgpgdDTVKQQKcNMFSLVFLGLGVHSFFTF-----FLQGFTFGKAGEILTT 784
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLL-------DDIFVEK-DLEALLLVPLAIIGLFLLrglasYLQTYLMAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 785 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 864
Cdd:cd18552 73 DLRNDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 865 FIAVAgiveMKMLAGNAKRD-KKEMEAAGKIAT---EAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITF 940
Cdd:cd18552 151 LAALP----IRRIGKRLRKIsRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 6981354 941 SISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVILVFSAIVL 981
Cdd:cd18552 227 PLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLL 267
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1033-1252 |
1.90e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLdGQeakklNVQwlraqLG 1112
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFDcsiakniaygDNSRVVsqDEIVRAA---KEANIHPFIETL---PQKYETRVGDkgtqLSGGQKQRIAIAR 1186
Cdd:COG0488 382 YFDQHQEELD----------PDKTVL--DELRDGApggTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1187 ALIRQPRVLLLDEATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVIDNGKVKEH 1252
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
395-618 |
1.94e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.85 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 395 DVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL-REFIGVVS 473
Cdd:PRK10575 16 NVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 474 QEPVLFSTTIAENIRYGR-------GNVTMDEIKKaVKEANAYDFIMKLPQKfdtLVGdrgaQLSGGQKQRIAIARALVR 546
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRypwhgalGRFGAADREK-VEEAISLVGLKPLAHR---LVD----SLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 547 NPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELIKKE 618
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1032-1253 |
1.96e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.63 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ-----EAKKLNVqw 1106
Cdd:PRK11000 3 SVTLRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAERGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1107 lraqlGIVSQEPILF-DCSIAKNIAYGDNSRVVSQDEI---VRAAKEanihpfIETLPQKYETRVGDkgtqLSGGQKQRI 1182
Cdd:PRK11000 78 -----GMVFQSYALYpHLSVAENMSFGLKLAGAKKEEInqrVNQVAE------VLQLAHLLDRKPKA----LSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDTESEkvVQEALDKA----REGRTCIVIAH-RLSTIQNADLIVVIDNGKVKEHG 1253
Cdd:PRK11000 143 AIGRTLVAEPSVFLLDEPLSNLDAALR--VQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
391-614 |
2.17e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.17 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRClrefIG 470
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR----IG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLF-STTIAENIRY-GR--GnVTMDEIKKAVKEanaydfimkLPQKFDtlVGDRGA----QLSGGQKQRIAIAR 542
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlARlkG-LSKAEAKRRADE---------WLERLG--LGDRANkkveELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 543 ALVRNPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVN-VELlkDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1048-1249 |
2.30e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL----RAQLGIVSQE-PILFD 1122
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNI----AYGDnsrvvsqdeIVRAAKEANIHPFIETLpqKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:PRK10535 101 LTAAQNVevpaVYAG---------LERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1199 EATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIDNGKV 1249
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1050-1233 |
2.64e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 88.33 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQW---LRAQ-LGIVSQ-EPILFDCS 1124
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAY----GDNSRVVSQDEIVRAAKEANIhpfietlpqkyETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEA 1200
Cdd:PRK11629 104 ALENVAMplliGKKKPAEINSRALEMLAAVGL-----------EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 6981354 1201 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS 1233
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
406-605 |
3.03e-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: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQD----------IRNFNVRclREFIGVVSQe 475
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqaspREILALR--RRTIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 476 pvlFSTTI----AENIrygrgnVTMDEIKKAVKEANAYDFIMKLPQKFDtlVGDRGAQL-----SGGQKQRIAIARALVR 546
Cdd:COG4778 101 ---FLRVIprvsALDV------VAEPLLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 547 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHrlstvrNADVIAGFEDGVI 605
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH------DEEVREAVADRVV 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
391-607 |
5.22e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREFI 469
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQE----PVLfstTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFD--TLVGDrgaqLSGGQKQRIAIARA 543
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 544 LVRNPKILLLDEATSALdTESEAEVQAALDKA--REGRTTIVIAHRLSTV-RNADVIAGFEDGVIVE 607
Cdd:PRK11288 155 LARNARVIAFDEPTSSL-SAREIEQLFRVIRElrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1033-1246 |
5.68e-19 |
|
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: 85.28 E-value: 5.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNypTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklnvqwlRAQLG 1112
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFDCSIakniaygdnsrvvsqdeivraaKEANIHPFietlpqkyetrvgdkGTQLSGGQKQRIAIARALIRQP 1192
Cdd:cd03223 68 FLPQRPYLPLGTL----------------------REQLIYPW---------------DDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1193 RVLLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHRLSTIQNADLIVVIDN 1246
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1029-1260 |
5.74e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.61 E-value: 5.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1029 FEGSVTFNEVVFNYPTRAnvpvlqglslevkkgqTLALVGSSGCGKSTVVQLLERFYDPMAG-----TVLLDGQEA-KKL 1102
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1103 NVQWLRAQLGIVSQEPILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFieTLPQKYETRVGDKGTQLSGGQKQRI 1182
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
126-347 |
6.74e-19 |
|
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: 88.52 E-value: 6.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 126 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18784 51 VAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 206 GFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:cd18784 131 MFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYK 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 286 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVGQA 347
Cdd:cd18784 211 LKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILYQLELGSC 268
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1048-1253 |
7.02e-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: 86.82 E-value: 7.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQeakklnVQW-LRAQLGIVSQ----EPILFD 1122
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPEltgrENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIakniaYGdnsrvVSQDEIvrAAKEANIHPFIEtLPQKYETRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATS 1202
Cdd:cd03220 109 GRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1203 ALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHG 1253
Cdd:cd03220 172 VGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
391-609 |
8.05e-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: 86.18 E-value: 8.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNvrclREFIG 470
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLF-STTIAENIRY-GR-GNVTMDEIKKAVKEanaydfimkLPQKFDtlVGD----RGAQLSGGQKQRIAIARA 543
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQlKGLKKEEARRRIDE---------WLERLE--LSEyankRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 544 LVRNPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 609
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVN-VELlkDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1048-1248 |
8.64e-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: 91.42 E-value: 8.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGTVLLDGQEAKKLNVQWL-RAQLGIVSQEPILF-DC 1123
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNIAYGD----NSRVVSQDEIVRAAKEANIHPFIETLPqkyETR-VGDKGtqlsGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:TIGR02633 94 SVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1199 EATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGK 1248
Cdd:TIGR02633 167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
403-585 |
9.02e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.08 E-value: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGvvSQEPVLFSTT 482
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 483 IAENIR-----YGRGNVTMDEIKKAVKEANAYDfimkLPQKFdtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK13539 90 VAENLEfwaafLGGEELDIAAALEAVGLAPLAH----LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 6981354 558 SALDTESEAEVqAALDKAREGRTTIVIA 585
Cdd:PRK13539 156 AALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1050-1249 |
1.05e-18 |
|
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: 85.18 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNV-QWLRAQLGIVSQEP----ILFDCS 1124
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAygdnsrvvsqdeivraakeanihpfietLPQkyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1204
Cdd:cd03215 95 VAENIA----------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1205 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVIDNGKV 1249
Cdd:cd03215 136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
406-561 |
1.13e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.37 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR---CLR-EFIGVVSQEPVLFST 481
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 482 TIA-ENIRYG---RGnvtmDEIKKAVKEANAYDFIMKLPQKFDTLvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK10584 103 LNAlENVELPallRG----ESSRQSRNGAKALLEQLGLGKRLDHL----PAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
....
gi 6981354 558 SALD 561
Cdd:PRK10584 175 GNLD 178
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
386-645 |
1.13e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 386 SIKGNLEFSDVHFSYPSRA--NIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEG-TISIDGQDIRNFN- 461
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 462 ---VRCLREFIGVVSQEP--VLFSTTIAENIRYGRGNVTMD--EIKKAVKEanaydfIMKLPQKFDTLVGDRGAQLSGGQ 534
Cdd:PRK13645 82 ikeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENkqEAYKKVPE------LLKLVQLPEDYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 535 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSH 611
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSP 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 612 SEL-----------IKKEGIYFRLVNMQTSGSQILS------EEFEVELSD 645
Cdd:PRK13645 236 FEIfsnqelltkieIDPPKLYQLMYKLKNKGIDLLNknirtiEEFAKELAK 286
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
409-618 |
1.21e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-IGVVSQE-PVLFSTTIAEN 486
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 487 IRYGR------GNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK09700 101 LYIGRhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 561 dTESEAE-VQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKE 618
Cdd:PRK09700 177 -TNKEVDyLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDD 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1048-1261 |
1.26e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.74 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQ-WLRAQLGIVSQEPILF-DCSI 1125
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 AKNIAYGD--NSR-VVSQDEIVRAAKEANIHPFIETLPQkyeTRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1202
Cdd:PRK11288 97 AENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1203 ALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIDNG-KVKEHG-----THQQLLAQ 1261
Cdd:PRK11288 170 SLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGrYVATFDdmaqvDRDQLVQA 236
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1046-1261 |
1.31e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.86 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1046 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNvqwlRAQLGIVSQEPILF-DCS 1124
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAY-----GdnsrvVSQDEIVRAAKEanihpFIETLpqKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDE 1199
Cdd:COG4152 88 VGEQLVYlarlkG-----LSKAEAKRRADE-----WLERL--GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1200 ATSALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:COG4152 156 PFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
710-967 |
1.42e-18 |
|
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: 87.49 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIaifgpgdDTVKQQKCNMFSLVFL-GLGVHSFFTFFLQGFTFGKAGEILTTRLRS 788
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLI-------DALSAGGSSGGLLALLvALFLLQAVLSALSSYLLGRTGERVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 789 MAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQgatgtrlALIAQNTANLGTGII-------ISFIYGWQLTLLLLS 861
Cdd:cd18551 74 RLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELITSGLPQLVTGVLtvvgavvLMFLLDWVLTLVTLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 862 VVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFS 941
Cdd:cd18551 145 VVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGP 224
|
250 260
....*....|....*....|....*.
gi 6981354 942 ISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18551 225 LMGLAVQLALLVVLGVGGARVASGAL 250
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-614 |
1.59e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.46 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 394 SDVHFSYPSRANIKILKGLNLKVKSGQT---------VALVGNSGCGKSTTVQLLQRLYDPTEG-----TISIDGQDIrn 459
Cdd:PRK14271 13 ADVDAAAPAMAAVNLTLGFAGKTVLDQVsmgfparavTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 460 FNVRCLREF---IGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQ 536
Cdd:PRK14271 91 FNYRDVLEFrrrVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
419-609 |
2.40e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.68 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 419 GQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN---VRCLREFIGVVSQEPV-------LFSTTIAENIR 488
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasldprqTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 489 YgRGNVTMDEIKKAV---------KEANAYDFimklPQKFdtlvgdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PRK10261 430 V-HGLLPGKAAAARVawllervglLPEHAWRY----PHEF-----------SGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6981354 560 LDTESEAE-VQAALDKARE-GRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 609
Cdd:PRK10261 494 LDVSIRGQiINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1051-1255 |
2.74e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 85.31 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRAQLGIVSQEP-ILFDCSIA 1126
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1127 KNIAYGDNSRVVSQDEIVRAAKEAnihpfietlpqkyETRVG--DKG----TQLSGGQKQRIAIARALIRQPRVLLLDEA 1200
Cdd:PRK10908 98 DNVAIPLIIAGASGDDIRRRVSAA-------------LDKVGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1201 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVIDNGKVkeHGTH 1255
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1029-1261 |
3.05e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.60 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1029 FEGSVTFNEVVFNYPTRA--NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLdGQEA-----KK 1101
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAipanlKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1102 LN-VQWLRAQLGIVSQEP--ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEAnihPFIETLPQKYETRvgdKGTQLSGGQ 1178
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPEL---LKLVQLPEDYVKR---SPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1179 KQRIAIARALIRQPRVLLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHG- 1253
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGs 234
|
250
....*....|...
gi 6981354 1254 -----THQQLLAQ 1261
Cdd:PRK13645 235 pfeifSNQELLTK 247
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1049-1255 |
3.24e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.58 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV-LLDGQEAKKlnVQWLRAQLGIVSQepilFD----- 1122
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPAR--ARLARARIGVVPQ----FDnldle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKN-IAYGDNSRVvSQDEIvraakEANIHPFIE--TLPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDE 1199
Cdd:PRK13536 129 FTVRENlLVFGRYFGM-STREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1200 ATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIDNG-KVKEHGTH 1255
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1050-1253 |
3.90e-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: 84.12 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILFDcsi 1125
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 akniayGdnsrvVSQDEIVRAAKEAnihpfietlpqkyetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALD 1205
Cdd:cd03217 91 ------G-----VKNADFLRYVNEG-----------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1206 TESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIDNGKVKEHG 1253
Cdd:cd03217 137 IDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1051-1258 |
4.24e-18 |
|
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: 84.73 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFDCSIA-KNI 1129
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1130 A-----YGDNSRVVSQ--DEIVRaakeanihpFIEtLPQKYETRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATS 1202
Cdd:cd03265 95 YiharlYGVPGAERREriDELLD---------FVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1203 ALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKEHGTHQQL 1258
Cdd:cd03265 161 GLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
391-620 |
6.09e-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: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNF-NVRCLREFI 469
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEPVLFS-TTIAENIRYGRGNVTMDEIKKAVKEAnaYDFIMKLPQKfdtlVGDRGAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 549 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS--TVRNADVIAGFEDGVIVEQGSHSELIKKEGI 620
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
397-609 |
7.53e-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: 83.74 E-value: 7.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 397 HFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnVRCLREF-IGVvsqE 475
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSLLGLgGGF---N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 476 PVLfstTIAENIRYgRG---NVTMDEIKKavKEANAYDFiMKLPQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILL 552
Cdd:cd03220 97 PEL---TGRENIYL-NGrllGLSRKEIDE--KIDEIIEF-SELGDFIDLPVK----TYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 553 LDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRN-ADVIAGFEDGVIVEQG 609
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
407-609 |
7.76e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.56 E-value: 7.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIR--NFNVRCLREfIGVVSQEPVLFST-TI 483
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRG-IGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 484 AENIrygrgnVTMDEIKKAVKEANAYDFIMKLPQKFDT--LVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK10895 96 YDNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6981354 562 TESEAEVQAALDKAREGRTTIVIAHRlsTVRnaDVIAGFEDGVIVEQG 609
Cdd:PRK10895 170 PISVIDIKRIIEHLRDSGLGVLITDH--NVR--ETLAVCERAYIVSQG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
383-606 |
9.28e-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: 83.92 E-value: 9.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 383 KPDSIKGNLEfsdvHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNV 462
Cdd:cd03267 15 KEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 463 RCLREfIGVV--SQEPVLFSTTIAENIRYGRG--NVTMDEIKKAVKEANAydfIMKLPQKFDTLVgdrgAQLSGGQKQRI 538
Cdd:cd03267 91 KFLRR-IGVVfgQKTQLWWDLPVIDSFYLLAAiyDLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQRMRA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 539 AIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIahrlsTVRNADVIAGFEDGVIV 606
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLL-----TSHYMKDIEALARRVLV 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
412-633 |
1.10e-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: 89.69 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 412 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfNVRCLREFIGVVSQEPVLFS-TTIAENIRYg 490
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILF- 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 491 rgnvtMDEIK-KAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQ 569
Cdd:TIGR01257 1027 -----YAQLKgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 570 AALDKAREGRTTIVIAHRLStvrNADVIAgfEDGVIVEQG----SHSELIKKE----GIYFRLV-NMQTSGSQ 633
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQGrlycSGTPLFLKNcfgtGFYLTLVrKMKNIQSQ 1169
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1053-1258 |
1.15e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.91 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1053 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN-VQWL--RAQLGIVSQEPIlfdCSIAKNI 1129
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPL---ASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1130 AYGD----NSRV----VSQDEI---VRA--AKEANIHPFIETLPQKYetrvgdkgtqlSGGQKQRIAIARALIRQPRVLL 1196
Cdd:PRK15079 116 TIGEiiaePLRTyhpkLSRQEVkdrVKAmmLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1197 LDEATSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1258
Cdd:PRK15079 185 CDEPVSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1048-1251 |
1.20e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 87.92 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---MAGTVLLDGQEAKKLNvqwLRA--QLGIV--SQE--- 1117
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKD---IRDseALGIViiHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1118 -PILfdcSIAKNIAYGdNSR----VVSQDEIVRAAKE------ANIHPfietlpqkyETRVGDKGTqlsgGQKQRIAIAR 1186
Cdd:NF040905 90 iPYL---SIAENIFLG-NERakrgVIDWNETNRRAREllakvgLDESP---------DTLVTDIGV----GKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1187 ALIRQPRVLLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIDNGKVKE 1251
Cdd:NF040905 153 ALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1050-1251 |
1.44e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.29 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQW---LRAQ-LGIVSQEPILFDCSI 1125
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 A-KNIAY-----GDNSRvVSQDEIVRAAKEANIHPFIETLPqkyetrvgdkgTQLSGGQKQRIAIARALIRQPRVLLLDE 1199
Cdd:PRK10584 105 AlENVELpallrGESSR-QSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1200 ATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIDNGKVKE 1251
Cdd:PRK10584 173 PTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
408-589 |
1.45e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.33 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF----IGVVSQ-EPVLFSTT 482
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 483 IAENirygrgnVTMDEI--KKAVKEANAYDFIMKLPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK11629 104 ALEN-------VAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 6981354 561 DTESEAEVQAALDK--AREGRTTIVIAHRLS 589
Cdd:PRK11629 177 DARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1051-1258 |
1.83e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.91 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLL----------ERFYDPMAGTVLLDGQEAKklNVQWLRAQLGIVSQEPIL 1120
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLAR--DIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 FD-CSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFIETLpqkyeTRVG------DKGTQLSGGQKQRIAIARALIRQPR 1193
Cdd:PRK09984 98 VNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1194 VLLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQL 1258
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
408-614 |
1.85e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.45 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLLQRLYDP----TEGTISIDGQDIRNFNVRCLREF----IGVVSQEPVL 478
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 479 -------FSTTIAENIRYGRGnvtMDeikkavKEANAYDFIMKLPQkfdtlVGDRGA---------QLSGGQKQRIAIAR 542
Cdd:PRK15134 104 slnplhtLEKQLYEVLSLHRG---MR------REAARGEILNCLDR-----VGIRQAakrltdyphQLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1035-1262 |
1.93e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1035 FNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQeakklnvqwlrAQLGIV 1114
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1115 SQEPILFD-CSIAKNIAYGDNSRVVSQDEIVRA-AKEANIHPFIETLPQK-----------YETRVGD--KG-------- 1171
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRALEAELEELeAKLAEPDEDLERLAELqeefealggweAEARAEEilSGlgfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1172 ----TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH-R--LSTIqnADLIV 1242
Cdd:COG0488 147 drpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSHdRyfLDRV--ATRIL 220
|
250 260
....*....|....*....|.
gi 6981354 1243 VIDNGKVKEH-GTHQQLLAQK 1262
Cdd:COG0488 221 ELDRGKLTLYpGNYSAYLEQR 241
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
100-339 |
2.77e-17 |
|
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: 84.00 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 100 LNPGRILEEEMTRYAYYYSGLGGGVLLAAYIQvSFWTLAAGRQI-RKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDI 178
Cdd:cd18541 29 LTAGTLTASQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 179 SKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKI-----------LSTFSDKelaaya 247
Cdd:cd18541 108 NAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKihkrfrkvqeaFSDLSDR------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 248 kagavAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTI 327
Cdd:cd18541 182 -----VQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITL 256
|
250
....*....|....
gi 6981354 328 GN--AMTVFFSILI 339
Cdd:cd18541 257 GDlvAFNSYLGMLI 270
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
391-603 |
2.96e-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: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIdGQDIRnfnvrclrefIG 470
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVsqepvlfsttiaenirygrgnvtmdeikkavkeanaydfimklpqkfdtlvgdrgAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03221 67 YF-------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 551 LLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH-R--LSTVrnADVIAGFEDG 603
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1053-1258 |
3.03e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.12 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1053 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLrAQLGIVS--QEPILF-DCSIAKNI 1129
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1130 aygdnsrVVSQDEIV---------------RAAKEAnihpfIETLPQKYEtRVG-------DKGTqLSGGQKQRIAIARA 1187
Cdd:PRK11300 102 -------LVAQHQQLktglfsgllktpafrRAESEA-----LDRAATWLE-RVGllehanrQAGN-LAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1188 LIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1258
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1050-1260 |
4.35e-17 |
|
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: 86.01 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGTVL----------------LDGQEAKKLNVQwlraql 1111
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVCGGT------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 gIVSQEPILFDCS------IAKNIA---------YGDNSRVV----SQDEIVRAAKEAnIHPFIETLPQ-KYETRVGDKG 1171
Cdd:TIGR03269 89 -LEPEEVDFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEA-VGRAVDLIEMvQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1172 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVIDNGK 1248
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|..
gi 6981354 1249 VKEHGTHQQLLA 1260
Cdd:TIGR03269 247 IKEEGTPDEVVA 258
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1048-1254 |
4.87e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.05 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklNVQWLRA-QLGIVSQ----EPILFD 1122
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLElGAGFHPEltgrENIYLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIakniaYGdnsrvVSQDEIVRAAKE----ANIHPFIETlPQKYetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:COG1134 113 GRL-----LG-----LSRKEIDEKFDEivefAELGDFIDQ-PVKT----------YSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1199 EATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGT 1254
Cdd:COG1134 172 EVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
408-616 |
9.86e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 9.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL--YDPT----EGTISIDGQDIrnfNVRCLREFIGVVSQEPVLFST 481
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTT---LMNALafRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 482 -TIAENI------RYGRgNVTMDEIKKAVKEanaydFI--MKLPQKFDTLVGDRGAQ--LSGGQKQRIAIARALVRNPKI 550
Cdd:TIGR00955 114 lTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 551 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLST--VRNADVIAGFEDGVIVEQGSHSELIK 616
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
409-603 |
1.12e-16 |
|
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: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREFIGVVSQEP----VLFSTTI 483
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdAIRAGIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 484 AENIrygrgnvtmdeikkavkeanaydfimklpqkfdTLvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:cd03215 96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6981354 564 SEAEVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFEDG 603
Cdd:cd03215 139 AKAEIYRLIRElADAGKAVLLISSELDELlGLCDRILVMYEG 180
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1049-1273 |
1.27e-16 |
|
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: 86.22 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIVSQEPILFD-CSIAK 1127
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1128 NIAYGDNSRVVSQDEivraaKEANIHPFIETLPQKYETrvGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1207
Cdd:TIGR01257 1023 HILFYAQLKGRSWEE-----AQLEMEAMLEDTGLHHKR--NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 1208 SEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVIDNGKVKEHGTHQQL--LAQKGIYFSMV----NIQA 1273
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGTPLFLknCFGTGFYLTLVrkmkNIQS 1168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
376-617 |
1.35e-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: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 376 SFSERGHKPDSIKGNLefsdVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGq 455
Cdd:COG1134 13 SYRLYHEPSRSLKELL----LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 456 dirnfNVRCLREFIGVVSQEpvlfsTTIAENIR-----YGrgnVTMDEIKKAVKEANAY----DFImklpqkfDTLVGdr 526
Cdd:COG1134 88 -----RVSALLELGAGFHPE-----LTGRENIYlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQPVK-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 527 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE----SEAEVQaalDKAREGRTTIVIAHRLSTVRN-ADVIAGFE 601
Cdd:COG1134 146 --TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAIWLE 220
|
250
....*....|....*.
gi 6981354 602 DGVIVEQGSHSELIKK 617
Cdd:COG1134 221 KGRLVMDGDPEEVIAA 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1033-1264 |
1.45e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.69 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAkklnVQW-----L 1107
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----TDWqtakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1108 RAQLGIVSQEPILFD-CSIAKNIAYGD--NSRVVSQDEIVRAakeanihpfIETLPQKYETRVGDKGTqLSGGQKQRIAI 1184
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQMLAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1185 ARALIRQPRVLLLDEATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
....*
gi 6981354 1260 AQKGI 1264
Cdd:PRK11614 226 ANEAV 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1040-1260 |
1.61e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.99 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1040 FNYPT----RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVS 1115
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1116 QEPilfdcSIAKN----IAYGDNSRVVSQDEIVRAAKEANIhpfIETLPQkyetrVG---DKGT----QLSGGQKQRIAI 1184
Cdd:PRK15112 94 QDP-----STSLNprqrISQILDFPLRLNTDLEPEQREKQI---IETLRQ-----VGllpDHASyyphMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1185 ARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLA 1260
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
406-607 |
1.82e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYdPT---EGTISIDGQdIRNFnvRCLR--EFIGVV--SQE--- 475
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGE-VCRF--KDIRdsEALGIViiHQElal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 476 -PVLfstTIAENIRYG-----RGNVTMDEIKKAVKEanaydfIMK---LPQKFDTLVGDRGAqlsgGQKQRIAIARALVR 546
Cdd:NF040905 90 iPYL---SIAENIFLGnerakRGVIDWNETNRRARE------LLAkvgLDESPDTLVTDIGV----GKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 547 NPKILLLDEATSAL-DTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVE 607
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1049-1199 |
1.95e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.07 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPMAGTVLLDGQEAKKLNVqWLRAQLGI--VSQEPil 1120
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEA-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 fdcSIAKNIAYGDNSRVVSqdEIVRAAKEAnIHPFIETLPQKYE-TRVGD-KGTQLSGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:COG1137 88 ---SIFRKLTVEDNILAVL--ELRKLSKKE-REERLEELLEEFGiTHLRKsKAYSLSGGERRRVEIARALATNPKFILLD 161
|
.
gi 6981354 1199 E 1199
Cdd:COG1137 162 E 162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
406-603 |
2.02e-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: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPTEGTISIDGQDIRNFNVR-CLREFIGVVSQEPVLF-ST 481
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 482 TIAENIRYG-----RGNVTMDEikKAVKEANAYDFIMKLPQKFDTL-VGDRGaqlsGGQKQRIAIARALVRNPKILLLDE 555
Cdd:TIGR02633 94 SVAENIFLGneitlPGGRMAYN--AMYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 556 ATSALdTESEAEVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 603
Cdd:TIGR02633 168 PSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
391-606 |
3.13e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVhfSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREF-I 469
Cdd:COG3845 258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEP-----VLfSTTIAENI--------RYGRGNVtmdeIKKAVKEANAYDFImklpQKFDTLVGDRGA---QLSGG 533
Cdd:COG3845 336 AYIPEDRlgrglVP-DMSVAENLilgryrrpPFSRGGF----LDRKAIRAFAEELI----EEFDVRTPGPDTparSLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIV 606
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1050-1245 |
3.20e-16 |
|
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: 78.69 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAKNI 1129
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1130 AY--GDNSRvvsqDEIVRAAKEANIHPFiETLPqkyetrvgdkGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTE 1207
Cdd:cd03231 95 RFwhADHSD----EQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 6981354 1208 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVID 1245
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELD 197
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1044-1229 |
3.31e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQ-EPILfd 1122
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 cSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPfIETLPQKYetrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1202
Cdd:PRK13539 89 -TVAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|....*..
gi 6981354 1203 ALDTESEKVVQEALdKAREGRTCIVIA 1229
Cdd:PRK13539 157 ALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1049-1249 |
3.51e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNV-QWLRAQLGIVS----QEPILFDC 1123
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNI---AYGDNSR--VVSQDEIVRAAKEanihpFIETL---PQKYETRVGdkgtQLSGGQKQRIAIARALIRQPRVL 1195
Cdd:COG1129 346 SIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1196 LLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVIDNGKV 1249
Cdd:COG1129 417 ILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
412-610 |
3.60e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.46 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 412 LNLKVK-----SGQTvALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ---DIRN-FNVRCLREFIGVVSQEPVLFS-T 481
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgICLPPEKRRIGYVFQDARLFPhY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 482 TIAENIRYGrgnvtMDEikkavkeanaydfimKLPQKFDTLVG--------DR-GAQLSGGQKQRIAIARALVRNPKILL 552
Cdd:PRK11144 92 KVRGNLRYG-----MAK---------------SMVAQFDKIVAllgiepllDRyPGSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 553 LDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGS 610
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1044-1258 |
3.94e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL---RAQLGIVSQEPIL 1120
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 F-DCSIAKNIAYGDNSRVVSQDEIVRAakeanihpfieTLPQKYETrVGDKG------TQLSGGQKQRIAIARALIRQPR 1193
Cdd:PRK11831 96 FtDMNVFDNVAYPLREHTQLPAPLLHS-----------TVMMKLEA-VGLRGaaklmpSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1194 VLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQL 1258
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
396-591 |
4.37e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.76 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 396 VHFSYPSRANI---KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI---RNFNVRCLREFI 469
Cdd:PRK10908 2 IRFEHVSKAYLggrQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 470 GVVSQEP-VLFSTTIAENIRYGR--GNVTMDEIKKAVKEANAYDFIMKLPQKFDTlvgdrgaQLSGGQKQRIAIARALVR 546
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6981354 547 NPKILLLDEATSALDTE-SEAEVQAALDKAREGRTTIVIAHRLSTV 591
Cdd:PRK10908 155 KPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
403-610 |
4.47e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI--RNFNVRCLREF------------ 468
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGVVSQEPV-----LFST--TIAENIRYGRGnVTMDEikkAVKEANAYDFIMKLPQKfDTLVGDRGAQLSGGQKQRIAIA 541
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG-ASREE---AMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 542 RALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRT--TIVIAHRLSTVRN-ADVIAGFEDGVIVEQGS 610
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1045-1261 |
9.21e-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: 81.77 E-value: 9.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1045 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTV-------LLDGQEAKKLNVQWLRAQLGIVSQE 1117
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1118 PILF-DCSIAKNIAygDNSRVVSQDEIvrAAKEANIHPFIETLPQKYETRVGDKGT-QLSGGQKQRIAIARALIRQPRVL 1195
Cdd:TIGR03269 374 YDLYpHRTVLDNLT--EAIGLELPDEL--ARMKAVITLKMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1196 LLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1048-1249 |
1.11e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPILF-DCS 1124
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKYEtrVGDkgtqlsggqKQRIAIARALIRQPRVLLLDEATSAL 1204
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLE--VAD---------RQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6981354 1205 D-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVIDNGKV 1249
Cdd:PRK15439 172 TpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
742-967 |
1.15e-15 |
|
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: 78.89 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 742 DDTVKQQKCNMFSLVFLGLGVHSFFTFFLQG-----FTFGKAGeiLTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRL 816
Cdd:cd18784 24 DGIVIEKSQDKFSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 817 ATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIAT 896
Cdd:cd18784 100 TSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 897 EAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18784 180 ETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
391-591 |
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 6981354 391 LEFSDVHFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLYDPT-EGTISIDGQDIRnfnvRCLRE 467
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFST-TIAENIRygrgnvtmdeikkavkeanaydFIMKLpqkfdtlvgdRGaqLSGGQKQRIAIARALVR 546
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6981354 547 NPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTV 591
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSAS 171
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
395-606 |
2.05e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.00 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 395 DVHFSYPSrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP---TEGTISIDGQDIRNFNVRCLR----E 467
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNklraE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEP----------------VLF-------STTIAENIRygrgnvTMDEIK--KAVKEANAYdfimklPQKFdtl 522
Cdd:PRK09473 98 QISMIFQDPmtslnpymrvgeqlmeVLMlhkgmskAEAFEESVR------MLDAVKmpEARKRMKMY------PHEF--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 523 vgdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStvrnadVIAGF 600
Cdd:PRK09473 163 --------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLG------VVAGI 228
|
....*.
gi 6981354 601 EDGVIV 606
Cdd:PRK09473 229 CDKVLV 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
108-555 |
2.23e-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: 81.00 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 108 EEMTRYAYYYSGLGGGVLLAAYI-QVSFWTLAAgRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIG 186
Cdd:COG4615 45 AALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQ-HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 187 DkVGMFFQAIATFFAGFIVGFIRGWKLtLVIMAITAILGLSTAVWAKilstfsdKELAAYAKAGAVAEEAL-GAIRTVIa 265
Cdd:COG4615 124 R-LPELLQSVALVLGCLAYLAWLSPPL-FLLTLVLLGLGVAGYRLLV-------RRARRHLRRAREAEDRLfKHFRALL- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 266 fGGqNKEL------------ERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLV-ISKEYTIGNAMT 332
Cdd:COG4615 194 -EG-FKELklnrrrrraffdEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGwADPAVLSGFVLV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 333 VFFsiLIGAFSVgqaapCIDAFPNArGAAYVIFDiidnnpKIDSFSERGHKPDSIKGN------------LEFSDVHFSY 400
Cdd:COG4615 272 LLF--LRGPLSQ-----LVGALPTL-SRANVALR------KIEELELALAAAEPAAADaaappapadfqtLELRGVTYRY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 401 PSRANIK--ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVL 478
Cdd:COG4615 338 PGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 479 FSTTiaenirYGRGNVTMDEikkavkEANAYDFIMKLPQK-------FDTLvgdrgaQLSGGQKQRIAIARALVRNPKIL 551
Cdd:COG4615 418 FDRL------LGLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALLVALLEDRPIL 479
|
....
gi 6981354 552 LLDE 555
Cdd:COG4615 480 VFDE 483
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
126-343 |
2.27e-15 |
|
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: 78.32 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 126 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18564 69 LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 206 GFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKK 285
Cdd:cd18564 149 MFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLR 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 286 IGIK-KAISANISMGIAfLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGAFS 343
Cdd:cd18564 229 AGLRaARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPG-DLLVFLAYLKNLYK 285
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
403-615 |
2.33e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.52 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 403 RANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI-------RNFNVRCL---------- 465
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyRSQRIRMIfqdpstslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 466 REFIGVVSQEPVLFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFImklpqkfdtlvgdrgaqLSGGQKQRIAIARALV 545
Cdd:PRK15112 103 RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM-----------------LAPGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 546 RNPKILLLDEATSALDTESEAE-VQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELI 615
Cdd:PRK15112 166 LRPKVIIADEALASLDMSMRSQlINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1039-1253 |
2.57e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1039 VFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN---VQWLRAQLGIVS 1115
Cdd:PRK10261 329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1116 QEPIlfdCSIAKNIAYGDnsrvvSQDEIVRA-------AKEANIHPFIEtlpqkyetRVGDKGT-------QLSGGQKQR 1181
Cdd:PRK10261 408 QDPY---ASLDPRQTVGD-----SIMEPLRVhgllpgkAAAARVAWLLE--------RVGLLPEhawryphEFSGGQRQR 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1182 IAIARALIRQPRVLLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHG 1253
Cdd:PRK10261 472 ICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1050-1259 |
3.23e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPIL-FDCSIAKN 1128
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1129 IAYG--------DNSRVVSQDEIVRAAKEANIhpfIETLPQKYETrvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1200
Cdd:PRK10253 102 VARGryphqplfTRWRKEDEEAVTKAMQATGI---THLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1201 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:PRK10253 171 TTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
752-985 |
3.43e-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: 77.52 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 752 MFSLVFLGLGVHSFFTFFLqgftFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 831
Cdd:cd18575 41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 832 ALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE 911
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTRE 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 912 RKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI--LVFSAIVLGAVA 985
Cdd:cd18575 195 DAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSqfVFYAVLAAGSVG 270
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1033-1248 |
3.45e-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: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGTvlldgqeakklnvqwLRAQLG 1112
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------AGE---------------LEPDEG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILfdcsiakNIAYgdnsrvvsqdeivraakeanihpfietlpqkYEtrvgdkgtQLSGGQKQRIAIARALIRQP 1192
Cdd:cd03221 56 IVTWGSTV-------KIGY-------------------------------FE--------QLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1193 RVLLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIDNGK 1248
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1045-1229 |
4.82e-15 |
|
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: 75.09 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1045 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCS 1124
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAY-----GDNSRVVSQdeivrAAKEANIHPFiETLPQKyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDE 1199
Cdd:TIGR01189 90 ALENLHFwaaihGGAQRTIED-----ALAAVGLTGF-EDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|
gi 6981354 1200 ATSALDTESEKVVQEALDkAREGRTCIVIA 1229
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
409-614 |
5.01e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREFIGVVS----QEPVLFSTTI 483
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 484 AENI------RYGRGNVtMDEiKKAVKEANAYdfIMKL---PQKFDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLD 554
Cdd:COG1129 348 RENItlasldRLSRGGL-LDR-RRERALAEEY--IKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 555 EATSALDTESEAEVQAALDK-AREGRTTIVIahrlST-----VRNADVIAGFEDGVIVEQGSHSEL 614
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1048-1247 |
7.50e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 7.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLG--IVSQEPILFD-CS 1124
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAYGDN-SRVVSQDEIVRAAK---EANIHPFIETLPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1200
Cdd:PRK09700 97 VLENLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981354 1201 TSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNG 1247
Cdd:PRK09700 173 TSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
407-646 |
8.59e-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: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRL--YDPTEGTIsidgqdIRNFNV--RCLR----EFIG-------- 470
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRI------IYHVALceKCGYverpSKVGepcpvcgg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLF---STTIAENIR-------------YGRGNV------TMDEIKKAVKEA--NAYDFI--MKLPQKFDTLVG 524
Cdd:TIGR03269 88 TLEPEEVDFwnlSDKLRRRIRkriaimlqrtfalYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSHRITHIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 525 DrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA--REGRTTIVIAHRLSTVRN-ADVIAGFE 601
Cdd:TIGR03269 168 D----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6981354 602 DGVIVEQGSHSELIKKegiYFRLVNMqtsgsqiLSEEFEVELSDE 646
Cdd:TIGR03269 244 NGEIKEEGTPDEVVAV---FMEGVSE-------VEKECEVEVGEP 278
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1030-1259 |
9.64e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 9.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1030 EGSVTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN------ 1103
Cdd:PRK10575 9 DTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSskafar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1104 -VQWLRAQL----GIVSQEPIlfdcSIAKNIAYGDNSRVVSQD--EIVRAAKEANIHPFIEtlpqkyetRVGDkgtQLSG 1176
Cdd:PRK10575 86 kVAYLPQQLpaaeGMTVRELV----AIGRYPWHGALGRFGAADreKVEEAISLVGLKPLAH--------RLVD---SLSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1177 GQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVIDNGKVKEH 1252
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQ 229
|
....*..
gi 6981354 1253 GTHQQLL 1259
Cdd:PRK10575 230 GTPAELM 236
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
52-342 |
9.89e-15 |
|
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: 76.28 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 52 LFMLLGTAMAIAhgsgLPLMMivfGEMTDKFVdNAGNFSLPVNFSLSMLnpgrileeemtryayyysGLGGGVLLAAYIQ 131
Cdd:cd18548 6 LFKLLEVLLELL----LPTLM---ADIIDEGI-ANGDLSYILRTGLLML------------------LLALLGLIAGILA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 132 VSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGW 211
Cdd:cd18548 60 GYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 212 KLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA 291
Cdd:cd18548 140 KLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAG 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 292 ISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-------AMTVFFSILIGAF 342
Cdd:cd18548 220 RLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDlvafinyLMQILMSLMMLSM 277
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1045-1258 |
1.00e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1045 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLR--------------AQ 1110
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1111 LGIVSQEPI-----LFDC--SIAKNIAYGDNsrvVSQDEIVRAAK----EANIhPFIETLPQKYETrvgdkgtQLSGGQK 1179
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAKrmldQVRI-PEAQTILSRYPH-------QLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1180 QRIAIARALIRQPRVLLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVIDNGKVKE 1251
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
....*..
gi 6981354 1252 HGTHQQL 1258
Cdd:PRK10261 250 TGSVEQI 256
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1035-1261 |
1.00e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.86 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1035 FNEVVFNYPTR--ANVPVlqglSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG 1112
Cdd:PRK10522 325 LRNVTFAYQDNgfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFDcsiakniaygdnsRVVSQDEivRAAKEANIHPFIETLPQKYETRVGD---KGTQLSGGQKQRIAIARALI 1189
Cdd:PRK10522 401 AVFTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1190 RQPRVLLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVIDNGKVKE-HGTHQQLLAQ 1261
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1051-1259 |
1.15e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL---------RAQLGIVSQEP--- 1118
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1119 ILFDCSIAKNIA----------YGdNSRVVSQDEIVRAAKEANihpfietlpqkyetRVGDKGTQLSGGQKQRIAIARAL 1188
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYG-DIRATAGDWLERVEIDAA--------------RIDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1189 IRQPRVLLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1054-1253 |
1.47e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.84 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1054 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQ----EAKKLNVQWLRAQLGIVSQEPILF-DC 1123
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdAEKGICLPPEKRRIGYVFQDARLFpHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1124 SIAKNIAYGDNSRVVSQ-DEIVRAAKeanihpfIETLPQKYETRvgdkgtqLSGGQKQRIAIARALIRQPRVLLLDEATS 1202
Cdd:PRK11144 92 KVRGNLRYGMAKSMVAQfDKIVALLG-------IEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1203 ALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVIDNGKVKEHG 1253
Cdd:PRK11144 158 SLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1043-1249 |
1.48e-14 |
|
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: 74.68 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1043 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklNVQW-----LRAQLGIV--S 1115
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1116 QEPILFDCSIAKNIAYgdNSRVVSQDEivrAAKEANIHPFIETLPQkyeTRVGDKGT-QLSGGQKQRIAIARALIRQPRV 1194
Cdd:cd03267 103 KTQLWWDLPVIDSFYL--LAAIYDLPP---ARFKKRLDELSELLDL---EELLDTPVrQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1195 LLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
710-967 |
1.77e-14 |
|
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: 75.53 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIAIFGPGDDTVKQQKcnMFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSM 789
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLL--RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 790 AFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVA 869
Cdd:cd18541 79 LFAHLLTLSPSFY--QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 870 GIVEMKMLagnAKRDKKEMEAAGKIATEAIEN---IRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAF 946
Cdd:cd18541 157 VYRLGKKI---HKRFRKVQEAFSDLSDRVQESfsgIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLL 233
|
250 260
....*....|....*....|.
gi 6981354 947 MYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18541 234 IGLSFLIVLWYGGRLVIRGTI 254
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
402-572 |
1.91e-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: 73.30 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFST 481
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 482 TIAENIRYGRGNVTMDEIKKAVKEANAydfimklpqkfdTLVGDRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGL------------NGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170
....*....|..
gi 6981354 561 DTESEAEVQAAL 572
Cdd:cd03231 157 DKAGVARFAEAM 168
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
765-967 |
2.68e-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: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 765 FFTFFLQG-FTF------GKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDaaqVQGATGTRLALIAQN 837
Cdd:cd18574 49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFDTHR--TGELVNRLTAD---VQEFKSSFKQCVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 838 TANLG--TGIIISFIY-GWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKF 914
Cdd:cd18574 124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 915 ESMYVEKLhgpyrNSVRKAHIY-GITFSISQAFMYFSYAG----CFRFGSYLIVNGHM 967
Cdd:cd18574 204 LELYEEEV-----EKAAKLNEKlGLGIGIFQGLSNLALNGivlgVLYYGGSLVSRGEL 256
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1051-1259 |
2.75e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----MAGTVLLDGqeaKKLNVQWLRAQLGIVSQEPILFDCSIA 1126
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1127 KN----IAYGDNSRVVSQDEivraaKEANIHPFIETLPQK--YETRVGDKGTQ--LSGGQKQRIAIARALIRQPRVLLLD 1198
Cdd:TIGR00955 117 REhlmfQAHLRMPRRVTKKE-----KRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1199 EATSALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIDNGKVKEHGTHQQLL 1259
Cdd:TIGR00955 192 EPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
52-329 |
3.19e-14 |
|
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: 74.75 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 52 LFMLLGTAMAIAhgsgLPLMMivfGEMTDKFVDNAGNfSLPVNFSlsmlnpgrileeEMTRYAYYYSGLGGGVLLAAYIQ 131
Cdd:cd18547 6 ILAIISTLLSVL----GPYLL---GKAIDLIIEGLGG-GGGVDFS------------GLLRILLLLLGLYLLSALFSYLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 132 VSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGW 211
Cdd:cd18547 66 NRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 212 KLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA 291
Cdd:cd18547 146 LLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQ 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 6981354 292 ISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 329
Cdd:cd18547 226 FYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGV 263
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
411-609 |
3.20e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.87 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 411 GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDI--------------RNF-NVRCLREFigvvsqe 475
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREM------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 476 pvlfstTIAENI-----RYGRGNVTMDEIKKAV---KEANAYDFIMKLPQKFDTL-VGDRGA-QLSGGQKQRIAIARALV 545
Cdd:PRK11300 96 ------TVIENLlvaqhQQLKTGLFSGLLKTPAfrrAESEALDRAATWLERVGLLeHANRQAgNLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 546 RNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIagfedgVIVEQG 609
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRI------YVVNQG 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
408-614 |
3.55e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.97 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP----TEGTISIDGQDIRNFNVRCLRefIGVVSQ------EPV 477
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGRK--IATIMQnprsafNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 478 LFSTTIAENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFdtlvgdrGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK10418 96 HTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLY-------PFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 558 SALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK10418 169 TDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
407-591 |
3.57e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnvrcLRefIGVVSQEPVLFST---TI 483
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQKLYLDTTlplTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 484 AENIRYgRGNVTMDEIKKAVKEANAYDFIMKLPQKfdtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:PRK09544 87 NRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190
....*....|....*....|....*....|
gi 6981354 564 SEAEVQAALDKARE--GRTTIVIAHRLSTV 591
Cdd:PRK09544 155 GQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1048-1248 |
3.95e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAK----KLNVQwlrAQLGIVSQEPILFD- 1122
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQE---AGIGIIHQELNLIPq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNIAYGDnsrvvsqdEIVRA---------AKEANihPFIETLPQKY--ETRVGDkgtqLSGGQKQRIAIARALIRQ 1191
Cdd:PRK10762 94 LTIAENIFLGR--------EFVNRfgridwkkmYAEAD--KLLARLNLRFssDKLVGE----LSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1192 PRVLLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIDNGK 1248
Cdd:PRK10762 160 SKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1041-1249 |
6.96e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1041 NYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPMAGTVLLDGQEAKKLNV-QWLRAQLGIVSQE 1117
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1118 P-----ILfDCSIAKNIAYGDNSR-------VVSQDEIVRAAKEAnihpfIEtlpqKYETRVGDKGT---QLSGGQKQRI 1182
Cdd:COG3845 342 RlgrglVP-DMSVAENLILGRYRRppfsrggFLDRKAIRAFAEEL-----IE----EFDVRTPGPDTparSLSGGNQQKV 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1047-1254 |
7.52e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.81 E-value: 7.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILfdcsia 1126
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHI------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1127 kniaygdNSRVVSQD-------------------EIVRAAkeanIHPF-IETLPQKYETrvgdkgtQLSGGQKQRIAIAR 1186
Cdd:COG4604 87 -------NSRLTVRElvafgrfpyskgrltaedrEIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1187 ALIRQPRVLLLDEATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVIDNGKVKEHGT 1254
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
695-1251 |
8.17e-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: 75.99 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 695 SFLKVLRlnKTEWPYFVVGTLCAIANGALqpafSIILSEMI--AIFGPGDDTVkqqkcnMFSLVFLGLGVHSFFTFFLQG 772
Cdd:COG4615 2 NLLRLLL--RESRWLLLLALLLGLLSGLA----NAGLIALInqALNATGAALA------RLLLLFAGLLVLLLLSRLASQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 773 FTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGtRLALIAQNTANlgtgIIISFIY- 851
Cdd:COG4615 70 LLLTRLGQHAVARLRLRLSRRILAAPLERLERI--GAARLLAALTEDVRTISQAFV-RLPELLQSVAL----VLGCLAYl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 852 GWQLTLLLLSVVPFIAVAGIVEMKMLagnaKRDKKEMEAAGKIATEAIENIRTVVS------LTQERKfESMYVEKLHGP 925
Cdd:COG4615 143 AWLSPPLFLLTLVLLGLGVAGYRLLV----RRARRHLRRAREAEDRLFKHFRALLEgfkelkLNRRRR-RAFFDEDLQPT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 926 ---YRNSVRKAH-IYGITFSISQAFMYFsyagcfrfgsyLIVnghmrfkdvILVFSAIVLGAVALGHASSFA-------- 993
Cdd:COG4615 218 aerYRDLRIRADtIFALANNWGNLLFFA-----------LIG---------LILFLLPALGWADPAVLSGFVlvllflrg 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 994 ---------PDYAKAKLSAAYLFSL---FERQPLIDSYSREGMWPDKFEgSVTFNEVVFNYPTRANVP--VLQGLSLEVK 1059
Cdd:COG4615 278 plsqlvgalPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGDEgfTLGPIDLTIR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1060 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLGIVSQEPILFDcsiakniaygdnsRVVS 1139
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-------------RLLG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1140 QDEIVRAAKeanIHPFIETLPQKYETRVGDKG---TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEAL 1216
Cdd:COG4615 424 LDGEADPAR---ARELLERLELDHKVSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFYTEL 500
|
570 580 590
....*....|....*....|....*....|....*..
gi 6981354 1217 --DKAREGRTCIVIAHRLSTIQNADLIVVIDNGKVKE 1251
Cdd:COG4615 501 lpELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
401-585 |
9.62e-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: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 401 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTtvqLLQRL------YDPTEGTISIDGQDIRNFNVRCLREFIgVVSQ 474
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYPGEII-YVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 475 EPVLFST-TIAEnirygrgnvTMDeikkAVKEANAYDFImklpqkfdtlvgdRGaqLSGGQKQRIAIARALVRNPKILLL 553
Cdd:cd03233 91 EDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190
....*....|....*....|....*....|...
gi 6981354 554 DEATSALDTESEAE-VQAALDKAREGRTTIVIA 585
Cdd:cd03233 143 DNSTRGLDSSTALEiLKCIRTMADVLKTTTFVS 175
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
397-620 |
1.06e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 397 HFSYPSRANIkILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ-RLYDPTE-------GTISIDGQDIRNFNVR---CL 465
Cdd:PRK13547 6 HLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPrlaRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 466 REFIGVVSQEPVLFSttIAENIRYGR----------GNVTMDEIKKAVKEANAydfimklpqkfDTLVGDRGAQLSGGQK 535
Cdd:PRK13547 85 RAVLPQAAQPAFAFS--AREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 536 QRIAIARAL---------VRNPKILLLDEATSALDTESEAEVQAAL-DKARE---GRTTIVIAHRLSTvRNADVIAGFED 602
Cdd:PRK13547 152 ARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrRLARDwnlGVLAIVHDPNLAA-RHADRIAMLAD 230
|
250
....*....|....*...
gi 6981354 603 GVIVEQGSHSELIKKEGI 620
Cdd:PRK13547 231 GAIVAHGAPADVLTPAHI 248
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
397-587 |
1.23e-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: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 397 HFSYPSRANIK-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPTEGTISIDGQDIrnfnvrclrefigvvS 473
Cdd:COG2401 33 AFGVELRVVERyVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------G 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 474 QEpvlfsTTIAENIrYGRGNV-TMDEIKKAVKEANAYDFImklpQKFDtlvgdrgaQLSGGQKQRIAIARALVRNPKILL 552
Cdd:COG2401 98 RE-----ASLIDAI-GRKGDFkDAVELLNAVGLSDAVLWL----RRFK--------ELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 6981354 553 LDEATSALDTESEAEVQAALDK-AREGRTTIVIA-HR 587
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKlARRAGITLVVAtHH 196
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
710-965 |
1.24e-13 |
|
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: 73.19 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIaifgpgDDTVKQQKCNM-----FSLVFLGLGVHSFFTFFLQGFTFGKAGEILTT 784
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAI------DDYIVPGQGDLqglllLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 785 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP 864
Cdd:cd18544 75 DLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 865 FIAVAgIVEMKMLAGNAKRDKKEMEAA--GKIAtEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKA-HIYGITFS 941
Cdd:cd18544 153 LLLLA-TYLFRKKSRKAYREVREKLSRlnAFLQ-ESISGMSVIQLFNREKREFEEF-DEINQEYRKANLKSiKLFALFRP 229
|
250 260
....*....|....*....|....
gi 6981354 942 ISQAFMYFSYAGCFRFGSYLIVNG 965
Cdd:cd18544 230 LVELLSSLALALVLWYGGGQVLSG 253
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
390-616 |
1.32e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 73.62 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 390 NLEFSDVHF---SYPSRANIKIlkglNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-P---TEGTISIDGQDIRNFNV 462
Cdd:PRK11022 5 NVDKLSVHFgdeSAPFRAVDRI----SYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 463 RCLREFIG----VVSQEPVlfsTTIaeNIRYGRGNVTMDEIK------KAVKEANAYDFImklpqkfdTLVG--DRGA-- 528
Cdd:PRK11022 81 KERRNLVGaevaMIFQDPM---TSL--NPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLL--------NQVGipDPASrl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 529 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGF 600
Cdd:PRK11022 148 dvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLelQQKENMALVLITHDLALVaEAAHKIIVM 227
|
250
....*....|....*.
gi 6981354 601 EDGVIVEQGSHSELIK 616
Cdd:PRK11022 228 YAGQVVETGKAHDIFR 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1046-1253 |
1.92e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1046 ANVPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGTVLLDGQ--EAKKLN---------------- 1103
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvAPCALRgrkiatimqnprsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1104 -VQWLRA-------QLGIVSQEPILFDCSIAknIAYGDNSRVVSqdeivraakeanIHPFietlpqkyetrvgdkgtQLS 1175
Cdd:PRK10418 94 pLHTMHTharetclALGKPADDATLTAALEA--VGLENAARVLK------------LYPF-----------------EMS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1176 GGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEH 1252
Cdd:PRK10418 143 GGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
.
gi 6981354 1253 G 1253
Cdd:PRK10418 223 G 223
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
116-329 |
2.10e-13 |
|
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: 72.37 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 116 YYSG-----LGGGVLLAAYIQVSFW--------TLAAG-----------RQIRKIRQKFFHAILRQEMGWFDIKGTTELN 171
Cdd:cd18590 17 YYTGrvidiLGGEYQHNAFTSAIGLmclfslgsSLSAGlrgglfmctlsRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 172 TRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGA 251
Cdd:cd18590 97 SRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 252 VAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 329
Cdd:cd18590 177 LAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGS 254
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
52-328 |
2.15e-13 |
|
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: 72.42 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 52 LFMLLGTAMAIAhgsgLPLMMIVFgemtdkfVDNagnfslpvnfslsMLNPGRILEEEMTRYAYYYSGLGGGVLLAAYIQ 131
Cdd:cd18544 6 LLLLLATALELL----GPLLIKRA-------IDD-------------YIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 132 VSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGW 211
Cdd:cd18544 62 TYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNW 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 212 KLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKA 291
Cdd:cd18544 142 RLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSI 221
|
250 260 270
....*....|....*....|....*....|....*..
gi 6981354 292 ISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 328
Cdd:cd18544 222 KLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG 258
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
419-609 |
2.55e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.50 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 419 GQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL----REFI-----GVVSQEPvlfsttiAENIRY 489
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHP-------RDGLRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 490 G---RGNVTmdEIKKAVKE-------ANAYDFIMKL---PQKFDtlvgDRGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:PRK11701 105 QvsaGGNIG--ERLMAVGArhygdirATAGDWLERVeidAARID----DLPTTFSGGMQQRLQIARNLVTHPRLVFMDEP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 557 TSALDTeseaEVQAA-LDKARE-----GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 609
Cdd:PRK11701 179 TGGLDV----SVQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
402-585 |
2.78e-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: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLRE--FIGVVSQ-EPVL 478
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilYLGHLPGlKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 479 fstTIAENIRYGR--GNVTMDEIKKAVKEANAYDFImklpqkfDTLVgdrgAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:TIGR01189 89 ---SALENLHFWAaiHGGAQRTIEDALAAVGLTGFE-------DLPA----AQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180
....*....|....*....|....*....
gi 6981354 557 TSALDTESEAEVQAALDkAREGRTTIVIA 585
Cdd:TIGR01189 155 TTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
418-606 |
3.16e-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: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 418 SGQTVALVGNSGCGKSTTVQLLQRLYDPTEGT-ISIDGQDIRNFNVRCLREFIgvvsqepvlfsttiaenirygrgnvtm 496
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 497 deikkavkeanaydfimklpqkfdtlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--- 573
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 6981354 574 ---KAREGRTTIVIAHRLSTVRNADVIAGFEDGVIV 606
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
123-332 |
3.62e-13 |
|
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: 71.81 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 123 GVLLAAYIqvSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISK--------ISEGIgdkvgmffQ 194
Cdd:cd18574 56 SLLTFAYI--SLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------R 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 195 AIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 274
Cdd:cd18574 126 SVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 275 RYQKHLENAKK--------IGIKKAISaNISMGIAFLLIYasyalafWYGSTLVISKEYTIGNAMT 332
Cdd:cd18574 206 LYEEEVEKAAKlneklglgIGIFQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGDLMS 263
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
409-591 |
4.89e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRnfnvRCLRE-FIGVVSQEPVL---FSTTIA 484
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSEEVdwsFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 485 ENIRYGR-GNVTMDEIKKA-----VKEANAYDFIMKLPQKfdtlvgdRGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:PRK15056 99 DVVMMGRyGHMGWLRRAKKrdrqiVTAALARVDMVEFRHR-------QIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|....
gi 6981354 559 ALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTV 591
Cdd:PRK15056 172 GVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
755-969 |
5.32e-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: 71.44 E-value: 5.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 755 LVFLGLGVHSFFTFfLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALI 834
Cdd:cd18565 59 LTVAAFLLESLFQY-LSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGANSI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 835 AQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVVSLTQE 911
Cdd:cd18565 136 IRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRI---EPRYRAVREAVGDLNArleNNLSGIAVIKAFTAE 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 912 RkFESMYVEKLHGPYRNSVRKAHIYGITFsisQAFMYF----SYAGCFRFGSYLIVNGHMRF 969
Cdd:cd18565 213 D-FERERVADASEEYRDANWRAIRLRAAF---FPVIRLvagaGFVATFVVGGYWVLDGPPLF 270
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
407-610 |
6.10e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLY--DPTEG--------TISIDGQDIRNfnVRCLREFIGVVSQEP 476
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiellgrTVQREGRLARD--IRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 477 VLFST-TIAENIRYGRGNVT------MDEIKKAVKEaNAYDFIMKLPQKFdtLVGDRGAQLSGGQKQRIAIARALVRNPK 549
Cdd:PRK09984 96 NLVNRlSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRVGMVH--FAHQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 550 ILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGS 610
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1049-1251 |
7.16e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERfydpmagtVLLDGQEAKKLNVQWLraqlgIVSQEPILFDCsIAKN 1128
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------ALKGTPVAGCVDVPDN-----QFGREASLIDA-IGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1129 iayGDNSRVVsqdEIVRAAKEANihpfietlPQKYETRVgdkgTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1208
Cdd:COG2401 110 ---GDFKDAV---ELLNAVGLSD--------AVLWLRRF----KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6981354 1209 EKVVQEALDKA--REGRTCIVIAHR---LSTIQnADLIVVIDNGKVKE 1251
Cdd:COG2401 172 AKRVARNLQKLarRAGITLVVATHHydvIDDLQ-PDLLIFVGYGGVPE 218
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
391-617 |
9.86e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.43 E-value: 9.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGTISIDGQDIRNFNVRCLR-E 467
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAgE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPV--------LFSTTIAENIRYGRGNVTMDEIKKAvkeanayDFI------MKLPQkfDTLVGDRGAQLSGG 533
Cdd:PRK09580 79 GIFMAFQYPVeipgvsnqFFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGFSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 534 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREG-RTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGS 610
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGD 229
|
....*..
gi 6981354 611 HSeLIKK 617
Cdd:PRK09580 230 FT-LVKQ 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1033-1232 |
1.02e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQeakklnvqwLRaqLG 1112
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEpILFDCSIAKNIaygdnSRV------VSQDEIVRAAKEANIHPFIETLPQKyetrvgdkgtqLSGGQKQRIAIAR 1186
Cdd:PRK09544 71 YVPQK-LYLDTTLPLTV-----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6981354 1187 ALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV--IAHRL 1232
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
394-588 |
1.12e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.07 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 394 SDVHFSYPSranIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIrNFNV--RCLREFIGV 471
Cdd:PRK10982 2 SNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSskEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 472 VSQE-PVLFSTTIAENI---RYGRGNVTMDEiKKAVKEANAYdfimklpqkFDTL-----VGDRGAQLSGGQKQRIAIAR 542
Cdd:PRK10982 78 VHQElNLVLQRSVMDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6981354 543 ALVRNPKILLLDEATSALdteSEAEVQ---AALDKARE-GRTTIVIAHRL 588
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSL---TEKEVNhlfTIIRKLKErGCGIVYISHKM 194
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1050-1264 |
1.14e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPilfdcSIAK 1127
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEA-----SIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1128 NIAYGDNSRVVSQ--DEIVRAAKEANIHPFIETLpqkYETRVGDK-GTQLSGGQKQRIAIARALIRQPRVLLLDEATSAL 1204
Cdd:PRK10895 92 RLSVYDNLMAVLQirDDLSAEQREDRANELMEEF---HIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1205 DTESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVIDNGKVKEHGTHQQLLAQKGI 1264
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
411-586 |
1.89e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 411 GLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRnfnvRCLREFI----------GVvsqEPVLfs 480
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEYHqdllylghqpGI---KTEL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 481 tTIAENIRY---GRGNVTMDEIKKAvkeanaydfimkLPQkfdtlVGDRG------AQLSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK13538 90 -TALENLRFyqrLHGPGDDEALWEA------------LAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 6981354 552 LLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH 586
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
406-583 |
2.27e-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: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREfIGVV----SQ----EPV 477
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR-IGVVfgqrSQlwwdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 478 LFSTTIAENIrYGrgnVTMDEIKKAVKEanaYDFIMKLPQKFDTLVgdRgaQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:COG4586 114 IDSFRLLKAI-YR---IPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180
....*....|....*....|....*..
gi 6981354 558 SALDTESEAEVQAALDK-AREGRTTIV 583
Cdd:COG4586 183 IGLDVVSKEAIREFLKEyNRERGTTIL 209
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
412-626 |
2.56e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 412 LNLKVKSGQTVALVGNSGCGKSTtvqLLQRLYD--PTEGTISIDGQDIRNFNVRCLREFIGVVSQE-PVLFSTTIAENI- 487
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 488 RYGRGNVTMDEIKKAVKE-ANAYDFIMKLPqkfdTLVGdrgaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSA 559
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 560 LDTESeaevQAALDK-----AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELIKKE------GIYFRLVN 626
Cdd:PRK03695 164 LDVAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEnlaqvfGVNFRRLD 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1044-1249 |
2.80e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.91 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLN-----------VQWLRAQLG 1112
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVSQEPILFDCSIAKNIAYGDNSRVVSQDEIvraakEANIHPFIETLPQK---YETRVGdkgtQLSGGQKQRIAIARALI 1189
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1190 RQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
710-967 |
3.02e-12 |
|
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: 68.97 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMI-AIFGPGDDTVKQQKCNMFSLVFLGLGVH--SFFTFFLQGFTFGKAGEILTTRL 786
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIdLIIEGLGGGGGVDFSGLLRILLLLLGLYllSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 787 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFI 866
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 867 AVAgiveMKMLAGNAKRD-KKEMEAAGKI---ATEAIENIRTVVSLTQERKFESMYvEKLHGPYRNSVRKAHIY-GITFS 941
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREEEAIEEF-DEINEELYKASFKAQFYsGLLMP 233
|
250 260
....*....|....*....|....*.
gi 6981354 942 ISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18547 234 IMNFINNLGYVLVAVVGGLLVINGAL 259
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1047-1254 |
3.51e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.13 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1047 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGTVLLDGQEAKKLNVQwLRAQLGI----------- 1113
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1114 -VSQEPILfdcsiakNIAYgdNSRVVSQDEivraaKEANIHPFIETLPQKYETrVGDKGTQL--------SGGQKQRIAI 1184
Cdd:CHL00131 98 gVSNADFL-------RLAY--NSKRKFQGL-----PELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1185 ARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVIDNGKVKEHGT 1254
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
294-555 |
3.51e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 294 ANISM----GIAFLLiyasyALAFWYGSTLVISkeyTIgnAMTVFF--SILIGAfsvgqaapcIDAFPNARgAAYVIFDI 367
Cdd:PRK10522 239 SNIMMlgaiGLVFYM-----ANSLGWADTNVAA---TY--SLTLLFlrTPLLSA---------VGALPTLL-SAQVAFNK 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 368 IdNNPKIDSFSERGHKPDSIKG--NLEFSDVHFSYPSRANIkiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDP 445
Cdd:PRK10522 299 L-NKLALAPYKAEFPRPQAFPDwqTLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 446 TEGTISIDGQDIRNFNVRCLREFIGVVSQEPVLFSTtiaenirygrgnvTMDEIKKAVKEANAYDFI--MKLPQKFdTLV 523
Cdd:PRK10522 376 QSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQ-------------LLGPEGKPANPALVEKWLerLKMAHKL-ELE 441
|
250 260 270
....*....|....*....|....*....|....
gi 6981354 524 GDRGA--QLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK10522 442 DGRISnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
710-973 |
3.76e-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: 68.63 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIaifgpgDDTVKQQKCNM---FSLVFLGL-GVHSFFTFFLQGFtfgkaGEILTTR 785
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYII------DDLLPSKNLRLiliIGAILLALyILRTLLNYFVTYW-----GHVMGAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 786 ----LRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVqgatgTRLA-------LIAqnTANLGTGIIISFIYGWQ 854
Cdd:cd18549 73 ietdMRRDLFEHLQKLSFSFFDNNK--TGQLMSRITNDLFDI-----SELAhhgpedlFIS--IITIIGSFIILLTINVP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 855 LTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMeaaGKI---ATEAIENIRTVVSLTQE----RKFESMYVEklhgpYR 927
Cdd:cd18549 144 LTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKI---GEInaqLEDSLSGIRVVKAFANEeyeiEKFDEGNDR-----FL 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 6981354 928 NSVRKAHIY-GITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 973
Cdd:cd18549 216 ESKKKAYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLV 262
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
408-601 |
3.92e-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: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL-QRLydpTEGTISidgQDIRNFNVRCLRE-F---IGVVSQEPV-LFST 481
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERV---TTGVIT---GGDRLVNGRPLDSsFqrsIGYVQQQDLhLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 482 TIAENIRYGRGNVTMDEIKKavKEANAY-DFIMKL---PQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILL-LDEA 556
Cdd:TIGR00956 852 TVRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6981354 557 TSALDTESEAEVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFE 601
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFD 971
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
404-589 |
3.94e-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: 70.55 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 404 ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDgQDIRNFNVRcLREFIGVVS-QEPVLFSTT 482
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP-AKGKLFYVP-QRPYMTLGTlRDQIIYPDS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 483 IAENIRYGRGNVTMDEIKKAVKeanaYDFIMKLPQKFDTlVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 562
Cdd:TIGR00954 541 SEDMKRRGLSDKDLEQILDNVQ----LTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|....*...
gi 6981354 563 ESEaevQAALDKARE-GRTTIVIAHRLS 589
Cdd:TIGR00954 616 DVE---GYMYRLCREfGITLFSVSHRKS 640
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
710-967 |
5.39e-12 |
|
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: 67.89 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMI--AIFGPGDDTVKqqkcnMFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLR 787
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdgPIAHGDRSALW-----PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 788 SMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGtRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIA 867
Cdd:cd18543 76 TDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 868 VAGIVEMKMLAGNAKRDKkemEAAGKIATEAIEN---IRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQ 944
Cdd:cd18543 153 LVARRFRRRYFPASRRAQ---DQAGDLATVVEESvtgIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLE 229
|
250 260
....*....|....*....|...
gi 6981354 945 AFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18543 230 ALPELGLAAVLALGGWLVANGSL 252
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
140-332 |
5.46e-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: 67.88 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 140 GRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLV-IM 218
Cdd:cd18589 65 SRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLtAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 219 AITAILGLSTAV--WAKILSTFSDKELAAYAKAGAvaeEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANI 296
Cdd:cd18589 145 GLPLLLLVPKFVgkFQQSLAVQVQKSLARANQVAV---ETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAV 221
|
170 180 190
....*....|....*....|....*....|....*....
gi 6981354 297 SM---GIAFLLIYASyalAFWYGSTLVISKEYTIGNAMT 332
Cdd:cd18589 222 SMwtsSFSGLALKVG---ILYYGGQLVTAGTVSSGDLVT 257
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1038-1261 |
6.17e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.60 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1038 VVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--MAGTVLLDGQE-----AKKLNVqwLRA 1109
Cdd:PRK09473 20 VTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREilnlpEKELNK--LRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 -QLGIVSQEP-----------------ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFietlpqkyetrvgdkg 1171
Cdd:PRK09473 97 eQISMIFQDPmtslnpymrvgeqlmevLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPH---------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1172 tQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVIDNGK 1248
Cdd:PRK09473 161 -EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMYAGR 239
|
250
....*....|...
gi 6981354 1249 VKEHGTHQQLLAQ 1261
Cdd:PRK09473 240 TMEYGNARDVFYQ 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
391-614 |
6.41e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSypsRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCL---RE 467
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFS-TTIAENIRYG-RGNVTMDE--IKKAVkeanaydfIMKLPQkfdtlVGDRGA------QLSGGQKQR 537
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKLEA-----VGLRGAaklmpsELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEA-------EVQAALdkareGRTTIVIAHR----LSTVRNADVIAgfeDGVIV 606
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGvlvklisELNSAL-----GVTCVVVSHDvpevLSIADHAYIVA---DKKIV 223
|
....*...
gi 6981354 607 EQGSHSEL 614
Cdd:PRK11831 224 AHGSAQAL 231
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1060-1245 |
6.79e-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: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1060 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVlldgqeakklnvqwlraqlgivsqepILFDCSIAkniaygdnsrvvs 1139
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDI------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1140 qdeivraakeanihpFIETLPQKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD-- 1217
Cdd:smart00382 42 ---------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180 190
....*....|....*....|....*....|...
gi 6981354 1218 -----KAREGRTCIVIAHRLSTIQNADLIVVID 1245
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
123-328 |
7.06e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 67.92 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 123 GVLLAAYIQVSFWTLAAGRQIRK--------IRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQ 194
Cdd:cd18563 47 LGLAGAYVLSALLGILRGRLLARlgeritadLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 195 AIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 274
Cdd:cd18563 127 NILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIK 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 275 RYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 328
Cdd:cd18563 207 RFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG 260
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1049-1249 |
7.25e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGTVLLDG---QEAKKLNVQWL-----RAQLGIVsqepil 1120
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgriIYEQDLIVARLqqdppRNVEGTV------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 FDcSIAKNIA--------YGDNSRVVSQDEIVRAAKE-ANIHPFIETLPQ-KYETRVGD-----------KGTQLSGGQK 1179
Cdd:PRK11147 84 YD-FVAEGIEeqaeylkrYHDISHLVETDPSEKNLNElAKLQEQLDHHNLwQLENRINEvlaqlgldpdaALSSLSGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1180 QRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1052-1230 |
9.86e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1052 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKL------NVQWLRAQLGIVS----QEPILF 1121
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKTeltaLENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1122 DCSIakniaygdnSRVVSQDEIVRAAKEANIHPFiETLPQKyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEAT 1201
Cdd:PRK13538 98 YQRL---------HGPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 6981354 1202 SALDTESEKVVQEALDK-AREGRTCIVIAH 1230
Cdd:PRK13538 158 TAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
416-589 |
1.24e-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: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 416 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTIS--IDGQDIrnfnvrcLREFIGVVSQEpvLFSTTIAENIRYGRGN 493
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdpPDWDEI-------LDEFRGSELQN--YFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 494 VTMDEIKKAVKeANAYDFIMKLPQ--KFDTLVG--------DRG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 562
Cdd:cd03236 94 QYVDLIPKAVK-GKVGELLKKKDErgKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 6981354 563 ESEAEVQAALDK-AREGRTTIVIAHRLS 589
Cdd:cd03236 173 KQRLNAARLIRElAEDDNYVLVVEHDLA 200
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
391-617 |
1.39e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.20 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYpsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGTISIDGQDIRNFNVRcLREF 468
Cdd:CHL00131 8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 469 IGV--VSQEPVlfstTIA--ENIRYGRGNVTMDEIKKAVKEANAYDFIMKLPQKFDtLVGDRGAQL--------SGGQKQ 536
Cdd:CHL00131 84 LGIflAFQYPI----EIPgvSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 537 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGShSE 613
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AE 237
|
....
gi 6981354 614 LIKK 617
Cdd:CHL00131 238 LAKE 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1054-1260 |
1.62e-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: 68.31 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1054 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PMAGTVLLDGQEAKKLN-VQWLRAQLGIVSQEP----ILFDCSIAK 1127
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1128 NIAYGDNSRVVSQDEIVRAAKEANIHPFIETLpqKYETRVGDKG-TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDT 1206
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1207 ESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVK----EHG-THQQLLA 1260
Cdd:TIGR02633 437 GAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1043-1249 |
3.78e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.88 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1043 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRaQLGIV----SQep 1118
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1119 ILFDCSIA------KNIaYGdnsrvVSQDEIvraakEANIHPFIETLpqkyetRVGDKGT----QLSGGQKQRIAIARAL 1188
Cdd:COG4586 107 LWWDLPAIdsfrllKAI-YR-----IPDAEY-----KKRLDELVELL------DLGELLDtpvrQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1189 IRQPRVLLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV 1249
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1033-1233 |
4.18e-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: 67.47 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVF-NYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklnvqwlRA 1109
Cdd:TIGR00954 447 YQDNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQEPILFDCSIAKNIAYGDNSrvvsQDEIVRAAKEANIHPFIETLPQKY--ETRVG-----DKGTQLSGGQKQRI 1182
Cdd:TIGR00954 516 KLFYVPQRPYMTLGTLRDQIIYPDSS----EDMKRRGLSDKDLEQILDNVQLTHilEREGGwsavqDWMDVLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAreGRTCIVIAHRLS 1233
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
782-967 |
4.76e-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: 65.05 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 782 LTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANlgTGIIISFIYG--WQLTLLL 859
Cdd:cd18590 67 LNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK--TLGMLGFMLSlsWQLTLLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 860 LSVVPFIAVAgiveMKMLAGNAKRDKKEME----AAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHI 935
Cdd:cd18590 143 LIEMPLTAIA----QKVYNTYHQKLSQAVQdsiaKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTV 218
|
170 180 190
....*....|....*....|....*....|..
gi 6981354 936 YGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18590 219 RAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
144-335 |
6.45e-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: 64.77 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 144 RKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDdISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAI 223
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 224 LGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFL 303
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
170 180 190
....*....|....*....|....*....|....*..
gi 6981354 304 LIYASYALAFWYGSTLVISKEYTIG-----NAMTVFF 335
Cdd:cd18570 234 ISLIGSLLILWIGSYLVIKGQLSLGqliafNALLGYF 270
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
769-916 |
6.54e-11 |
|
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: 64.84 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 769 FLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIIS 848
Cdd:cd18564 72 YAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRR--TGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVM 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 849 FIYGWQLTLLLLSVVPFIAVAGIV---EMKMLAGNAKRDKKEMEAagkIATEAIENIRTVVSLTQERKFES 916
Cdd:cd18564 150 FWLDWQLALIALAVAPLLLLAARRfsrRIKEASREQRRREGALAS---VAQESLSAIRVVQAFGREEHEER 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1045-1254 |
6.62e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1045 RANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPMA-------GTVLLDGQEAKKLNVQWL---RAQLGI 1113
Cdd:PRK13547 12 RHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1114 VSQEPILFdcsiakniaygdnsrvvSQDEIV--------RAAKEANIHPFiETLPQKYE-----TRVGDKGTQLSGGQKQ 1180
Cdd:PRK13547 91 AAQPAFAF-----------------SAREIVllgryphaRRAGALTHRDG-EIAWQALAlagatALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1181 RIAIARAL---------IRQPRVLLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVIDNGK 1248
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGA 232
|
....*.
gi 6981354 1249 VKEHGT 1254
Cdd:PRK13547 233 IVAHGA 238
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1032-1254 |
8.25e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.76 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVvfNYPTRAnvpvLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGTVLLDGQEAKKLNVQWL 1107
Cdd:PRK11022 10 SVHFGDE--SAPFRA----VDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1108 R----AQLGIVSQEPIL---------FDCSIAKNIAYGDNSRVVSQdeivRAakeanihpfIETLPQ----KYETRVGDK 1170
Cdd:PRK11022 84 RnlvgAEVAMIFQDPMTslnpcytvgFQIMEAIKVHQGGNKKTRRQ----RA---------IDLLNQvgipDPASRLDVY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1171 GTQLSGGQKQRIAIARALIRQPRVLLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIDNG 1247
Cdd:PRK11022 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAG 230
|
....*..
gi 6981354 1248 KVKEHGT 1254
Cdd:PRK11022 231 QVVETGK 237
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1050-1272 |
1.12e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPMAGTVLLDGqeaKKLNVQWLRaQLGIVSQEPILFD----- 1122
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---RKPTKQILK-RTGFVTQDDILYPhltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 -----CSIAKNiaygdnSRVVSQDEIVRAAkEANIHPFieTLPQKYETRVGDKGTQ-LSGGQKQRIAIARALIRQPRVLL 1196
Cdd:PLN03211 159 etlvfCSLLRL------PKSLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1197 LDEATSALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIDNGKVKEHGTHQQLLAqkgiYFSMVNIQ 1272
Cdd:PLN03211 230 LDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
400-613 |
1.45e-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: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 400 YPSRANIKILKGLNLKVKSG-----QTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDirnfnvrclrefigvVSQ 474
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 475 EPVLFSTTIAENIRYgrgnvTMDEIKKAVKEANAYDF-IMKlPQKFDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:cd03237 66 KPQYIKADYEGTVRD-----LLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 554 DEATSALDTESEAEVQAALDKAREG--RTTIVIAHrlsTVRNADVIAgfeDGVIVEQGSHSE 613
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 ... |
1031-1247 |
1.67e-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: 61.88 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1031 GSVTFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-ERFYD-PMAGTVLLDGQEAKKLnvqwL 1107
Cdd:cd03232 2 SVLTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDKN----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1108 RAQLGIVSQEPILFDCSiakniaygdnsrvvsqdeIVRAAKE--ANIhpfietlpqkyetrvgdKGtqLSGGQKQRIAIA 1185
Cdd:cd03232 78 QRSTGYVEQQDVHSPNL------------------TVREALRfsALL-----------------RG--LSVEQRKRLTIG 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1186 RALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVIDNG 1247
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1037-1260 |
1.95e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1037 EVVF---NY----PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM-AGTVLLDGQEAKKLN-VQWL 1107
Cdd:PRK13549 257 EVILevrNLtawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNpQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1108 RAQLGIVSQEP----ILFDCSIAKNIAYGDNSRVVSQDEIVRAAKEANIHPFIETLPQKY---ETRVGdkgtQLSGGQKQ 1180
Cdd:PRK13549 337 AQGIAMVPEDRkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTaspELAIA----RLSGGNQQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1181 RIAIARALIRQPRVLLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVK----- 1250
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdlin 489
|
250
....*....|
gi 6981354 1251 EHGTHQQLLA 1260
Cdd:PRK13549 490 HNLTQEQVME 499
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1032-1235 |
4.08e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.21 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1032 SVTFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQL 1111
Cdd:PRK15056 6 GIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 GiVSQE-----PILFDcSIAKNIAYGDNS---RVVSQD-EIVRAAKEAnihpfIETLPQKYEtRVGdkgtQLSGGQKQRI 1182
Cdd:PRK15056 84 P-QSEEvdwsfPVLVE-DVVMMGRYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1183 AIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1235
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1054-1259 |
5.28e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.49 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1054 LSLEVKKGQTLALVGSSGCGKSTvvqLLERfydpMAGT------VLLDGQ-----EAKKLNVQwlRAQLgiVSQEPILFD 1122
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLAR----MAGLlpgsgsIQFAGQpleawSAAELARH--RAYL--SQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSI---------AKNIAYGDNSRVvsqDEIVRAAKeanihpfietLPQKYETRVGdkgtQLSGGQKQRIAIArALIRQ-- 1191
Cdd:PRK03695 84 MPVfqyltlhqpDKTRTEAVASAL---NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLA-AVVLQvw 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1192 ----P--RVLLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVIDNGKVKEHGTHQQL 1258
Cdd:PRK03695 146 pdinPagQLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEV 220
|
.
gi 6981354 1259 L 1259
Cdd:PRK03695 221 L 221
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1049-1261 |
6.29e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.35 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGTVLLDGQEAKKLNVQwLRAQLGI--VSQEPI----- 1119
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1120 ----LFDCSIAKNIAYGDnsrvvsQDEIVRAAKEANIHPFIETL--PQKYETRVGDKGtqLSGGQKQRIAIARALIRQPR 1193
Cdd:PRK09580 94 snqfFLQTALNAVRSYRG------QEPLDRFDFQDLMEEKIALLkmPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1194 VLLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVIDNGKVKEHGTH---QQLLAQ 1261
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1037-1239 |
6.44e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1037 EVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWlRAQLGIVSQ 1116
Cdd:PRK13540 6 ELDFDYHDQ---PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1117 EP-ILFDCSIAKNIAYG--DNSRVVSQDEIVRAAKEANIHPFIETLpqkyetrvgdkgtqLSGGQKQRIAIARALIRQPR 1193
Cdd:PRK13540 82 RSgINPYLTLRENCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6981354 1194 VLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1239
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
751-967 |
1.01e-09 |
|
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: 61.31 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 751 NMFSLVFLGLGV-HSFFTFFlQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLaTDAAQVQGA-TG 828
Cdd:cd18570 42 NIISIGLILLYLfQSLLSYI-RSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRK--TGEIISRF-NDANKIREAiSS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 829 TRLALIAQNTANLGTGIIIsFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTV 905
Cdd:cd18570 118 TTISLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYILIILLFNKPF---KKKNREVMESNAELNSyliESLKGIETI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 906 VSLTQERKFesmyVEKLHGPYRNSVRKAHIYGITFSISQAFM----YFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18570 194 KSLNAEEQF----LKKIEKKFSKLLKKSFKLGKLSNLQSSIKglisLIGSLLILWIGSYLVIKGQL 255
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
391-595 |
1.07e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG 470
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPVLFSTTIAEN----IRYGRGNVTMDEIKKAVKEANAYDFIMKLpqkfdtlvgdrgaqLSGGQKQRIAIARALVR 546
Cdd:PRK13540 79 VGHRSGINPYLTLRENclydIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6981354 547 NPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRNAD 595
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
407-586 |
1.66e-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: 61.87 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDgQDIRnfnvrclrefIGVVSQEPVLFST-TIAE 485
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK----------VGYLPQEPQLDPTkTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 486 NIRYGrgnvtMDEIKKAVKE-------------------------------ANAYDFIMKLPQKFDTL---VGD-RGAQL 530
Cdd:TIGR03719 88 NVEEG-----VAEIKDALDRfneisakyaepdadfdklaaeqaelqeiidaADAWDLDSQLEIAMDALrcpPWDaDVTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981354 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH 586
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
784-965 |
1.76e-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: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 784 TRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVV 863
Cdd:cd18589 69 SRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 864 PFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGI---TF 940
Cdd:cd18589 147 PLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVsmwTS 226
|
170 180
....*....|....*....|....*
gi 6981354 941 SISQAFMyfsYAGCFRFGSYLIVNG 965
Cdd:cd18589 227 SFSGLAL---KVGILYYGGQLVTAG 248
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1048-1248 |
1.95e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1048 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAK-KLNVQWLRAQLGIVSQE-PILFDCSI 1125
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 AKNIAYGDNSR---VVSQDEIVRAAKEANIHPFIETLPQkyetrvgDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1202
Cdd:PRK10982 91 MDNMWLGRYPTkgmFVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1203 ALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVIDNGK 1248
Cdd:PRK10982 164 SL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
755-973 |
2.01e-09 |
|
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: 60.10 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 755 LVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA--TGTRLA 832
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFvmMLLRML 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 833 LIAqnTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQE- 911
Cdd:cd18548 121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 912 ---RKFESMyVEKLhgpYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 973
Cdd:cd18548 199 yeeERFDKA-NDDL---TDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLV 259
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
122-342 |
2.05e-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: 60.16 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 122 GGVLLAAYI-------QVSFWTLAAGRQI-RKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISE----GIGDkv 189
Cdd:cd18549 45 GAILLALYIlrtllnyFVTYWGHVMGARIeTDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 190 gmFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLST--------AVWAKILSTFSDkelaayakAGAVAEEALGAIR 261
Cdd:cd18549 123 --LFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTiyfnkkmkKAFRRVREKIGE--------INAQLEDSLSGIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 262 TVIAFGGQNKELERYQK---HLENAKKIGIKkaISANISMGIAFL--LIYASyALAFwyGSTLVISKEYTIGNAMTvfFS 336
Cdd:cd18549 193 VVKAFANEEYEIEKFDEgndRFLESKKKAYK--AMAYFFSGMNFFtnLLNLV-VLVA--GGYFIIKGEITLGDLVA--FL 265
|
....*.
gi 6981354 337 ILIGAF 342
Cdd:cd18549 266 LYVNVF 271
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
382-606 |
2.10e-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: 61.38 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 382 HKPDSIKGN-LEFSDVHFSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPT-EGTISIDGQ--DI 457
Cdd:TIGR02633 248 HEPHEIGDViLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 458 RNfnvrCL-------------REFIGVVSQEPVLFSTTIAENIRY-GRGNVT----MDEIKKAVKEANAYDFIMKLPQkf 519
Cdd:TIGR02633 328 RN----PAqairagiamvpedRKRHGIVPILGVGKNITLSVLKSFcFKMRIDaaaeLQIIGSAIQRLKVKTASPFLPI-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 520 dtlvgdrgAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVrnadviA 598
Cdd:TIGR02633 402 --------GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEV------L 467
|
....*...
gi 6981354 599 GFEDGVIV 606
Cdd:TIGR02633 468 GLSDRVLV 475
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
391-569 |
2.32e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPsrANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTIsidgqdIRNFNVRclrefIG 470
Cdd:PLN03073 509 ISFSDASFGYP--GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPV----LFSTTIaenirygrgnVTMDEIKKAVKEanaydfimklpQKFDTLVGDRGAQ----------LSGGQKQ 536
Cdd:PLN03073 576 VFSQHHVdgldLSSNPL----------LYMMRCFPGVPE-----------QKLRAHLGSFGVTgnlalqpmytLSGGQKS 634
|
170 180 190
....*....|....*....|....*....|....
gi 6981354 537 RIAIARALVRNPKILLLDEATSALDTES-EAEVQ 569
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
401-591 |
2.84e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 401 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYD-PTEGTISIDGQ--DIRNfnvrCL------------ 465
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRN----PQqaiaqgiamvpe 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 466 -REFIGVVSQEPVLFSTTIAENIRYGRGNVtmdeIKKAVKEANAYDFIMKLPQKFDTLVGdRGAQLSGGQKQRIAIARAL 544
Cdd:PRK13549 346 dRKRDGIVPVMGVGKNITLAALDRFTGGSR----IDDAAELKTILESIQRLKVKTASPEL-AIARLSGGNQQKAVLAKCL 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6981354 545 VRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTV 591
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEV 468
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1049-1264 |
2.99e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVlldgqeakklnvQWL-RAQLGIVSQEP--------I 1119
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeNANIGYYAQDHaydfendlT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1120 LFDCsIAKNIAYGDNSRVV---------SQDEIVRAAKeanihpfietlpqkyetrvgdkgtQLSGGQKQRIAIARALIR 1190
Cdd:PRK15064 401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVK------------------------VLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1191 QPRVLLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVIDNGKVKEHGTHQQLLAQKGI 1264
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
126-343 |
3.76e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 59.42 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 126 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18550 54 LLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 206 GFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGA--IRTVIAFGGQNKELERYQKHLENA 283
Cdd:cd18550 134 MLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSREL 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 284 KKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAFS 343
Cdd:cd18550 214 RDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTlvAFTALLGRLYGPLT 275
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
381-590 |
4.58e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 381 GHKPDSikgnlefSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ-RLYDPT-EGTISIDGqdiR 458
Cdd:PLN03211 66 GHKPKI-------SDETRQIQERT---ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---R 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 459 NFNVRCLREfIGVVSQEPVLFS-TTIAENIRYGRGNVTMDEIKKAVKEANAYDFI--MKLPQKFDTLVGD---RGaqLSG 532
Cdd:PLN03211 133 KPTKQILKR-TGFVTQDDILYPhLTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISG 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 533 GQKQRIAIARALVRNPKILLLDEATSALD-TESEAEVQAALDKAREGRTTIVIAHRLST 590
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) ... |
1042-1254 |
9.12e-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: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1042 YPTRANVPVLQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLerfydpmAGTVLLDGQEAKKLNVQwlraqlgiVSQ 1116
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT--------VSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1117 EPilfdcsiaKNIAYGDNSRVvsQDEIVRAAKEANIHPFIET-------LPQKYETRVgdkgTQLSGGQKQRIAIARALI 1189
Cdd:cd03237 66 KP--------QYIKADYEGTV--RDLLSSITKDFYTHPYFKTeiakplqIEQILDREV----PELSGGELQRVAIAACLS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1190 RQPRVLLLDEATSALDTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVIDnGKVKEHGT 1254
Cdd:cd03237 132 KDADIYLLDEPSAYLDVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
752-967 |
1.12e-08 |
|
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: 57.90 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 752 MFSLVFLGLGVHSFFTFFLQ---GFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG-AT 827
Cdd:cd18563 41 LLLLLVLGLAGAYVLSALLGilrGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDfLS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 828 GTRLALIAQNTANLGTGIIIsFIYGWQLTLLLLSVVPFIAVAGIVEMKML-AGNAKRDKKEMEAAGKIAtEAIENIRTVV 906
Cdd:cd18563 119 DGLPDFLTNILMIIGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIrRLFHRQWRRWSRLNSVLN-DTLPGIRVVK 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 907 SLTQErKFESMYVEKLHGPYRNSVRKAH--------IYGITFSISQAFMYFsyagcfrFGSYLIVNGHM 967
Cdd:cd18563 197 AFGQE-KREIKRFDEANQELLDANIRAEklwatffpLLTFLTSLGTLIVWY-------FGGRQVLSGTM 257
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
710-933 |
1.54e-08 |
|
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: 57.55 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 710 FVVGTLCAIANGALQPAFSIILSEMIAIFGPGddtvKQQKCNMFSLVFLGLGVHSF--FTFFLQGFTFGKAGEILTTRLR 787
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIG----SKSLGLLLGLALLLLGAYLLraLLNFLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 788 SMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQgatgtRLAL--IAQNTANLGTGIIIS---FIYGWQLTLLLLSV 862
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDR--QTGDLMSRVINDVANVE-----RLIAdgIPQGITNVLTLVGVAiilFSINPKLALLTLIP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 863 VPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSLTQERKfESMYVEKLHGPYRNSVRKA 933
Cdd:cd18778 150 IPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEE-EAKRFEALSRRYRKAQLRA 219
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
754-967 |
1.75e-08 |
|
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: 57.50 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 754 SLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLAL 833
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERET--SGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 834 IAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKmLAGNAKRDKKEmEAAGKIAT--EAIENIRTVVSLTQE 911
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR-RSSRAYRRARE-RIAAVNADlqETLAGIRVVQAFRRE 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 912 RKFESMYVEkLHGPYRNSVRKAHIYgitFSISQAFMYF----SYAGCFRFGSYLIVNGHM 967
Cdd:cd18546 198 RRNAERFAE-LSDDYRDARLRAQRL---VAIYFPGVELlgnlATAAVLLVGAWRVAAGTL 253
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1051-1241 |
1.86e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1051 LQGLSLEV-----KKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLldgqeaKKLNV----QWLRA-QLGIVSQepil 1120
Cdd:PRK13409 350 LGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELKIsykpQYIKPdYDGTVED---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1121 FDCSIAKNIaygDNSRVvsQDEIVRaakeanihPFieTLPQKYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEA 1200
Cdd:PRK13409 420 LLRSITDDL---GSSYY--KSEIIK--------PL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6981354 1201 TSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIqnaDLI 1241
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
148-342 |
1.92e-08 |
|
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: 57.13 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 148 QKFFHAILRQEMGWFDIKGTTELNTRLtDDISKISEGIGDKVGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLS 227
Cdd:cd18555 79 SDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 228 TAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYA 307
Cdd:cd18555 158 LLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFI 237
|
170 180 190
....*....|....*....|....*....|....*
gi 6981354 308 SYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF 342
Cdd:cd18555 238 APLLILWIGAYLVINGELTLG--ELIAFSSLAGSF 270
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1036-1233 |
2.02e-08 |
|
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: 56.61 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1036 NEVVFNYPtrANVPVLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDPMAGTVLLD---GQEAKKLNV 1104
Cdd:cd03236 4 DEPVHRYG--PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1105 QWLRAQLGI------VSQEPILFDCSIAKNIAYGDNSRVvsQDEIVraaKEANIHPFIETlpqkyetrvgdKGTQLSGGQ 1178
Cdd:cd03236 81 KLLEGDVKVivkpqyVDLIPKAVKGKVGELLKKKDERGK--LDELV---DQLELRHVLDR-----------NIDQLSGGE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1179 KQRIAIARALIRQPRVLLLDEATSALDTESE----KVVQEAldkAREGRTCIVIAHRLS 1233
Cdd:cd03236 145 LQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaRLIREL---AEDDNYVLVVEHDLA 200
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
110-328 |
2.94e-08 |
|
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: 56.71 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 110 MTRYAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKV 189
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 190 GMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQ 269
Cdd:cd18545 119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFARE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 270 NKELERYQKHLENAKKIGIkKAISANISMGIAFLLIYA-SYALAFWYGSTLVISKEYTIG 328
Cdd:cd18545 199 DENEEIFDELNRENRKANM-RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG 257
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
416-588 |
2.97e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 416 VKSGQTVALVGNSGCGKSTTVQLLQrlydptegtisidGQDIRNFnvrclrefiGVVSQEPvlfstTIAENIRYGRGNVT 495
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------------GELIPNL---------GDYEEEP-----SWDEVLKRFRGTEL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 496 MD--------EIKKAVKeaNAYdfIMKLPQKFDTLVGD-------RGA-------------------QLSGGQKQRIAIA 541
Cdd:PRK13409 149 QNyfkklyngEIKVVHK--PQY--VDLIPKVFKGKVREllkkvdeRGKldevverlglenildrdisELSGGELQRVAIA 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6981354 542 RALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 588
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
402-610 |
5.13e-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: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVqlLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG---VVSQEPV- 477
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 478 ------------LFsTTIAE----------------NIRYgRGNVTMDEIKKAVKEAnaYDFIMKLPQ---KFDTLV--- 523
Cdd:cd03271 82 rtprsnpatytgVF-DEIRElfcevckgkrynretlEVRY-KGKSIADVLDMTVEEA--LEFFENIPKiarKLQTLCdvg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 524 ------GDRGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN 593
Cdd:cd03271 158 lgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKC 237
|
250 260
....*....|....*....|...
gi 6981354 594 ADVI------AGFEDGVIVEQGS 610
Cdd:cd03271 238 ADWIidlgpeGGDGGGQVVASGT 260
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
376-586 |
5.51e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 376 SFSERGHKPDSikgnleFSDVHFSYPSRanIKILKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLLQRLYDPTEGTI 450
Cdd:PRK13409 325 EFEERPPRDES------ERETLVEYPDL--TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 451 SID------GQDIRNfnvrclrEFIGVVSQepVLFSttIAENIRygrGNVTMDEIKKAvkeanaydfiMKLPQKFDTLVG 524
Cdd:PRK13409 397 DPElkisykPQYIKP-------DYDGTVED--LLRS--ITDDLG---SSYYKSEIIKP----------LQLERLLDKNVK 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 525 DrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAH 586
Cdd:PRK13409 453 D----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1044-1242 |
6.27e-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: 55.31 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVqlLERFYDPMAGTVLLDGQEAKKLNVQWLRAQLG---IVSQEPI- 1119
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1120 ------------LFD------CSIAKNIAYgdNSRVV-------SQDEI----VRAAKE-----ANIHPFIETLPQ---K 1162
Cdd:cd03271 82 rtprsnpatytgVFDeirelfCEVCKGKRY--NRETLevrykgkSIADVldmtVEEALEffeniPKIARKLQTLCDvglG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1163 YeTRVGDKGTQLSGGQKQRIAIARALIRQPR---VLLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNA 1238
Cdd:cd03271 160 Y-IKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCA 238
|
....
gi 6981354 1239 DLIV 1242
Cdd:cd03271 239 DWII 242
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
413-613 |
6.86e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRnfnVRCLREFI--GVV------SQEPVLFSTTIA 484
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRSPRDAIraGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 485 ENI------RYGRGNVTMDEIKKAvkeANAYDFIMKLPQKF---DTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK11288 350 DNInisarrHHLRAGCLINNRWEA---ENADRFIRSLNIKTpsrEQLIM----NLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 556 ATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSE 613
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
151-340 |
8.15e-08 |
|
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: 55.28 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 151 FHAILRQEMGWFDIKGTTELNTRLTDdISKISEgigdkvgmFF--QAIATF----FAG--FIVGFIRGWKLTLVIMAITA 222
Cdd:cd18566 82 FEHLLSLPLSFFEREPSGAHLERLNS-LEQIRE--------FLtgQALLALldlpFVLifLGLIWYLGGKLVLVPLVLLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 223 ILglstAVWAKILSTFSDKELAAYAKAGAVAE----EALGAIRTVIAFGGQNKELERYQKHLENAKKIGIKKAISANISM 298
Cdd:cd18566 153 LF----VLVAILLGPILRRALKERSRADERRQnfliETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQ 228
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6981354 299 GIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIG 340
Cdd:cd18566 229 TLGQLFSQVSMVAVVAFGALLVINGDLTVG--ALIACTMLSG 268
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
406-611 |
8.50e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 8.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 406 IKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLL--QRLYDPTEGTISIDG-----QDIRNFNVRCLREFI---GVVSQE 475
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqETFARISGYCEQNDIhspQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 476 PVLFSTTIAENIRYGRGNVTM--DEIKKAVKEANAYDFIMKLPqkfdtlvGDRGaqLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PLN03140 973 SLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 554 DEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTvrnaDVIAGFEDGVIVEQGSH 611
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1055-1259 |
1.26e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeaKKLNV----QWLRAqlGIV------SQEPILFDCS 1124
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIrsprDAIRA--GIMlcpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1125 IAKNIAYGDNSRVVSQDEIVRAAKEA-NIHPFIETLPQKyeTRVGD-KGTQLSGGQKQRIAIARALIRQPRVLLLDEATS 1202
Cdd:PRK11288 348 VADNINISARRHHLRAGCLINNRWEAeNADRFIRSLNIK--TPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1203 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKV-----KEHGTHQQLL 1259
Cdd:PRK11288 426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
426-561 |
1.32e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 426 GNSGCGKSTTVQLLQRLYDPTEGTISIDGQ--DIRNFNVRcLRefIGVVSQEpvlFS----TTIAENIR-----YGrgnV 494
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIATR-RR--VGYMSQA---FSlygeLTVRQNLElharlFH---L 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 495 TMDEIKKAVKEanaydfimkLPQKFD--TLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:NF033858 370 PAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
417-590 |
1.43e-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: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 417 KSGQTVALVGNSGCGKSTTVQLLQrlydptegtisidGQDIRNFnvrclrefiGVVSQEPvlfstTIAENIRYGRGNVTM 496
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------------GELKPNL---------GDYDEEP-----SWDEVLKRFRGTELQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 497 D--------EIKKAVKEanayDFIMKLPQKFDTLVGD-------RGA-------------------QLSGGQKQRIAIAR 542
Cdd:COG1245 150 DyfkklangEIKVAHKP----QYVDLIPKVFKGTVREllekvdeRGKldelaeklglenildrdisELSGGELQRVAIAA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLST 590
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIYQRLNVARLIrELAEEGKYVLVVEHDLAI 274
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
392-563 |
1.48e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 392 EFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQ-DIRNFNVRclREFIg 470
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQH--RAEL- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 vvsqEPvlfSTTIAENIRYGRGNVTMDEIKKAVKeanAY--DFIMKlPQKFDTLVgdrgAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK11147 395 ----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLKPS 459
|
170
....*....|....*
gi 6981354 549 KILLLDEATSALDTE 563
Cdd:PRK11147 460 NLLILDEPTNDLDVE 474
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
416-601 |
1.83e-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: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 416 VKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGqdirnfnvrclrefigvvsqepvlfsttiaenirygrgnvt 495
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 496 mdeIKKAVKeanaydfimklPQKFDtlvgdrgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA 575
Cdd:cd03222 61 ---ITPVYK-----------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 6981354 576 RE--GRTTIVIAHRLSTVRN-ADVIAGFE 601
Cdd:cd03222 118 SEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
408-585 |
1.93e-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: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 408 ILKGLNLKVKSGQTVALVGNSGCGKST-----TVQLLQRLYDpTEGTISIDG---QDIRNFnvrcLREFIGVVSQEPVLF 479
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGitpEEIKKH----YRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 480 -STTIAENIRYG--------RGNvTMDEIKKAVKEANAYDFIMKLPQKFDTLVGD---RGaqLSGGQKQRIAIARALVRN 547
Cdd:TIGR00956 151 pHLTVGETLDFAarcktpqnRPD-GVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGG 227
|
170 180 190
....*....|....*....|....*....|....*....
gi 6981354 548 PKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA 585
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALkTSANILDTTPLVA 266
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
487-615 |
2.16e-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: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 487 IRYgRGNVTMDEIKKAVKEAnaYDFIMKLP---QKFDTLVgDRGAQ----------LSGGQKQRIAIARALVR---NPKI 550
Cdd:TIGR00630 778 VKY-KGKNIADVLDMTVEEA--YEFFEAVPsisRKLQTLC-DVGLGyirlgqpattLSGGEAQRIKLAKELSKrstGRTL 853
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 551 LLLDEATSALDTESEAE----VQAALDKareGRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQGSHSELI 615
Cdd:TIGR00630 854 YILDEPTTGLHFDDIKKllevLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEVA 925
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
528-682 |
3.01e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 528 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdKAREGrTTIVIAHRLSTVRN-ADVIAGFEDGVIV 606
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKLV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 607 E-QGSHSE-LIKKEGiYFRLVNMQtsgsqilSEEFEVELSDEKAaggvapngW-----KARIFRNSTK-KSLKSSR-AHQ 677
Cdd:PRK11147 233 SyPGNYDQyLLEKEE-ALRVEELQ-------NAEFDRKLAQEEV--------WirqgiKARRTRNEGRvRALKALRrERS 296
|
....*
gi 6981354 678 NRLDV 682
Cdd:PRK11147 297 ERREV 301
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
391-620 |
3.42e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTIsidgQDIRNFNvrclrefIG 470
Cdd:PRK15064 320 LEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSENAN-------IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQEPV--------LFS-----TTIAEN---IR--YGRGNVTMDEIKKAVKeanaydfimklpqkfdtlvgdrgaQLSG 532
Cdd:PRK15064 386 YYAQDHAydfendltLFDwmsqwRQEGDDeqaVRgtLGRLLFSQDDIKKSVK------------------------VLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKArEGrTTIVIAH------RLSTvrnaDVIAGFEDGVIV 606
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
|
250
....*....|....
gi 6981354 607 EQGSHSELIKKEGI 620
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1057-1254 |
3.48e-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: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1057 EVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGTVLLDGQEA-KKLNV----QWLRAQLGIVSQEpILFDcSIAKNIay 1131
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVdEDLKIsykpQYISPDYDGTVEE-FLRS-ANTDDF-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1132 gDNSRVvsQDEIVRaakeanihPF-IETLpqkYETRVGDkgtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEK 1210
Cdd:COG1245 431 -GSSYY--KTEIIK--------PLgLEKL---LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981354 1211 VVQEALDKAREGR--TCIVIAHRLSTIqnaDLI---VVIDNGKVKEHGT 1254
Cdd:COG1245 493 AVAKAIRRFAENRgkTAMVVDHDIYLI---DYIsdrLMVFEGEPGVHGH 538
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
381-588 |
3.93e-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: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 381 GHKPDSIKGNlEFSDVHFSYPSRANIKILKGlnlkVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNf 460
Cdd:TIGR01257 1932 GNKTDILRLN-ELTKVYSGTSSPAVDRLCVG----VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 461 NVRCLREFIGVVSQ-EPVLFSTTIAENIR-YGR-GNVTMDEIKKAvkeANAYDFIMKLPQKFDTLVGdrgaQLSGGQKQR 537
Cdd:TIGR01257 2006 NISDVHQNMGYCPQfDAIDDLLTGREHLYlYARlRGVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRK 2078
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6981354 538 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRL 588
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1055-1261 |
4.28e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG--------TVLLDGQEAKKL-NVQWLRAQLGIVSQEPILFdcsi 1125
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshITRLSFEQLQKLvSDEWQRNNTDMLSPGEDDT---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1126 akniayGDNSRVVSQDEIVRAAkeanihpfietLPQKYETRVGDKG------TQLSGGQKQRIAIARALIRQPRVLLLDE 1199
Cdd:PRK10938 99 ------GRTTAEIIQDEVKDPA-----------RCEQLAQQFGITAlldrrfKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 1200 ATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQ 1261
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
407-586 |
4.77e-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: 54.02 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLLQRLYDPTEG------TISIDGQDIRNFNVRCLREFIGVVSQE 475
Cdd:COG1245 349 KSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlKISYKPQYISPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 476 PvlFSTTIAENirygrgnvtmdEIKKAvkeanaydfiMKLPQKFDTLVGDrgaqLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:COG1245 429 D--FGSSYYKT-----------EIIKP----------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190
....*....|....*....|....*....|...
gi 6981354 556 ATSALDTESEAEVQAALDKAREGR--TTIVIAH 586
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDH 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
407-564 |
5.41e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 407 KILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDgQDIRnfnvrclrefIGVVSQEPVLFST-TIAE 485
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK----------VGYLPQEPQLDPEkTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 486 NIRYGrgnvtMDEIKKAVKEANAYDFIMKLPQ-KFDTLVGDRG----------------------------------AQL 530
Cdd:PRK11819 90 NVEEG-----VAEVKAALDRFNEIYAAYAEPDaDFDALAAEQGelqeiidaadawdldsqleiamdalrcppwdakvTKL 164
|
170 180 190
....*....|....*....|....*....|....
gi 6981354 531 SGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1147-1247 |
6.20e-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: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1147 AKEANIHPFIETLPQ---KYeTRVGDKGTQLSGGQKQRIAIARALIRQ---PRVLLLDEATSALDTESEK----VVQEAL 1216
Cdd:TIGR00630 801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
|
90 100 110
....*....|....*....|....*....|.
gi 6981354 1217 DKareGRTCIVIAHRLSTIQNADLIvvIDNG 1247
Cdd:TIGR00630 880 DK---GNTVVVIEHNLDVIKTADYI--IDLG 905
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
120-340 |
6.95e-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: 52.59 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 120 LGGGVLLAAYIQVSF-------WTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLtDDISKISEGIGDkvgmf 192
Cdd:cd18782 44 IGVVMLVAALLEAVLtalrtylFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTG----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 193 fQAIATFF-AGFIVGFIR-----GWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAf 266
Cdd:cd18782 118 -TALTTLLdVLFSVIYIAvlfsySPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 267 ggQNKEL-------ERYQKHLENAKKIGIKKAISANISMGIAFLliyaSYALAFWYGSTLVISKEYTIGNAMTvfFSILI 339
Cdd:cd18782 196 --QNAELkarwrwqNRYARSLGEGFKLTVLGTTSGSLSQFLNKL----SSLLVLWVGAYLVLRGELTLGQLIA--FRILS 267
|
.
gi 6981354 340 G 340
Cdd:cd18782 268 G 268
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1035-1263 |
7.15e-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: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1035 FNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKlNVQWLRAQLGIV 1114
Cdd:TIGR01257 1940 LNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1115 SQEPILFDCSIAKNIAY-GDNSRVVSQDEIVRAAKEAnihpfIETLPQK-YETRVGdkGTqLSGGQKQRIAIARALIRQP 1192
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYlYARLRGVPAEEIEKVANWS-----IQSLGLSlYADRLA--GT-YSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1193 RVLLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIDNGKVKEHGTHQQLLAQKG 1263
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1172-1208 |
7.17e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 7.17e-07
10 20 30
....*....|....*....|....*....|....*..
gi 6981354 1172 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1208
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1050-1216 |
7.79e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLdgqeAKKLnvqwlraQLGIVSQEpilfdcsiakni 1129
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGI-------KLGYFAQH------------ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1130 aygdnsrvvsQDEIVRAaKEANIHPFIETLPQKYETRV----------GDKGT----QLSGGQKQRIAIARALIRQPRVL 1195
Cdd:PRK10636 384 ----------QLEFLRA-DESPLQHLARLAPQELEQKLrdylggfgfqGDKVTeetrRFSGGEKARLVLALIVWQRPNLL 452
|
170 180
....*....|....*....|.
gi 6981354 1196 LLDEATSALDTESEKVVQEAL 1216
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1172-1208 |
1.07e-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: 53.02 E-value: 1.07e-06
10 20 30
....*....|....*....|....*....|....*..
gi 6981354 1172 TQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTES 1208
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1033-1256 |
1.17e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1033 VTFNEVVFNYPtraNVPVL-QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLldgQEAKklnvqwlrAQL 1111
Cdd:PLN03073 509 ISFSDASFGYP---GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAK--------VRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 GIVSQEPIlfdcsiakniaygDNSRVVSQDEIVRAakeaniHPFIETLPQKYETRVGDKGTQ----------LSGGQKQR 1181
Cdd:PLN03073 575 AVFSQHHV-------------DGLDLSSNPLLYMM------RCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSR 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1182 IAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVIDNGKVKE-HGTHQ 1256
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1058-1230 |
1.65e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1058 VKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGqeakklnvQWlraQLGIVSQEPILFDCSIAKNIAYGDnsRV 1137
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------NW---QLAWVNQETPALPQPALEYVIDGD--RE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1138 VSQDEI-VRAAKEANIHPFIETLPQKYET---------------RVGDKGTQL-------SGGQKQRIAIARALIRQPRV 1194
Cdd:PRK10636 91 YRQLEAqLHDANERNDGHAIATIHGKLDAidawtirsraasllhGLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSDL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 6981354 1195 LLLDEATSALDTESEKVVQEALdKAREGrTCIVIAH 1230
Cdd:PRK10636 171 LLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISH 204
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
126-344 |
1.94e-06 |
|
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: 51.41 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 126 LAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFFQAIATFFAGFIV 205
Cdd:cd18565 69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 206 GFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKk 285
Cdd:cd18565 149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYR- 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 286 igiKKAISAnISMGIAF-----LLIYASYALAFWYGSTLVISKEYTIGNAMTVffsiliGAFSV 344
Cdd:cd18565 228 ---DANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
715-912 |
2.10e-06 |
|
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: 50.94 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 715 LCAIANGALQPAFSIILSEMI--AIFGPGDDTVkqqkcNMFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSMAFK 792
Cdd:cd18550 6 LLILLSALLGLLPPLLLREIIddALPQGDLGLL-----VLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 793 AMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVP-FIAVAGI 871
Cdd:cd18550 81 HLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPlFVLPTRR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6981354 872 VemkmlaGNAKRdkkemeaagKIATEAIENIRTVVSLTQER 912
Cdd:cd18550 159 V------GRRRR---------KLTREQQEKLAELNSIMQET 184
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1055-1217 |
2.13e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVlldgQEAKKLNVQWL---RAQLgivsqEPilfDCSIAKNIAY 1131
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFdqhRAEL-----DP---EKTVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1132 GD-----NSR---VVS--QDEIvraakeanIHPFIETLPQKyetrvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEAT 1201
Cdd:PRK11147 407 GKqevmvNGRprhVLGylQDFL--------FHPKRAMTPVK----------ALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
170
....*....|....*.
gi 6981354 1202 SALDTESEKVVQEALD 1217
Cdd:PRK11147 469 NDLDVETLELLEELLD 484
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
391-613 |
2.26e-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: 51.86 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 391 LEFSDVHFSYPSRAnikILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIdGQDIRnfnvrclrefIG 470
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 471 VVSQ--EPVLFSTTIAENIRYGrgnvtMDEIKKAVKEAN--AY----DFIMKLPQKfdtLVGdrgaQLSGGQKQRIAIAR 542
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGG-----LDIIKLGKREIPsrAYvgrfNFKGSDQQK---KVG----QLSGGERNRVHLAK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981354 543 ALVRNPKILLLDEATSALDTESEAEVQAALDKAreGRTTIVIAH-RLSTVRNADVIAGFEDGVIVE--QGSHSE 613
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdRWFLDRIATHILAFEGDSHVEwfEGNFSE 528
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
751-967 |
2.50e-06 |
|
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: 50.66 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 751 NMFSLVFLGLGVHSFFTFFLQGF---TFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQGAT 827
Cdd:cd18566 39 PTLQVLVIGVVIAILLESLLRLLrsyILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 828 GTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVS 907
Cdd:cd18566 116 TGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 908 LTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18566 196 MAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDL 255
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
752-967 |
2.56e-06 |
|
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: 50.94 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 752 MFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 831
Cdd:cd18540 43 GFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 832 ALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIA-VAGIVEMKMLAGNAKRDKKEMEAAGKIaTEAIENIRTVVSLTQ 910
Cdd:cd18540 121 VDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAvVSIYFQKKILKAYRKVRKINSRITGAF-NEGITGAKTTKTLVR 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 911 ERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18540 200 EEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAI 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1049-1260 |
2.62e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLDGQEAKKLNVQWLRAQlGIV------SQEPILFD 1122
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1123 CSIAKNI---AYGDNSRVVSQdeIVRAAKEANIHPFIETLPQKYETR---VGDkgtqLSGGQKQRIAIARALIRQPRVLL 1196
Cdd:PRK10762 345 MSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMeqaIGL----LSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1197 LDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIDNGKV-----KEHGTHQQLLA 1260
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1173-1244 |
3.65e-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: 3.65e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1173 QLSGGQKQRIAIARALIRQPRVLLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVI 1244
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
402-609 |
3.90e-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: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQllQRLYDPTEgtisidgqdirnfnvRCLREFIGVVSQEPVLF-- 479
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGK---------------ARLISFLPKFSRNKLIFid 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 480 --STTIAENIRYgrgnvtmdeikkavkeanaydfiMKLPQKFDTLvgdrgaqlSGGQKQRIAIARALVRNPK--ILLLDE 555
Cdd:cd03238 67 qlQFLIDVGLGY-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 556 ATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQG 609
Cdd:cd03238 116 PSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
120-338 |
5.62e-06 |
|
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: 49.79 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 120 LGGGVLLAAYIQ-VSFWT-------LAAGRQIRkIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGdKVGM 191
Cdd:cd18543 41 LVLLLLALGVAEaVLSFLrrylagrLSLGVEHD-LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 192 FFQAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNK 271
Cdd:cd18543 119 LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERR 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 272 ELERYQKHLENAKKIGIKKA-ISANISMGIAfLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSIL 338
Cdd:cd18543 199 ELDRFEAAARRLRATRLRAArLRARFWPLLE-ALPELGLAAVLALGGWLVANGSLTLG-TLVAFSAYL 264
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1058-1244 |
7.60e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1058 VKKGQTLALVGSSGCGKSTVVQLL---------------------ERFydpmAGTVLLDgqEAKKLNVQWLRAQLGI--V 1114
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTELQN--YFKKLYNGEIKVVHKPqyV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1115 SQEPILFDCSIAKNIAYGDNSRVVsqDEIVraaKEANIHPFIetlpqkyetrvgDKG-TQLSGGQKQRIAIARALIRQPR 1193
Cdd:PRK13409 170 DLIPKVFKGKVRELLKKVDERGKL--DEVV---ERLGLENIL------------DRDiSELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1194 VLLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVVI 1244
Cdd:PRK13409 233 FYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
409-585 |
9.99e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFN-----------VRCLREFIGVVSQEPV 477
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 478 LFSTTIAeNIRYGRGNVTMDEIKKAVKEANAYDFIM--KLPQKfDTLVGdrgaQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK10982 344 GFNSLIS-NIRNYKNKVGLLDNSRMKSDTQWVIDSMrvKTPGH-RTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190
....*....|....*....|....*....|.
gi 6981354 556 ATSALDTESEAEV-QAALDKAREGRTTIVIA 585
Cdd:PRK10982 418 PTRGIDVGAKFEIyQLIAELAKKDKGIIIIS 448
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1043-1205 |
1.09e-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: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1043 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPmAGTVLLDGQEAKKlnvqwlraqlgivsqep 1118
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKE----------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1119 ilfdcsiAKNIAYGDNSRVVSQDeivraakeanIHPFIETLPQKYETRVGDKGTQ----LSGGQKQRIAIARALIRQPRV 1194
Cdd:cd03233 77 -------FAEKYPGEIIYVSEED----------VHFPTLTVRETLDFALRCKGNEfvrgISGGERKRVSIAEALVSRASV 139
|
170
....*....|.
gi 6981354 1195 LLLDEATSALD 1205
Cdd:cd03233 140 LCWDNSTRGLD 150
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1046-1248 |
1.11e-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: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1046 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ-------------LLERFYDPMagTVLLDgqeakklnvqwlraQLG 1112
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeglyasgkarlisFLPKFSRNK--LIFID--------------QLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1113 IVsqepilfdcsIAKNIAYgdnsrvvsqdeivraakeanihpfiETLPQKYETrvgdkgtqLSGGQKQRIAIARALIRQP 1192
Cdd:cd03238 70 FL----------IDVGLGY-------------------------LTLGQKLST--------LSGGELQRVKLASELFSEP 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 1193 R--VLLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIvvIDNGK 1248
Cdd:cd03238 107 PgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWI--IDFGP 163
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1134-1248 |
1.17e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1134 NSRVVSQDEIVRAAKEANIHPFIETLPQKYETRVGD---KGtqLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESek 1210
Cdd:TIGR00956 169 QNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT-- 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 6981354 1211 vvqeALDKAREGRTCIVIAHRLSTI------QNA----DLIVVIDNGK 1248
Cdd:TIGR00956 245 ----ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
124-342 |
1.23e-05 |
|
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: 48.71 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 124 VLLAAYIQVSFWTLAAG--RQI------RKIR----QKFFHAILRQEMGWFDikgttelnTRLTDDI-SKISEGigDKVG 190
Cdd:cd18568 43 LILIGLLIVGIFQILLSavRQYlldyfaNRIDlsllSDFYKHLLSLPLSFFA--------SRKVGDIiTRFQEN--QKIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 191 MFF--QAIATF------FAGFIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRT 262
Cdd:cd18568 113 RFLtrSALTTIldllmvFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIAT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 263 VIAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIG 340
Cdd:cd18568 193 IKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQlvAFNMLFGSVIN 272
|
..
gi 6981354 341 AF 342
Cdd:cd18568 273 PL 274
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1168-1263 |
1.45e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1168 GDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVID 1245
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|....*...
gi 6981354 1246 NGKVKEHGTHQQLLAQKG 1263
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
409-647 |
1.65e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQdirnfnVRCLREFIGVVSQepvlfsTTIAENIR 488
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------VSVIAISAGLSGQ------LTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 489 YGR--GNVTMDEIKKAVKEANAY----DFIMKLPQKFdtlvgdrgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDt 562
Cdd:PRK13546 108 FKMlcMGFKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 563 esEAEVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELIKKegiYFRLVNMQTSGSQILSE 637
Cdd:PRK13546 176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAFLNDFKKKSKAEQK 250
|
250
....*....|
gi 6981354 638 EFEVELSDEK 647
Cdd:PRK13546 251 EFRNKLDESR 260
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1036-1239 |
1.67e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1036 NEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE----RFYdpmAGTVLLDGQeakklnvqwlraQL 1111
Cdd:PRK10938 264 NNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGY---SNDLTLFGR------------RR 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1112 GivSQEPIlFDcsIAKNIAYGDNS-----RVVSQ----------DEI--VRAAKEANihpfiETLPQKYETRVG-DKGT- 1172
Cdd:PRK10938 326 G--SGETI-WD--IKKHIGYVSSSlhldyRVSTSvrnvilsgffDSIgiYQAVSDRQ-----QKLAQQWLDILGiDKRTa 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1173 -----QLSGGQkQRIA-IARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRT--------------CivIAHR 1231
Cdd:PRK10938 396 dapfhSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHR 472
|
....*...
gi 6981354 1232 LSTIQNAD 1239
Cdd:PRK10938 473 LEFVPDGD 480
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
742-967 |
1.92e-05 |
|
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: 47.89 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 742 DDTVKQQKCNMFSLVFLGLGvhsFFTFFLQGFTF--GKAGEILTTRL-RSMA---FKAMLRQDMSWFDdhKNSTGALSTR 815
Cdd:cd18555 30 DNVIVPGNLNLLNVLGIGIL---ILFLLYGLFSFlrGYIIIKLQTKLdKSLMsdfFEHLLKLPYSFFE--NRSSGDLLFR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 816 lATDAAQVQGATGTRLALIAQNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLAgnaKRDKKEMEAAGK-- 893
Cdd:cd18555 105 -ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIK---KLNQEEIVAQTKvq 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 894 -IATEAIENIRTVVSLTQERKFESMYVEKLHGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18555 181 sYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1050-1234 |
1.96e-05 |
|
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: 48.78 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVLLdGQEAKklnvqwlraqlgivsqepilfdcsiaknI 1129
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------------------------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1130 AYGDNSR-----------VVS--QDEIVRAAKEANihpfietlPQKYETRVGDKGT-------QLSGGQKQRIAIARALI 1189
Cdd:TIGR03719 388 AYVDQSRdaldpnktvweEISggLDIIKLGKREIP--------SRAYVGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLK 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6981354 1190 RQPRVLLLDEATSALDTESEKVVQEALDKAreGRTCIVIAH------RLST 1234
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
751-967 |
2.29e-05 |
|
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: 47.85 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 751 NMFSLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA-TGT 829
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLlSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 830 RLALIAqNTANLGTGIIISFIYGWQLTLLLLSVVPFIAVAgiveMKMLAGNAKRdkKEMEAAGKIAT------EAIENIR 903
Cdd:cd18545 118 LINLIP-DLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLV----VFLLRRRARK--AWQRVRKKISNlnaylhESISGIR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 904 TVVSLTQE----RKFESMYVEKLHGpYRNSVRKAHIYG----ITFSISQAFMYFsyagcfrFGSYLIVNGHM 967
Cdd:cd18545 191 VIQSFAREdeneEIFDELNRENRKA-NMRAVRLNALFWplveLISALGTALVYW-------YGGKLVLGGAI 254
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
409-568 |
2.79e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREFIGVVSQEP-----VL---- 478
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdglVLgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 479 ---FSTTIAENIRYGRGNVTMDEIKKAVKeanayDFIM----KLPQKfDTLVGDrgaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK10762 348 kenMSLTALRYFSRAGGSLKHADEQQAVS-----DFIRlfniKTPSM-EQAIGL----LSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|....*..
gi 6981354 552 LLDEATSALDTESEAEV 568
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEI 434
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1166-1247 |
2.92e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1166 RVGDKGTQLSGGQKQRIAIARALIRQP--RVL-LLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1238
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
....*....
gi 6981354 1239 DLIvvIDNG 1247
Cdd:PRK00349 900 DWI--IDLG 906
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
113-348 |
3.38e-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: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 113 YAYYYSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDikgTTE----LNtRLTDDISKISEGIGDK 188
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFD---TTPsgriLN-RFSKDIGLIDEELPLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 189 VGMFFQAIATFFAGFIVGFIRGWKLTLVIMAITAILG------LSTAVWAK---------ILSTFSdkelaayakagava 253
Cdd:cd18580 117 LLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYllqryyLRTSRQLRrlesesrspLYSHFS-------------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 254 eEALGAIRTVIAFGGQNKELERYQKHLenakkigikkaisaNISMGIAFLLIYASYALAFWYG--STLVIskeytignAM 331
Cdd:cd18580 183 -ETLSGLSTIRAFGWQERFIEENLRLL--------------DASQRAFYLLLAVQRWLGLRLDllGALLA--------LV 239
|
250
....*....|....*...
gi 6981354 332 TVFFSILI-GAFSVGQAA 348
Cdd:cd18580 240 VALLAVLLrSSISAGLVG 257
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
845-967 |
3.49e-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: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 845 IIISFIYGWQLTLLLLSVVPFIAVAGIVEMKMLagNAKRDKKEMEAAGKIA--TEAIENIRTVVSLTQERKFESMYVEKL 922
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPIL--RRRLEEKFQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEELL 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6981354 923 HGPYRNSVRKAHIYGITFSISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18588 211 ARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGEL 255
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
426-597 |
4.66e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 426 GNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNfnvrCLREFIGVVSQEPVL-FSTTIAENIRYgrgnvtMDEIKKAVK 504
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN----IAKPYCTYIGHNLGLkLEMTVFENLKF------WSEIYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 505 EANAYDFIMKLpqkfDTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD-KAREGRTTIV 583
Cdd:PRK13541 103 TLYAAIHYFKL----HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLL 178
|
170
....*....|....
gi 6981354 584 IAHRLSTVRNADVI 597
Cdd:PRK13541 179 SSHLESSIKSAQIL 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
404-609 |
4.90e-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: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 404 ANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVqllqrlYDptegTISIDGQ-----DIRNFnvrcLREFIGVVSQEPVL 478
Cdd:cd03270 6 AREHNLKNVDVDIPRNKLVVITGVSGSGKSSLA------FD----TIYAEGQrryveSLSAY----ARQFLGQMDKPDVD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 479 FST-----------TIAENIRYGRGNVTmdEIkkavkeanaYDFI------MKLPQKFDTLVG--------DRGAQ-LSG 532
Cdd:cd03270 72 SIEglspaiaidqkTTSRNPRSTVGTVT--EI---------YDYLrllfarVGIRERLGFLVDvglgyltlSRSAPtLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 533 GQKQRIAIARALVRNPK--ILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVI------AGFEDG 603
Cdd:cd03270 141 GEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVidigpgAGVHGG 220
|
....*.
gi 6981354 604 VIVEQG 609
Cdd:cd03270 221 EIVAQG 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
413-614 |
5.96e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 413 NLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVRCLREFIG---------VVSQEPVLFSTTI 483
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSdewqrnntdMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 484 AENIRygrgnvtmDEIKKAVKeanaydfIMKLPQKF--DTLVGDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK10938 103 AEIIQ--------DEVKDPAR-------CEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 562 TESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 614
Cdd:PRK10938 168 VASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEI 222
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
203-343 |
7.10e-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: 46.34 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 203 FIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLEN 282
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 283 AKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAFS 343
Cdd:cd18588 213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIG--QLIAFNMLAGQVS 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1161-1230 |
7.87e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 7.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1161 QKYETRvgdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKAreGRTCIVIAH 1230
Cdd:PLN03073 338 QVKATK------TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSH 399
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1173-1260 |
9.11e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.33 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1173 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIDNGKV 1249
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 6981354 1250 KEHGTHQQLLA 1260
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
118-335 |
9.32e-05 |
|
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: 45.94 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 118 SGLGGGVLLAAYIQVSFWTLAAGRQ----IRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISEGIGDKVGMFF 193
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTgerlLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 194 QAIATFFAGFIVGFIRGWKLTLVIMAITAILGLSTAVW---------------AKILSTFSdkelaayakagavaeEALG 258
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFrrrssrayrrareriAAVNADLQ---------------ETLA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 259 AIRTVIAFGGQNKELERYQKHLENAKKIGIKkaisANISMGIAF----LLIYASYALAFWYGSTLVISKEYTIGnAMTVF 334
Cdd:cd18546 187 GIRVVQAFRRERRNAERFAELSDDYRDARLR----AQRLVAIYFpgveLLGNLATAAVLLVGAWRVAAGTLTVG-VLVAF 261
|
.
gi 6981354 335 F 335
Cdd:cd18546 262 L 262
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
529-620 |
9.32e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 529 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFEDGVIV 606
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
|
90
....*....|....
gi 6981354 607 EQGSHSELIKKEGI 620
Cdd:PRK09700 489 QILTNRDDMSEEEI 502
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1044-1251 |
9.90e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1044 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPMA-GTVLLDGQEAK-KLNVQWLRAQLGIVSQ--- 1116
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISpRSPLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1117 EPILF-DCSIAKNIAygdnsrvvsqdeIVRAAKEANIHPFIETLPQKYETRVGDKG---------------TQLSGGQKQ 1180
Cdd:PRK09700 349 DNGFFpNFSIAQNMA------------ISRSLKDGGYKGAMGLFHEVDEQRTAENQrellalkchsvnqniTELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981354 1181 RIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIDNGKVKE 1251
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
372-595 |
1.08e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 372 PKIDSFSERGHKPDSIKgNLEFSDVHFSYPSRaniKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQ----------- 440
Cdd:PRK10938 243 PEPDEPSARHALPANEP-RIVLNNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndl 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 441 RLYDPTEGTisidGQDIRNfnvrcLREFIGVVSQEPVL---FSTTIAENIRYGrgnvTMDEIK--KAVKEANaydfiMKL 515
Cdd:PRK10938 319 TLFGRRRGS----GETIWD-----IKKHIGYVSSSLHLdyrVSTSVRNVILSG----FFDSIGiyQAVSDRQ-----QKL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 516 PQKFDTLVG--DRGAQ-----LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV--- 583
Cdd:PRK10938 381 AQQWLDILGidKRTADapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvs 459
|
250 260
....*....|....*....|.
gi 6981354 584 ---------IAHRLSTVRNAD 595
Cdd:PRK10938 460 hhaedapacITHRLEFVPDGD 480
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
1058-1203 |
1.16e-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: 45.66 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1058 VKKGQTLaLVGSSGCGKSTVVQLLER-FYDPMAGtvllDGQEakklnvqwlraqlGIVSqepilfDCSIAKniaygdnsr 1136
Cdd:pfam09818 77 IPKGITL-IVGGGFHGKSTLLEALERgVYNHIPG----DGRE-------------FVVT------DPDAVK--------- 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1137 VVSQDEivRAAKEANIHPFIETLPQkyetrvGDKGTQL-----SGGQKQRIAIARALIRQPRVLLLDEATSA 1203
Cdd:pfam09818 124 IRAEDG--RSVHGVDISPFINNLPP------GKDTTDFstedaSGSTSQAANIMEALEAGASLLLIDEDTSA 187
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
751-922 |
1.31e-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: 45.60 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 751 NMFSLVFLGL-GVHSFFTFFlQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGT 829
Cdd:cd18605 42 NFFLTVYGFLaGLNSLFTLL-RAFLFAYGGLRAARRLHNKLLSSILFAKMSFFD--KTPVGRILNRFSSDVYTIDDSLPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 830 RL-ALIAQNTANLGTGIIISFIYGWqltlLLLSVVPFIAVAGIVEMKMLAGNakRDKKEMEAA--GKIAT---EAIENIR 903
Cdd:cd18605 119 ILnILLAQLFGLLGYLVVICYQLPW----LLLLLLPLAFIYYRIQRYYRATS--RELKRLNSVnlSPLYThfsETLKGLV 192
|
170
....*....|....*....
gi 6981354 904 TVVSLTQERKFESMYVEKL 922
Cdd:cd18605 193 TIRAFRKQERFLKEYLEKL 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
529-586 |
1.37e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 529 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAreGRTTIVIAH 586
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSH 399
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1173-1242 |
1.63e-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: 1.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1173 QLSGGQKQRIAIARALI---RQPRVL-LLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1242
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1174-1245 |
1.67e-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: 43.71 E-value: 1.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981354 1174 LSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVID 1245
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
529-600 |
1.77e-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: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 529 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTEseaEVQAALDKARE----GRTTIVIAHRLSTVRNADVIAGF 600
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR---DGQALAEAILEhlvkGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1068-1241 |
1.81e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1068 GSSGCGKSTVVQLLERFYDPMAGTVL---LDGQEAKKLNVQWLRAQLGIVSqepilfDCSIAKNIAYGdnSRVVSQDEIV 1144
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYyknCNINNIAKPYCTYIGHNLGLKL------EMTVFENLKFW--SEIYNSAETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1145 RAAkeanIHPFietlpqKYETRVGDKGTQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD-KAREGR 1223
Cdd:PRK13541 105 YAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGG 174
|
170
....*....|....*...
gi 6981354 1224 TCIVIAHRLSTIQNADLI 1241
Cdd:PRK13541 175 IVLLSSHLESSIKSAQIL 192
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
770-973 |
1.81e-04 |
|
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: 44.89 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 770 LQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQG-ATGTRLALIAqNTANLGTGIIIS 848
Cdd:cd18782 61 LRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPVGELSTRIS-ELDTIRGfLTGTALTTLL-DVLFSVIYIAVL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 849 FIYGWQLTLLLLSVVPFIAVAGIVEMKMLagnAKRDKKEMEAAGKIAT---EAIENIRTVVSLTQERKFESMYvEKLHGP 925
Cdd:cd18782 137 FSYSPLLTLVVLATVPLQLLLTFLFGPIL---RRQIRRRAEASAKTQSylvESLTGIQTVKAQNAELKARWRW-QNRYAR 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981354 926 YRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHMRFKDVI 973
Cdd:cd18782 213 SLGEGFKLTVLGTTSGsLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLI 261
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
524-607 |
2.09e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 524 GDRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIV----------IAHRLSTVR 592
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLttqymeeaeqLAHELTVID 218
|
90
....*....|....*
gi 6981354 593 NADVIAgfeDGVIVE 607
Cdd:NF000106 219 RGRVIA---DGKVDE 230
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
402-617 |
2.27e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 402 SRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTV---------QLLQRLYDPT----EGTI----------------SI 452
Cdd:PRK00635 604 SKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLIndtlvpaveEFIEQGFCSNlsiqWGAIsrlvhitrdlpgrsqrSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 453 DGQDIRNFN---------VRCLR------EF-----IGVVSQEPVLFSTTIAEN--------------------IRYGRG 492
Cdd:PRK00635 684 PLTYIKAFDdlrelfaeqPRSKRlgltksHFsfntpLGACAECQGLGSITTTDNrtsipcpsclgkrflpqvleVRYKGK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 493 NVTmdeikkAVKEANAYD---FIMKLP---QKFDTL---------VGDRGAQLSGGQKQRIAIARAL---VRNPKILLLD 554
Cdd:PRK00635 764 NIA------DILEMTAYEaekFFLDEPsihEKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLD 837
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 555 EATSALDTES-EAEVQAALDKAREGRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQGSHSELIKK 617
Cdd:PRK00635 838 EPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVlelgpeGGNLGGYLLASCSPEELIHL 907
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
124-342 |
2.37e-04 |
|
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: 44.78 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 124 VLLAAYIQVSFWtlaagrqiRKIRQKFFHAILRQEMGWFDIKGTTELNTRLTDDISKISE----GIGDkvgmFFQAIATF 199
Cdd:cd18540 63 IRLAGKIEMGVS--------YDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEiiswGLVD----LVWGITYM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 200 FAGFIVGFIRGWKLTLVIMAITAILGLsTAVW----------------AKILSTFSdkelaayakagavaeEALGAIRTV 263
Cdd:cd18540 131 IGILIVMLILNWKLALIVLAVVPVLAV-VSIYfqkkilkayrkvrkinSRITGAFN---------------EGITGAKTT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 264 IAFGGQNKELERYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGAF 342
Cdd:cd18540 195 KTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIG-TLVAFISYATQFF 272
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
401-584 |
3.60e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.78 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 401 PSRANIKILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLLQRLYDP-TEGTISIDGQDIRNFNVRCL-----------RE 467
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 468 FIGVVSQEPVLFSTTIAENIRYGRGNVtMDEIKKaVKEANAY--DFIMKLPQKFDTLVgdrgaQLSGGQKQRIAIARALV 545
Cdd:NF040905 348 GYGLNLIDDIKRNITLANLGKVSRRGV-IDENEE-IKVAEEYrkKMNIKTPSVFQKVG-----NLSGGNQQKVVLSKWLF 420
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6981354 546 RNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVI 584
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVI 460
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1173-1263 |
3.89e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1173 QLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKvvQ-----EALDKAREGRTCIViahrlST--IQNA---DLIV 1242
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLV-----ATayMEEAerfDWLV 208
|
90 100
....*....|....*....|.
gi 6981354 1243 VIDNGKVKEHGTHQQLLAQKG 1263
Cdd:NF033858 209 AMDAGRVLATGTPAELLARTG 229
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
114-280 |
4.48e-04 |
|
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: 43.61 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 114 AYY---YSGLGGGVLLAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEMGWFDikgTT---ELNTRLTDDISKISEGIGD 187
Cdd:cd18604 43 LYYlgiYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLD---TTpvgRILNRFSKDIETIDSELAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 188 KVGMFFQAIATFFAGFIVGFIRGWkLTLVIMAITAILGLSTAVW--------------AK--ILSTFSdkelaayakaga 251
Cdd:cd18604 120 SLSSLLESTLSLLVILIAIVVVSP-AFLLPAVVLAALYVYIGRLylrasrelkrlesvARspILSHFG------------ 186
|
170 180
....*....|....*....|....*....
gi 6981354 252 vaeEALGAIRTVIAFGGQnkelERYQKHL 280
Cdd:cd18604 187 ---ETLAGLVTIRAFGAE----ERFIEEM 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
412-620 |
4.61e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.27 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 412 LNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPTEGTISIDGQDIRNFNVR-CLREfiGVV-----SQEPVLF------ 479
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLAR--GLVylpedRQSSGLYldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 480 ----STTIAEN---IRYGRGNVTMDEIKKAvkeanaydfimkLPQKFDTLvgDRGAQ-LSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK15439 360 wnvcALTHNRRgfwIKPARENAVLERYRRA------------LNIKFNHA--EQAARtLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981354 552 LLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLstvrnaDVIAGFEDGVIV-EQGSHSELIKKEGI 620
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIyQLIRSIAAQNVAVLFISSDL------EEIEQMADRVLVmHQGEISGALTGAAI 490
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
195-336 |
7.10e-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: 43.22 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 195 AIATFfagfIVGFIRGWKLTLVIMAITAILGLSTAVWAKILSTFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 274
Cdd:cd18567 129 AILTL----VMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREA 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 275 RYQKHLENAKKIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFS 336
Cdd:cd18567 205 RWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVG-MLFAFLA 265
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
529-615 |
7.14e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 529 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVI 605
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 6981354 606 VEQGSHSELI 615
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1172-1245 |
1.03e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 1.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981354 1172 TQLSGGQKQRIAIARALIR--QPRVL-LLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIvvID 1245
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWI--ID 900
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
501-597 |
1.21e-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: 41.82 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 501 KAVKEANAYDFIMKLPQ-KFDTLVGDRGAQLSGGQKQ------RIAIARALVRNPKILLLDEATSALDTESEAEVQAALD 573
Cdd:cd03240 86 TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEII 165
|
90 100
....*....|....*....|....*..
gi 6981354 574 KAREG---RTTIVIAHRLSTVRNADVI 597
Cdd:cd03240 166 EERKSqknFQLIVITHDEELVDAADHI 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1161-1217 |
1.51e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1161 QKyetRVGdkgtQLSGGQKQRIAIARALIRQPRVLLLDEATSALDTESEKVVQEALD 1217
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 ... |
845-967 |
1.53e-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: 42.16 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 845 IIISFIYGWQLTLLLLSVVP-FIAVAGIVEMKMLAGNAKRDKKEMEAAGKIaTEAIENIRTVVSLTQERKFESmYVEKLH 923
Cdd:cd18568 133 LGLMFYYNLQLTLIVLAFIPlYVLLTLLSSPKLKRNSREIFQANAEQQSFL-VEALTGIATIKALAAERPIRW-RWENKF 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6981354 924 GPYRNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18568 211 AKALNTRFRGQKLSIVLQlISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
754-967 |
2.44e-03 |
|
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: 41.29 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 754 SLVFLGLGVHSFFTFFLQGFTFGKAGEILTTRLRSMAFKAMLRQDMSWFddHKNSTGALSTRL-ATDAAQ---VQGATGT 829
Cdd:cd18567 45 AIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYF--EKRHLGDIVSRFgSLDEIQqtlTTGFVEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 830 RL-ALIAqntanLGTGIIIsFIYGWQLTLLllsVVPFIAVAGIVEMKMLAGNAKRDKKEMEAAGKIATEAIENIRTVVSL 908
Cdd:cd18567 123 LLdGLMA-----ILTLVMM-FLYSPKLALI---VLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 909 -------TQERKFESMYVEKLhgpyrNSVRKAHIYGITFS-ISQAFMYFSYAGCFRFGSYLIVNGHM 967
Cdd:cd18567 194 klfgreaEREARWLNLLVDAI-----NADIRLQRLQILFSaANGLLFGLENILVIYLGALLVLDGEF 255
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1167-1253 |
4.10e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1167 VGDKGTQLSGGQKQRIAIARALI---RQPRVLLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1242
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
90
....*....|.
gi 6981354 1243 VIDNGKVKEHG 1253
Cdd:PRK00635 1773 EMGPGSGKTGG 1783
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1043-1228 |
4.24e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1043 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-MAGTVLLDGQEAKKLNVQWL-----------RA 1109
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 1110 QLGIVSQEPILFDCSIA--KNIAygdNSRVVSQDEIVRAAKEanihpFIETLPQKYETrVGDKGTQLSGGQKQRIAIARA 1187
Cdd:NF040905 348 GYGLNLIDDIKRNITLAnlGKVS---RRGVIDENEEIKVAEE-----YRKKMNIKTPS-VFQKVGNLSGGNQQKVVLSKW 418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6981354 1188 LIRQPRVLLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1228
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1051-1081 |
4.25e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 4.25e-03
10 20 30
....*....|....*....|....*....|..
gi 6981354 1051 LQGLSLEVKKGQTLALVGSSGCGKSTVV-QLL 1081
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
508-621 |
4.83e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 508 AYDF---IMKLPQKFDTLV---------GDRGAQLSGGQKQRIAIARALVRNP--KIL-LLDEATSALDTESEA---EV- 568
Cdd:PRK00349 797 ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRkllEVl 876
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981354 569 QAALDKareGRTTIVIAHRLSTVRNADVIA--GFEDGV----IVEQGSHSELIKKEGIY 621
Cdd:PRK00349 877 HRLVDK---GNTVVVIEHNLDVIKTADWIIdlGPEGGDgggeIVATGTPEEVAKVEASY 932
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1172-1242 |
8.40e-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: 8.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981354 1172 TQLSGGQKQRIAIarALI-----RQPRVL-LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIV 1242
Cdd:pfam02463 1076 DLLSGGEKTLVAL--ALIfaiqkYKPAPFyLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1174-1242 |
8.84e-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: 8.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981354 1174 LSGGQKQRIAIARALIRQPRVLL--LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1242
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
398-564 |
8.98e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.60 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 398 FSYPSRANIKILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPT---EGTISIDGQDIRNFNVRCLREFIgvvSQ 474
Cdd:PLN03140 170 INLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSAYI---SQ 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981354 475 EPV-LFSTTIAENIRY-------GRGNVTMDEIKKAVKEANAY-----DFIMK---------------------LPQKFD 520
Cdd:PLN03140 247 NDVhVGVMTVKETLDFsarcqgvGTRYDLLSELARREKDAGIFpeaevDLFMKatamegvksslitdytlkilgLDICKD 326
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6981354 521 TLVGD---RGaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:PLN03140 327 TIVGDemiRG--ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSST 371
|
|
| |
