|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-1464 |
0e+00 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 2902.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1 MKKDQRQSIDNNSGGSNLSIKDEVEKELNKKGTFELYKKIKTQRIPFFLPFKCLPPSHKKLLGVSFVCATISGGSLPFFV 80
Cdd:PTZ00265 1 MKKDQRQKKDNNSGGGNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 81 SVFGVIMKNMNLGENVDDIIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNNPGSKLTSDL 160
Cdd:PTZ00265 81 SVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 161 DFYLEQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYICGVICNKKAKINKKTSLLYNNNTMSIIE 240
Cdd:PTZ00265 161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 241 EALVGIRTVVSYCGEHTILKKFNLSEKLYSKYMLKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNAQSNNDFH 320
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 321 GGSVISILLGVLISMFMLTIVLPNITEYMKSLEATNSLYEIINRKPLVENNNDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
Cdd:PTZ00265 321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
Cdd:PTZ00265 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 481 KYSLYSLKDLEYLSDQLNEDGSASQDGLDKRNSCRAKCAGDLNDMMKTTDSDGLIHARKNYNIIDDSEVVNVSKKVLIHD 560
Cdd:PTZ00265 481 KYSLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLIHD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PTZ00265 561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 641 STIRYANTIFVLSNREKGNRSTVDVDiiGEDPTKDNKENKQKNGKKG----DTNKNEKMSNAGSYIIEQGTHDALMKNKN 716
Cdd:PTZ00265 641 STIRYANTIFVLSNRERGSTVDVDII--GEDPTKDNKENNNKNNKDDnnnnNNNNNNKINNAGSYIIEQGTHDALMKNKN 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 717 GIYYTMINNQKVSSKTSNNNDNDKDSDMKSSVYKDSERGYDPDEMNGNTKNGNESASDKKSNKMSDENASSKNAGGKLSF 796
Cdd:PTZ00265 719 GIYYTMINNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENASENNAGGKLPF 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 797 LRNLFKRKPKAPNNLRMVYREIFSYKKDVVIIALSIIVAGGLYPMFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIA 876
Cdd:PTZ00265 799 LRNLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIA 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 877 MFISETLKNYYNNVIGEKVEKTMKHRLFENILYQEISFFDQDCHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIV 956
Cdd:PTZ00265 879 MFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLV 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 957 SMIMSFYFCPIVAAVLTGTYFIFMRVFAIRARLSANKDVEKKGINQPGTVFLYNNDDEIFKDPSFLIQEAFYNMNTVIIY 1036
Cdd:PTZ00265 959 SMVMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIQEAFYNMNTVIIY 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1037 GLEDYFCKLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTIEVDDFMKSLFTFLFTGSYAGK 1116
Cdd:PTZ00265 1039 GLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGK 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1117 LMSLKGDSENAKLSFEKYYPLIMRKSNIDVRDNGGIRIKNTNDIDGKIEIMDVNFTYMSRPNVPIYKDLTFSCDSKKTTA 1196
Cdd:PTZ00265 1119 LMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTA 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1197 IVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTDDVNNEKKEQGDEEQNVGMKNVNEFSLTKEGSHGDNSAVFKNSGK 1276
Cdd:PTZ00265 1199 IVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVFKNSGK 1278
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1277 ILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKS 1356
Cdd:PTZ00265 1279 ILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKS 1358
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKRSDKIVVFNNPDRTG 1436
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTG 1438
|
1450 1460
....*....|....*....|....*...
gi 221056887 1437 SFVQAEGTHEELLSVQDGVYKKYVKLAK 1464
Cdd:PTZ00265 1439 SFVQAHGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
811-1462 |
4.68e-132 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 420.73 E-value: 4.68e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 811 LRMVYREIFSYKKDVVIIALSIIVAGGLYPMFALLYAKYVSTLFDFANLEAnSNKYSLYILVIAIAMFISETLKNYYNNV 890
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA-LLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 891 IGEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCP---I 967
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWrlaL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 968 VAAVLTGTYFIFMRVFAIRARLSANKDVEKKG-INQpgtvflynnddeifkdpsfLIQEAFYNMNTVIIYGLEDY----F 1042
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAeLNG-------------------RLQESLSGIRVVKAFGREERelerF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1043 CKLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFInsfaYWFGSFLIRRGTIEVDDFMksLFTFLFTGSYA--GKLMSL 1120
Cdd:COG1132 227 REANEELRRANLRAARLSALFFPLMELLGNLGLALV----LLVGGLLVLSGSLTVGDLV--AFILYLLRLFGplRQLANV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1121 KGDSENAKLSFEKYYPLIMRKSNIDVRDNGgiriKNTNDIDGKIEIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGE 1200
Cdd:COG1132 301 LNQLQRALASAERIFELLDEPPEIPDPPGA----VPLPPVRGEIEFENVSFSY--PGDRPVLKDISLTIPPGETVALVGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1201 TGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegshgdnsavfkNSGKILLD 1280
Cdd:COG1132 375 SGSGKSTLVNLLLRFYDP------------------------------------------------------TSGRILID 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1281 GVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGG 1360
Cdd:COG1132 401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGG 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1361 QKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADRTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQ 1440
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRNADRILVLDD----GR-IV 553
|
650 660
....*....|....*....|..
gi 221056887 1441 AEGTHEELLSvQDGVYKKYVKL 1462
Cdd:COG1132 554 EQGTHEELLA-RGGLYARLYRL 574
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
58-726 |
1.55e-127 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 408.40 E-value: 1.55e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 58 HKKLLGVSFVCATISGGSLPFFVSVFGVIMKNMNLGENVDDIIFS---LVLIGIFQFVMSFISSFCMDIVTTKILKTLKV 134
Cdd:COG1132 19 YRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLlllLLGLALLRALLSYLQRYLLARLAQRVVADLRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 135 EFLKSVFYQDGQFHDNNP-G---SKLTSDLDfyleQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLI 210
Cdd:COG1132 99 DLFEHLLRLPLSFFDRRRtGdllSRLTNDVD----AVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 211 YICGVICNKKAKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEHTILKKFN-LSEKLYSKYMlKANFMESLHIGMING 289
Cdd:COG1132 175 LLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFReANEELRRANL-RAARLSALFFPLMEL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 290 FILASYAFGFWYGTRIIISDlsnaqsnndfhggsviSILLGVLISMFMLTIVLPN--------ITEYMKSLEATNSLYEI 361
Cdd:COG1132 254 LGNLGLALVLLVGGLLVLSG----------------SLTVGDLVAFILYLLRLFGplrqlanvLNQLQRALASAERIFEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 362 INRKPLVENNNDGKKLKDIK-KIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG 440
Cdd:COG1132 318 LDEPPEIPDPPGAVPLPPVRgEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 441 DIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdleylsdqlnedgsasqdgldkrnscrakcaG 520
Cdd:COG1132 396 RILIDG-VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRY-------------------------------------G 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 521 DLNdmmkttdsdgliharknyniIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKI 600
Cdd:COG1132 438 RPD--------------------ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPI 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 601 LILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrekgnrstvdvdiigedptkdnkenk 680
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTIRNADRILVL---------------------------- 547
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 221056887 681 qKNGKkgdtnknekmsnagsyIIEQGTHDALMKnKNGIYYTMINNQ 726
Cdd:COG1132 548 -DDGR----------------IVEQGTHEELLA-RGGLYARLYRLQ 575
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1164-1463 |
1.66e-112 |
|
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: 354.15 E-value: 1.66e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATR 1323
Cdd:cd03249 56 -----------------------------TSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:cd03249 107 EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA- 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1404 dKADRTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAEGTHEELLSvQDGVYKKYVKLA 1463
Cdd:cd03249 186 -MKGRTTIVIAHRLSTIRNADLIAVLQN-----GQVVEQGTHDELMA-QKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
383-726 |
2.90e-109 |
|
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: 345.29 E-value: 2.90e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKI 462
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG-VDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNSIKNNIKYSLYSlkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyn 542
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPD-------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03249 104 -ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 623 NNLKgnENRITIIIAHRLSTIRYANTIFVLSNrekgnrstvdvdiigedptkdnkenkqkngkkgdtnknekmsnagSYI 702
Cdd:cd03249 183 DRAM--KGRTTIVIAHRLSTIRNADLIAVLQN---------------------------------------------GQV 215
|
330 340
....*....|....*....|....
gi 221056887 703 IEQGTHDALMKNKnGIYYTMINNQ 726
Cdd:cd03249 216 VEQGTHDELMAQK-GVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
801-1461 |
1.70e-104 |
|
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: 349.52 E-value: 1.70e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 801 FKRKPKAPNNLRMVYREIFSYKKDVVIIALSIIVAGglypMFALLYAKYVSTLFDFAnlEANSNKYSLYILVIAIAM--- 877
Cdd:COG2274 134 FDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLIN----LLALATPLFTQVVIDRV--LPNQDLSTLWVLAIGLLLall 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 878 --FISETLKNYYNNVIGEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHInRDVH----LLKTGLVNNIVIFThFI 951
Cdd:COG2274 208 feGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES--RSVGDLASRF-RDVEsireFLTGSLLTALLDLL-FV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 952 VLFIVsmIMSFY-----FCPIVAAVLtgtYFIFMRVFAIRARLSANKDVEKKGINQpgtvflynnddeifkdpSFLIqEA 1026
Cdd:COG2274 284 LIFLI--VLFFYspplaLVVLLLIPL---YVLLGLLFQPRLRRLSREESEASAKRQ-----------------SLLV-ET 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1027 FYNMNTVIIYGLEDYFCKLIEKAI-DYSNKGQKRKTLVNSMLWgFSQSAQLFINSFAYWFGSFLIRRGTIEVDDFMK-SL 1104
Cdd:COG2274 341 LRGIETIKALGAESRFRRRWENLLaKYLNARFKLRRLSNLLST-LSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAfNI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1105 FTFLFTGSyAGKLMSLKGDSENAKLSFEKYYPLImrksNIDVRDNGGIRIKNTNDIDGKIEIMDVNFTYmSRPNVPIYKD 1184
Cdd:COG2274 420 LSGRFLAP-VAQLIGLLQRFQDAKIALERLDDIL----DLPPEREEGRSKLSLPRLKGDIELENVSFRY-PGDSPPVLDN 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1185 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegsh 1264
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP---------------------------------------------- 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1265 gdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPN 1344
Cdd:COG2274 528 --------TSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPM 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1345 KYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADRTIITIAHRIASIKRSD 1424
Cdd:COG2274 600 GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLAD 677
|
650 660 670
....*....|....*....|....*....|....*..
gi 221056887 1425 KIVVFNNpdrtGSFVQaEGTHEELLSvQDGVYKKYVK 1461
Cdd:COG2274 678 RIIVLDK----GRIVE-DGTHEELLA-RKGLYAELVQ 708
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
58-726 |
3.89e-95 |
|
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: 323.32 E-value: 3.89e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 58 HKKLLGVSFVCATISGG---SLPFFVSVFgvimknmnlgenVDDIIFS------------LVLIGIFQFVMSFISSFCMD 122
Cdd:COG2274 154 YRRLLLQVLLASLLINLlalATPLFTQVV------------IDRVLPNqdlstlwvlaigLLLALLFEGLLRLLRSYLLL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 123 IVTTKILKTLKVEFLKSVFYQDGQFHDNNPGSKLTSDLdFYLEQVNAGIGTKFLTIFTyTSAFLGLYFWSLFK-NARLTL 201
Cdd:COG2274 222 RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALL-DLLFVLIFLIVLFFySPPLAL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 202 CVTCVFPLIYICGVICNKK-AKINKKTSLLYNNNTmSIIEEALVGIRTVVSYCGEHTILKKFnlsEKLYSKYmLKANFmE 280
Cdd:COG2274 300 VVLLLIPLYVLLGLLFQPRlRRLSREESEASAKRQ-SLLVETLRGIETIKALGAESRFRRRW---ENLLAKY-LNARF-K 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 281 SLHIGMINGFI-----LASYAFGFWYGTRIIIsdlsnaqsNNDFHGGSVI--SILLGVLISMFMLTIVLpnITEYMKSLE 353
Cdd:COG2274 374 LRRLSNLLSTLsgllqQLATVALLWLGAYLVI--------DGQLTLGQLIafNILSGRFLAPVAQLIGL--LQRFQDAKI 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 354 ATNSLYEIINRKPLVENNNDGKKLKDIK-KIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIE 432
Cdd:COG2274 444 ALERLDDILDLPPEREEGRSKLSLPRLKgDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 433 RLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleylsdqlnedgsasqdgldkrn 512
Cdd:COG2274 523 GLYEPTSGRILIDG-IDLRQIDPASLRRQIGVVLQDVFLFSGTIRENI-------------------------------- 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 513 scrakCAGDLNdmmkttdsdgliharknyniIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIAR 592
Cdd:COG2274 570 -----TLGDPD--------------------ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIAR 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 593 AIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGneNRITIIIAHRLSTIRYANTIFVLsnrekgnrstvdvdiigedp 672
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVL-------------------- 682
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 221056887 673 tkdnkenkqKNGKkgdtnknekmsnagsyIIEQGTHDALMKnKNGIYYTMINNQ 726
Cdd:COG2274 683 ---------DKGR----------------IVEDGTHEELLA-RKGLYAELVQQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1164-1459 |
9.89e-82 |
|
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: 268.33 E-value: 9.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATR 1323
Cdd:cd03251 55 -----------------------------DSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYGRPGATR 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdik 1403
Cdd:cd03251 106 EEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAAL---- 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 1404 DK--ADRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEELLSvQDGVYKKY 1459
Cdd:cd03251 182 ERlmKNRTTFVIAHRLSTIENADRIVVLED----GKIVE-RGTHEELLA-QGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
57-725 |
1.87e-78 |
|
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: 271.20 E-value: 1.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 57 SHKKLLGVSFVCATISGGSLPFFVSVFGVIMKNMNLGENVDDIIF-SLVLIGIF--QFVMSFISSFCMDIVTTKILKTLK 133
Cdd:TIGR02203 11 PYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWvPLVVIGLAvlRGICSFVSTYLLSWVSNKVVRDIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 134 VEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYIC 213
Cdd:TIGR02203 91 VRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSIL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 214 GVICNKKAK-INKKTSLLyNNNTMSIIEEALVGIRTVVSYCGEHTILKKFNLSEKLYSKYMLKANFMESLHIGMINgfIL 292
Cdd:TIGR02203 171 MRRVSKRLRrISKEIQNS-MGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQ--LI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 293 ASYAFGFwygtrIIISDLSNAQSNNDFHGGsvisiLLGVLISMFMLTIVLPNITE----YMKSLEATNSLYEIINRKPLV 368
Cdd:TIGR02203 248 ASLALAV-----VLFIALFQAQAGSLTAGD-----FTAFITAMIALIRPLKSLTNvnapMQRGLAAAESLFTLLDSPPEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 369 EnnnDGKKLKD--IKKIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInD 446
Cdd:TIGR02203 318 D---TGTRAIEraRGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL-D 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 447 SHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdleylsdqlnedgsasqdgldkrnscrakcaGDLNDmm 526
Cdd:TIGR02203 393 GHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAY-------------------------------------GRTEQ-- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 527 kttdsdgliharknyniIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEA 606
Cdd:TIGR02203 434 -----------------ADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 607 TSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrekgnrstvdvdiigedptkdnkenkqKNGKk 686
Cdd:TIGR02203 497 TSALDNESERLVQAALERLM--QGRTTLVIAHRLSTIEKADRIVVM-----------------------------DDGR- 544
|
650 660 670
....*....|....*....|....*....|....*....
gi 221056887 687 gdtnknekmsnagsyIIEQGTHDALMkNKNGiYYTMINN 725
Cdd:TIGR02203 545 ---------------IVERGTHNELL-ARNG-LYAQLHN 566
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1164-1458 |
8.96e-78 |
|
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: 256.77 E-value: 8.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDV------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATR 1323
Cdd:cd03253 54 -----------------------------SSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRPDATD 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:cd03253 105 EEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV- 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1404 dKADRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEELLSvQDGVYKK 1458
Cdd:cd03253 184 -SKGRTTIVIAHRLSTIVNADKIIVLKD----GRIVE-RGTHEELLA-KGGLYAE 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1162-1449 |
8.06e-77 |
|
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: 254.07 E-value: 8.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1162 GKIEIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekkeq 1241
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1242 gdeeqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDA 1321
Cdd:cd03254 55 ------------------------------PQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNA 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1322 TREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:cd03254 105 TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 221056887 1402 IKDkaDRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEELL 1449
Cdd:cd03254 185 LMK--GRTSIIIAHRLSTIKNADKILVLDD----GKIIE-EGTHDELL 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
893-1460 |
4.77e-76 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 268.13 E-value: 4.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 893 EKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCP---IVA 969
Cdd:TIGR00958 230 ARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrltMVT 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 970 AVLTGTYFIFMRVFAIRARLSANKDVEkkGINQPGTVflynnddeifkdpsflIQEAFYNMNTVIIYGLEDYFCKLIEKA 1049
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQE--AVAKANQV----------------AEEALSGMRTVRSFAAEEGEASRFKEA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1050 IDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTIEVDDfmksLFTFLF----TGSYAGKLMSLKGDSE 1125
Cdd:TIGR00958 370 LEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGN----LVSFLLyqeqLGEAVRVLSYVYSGMM 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1126 NAKLSFEKYYPLIMRKSNIDvrDNGGIRIKNTNdidGKIEIMDVNFTYMSRPNVPIYKDLTFSCDSKKTTAIVGETGSGK 1205
Cdd:TIGR00958 446 QAVGASEKVFEYLDRKPNIP--LTGTLAPLNLE---GLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGK 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1206 STVMSLLMRFYDlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDIC 1285
Cdd:TIGR00958 521 STVAALLQNLYQ------------------------------------------------------PTGGQVLLDGVPLV 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1286 DYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRV 1365
Cdd:TIGR00958 547 QYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1366 AIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKADRTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaEGTH 1445
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVL----KKGSVVE-MGTH 697
|
570
....*....|....*
gi 221056887 1446 EELLSvQDGVYKKYV 1460
Cdd:TIGR00958 698 KQLME-DQGCYKHLV 711
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
59-652 |
2.12e-75 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 266.20 E-value: 2.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 59 KKLLGVSFV---CATISGGSLPFFVsvfgvimknmnlGENVDDI------------IFSLVLIGIFQFVMSFISSFCMDI 123
Cdd:TIGR00958 160 WPWLISAFVfltLSSLGEMFIPFYT------------GRVIDTLggdkgppalasaIFFMCLLSIASSVSAGLRGGSFNY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 124 VTTKILKTLKVEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQV--NAGIGTKFLTIFtytsafLGLYFWSLFKNA 197
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTgeltSRLSSDTQTMSRSLslNVNVLLRNLVML------LGLLGFMLWLSP 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 198 RLTLcVTCVF-PLIYICGVICNKK-AKINKKT--SLLYNNNtmsIIEEALVGIRTVVSYCGEHTILKKFN--LSEKL--- 268
Cdd:TIGR00958 302 RLTM-VTLINlPLVFLAEKVFGKRyQLLSEELqeAVAKANQ---VAEEALSGMRTVRSFAAEEGEASRFKeaLEETLqln 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 269 ------YSKYMLKanfMESLHIGMINGfILasyafgfWYGTRIIISdlsnaqsnNDFHGGSVISILL---------GVLI 333
Cdd:TIGR00958 378 krkalaYAGYLWT---TSVLGMLIQVL-VL-------YYGGQLVLT--------GKVSSGNLVSFLLyqeqlgeavRVLS 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 334 SMFmltivlpniTEYMKSLEATNSLYEIINRKPLVENNNDGKKLKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKT 413
Cdd:TIGR00958 439 YVY---------SGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEV 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 414 YAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdleyl 493
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAY----------- 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 494 sdqlnedgsasqdGLDKRnscrakcagdlndmmkttdsdgliharknyniiDDSEVVNVSKKVLIHDFVSALPDKYETLV 573
Cdd:TIGR00958 578 -------------GLTDT---------------------------------PDEEIMAAAKAANAHDFIMEFPNGYDTEV 611
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQktinNLKGNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVL 686
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1161-1456 |
2.76e-75 |
|
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: 262.83 E-value: 2.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1161 DGKIEIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekke 1240
Cdd:COG5265 355 GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV---------------------- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1241 qgdeeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKED 1320
Cdd:COG5265 411 --------------------------------TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1321 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:COG5265 459 ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1401 DIkdKADRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEELLSvQDGVY 1456
Cdd:COG5265 539 EV--ARGRTTLVIAHRLSTIVDADEILVLEA----GRIVE-RGTHAELLA-QGGLY 586
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
383-722 |
2.83e-75 |
|
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: 249.84 E-value: 2.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
Cdd:cd03251 1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-DGHDVRDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNSIKNNIKYSlyslkdleylsdqlnedgsasqdgldKRNSCRAkcagdlndmmkttdsdgliharknyn 542
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYG--------------------------RPGATRE-------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iiddsEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03251 107 -----EVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAAL 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 623 NNLKgnENRITIIIAHRLSTIRYANTIFVLsnrEKGNrstvdvdiigedptkdnkenkqkngkkgdtnknekmsnagsyI 702
Cdd:cd03251 182 ERLM--KNRTTFVIAHRLSTIENADRIVVL---EDGK------------------------------------------I 214
|
330 340
....*....|....*....|
gi 221056887 703 IEQGTHDALMKnKNGIYYTM 722
Cdd:cd03251 215 VERGTHEELLA-QGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
383-726 |
1.44e-73 |
|
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: 244.83 E-value: 1.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
Cdd:cd03253 1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI-DGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNSIKNNIKYslyslkdleylsdqlnedgsasqdgldkrnscrakcaGDLNdmmkttdsdgliharknyn 542
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRY-------------------------------------GRPD------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03253 102 -ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAAL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 623 NNLKgnENRITIIIAHRLSTIRYANTIFVLsnrekgnrstvdvdiigedptkdnkenkqKNGKkgdtnknekmsnagsyI 702
Cdd:cd03253 181 RDVS--KGRTTIVIAHRLSTIVNADKIIVL-----------------------------KDGR----------------I 213
|
330 340
....*....|....*....|....
gi 221056887 703 IEQGTHDALMkNKNGIYYTMINNQ 726
Cdd:cd03253 214 VERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
331-726 |
2.77e-73 |
|
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: 257.06 E-value: 2.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 331 VLISMFMLTIVLP-NI--TEY--MK-SLEATNSLYEIINRKPLVENNNDGKKLK-DIKKIQFKNVRFHYDTRKdvEIYKD 403
Cdd:COG5265 299 VLVNAYLIQLYIPlNFlgFVYreIRqALADMERMFDLLDQPPEVADAPDAPPLVvGGGEVRFENVSFGYDPER--PILKG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI-DGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 484 lyslkdleylsdqlNEDgsASQDgldkrnscrakcagdlndmmkttdsdgliharknyniiddsEVVNVSKKVLIHDFVS 563
Cdd:COG5265 456 --------------RPD--ASEE-----------------------------------------EVEAAARAAQIHDFIE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTI 643
Cdd:COG5265 479 SLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA--RGRTTLVIAHRLSTI 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 644 RYANTIFVLsnrEKGNrstvdvdiigedptkdnkenkqkngkkgdtnknekmsnagsyIIEQGTHDALMKnKNGIYYTMI 723
Cdd:COG5265 557 VDADEILVL---EAGR------------------------------------------IVERGTHAELLA-QGGLYAQMW 590
|
...
gi 221056887 724 NNQ 726
Cdd:COG5265 591 ARQ 593
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
382-660 |
1.10e-69 |
|
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: 233.66 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
Cdd:cd03254 2 EIEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI-DGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSNSIKNNIKYslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharkNY 541
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRL---------------------------------------------------------GR 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 NIIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03254 102 PNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEA 181
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 221056887 622 INNLkgNENRITIIIAHRLSTIRYANTIFVLSN---REKGNR 660
Cdd:cd03254 182 LEKL--MKGRTSIIIAHRLSTIKNADKILVLDDgkiIEEGTH 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1164-1450 |
2.45e-69 |
|
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: 244.28 E-value: 2.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNVPiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgd 1243
Cdd:COG4988 337 IELEDVSFSYPGGRPAL--DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP------------------------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATR 1323
Cdd:COG4988 390 -----------------------------YSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASD 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:COG4988 441 EELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL- 519
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 221056887 1404 dKADRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEELLS 1450
Cdd:COG4988 520 -AKGRTVILITHRLALLAQADRILVLDD----GRIVE-QGTHEELLA 560
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
818-1458 |
1.47e-66 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 236.84 E-value: 1.47e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 818 IFSYKKDVVI--IALsIIVAGGLYPMFALLyakyvSTLFD--FANleANSNKYSLYILVIAIAMF---ISETLKNYYNNV 890
Cdd:PRK11176 20 IAPFKAGLIVagVAL-ILNAASDTFMLSLL-----KPLLDdgFGK--ADRSVLKWMPLVVIGLMIlrgITSFISSYCISW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 891 IGEKVEKTMKHRLFENILYQEISFFDQDchAPGLLSSHINRD---VHLLKTGLVNNIV-----IFTHFIVLFIVSMIMS- 961
Cdd:PRK11176 92 VSGKVVMTMRRRLFGHMMGMPVSFFDKQ--STGTLLSRITYDseqVASSSSGALITVVregasIIGLFIMMFYYSWQLSl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 962 --FYFCPIVAavltgtyfifmrvFAIRArlsankdVEKKginqpgtvflynnddeiFKDPSFLIQEAFYNMNT------- 1032
Cdd:PRK11176 170 ilIVIAPIVS-------------IAIRV-------VSKR-----------------FRNISKNMQNTMGQVTTsaeqmlk 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1033 ----VIIYGLEdyfcKLIEKAIDY-SNK-GQKRKTLVNSMlwGFSQSAQLFINSFAYWFGSFLIrrgtiEVDDFMKSL-- 1104
Cdd:PRK11176 213 ghkeVLIFGGQ----EVETKRFDKvSNRmRQQGMKMVSAS--SISDPIIQLIASLALAFVLYAA-----SFPSVMDTLta 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1105 --FTFLFTGSYAgkLMS-LKGDSeNAKLSFEK--------YYPLIMRKSnidvRDNGGIRIKNTNdidGKIEIMDVNFTY 1173
Cdd:PRK11176 282 gtITVVFSSMIA--LMRpLKSLT-NVNAQFQRgmaacqtlFAILDLEQE----KDEGKRVIERAK---GDIEFRNVTFTY 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1174 MSRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgdeeqnvgmknv 1253
Cdd:PRK11176 352 PGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI----------------------------------- 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1254 nefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDA-TREDVKRACKF 1332
Cdd:PRK11176 396 -------------------DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARM 456
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1333 AAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDRTIIT 1412
Cdd:PRK11176 457 AYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLV 534
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 221056887 1413 IAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEELLSvQDGVYKK 1458
Cdd:PRK11176 535 IAHRLSTIEKADEILVVED----GEIVE-RGTHAELLA-QNGVYAQ 574
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
383-654 |
7.54e-66 |
|
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: 219.95 E-value: 7.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKI 462
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG-VDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNSIKNNIkyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyn 542
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI-------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iiddsevvnvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03228 97 -------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEAL 139
|
250 260 270
....*....|....*....|....*....|..
gi 221056887 623 NNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03228 140 RALA--KGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
349-654 |
2.58e-64 |
|
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: 229.64 E-value: 2.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 349 MKSLEATNSLYEIINR-KPLVENNNDGKKLKDIKKIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTI 427
Cdd:COG4988 302 ANGIAAAEKIFALLDApEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 428 LKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleylsdqlnedgsasqdg 507
Cdd:COG4988 380 LNLLLGFLPPYSGSILING-VDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL--------------------------- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 508 ldkrnscrakcagdlndMMKTTDsdgliharknyniIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQR 587
Cdd:COG4988 432 -----------------RLGRPD-------------ASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQR 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 588 ISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLALLAQADRILVLDD 546
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
99-659 |
1.68e-63 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 227.98 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 99 IIFSLVLIG--IFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFL 176
Cdd:PRK11176 65 KWMPLVVIGlmILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 177 TIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLI-YICGVICNKKAKINKKTsllynNNTM----SIIEEALVGIRTVVS 251
Cdd:PRK11176 145 TVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVsIAIRVVSKRFRNISKNM-----QNTMgqvtTSAEQMLKGHKEVLI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 252 YCGEHTILKKFN-LSEKL--YSKYMLKANFMESLHIGMINGFILAS--YAFGFwygtRIIISDLSnaqsnndfhGGSvIS 326
Cdd:PRK11176 220 FGGQEVETKRFDkVSNRMrqQGMKMVSASSISDPIIQLIASLALAFvlYAASF----PSVMDTLT---------AGT-IT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 327 IllgVLISMFMLTIVLPNIT----EYMKSLEATNSLYEIINRKPlvENNNDGKKLKDIK-KIQFKNVRFHYDTrKDVEIY 401
Cdd:PRK11176 286 V---VFSSMIALMRPLKSLTnvnaQFQRGMAACQTLFAILDLEQ--EKDEGKRVIERAKgDIEFRNVTFTYPG-KEVPAL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIK 481
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIA 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 482 YS---LYSLKDLEYlsdqlnedgsasqdgldkrnscRAKCAgdlndmmkttdsdgliHARknyniiddsevvnvskkvli 558
Cdd:PRK11176 439 YArteQYSREQIEE----------------------AARMA----------------YAM-------------------- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 559 hDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAH 638
Cdd:PRK11176 461 -DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAH 537
|
570 580
....*....|....*....|....
gi 221056887 639 RLSTIRYANTIFVLSN---REKGN 659
Cdd:PRK11176 538 RLSTIEKADEILVVEDgeiVERGT 561
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
812-1456 |
2.64e-63 |
|
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: 226.91 E-value: 2.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 812 RMVYREIFSYKKDVVIIALSIIVAGGLYPMFALLYAKYVSTLFDFANLEAnSNKYSLYILVIAIAMFISETLKNYYNNVI 891
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSV-LWWVPLVVIGLAVLRGICSFVSTYLLSWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 892 GEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTH----FIVLFIVSMIMSFYFCPI 967
Cdd:TIGR02203 82 SNKVVRDIRVRMFEKLLGLPVSFFDR--QPTGTLLSRITFDSEQVASAATDAFIVLVRetltVIGLFIVLLYYSWQLTLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 968 VAAVLTGTYFIfMRVFAIRARlSANKDVEKKgINQPGTVflynnddeifkdpsflIQEAFYNMNTVIIYGLEDYFCKLIE 1047
Cdd:TIGR02203 160 VVVMLPVLSIL-MRRVSKRLR-RISKEIQNS-MGQVTTV----------------AEETLQGYRVVKLFGGQAYETRRFD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1048 KAIDYSNKGQKRKTLVNSMLWGFSQ-------SAQLFInsfaywfGSFLIRRGTIEVDDFMKSLFTFLFTGSYAGKLMSL 1120
Cdd:TIGR02203 221 AVSNRNRRLAMKMTSAGSISSPITQliaslalAVVLFI-------ALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1121 KGDSENAKLSFEKYYPLImrkSNIDVRDNGGIRIKNtndIDGKIEIMDVNFTYMSRpNVPIYKDLTFSCDSKKTTAIVGE 1200
Cdd:TIGR02203 294 NAPMQRGLAAAESLFTLL---DSPPEKDTGTRAIER---ARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1201 TGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegshgdnsavfKNSGKILLD 1280
Cdd:TIGR02203 367 SGSGKSTLVNLIPRFYE------------------------------------------------------PDSGQILLD 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1281 GVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGK-EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSG 1359
Cdd:TIGR02203 393 GHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSG 472
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1360 GQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDRTIITIAHRIASIKRSDKIVVFNNpdrtGSFV 1439
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDD----GRIV 546
|
650
....*....|....*..
gi 221056887 1440 QAeGTHEELLSvQDGVY 1456
Cdd:TIGR02203 547 ER-GTHNELLA-RNGLY 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1164-1462 |
2.77e-61 |
|
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: 220.79 E-value: 2.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgd 1243
Cdd:COG4987 334 LELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP------------------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATR 1323
Cdd:COG4987 388 -----------------------------QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:COG4987 439 EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA- 517
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1404 dKADRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAeGTHEELLSvQDGVYKKYVKL 1462
Cdd:COG4987 518 -LAGRTVLLITHRLAGLERMDRILVLED----GRIVEQ-GTHEELLA-QNGRYRQLYQR 569
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
822-1144 |
6.08e-61 |
|
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: 211.93 E-value: 6.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 822 KKDVVIIALSII---VAGGLYPMFALLYAKYVSTLF--DFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVE 896
Cdd:cd18578 5 KPEWPLLLLGLIgaiIAGAVFPVFAILFSKLISVFSlpDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 897 KTMKHRLFENILYQEISFFDQDCHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCPIVAAVLTGTY 976
Cdd:cd18578 85 RRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 977 FIFMRVFAIRARLSANKDvekkginqpgtvflyNNDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCKLIEKAIDYSNKG 1056
Cdd:cd18578 165 PLLLLAGYLRMRLLSGFE---------------EKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1057 QKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTIEVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYP 1136
Cdd:cd18578 230 GLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFR 309
|
....*...
gi 221056887 1137 LIMRKSNI 1144
Cdd:cd18578 310 LLDRKPEI 317
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
147-719 |
6.30e-61 |
|
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: 219.96 E-value: 6.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 147 FHDNNPGSKLTSDLDFYLEQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYICGVICNKKAKINKK 226
Cdd:TIGR02204 108 FFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 227 TSLLYNNNTMSIIEEALVGIRTVVSYCGEHTILKKFNLS-EKLYsKYMLKANFMESLHIGMINGFILASYAFGFWYGTRI 305
Cdd:TIGR02204 188 ESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAvEKAY-EAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHD 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 306 IISDLSNAQSNNDFhggsvisILLGVLISMFMLTI--VlpnITEYMKSLEATNSLYEIINRKPLVENNNDGKKL--KDIK 381
Cdd:TIGR02204 267 VIAGKMSAGTLGQF-------VFYAVMVAGSIGTLseV---WGELQRAAGAAERLIELLQAEPDIKAPAHPKTLpvPLRG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
Cdd:TIGR02204 337 EIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILL-DGVDLRQLDPAELRAR 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSNSIKNNIKYSlyslkdleylsdqlNEDGSasqdgldkrnscrakcagdlndmmkttdsdgliharkny 541
Cdd:TIGR02204 416 MALVPQDPVLFAASVMENIRYG--------------RPDAT--------------------------------------- 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 niidDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:TIGR02204 443 ----DEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQA 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 622 INNLKgnENRITIIIAHRLSTIRYANTIFVLsnrEKGNrstvdvdiigedptkdnkenkqkngkkgdtnknekmsnagsy 701
Cdd:TIGR02204 519 LETLM--KGRTTLIIAHRLATVLKADRIVVM---DQGR------------------------------------------ 551
|
570
....*....|....*...
gi 221056887 702 IIEQGTHDALMKnKNGIY 719
Cdd:TIGR02204 552 IVAQGTHAELIA-KGGLY 568
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1164-1431 |
9.96e-61 |
|
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: 205.31 E-value: 9.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIkfgkedatr 1323
Cdd:cd03228 55 -----------------------------TSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI--------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 edvkrackfaaidefieslpnkydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:cd03228 97 ---------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALA 143
|
250 260
....*....|....*....|....*...
gi 221056887 1404 DkaDRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03228 144 K--GKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1159-1428 |
2.45e-60 |
|
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: 206.55 E-value: 2.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1159 DIDGKIEIMDVNFTYMSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtddvnnek 1238
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1239 keqgdeeqnvgmknvnefsltkegshgdnsavfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGK 1318
Cdd:cd03248 69 ------------------------------------GQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1319 EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:cd03248 113 QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQA 192
|
250 260 270
....*....|....*....|....*....|
gi 221056887 1399 IVDikDKADRTIITIAHRIASIKRSDKIVV 1428
Cdd:cd03248 193 LYD--WPERRTVLVIAHRLSTVERADQILV 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1145-1449 |
4.25e-59 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 214.82 E-value: 4.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1145 DVRDNGGIRikNTNDIDGKIEIMDVNFTY-MSRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhh 1223
Cdd:PRK13657 318 DVRDPPGAI--DLGRVKGAVEFDDVSFSYdNSRQGV---EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ---- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1224 ivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQEP 1303
Cdd:PRK13657 389 --------------------------------------------------SGRILIDGTDIRTVTRASLRRNIAVVFQDA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1304 ILFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEA 1383
Cdd:PRK13657 419 GLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1384 TSSLDSNSEKLIEKTIVDIKDkaDRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAeGTHEELL 1449
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDN----GRVVES-GSFDELV 557
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
62-358 |
2.61e-57 |
|
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: 200.78 E-value: 2.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 62 LGVSFVCATISGGSLPFFVSVFGVIMKNMN-----------LGENVDDIIFSLVLIGIFQFVMSFISSFCMDIVTTKILK 130
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgesspdeFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 131 TLKVEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLI 210
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 211 YICGVICNKKAKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEHTILKKFNLSEKLYSKYMLKANFMESLHIGMINGF 290
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 291 ILASYAFGFWYGTRIIISDLSNaqsnndfhGGSVISILLGVLISMFMLTIVLPNITEYMKSLEATNSL 358
Cdd:cd18577 241 IFAMYALAFWYGSRLVRDGEIS--------PGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
382-658 |
5.25e-57 |
|
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: 196.92 E-value: 5.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL-DGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSNSIKNNIKYSLyslkdleylsdqlnedGSASqdgldkrnscrakcagdlndmmkttdsdgliharkny 541
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGL----------------QSCS------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 niidDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03248 117 ----FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQA 192
|
250 260 270
....*....|....*....|....*....|....*..
gi 221056887 622 INNlkGNENRITIIIAHRLSTIRYANTIFVLsnrEKG 658
Cdd:cd03248 193 LYD--WPERRTVLVIAHRLSTVERADQILVL---DGG 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
383-726 |
8.98e-55 |
|
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: 191.16 E-value: 8.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYdtRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-DGHDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSNSIKNNIkyslyslkdleylsdqlnedgSASQDGLDKRnscrakcagdlndmmkttdsdgliharkny 541
Cdd:cd03252 78 VGVVLQENVLFNRSIRDNI---------------------ALADPGMSME------------------------------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 niiddsEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03252 107 ------RVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 622 INNLkgNENRITIIIAHRLSTIRYANTIFVLsnrEKGNrstvdvdiigedptkdnkenkqkngkkgdtnknekmsnagsy 701
Cdd:cd03252 181 MHDI--CAGRTVIIIAHRLSTVKNADRIIVM---EKGR------------------------------------------ 213
|
330 340
....*....|....*....|....*
gi 221056887 702 IIEQGTHDALMKnKNGIYYTMINNQ 726
Cdd:cd03252 214 IVEQGSHDELLA-ENGLYAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
358-659 |
6.20e-54 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 199.80 E-value: 6.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 358 LYEIINRKPLVENNNDGKKLKDIK-KIQFKNVRFHYD-TRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435
Cdd:PRK13657 309 FFEVEDAVPDVRDPPGAIDLGRVKgAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 436 DPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdleylsdqlNEDGSasqdgldkrnscr 515
Cdd:PRK13657 386 DPQSGRILI-DGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG--------------RPDAT------------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 516 akcagdlndmmkttdsdgliharknyniidDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAII 595
Cdd:PRK13657 438 ------------------------------DEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALL 487
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 596 RNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNR---EKGN 659
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRNADRILVFDNGrvvESGS 552
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1162-1431 |
1.09e-53 |
|
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: 187.32 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1162 GKIEIMDVNFTYmsRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekke 1240
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1241 qgdeeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIK-FGKe 1319
Cdd:cd03244 57 --------------------------------SSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLDpFGE- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 dATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTi 1399
Cdd:cd03244 104 -YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT- 181
|
250 260 270
....*....|....*....|....*....|...
gi 221056887 1400 vdIKDK-ADRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03244 182 --IREAfKDCTVLTIAHRLDTIIDSDRILVLDK 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
321-722 |
3.39e-52 |
|
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: 194.21 E-value: 3.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 321 GGSVISILL------------GVLISMFMLTIV--------LPN-ITEYMKSLEATNSLYEIINRKPLVENNNDGKKLKD 379
Cdd:COG4987 251 GLAVVAVLWlaaplvaagalsGPLLALLVLAALalfealapLPAaAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 380 IKKIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWR 459
Cdd:COG4987 331 GPSLELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG-VDLRDLDEDDLR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQDPLLFSNSIKNNIKYslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdglihARK 539
Cdd:COG4987 409 RRIAVVPQRPHLFDTTLRENLRL------------------------------------------------------ARP 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 NyniIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG4987 435 D---ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 620 KTInnLKGNENRITIIIAHRLSTIRYANTIFVLsnrekgnrstvdvdiigedptkdnkenkqKNGKkgdtnknekmsnag 699
Cdd:COG4987 512 ADL--LEALAGRTVLLITHRLAGLERMDRILVL-----------------------------EDGR-------------- 546
|
410 420
....*....|....*....|...
gi 221056887 700 syIIEQGTHDALMKnKNGIYYTM 722
Cdd:COG4987 547 --IVEQGTHEELLA-QNGRYRQL 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1164-1462 |
5.55e-52 |
|
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: 183.07 E-value: 5.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtddvnnekkeqg 1242
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1243 deeqnvgmknvnefsltkegshgdnsavFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDAT 1322
Cdd:cd03252 53 ----------------------------VPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1323 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:cd03252 105 MERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1403 kdKADRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAeGTHEELLSvQDGVYKKYVKL 1462
Cdd:cd03252 185 --CAGRTVIIIAHRLSTVKNADRIIVMEK----GRIVEQ-GSHDELLA-ENGLYAYLYQL 236
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
153-658 |
8.18e-50 |
|
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: 189.57 E-value: 8.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 153 GSKLTSDLDFyleqvnagigtkfltIFTYTsaFLGLYFWSlfkNARLTLCV----TCVFPLIYICGVICNKKakINKKTS 228
Cdd:TIGR01846 254 GSALTVVLDL---------------LFVVV--FLAVMFFY---SPTLTGVVigslVCYALLSVFVGPILRKR--VEDKFE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 229 LLYNNNtmSIIEEALVGIRTVVSYCGEHTILKKFN--LSEKLYSKYML-KANFMESLHIGMINGFilaSYAFGFWYGTRI 305
Cdd:TIGR01846 312 RSAAAT--SFLVESVTGIETIKATATEPQFQNRWDrqLAAYVAASFRVtNLGNIAGQAIELIQKL---TFAILLWFGAHL 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 306 IIS-DLSNAQSnndfhggsvisillgVLISMFMLTIVLPNI------TEYMKSLEATNSLYEIINRKplVENNNDGK-KL 377
Cdd:TIGR01846 387 VIGgALSPGQL---------------VAFNMLAGRVTQPVLrlaqlwQDFQQTGIALERLGDILNSP--TEPRSAGLaAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 378 KDIK-KIQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLK 456
Cdd:TIGR01846 450 PELRgAITFENIRFRYA-PDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLV-DGVDLAIADPA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 457 WWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleylsdqlnedgsasqdgldkrnscrakCAGDLNdmmkttdsdglih 536
Cdd:TIGR01846 528 WLRRQMGVVLQENVLFSRSIRDNI-------------------------------------ALCNPG------------- 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 537 arknyniIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:TIGR01846 558 -------APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEA 630
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 221056887 617 LVQKTINNLkgNENRITIIIAHRLSTIRYANTIFVLsnrEKG 658
Cdd:TIGR01846 631 LIMRNMREI--CRGRTVIIIAHRLSTVRACDRIIVL---EKG 667
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1162-1431 |
2.99e-47 |
|
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: 168.92 E-value: 2.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1162 GKIEIMDVNFTYmsrPNVPI--YKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekk 1239
Cdd:cd03245 1 GRIEFRNVSFSY---PNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK---------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1240 eqgdeeqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKE 1319
Cdd:cd03245 56 --------------------------------PTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGAP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSE-KLIEKt 1398
Cdd:cd03245 104 LADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEeRLKER- 182
|
250 260 270
....*....|....*....|....*....|....
gi 221056887 1399 ivdIKD-KADRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03245 183 ---LRQlLGDKTLIIITHRPSLLDLVDRIIVMDS 213
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
62-309 |
8.57e-47 |
|
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: 169.36 E-value: 8.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 62 LGVSFVCATISGGSLPFFVSVFGVIMKNM---NLGENVDDIIFSLVLI--GIFQFVMSFISSFCMDIVTTKILKTLKVEF 136
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLlpdGDPETQALNVYSLALLllGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 137 LKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYICGVI 216
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 217 CNKKAKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEHTILKKFNLSEKLYSKYMLKANFMESLHIGMINGFILASYA 296
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250
....*....|...
gi 221056887 297 FGFWYGTRIIISD 309
Cdd:pfam00664 241 LALWFGAYLVISG 253
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
349-652 |
4.31e-45 |
|
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: 172.09 E-value: 4.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 349 MKSLEATNSLYEIINRKPLVENNNDGKKLKDIKKIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTIL 428
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 429 KLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdleylsdqlnedgsasqdgl 508
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGV-PLADADADSWRDQIAWVPQHPFLFAGTIAENIR--------------------------- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 509 dkrnscrakcagdlndmmkttdsdgliHARKNyniIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRI 588
Cdd:TIGR02857 418 ---------------------------LARPD---ASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRL 467
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 589 SIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
382-654 |
1.14e-44 |
|
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: 161.51 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS 460
Cdd:cd03244 2 DIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI-DGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPLLFSNSIKNNikyslyslkdleylsdqlnedgsasqdgLDKRNSCrakcagdlndmmkttdsdgliharkn 540
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSN----------------------------LDPFGEY-------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03244 105 ----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQK 180
|
250 260 270
....*....|....*....|....*....|....*
gi 221056887 621 TI-NNLKgneNRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03244 181 TIrEAFK---DCTVLTIAHRLDTIIDSDRILVLDK 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1164-1428 |
1.32e-44 |
|
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: 170.55 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNVPiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekkeqgd 1243
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-------------------------- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATR 1323
Cdd:TIGR02857 374 ----------------------------PTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASD 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:TIGR02857 426 AEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA 505
|
250 260
....*....|....*....|....*
gi 221056887 1404 DkaDRTIITIAHRIASIKRSDKIVV 1428
Cdd:TIGR02857 506 Q--GRTVLLVTHRLALAALADRIVV 528
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
825-1110 |
1.88e-44 |
|
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: 162.81 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 825 VVIIALSIIVAGGLYPMFALLYAKYVSTLFDFANLEAN-SNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRL 903
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 904 FENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCPIVAAVLTGTYFIFMRVF 983
Cdd:pfam00664 81 FKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 984 AIRAR-LSANKDVEKKGINQPGTVFlynnddeifkdpsfliQEAFYNMNTVIIYGLEDYFCKLIEKAIDYSNKGQKRKTL 1062
Cdd:pfam00664 159 AVFAKiLRKLSRKEQKAVAKASSVA----------------EESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAV 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 221056887 1063 VNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTIEVDDF--MKSLFTFLFT 1110
Cdd:pfam00664 223 ANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLvaFLSLFAQLFG 272
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
382-652 |
6.61e-44 |
|
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: 159.29 E-value: 6.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL-DGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSNSIKNNIKYSlyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharknY 541
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLG---------------------------------------------------------A 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 NIIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03245 103 PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER 182
|
250 260 270
....*....|....*....|....*....|.
gi 221056887 622 INNLKGneNRITIIIAHRLSTIRYANTIFVL 652
Cdd:cd03245 183 LRQLLG--DKTLIIITHRPSLLDLVDRIIVM 211
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
58-366 |
1.93e-42 |
|
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: 158.38 E-value: 1.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 58 HKKLLGVSFVCATISGGSLPFFVSVFGVIMKNMNLGENVDDI----IFSL--VLIGIFQFVMSFISSFCMDIVTTKILKT 131
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRseanFWALmfLVLAIVAGIAYFLQGYLFGIAGERLTRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 132 LKVEFLKSVFYQDGQFHD---NNPGSkLTSDLDFYLEQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFP 208
Cdd:cd18578 87 LRKLAFRAILRQDIAWFDdpeNSTGA-LTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 209 LIYICGVIcnkKAKINKKTSLLYNN---NTMSIIEEALVGIRTVVSYCGEHTILKKFNLSEKLYSKYMLKANFMESLHIG 285
Cdd:cd18578 166 LLLLAGYL---RMRLLSGFEEKNKKayeESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 286 MINGFILASYAFGFWYGTRIIISDLSNAQsnndfhggSVISILLGVLISMFMLTIVLPNITEYMKSLEATNSLYEIINRK 365
Cdd:cd18578 243 LSQSLTFFAYALAFWYGGRLVANGEYTFE--------QFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRK 314
|
.
gi 221056887 366 P 366
Cdd:cd18578 315 P 315
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1075-1458 |
3.87e-42 |
|
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: 166.45 E-value: 3.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1075 QLFINSFAYWFGSFLIRRGTIEVDdfmkSLFTFLFTGSY----AGKLMSLKGDSENAKLSFEKYYPLIMrksnIDVRDNG 1150
Cdd:TIGR01193 389 KLILNVVILWTGAYLVMRGKLTLG----QLITFNALLSYfltpLENIINLQPKLQAARVANNRLNEVYL----VDSEFIN 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1151 GIRIKNTNDIDGKIEIMDVNFTYMSrpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneh 1230
Cdd:TIGR01193 461 KKKRTELNNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ------------- 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1231 tddvnnekkeqgdeeqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSI 1310
Cdd:TIGR01193 526 -----------------------------------------ARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSI 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1311 YENIKFG-KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDS 1389
Cdd:TIGR01193 565 LENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1390 NSEKLIEKTIVDIKDKadrTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEELLSvQDGVYKK 1458
Cdd:TIGR01193 645 ITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDH----GKIIE-QGSHDELLD-RNGFYAS 704
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
382-652 |
2.08e-41 |
|
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: 163.96 E-value: 2.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
Cdd:TIGR03796 477 YVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILF-DGIPREEIPREVLANS 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSNSIKNNIkySLYslkdleylsdqlneDGSasqdgldkrnscrakcagdlndmmkttdsdgliharkny 541
Cdd:TIGR03796 555 VAMVDQDIFLFEGTVRDNL--TLW--------------DPT--------------------------------------- 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 niIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVqkt 621
Cdd:TIGR03796 580 --IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII--- 654
|
250 260 270
....*....|....*....|....*....|...
gi 221056887 622 INNLKgneNR--ITIIIAHRLSTIRYANTIFVL 652
Cdd:TIGR03796 655 DDNLR---RRgcTCIIVAHRLSTIRDCDEIIVL 684
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1274-1450 |
2.44e-39 |
|
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: 155.68 E-value: 2.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENI-KFGkeDATREDVKRACKFAAIDEFIESLPNKYDTNVGP 1352
Cdd:COG4618 386 AGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGE 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1353 YGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADRTIITIAHRIASIKRSDKIVVFNNp 1432
Cdd:COG4618 464 GGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSLLAAVDKLLVLRD- 541
|
170
....*....|....*...
gi 221056887 1433 drtGSfVQAEGTHEELLS 1450
Cdd:COG4618 542 ---GR-VQAFGPRDEVLA 555
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1159-1457 |
2.52e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 155.77 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1159 DIDGKIEIMDVNFTYMSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtddvnnek 1238
Cdd:PRK11174 343 ASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF----------------------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1239 keqgdeeqnvgmknvnefsLTKEGShgdnsavfknsgkILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGK 1318
Cdd:PRK11174 400 -------------------LPYQGS-------------LKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1319 EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1399 IVDIkdKADRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEElLSVQDGVYK 1457
Cdd:PRK11174 528 LNAA--SRRQTTLMVTHQLEDLAQWDQIWVMQD----GQIVQ-QGDYAE-LSQAGGLFA 578
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
321-652 |
3.64e-39 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 155.26 E-value: 3.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 321 GGS--VI--SILLGVLIS--MFMLTIVLP--------NITEymKSLEATNSLYEIINRKPLVennNDGKK-LKDIKKIQF 385
Cdd:PRK10789 241 GGSwmVVngSLTLGQLTSfvMYLGLMIWPmlalawmfNIVE--RGSAAYSRIRAMLAEAPVV---KDGSEpVPEGRGELD 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 386 KNVR-FHYDTrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGV 464
Cdd:PRK10789 316 VNIRqFTYPQ-TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD-IPLTKLQLDSWRSRLAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 465 VSQDPLLFSNSIKNNIkyslyslkdleylsdqlnedgsasqdGLDKRNSCRAkcagdlndmmkttdsdgliharknynii 544
Cdd:PRK10789 394 VSQTPFLFSDTVANNI--------------------------ALGRPDATQQ---------------------------- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 545 ddsEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYlvqKTINN 624
Cdd:PRK10789 420 ---EIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH---QILHN 493
|
330 340
....*....|....*....|....*....
gi 221056887 625 LKG-NENRITIIIAHRLSTIRYANTIFVL 652
Cdd:PRK10789 494 LRQwGEGRTVIISAHRLSALTEASEILVM 522
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
401-608 |
4.14e-39 |
|
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: 142.79 E-value: 4.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSN-SIKNN 479
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG-QDLTDDERKSLRKEIGYVFQDPQLFPRlTVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 480 IKYSLYslkdleylsdqlnedgsasqdgldkrnscrakcagdLNDMMKTTDSDGLIHARKNYNiiddsevvnvskkvlih 559
Cdd:pfam00005 80 LRLGLL------------------------------------LKGLSKREKDARAEEALEKLG----------------- 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 221056887 560 dfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
Cdd:pfam00005 107 -----LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
383-652 |
1.07e-38 |
|
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: 144.57 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWR 459
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQDPLLFSN---SIKNNIKYSLYSLKDLEYlsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliH 536
Cdd:cd03257 82 KEIQMVFQDPMSSLNprmTIGEQIAEPLRIHGKLSK-------------------------------------------K 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 537 ARKNYNIIDDSEVVNVSKKVLihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:cd03257 119 EARKEAVLLLLVGVGLPEEVL---------NRY-------PHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQA 182
|
250 260 270
....*....|....*....|....*....|....*...
gi 221056887 617 LVQKTINNLKgNENRITII-IAHRLSTIRY-ANTIFVL 652
Cdd:cd03257 183 QILDLLKKLQ-EELGLTLLfITHDLGVVAKiADRVAVM 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1166-1457 |
1.14e-38 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 153.71 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1166 IMDVNFTYMSRP--NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgd 1243
Cdd:PRK10789 313 ELDVNIRQFTYPqtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV------------------------- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATR 1323
Cdd:PRK10789 368 -----------------------------SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:PRK10789 419 QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG 498
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 221056887 1404 DKadRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEELLSvQDGVYK 1457
Cdd:PRK10789 499 EG--RTVIISAHRLSALTEASEILVMQH----GHIAQ-RGNHDQLAQ-QSGWYR 544
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1162-1459 |
1.31e-38 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 153.72 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1162 GKIEIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeq 1241
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL----------------------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1242 gdeeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKeDA 1321
Cdd:PRK10790 394 -------------------------------TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1322 TREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PRK10790 442 SEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 1402 IKDKAdrTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEELLSVQDGVYKKY 1459
Cdd:PRK10790 522 VREHT--TLVVIAHRLSTIVEADTILVLHR----GQAVE-QGTHQQLLAAQGRYWQMY 572
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1162-1462 |
3.22e-38 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 152.29 E-value: 3.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1162 GKIEIMDVNFTYMSRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekkeq 1241
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD------------------------ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1242 gdeeqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDA 1321
Cdd:PRK11160 392 ------------------------------PQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1322 TREDVKRACKFAAIDEFIESlPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PRK11160 442 SDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 1402 IkdKADRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAEGTHEELLSVQDGVYKKYVKL 1462
Cdd:PRK11160 521 H--AQNKTVLMITHRLTGLEQFDRICVMDN----GQII-EQGTHQELLAQQGRYYQLKQRL 574
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
383-656 |
8.08e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.11 E-value: 8.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKI 462
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK-PLSAMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNSIKNNIKYSlYSLKDLEYLSDQLNEDgsASQDGLDKrnscrakcagdlnDMMKTtdsdgliharknyn 542
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFP-FQLRERKFDRERALEL--LERLGLPP-------------DILDK-------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iiddsevvnvskkvlihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:COG4619 127 ---------------------------------PVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELL 173
|
250 260 270
....*....|....*....|....*....|....*
gi 221056887 623 NNLKGNENRITIIIAHRLSTI-RYANTIFVLSNRE 656
Cdd:COG4619 174 REYLAEEGRAVLWVSHDPEQIeRVADRVLTLEAGR 208
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1162-1461 |
1.01e-37 |
|
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: 152.42 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1162 GKIEIMDVNFTYmsRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtddvnnEKKE 1240
Cdd:TIGR03797 450 GAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGF---------------------ETPE 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1241 qgdeeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKfGKED 1320
Cdd:TIGR03797 507 ---------------------------------SGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAP 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1321 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIv 1400
Cdd:TIGR03797 553 LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL- 631
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 1401 dikDKADRTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaEGTHEELLSVqDGVYKKYVK 1461
Cdd:TIGR03797 632 ---ERLKVTRIVIAHRLSTIRNADRIYVLDA----GRVVQ-QGTYDELMAR-EGLFAQLAR 683
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1164-1431 |
1.48e-37 |
|
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: 141.16 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDhhivfknehtddvnnekkeqgd 1243
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG---------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavFKNSGKILLDGVDIC--DYNLKDLRNLFSIVSQEPILFNMSIYENIKFG---- 1317
Cdd:cd03260 56 ---------------------------APDEGEVLLDGKDIYdlDVDVLELRRRVGMVFQKPNPFPGSIYDNVAYGlrlh 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 ---KEDATREDVKRACKFAAidefiesLPNKYDTNVGPYGksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKL 1394
Cdd:cd03260 109 gikLKEELDERVEEALRKAA-------LWDEVKDRLHALG--LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAK 179
|
250 260 270
....*....|....*....|....*....|....*...
gi 221056887 1395 IEKTIVDIKDkaDRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03260 180 IEELIAELKK--EYTIVIVTHNMQQAARvADRTAFLLN 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1161-1428 |
2.46e-36 |
|
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: 137.16 E-value: 2.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1161 DGKIEIMDVNFTYmsRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtddvnnekk 1239
Cdd:cd03369 4 HGEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEE------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1240 eqgdeeqnvgmknvnefsltkegshgdnsavfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENI-KFGK 1318
Cdd:cd03369 63 -----------------------------------GKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLdPFDE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1319 EDAtredvkrackfaaiDEFIESLpnkydtNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:cd03369 108 YSD--------------EEIYGAL------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT 167
|
250 260 270
....*....|....*....|....*....|
gi 221056887 1399 IVdiKDKADRTIITIAHRIASIKRSDKIVV 1428
Cdd:cd03369 168 IR--EEFTNSTILTIAHRLRTIIDYDKILV 195
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
383-654 |
2.50e-36 |
|
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: 137.85 E-value: 2.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKI 462
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG-KDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPL--LFSNSIKNNIKYSLYSLkdleylsdqlnedgsasqdGLDKRNscrakcagdlndmmkttdsdglIHARkn 540
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAFGPENL-------------------GLPREE----------------------IRER-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniIDDS-EVVNVskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG1122 115 ---VEEAlELVGL-----------------EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELL 174
|
250 260 270
....*....|....*....|....*....|....*..
gi 221056887 620 KTINNLkgNENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:COG1122 175 ELLKRL--NKEGKTVIIVtHDLDLVaELADRVIVLDD 209
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
826-1118 |
2.69e-36 |
|
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: 139.92 E-value: 2.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 826 VIIALSIIVAGGLYPMFALLYAKYVSTLFDFANLEANS-------NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKT 898
Cdd:cd18577 2 IIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPdeflddvNKYALYFVYLGIGSFVLSYIQTACWTITGERQARR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 899 MKHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCPIVAAVLTGTY-- 976
Cdd:cd18577 82 IRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLpl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 977 -FIFMRVFAIRARLSANKdvEKKGINQPGTVflynnddeifkdpsflIQEAFYNMNTVIIYGLEDYFCKLIEKAIDYSNK 1055
Cdd:cd18577 160 iAIVGGIMGKLLSKYTKK--EQEAYAKAGSI----------------AEEALSSIRTVKAFGGEEKEIKRYSKALEKARK 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 1056 GQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTIEVDDFMKSLFTFLFTGSYAGKLM 1118
Cdd:cd18577 222 AGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIA 284
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
37-725 |
4.34e-36 |
|
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: 147.58 E-value: 4.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 37 YKKIKtQRIPFFLPFKCLPPSHKKLLGVSFVCATIS-----GGSLpFFVSVFGVIMKNMNLGeNVDDIIFSLVLIGIFQF 111
Cdd:TIGR01193 134 YKPIK-EKENSLLKFIPLITRQKKLIVNIVIAAIIVtlisiAGSY-YLQKIIDTYIPHKMMG-TLGIISIGLIIAYIIQQ 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 112 VMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAgIGTKFLTIFTYTSAFLGLYFW 191
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDA-LASTILSLFLDMWILVIVGLF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 192 SLFKNARLTLCVTCVFPlIYICGVICNKK--AKINKKTslLYNNNTM--SIIEEaLVGIRTVVSYCGEHTILKKFNLSEK 267
Cdd:TIGR01193 290 LVRQNMLLFLLSLLSIP-VYAVIIILFKRtfNKLNHDA--MQANAVLnsSIIED-LNGIETIKSLTSEAERYSKIDSEFG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 268 LYSKYMLKANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnaqsnNDFHGGSVISilLGVLISMFmlTIVLPNITE 347
Cdd:TIGR01193 366 DYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMR--------GKLTLGQLIT--FNALLSYF--LTPLENIIN 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 348 YMKSLEATNSLYEIINRKPLVENNNDGKKLKDIKK-----IQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGC 422
Cdd:TIGR01193 434 LQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNnlngdIVINDVSYSYGYGS--NILSDISLTIKMNSKTTIVGMSGS 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 423 GKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleylsdqlnedgs 502
Cdd:TIGR01193 512 GKSTLAKLLVGFFQARSGEILLN-GFSLKDIDRHTLRQFINYLPQEPYIFSGSILENL---------------------- 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 503 asqdgldkrnscrakcagdlndmmkttdsdgLIHARKNYNIIDDSEVVNVSKkvlIHDFVSALPDKYETLVGSNASKLSG 582
Cdd:TIGR01193 569 -------------------------------LLGAKENVSQDEIWAACEIAE---IKDDIENMPLGYQTELSEEGSSISG 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 583 GQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSnrekgnrst 662
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLD--------- 682
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 663 vdvdiigedptkdnkenkqkNGKkgdtnknekmsnagsyIIEQGTHDALMkNKNGIYYTMINN 725
Cdd:TIGR01193 683 --------------------HGK----------------IIEQGSHDELL-DRNGFYASLIHN 708
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
383-652 |
8.75e-36 |
|
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: 143.89 E-value: 8.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRK--DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWW 458
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 459 RSKIGVVSQDPllfsnsiknnikyslyslkdleYLSdqlnedgsasqdgldkrnscrakcagdLNDMMKTTDSdgLIHAR 538
Cdd:COG1123 341 RRRVQMVFQDP----------------------YSS---------------------------LNPRMTVGDI--IAEPL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 539 KNYNIIDDSE----VVNVSKKV-LIHDFVSALPdkYEtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDnk 613
Cdd:COG1123 370 RLHGLLSRAErrerVAELLERVgLPPDLADRYP--HE---------LSGGQRQRVAIARALALEPKLLILDEPTSALD-- 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 221056887 614 seYLVQKTI-NNLKG--NENRITII-IAHRLSTIRY-ANTIFVL 652
Cdd:COG1123 437 --VSVQAQIlNLLRDlqRELGLTYLfISHDLAVVRYiADRVAVM 478
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1164-1450 |
6.41e-35 |
|
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: 133.61 E-value: 6.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfknehtddvnnekkeqgd 1243
Cdd:COG1122 1 IELENLSFSY--PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPI--LFNMSIYENIKFG---- 1317
Cdd:COG1122 55 ------------------------------SGEVLVDGKDITKKNLRELRRKVGLVFQNPDdqLFAPTVEEDVAFGpenl 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 --KEDATREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:COG1122 105 glPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRREL 173
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1396 EKTIVDIKdKADRTIITIAHRIASI-KRSDKIVVFNNpdrtGSfVQAEGTHEELLS 1450
Cdd:COG1122 174 LELLKRLN-KEGKTVIIVTHDLDLVaELADRVIVLDD----GR-IVADGTPREVFS 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
206-1460 |
6.87e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 145.89 E-value: 6.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 206 VFPLIYICGVICNKKAKINKKtSLLYNNNTMSIIEEALVGIRTVVSYCGEHTILKKFNLSEKLYSKYMLKANFMESLHIG 285
Cdd:PLN03232 450 LFLLIPLQTLIVRKMRKLTKE-GLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSF 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 286 MINGFILASYAFGFwyGTRIIIS-DLSNAQSnndFHGGSVISILLGVLismFMLTIVLPNITEYMKSLEATNSLY----E 360
Cdd:PLN03232 529 ILNSIPVVVTLVSF--GVFVLLGgDLTPARA---FTSLSLFAVLRSPL---NMLPNLLSQVVNANVSLQRIEELLlseeR 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 361 IINRKPLVEnnndgkklKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG 440
Cdd:PLN03232 601 ILAQNPPLQ--------PGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 441 DIIIndshnlkdinlkwWRSKIGVVSQDPLLFSNSIKNNIKYSlyslKDLEylsdqlnedgsasqdgldkrnscrakcag 520
Cdd:PLN03232 673 SSVV-------------IRGSVAYVPQVSWIFNATVRENILFG----SDFE----------------------------- 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 521 dlndmmkttdsdglihARKNYNIIDDSevvnvskkVLIHDfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKI 600
Cdd:PLN03232 707 ----------------SERYWRAIDVT--------ALQHD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDI 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 601 LILDEATSSLDNKSEYLVQKTI--NNLKGnenRITIIIAHRLSTIRYANTIFVLSnrekgnrstvdvdiigedptkdnke 678
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVFDSCmkDELKG---KTRVLVTNQLHFLPLMDRIILVS------------------------- 813
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 679 nkqkngkkgdtnknEKMsnagsyIIEQGTHDALMKNKNGIYYTMINNQKVSSKTSNNNDNDKDSDMKSSVYKD-SERGYd 757
Cdd:PLN03232 814 --------------EGM------IKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDENILKLGPTVTIDvSERNL- 872
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 758 pdemnGNTKNGNEsasdKKSNKMSDENASSknagGKLSFlrNLFKRKPKAPNNLRMVYREIFSYKKDVVIIALSiivagg 837
Cdd:PLN03232 873 -----GSTKQGKR----GRSVLVKQEERET----GIISW--NVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSS------ 931
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 838 lypmfallyakyvSTLFDFANLEANSNKYS--LYILVIAIAMF--ISETLKNYYNNVIGE-KVEKTMKHRLFENILYQEI 912
Cdd:PLN03232 932 -------------STWLSIWTDQSTPKSYSpgFYIVVYALLGFgqVAVTFTNSFWLISSSlHAAKRLHDAMLNSILRAPM 998
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 913 SFFDQDchAPGLLSSHINRDVHLLKTGLVNNIVIFTH--------FIVLFIVSMIMSFYFCPIVAaVLTGTYFIFMrvfa 984
Cdd:PLN03232 999 LFFHTN--PTGRVINRFSKDIGDIDRNVANLMNMFMNqlwqllstFALIGTVSTISLWAIMPLLI-LFYAAYLYYQ---- 1071
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 985 irarlSANKDVEKKginqpgtvflynndDEIFKDPSF-LIQEAFYNMNTVIIYGLEDYFCKLIEKAIDysnkGQKRKTLV 1063
Cdd:PLN03232 1072 -----STSREVRRL--------------DSVTRSPIYaQFGEALNGLSSIRAYKAYDRMAKINGKSMD----NNIRFTLA 1128
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1064 NSMLWGFSQSAQLFINSFAYWF-GSF-LIRRGTIEVDDFMKSLFTFLFtgSYAGKLMSL-------KGDSENAKLSFEky 1134
Cdd:PLN03232 1129 NTSSNRWLTIRLETLGGVMIWLtATFaVLRNGNAENQAGFASTMGLLL--SYTLNITTLlsgvlrqASKAENSLNSVE-- 1204
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1135 yplimRKSN-IDVRDNGGIRIKNTNDID-----GKIEIMDVNFTYmsRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKST 1207
Cdd:PLN03232 1205 -----RVGNyIDLPSEATAIIENNRPVSgwpsrGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSS 1277
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1208 VMSLLMRFYDLKNdhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegshgdnsavfknsGKILLDGVDICDY 1287
Cdd:PLN03232 1278 MLNALFRIVELEK------------------------------------------------------GRIMIDDCDVAKF 1303
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1288 NLKDLRNLFSIVSQEPILFNMSIYENIKFGKE--DAtreDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRV 1365
Cdd:PLN03232 1304 GLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEhnDA---DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLL 1380
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1366 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikDKADRTIITIAHRIASIKRSDKIVVFNnpdrTGSFVQAEgTH 1445
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDCDKILVLS----SGQVLEYD-SP 1453
|
1290
....*....|....*
gi 221056887 1446 EELLSVQDGVYKKYV 1460
Cdd:PLN03232 1454 QELLSRDTSAFFRMV 1468
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1177-1450 |
9.63e-35 |
|
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: 141.33 E-value: 9.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1177 PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgdeeqnVGmknvnef 1256
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI-----------------------------------VG------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1257 sltkegshgdnsAVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENI-KFGkEDATREDVKRACKFAAI 1335
Cdd:TIGR01842 367 ------------IWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFG-ENADPEKIIEAAKLAGV 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1336 DEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADRTIITIAH 1415
Cdd:TIGR01842 434 HELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITH 512
|
250 260 270
....*....|....*....|....*....|....*
gi 221056887 1416 RIASIKRSDKIVVFNNpdrtGSfVQAEGTHEELLS 1450
Cdd:TIGR01842 513 RPSLLGCVDKILVLQD----GR-IARFGERDEVLA 542
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
382-654 |
1.69e-34 |
|
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: 142.40 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYdtRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS 460
Cdd:TIGR03797 451 AIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFY-DGQDLAGLDVQAVRR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPLLFSNSIKNNIKYSlyslkdlEYLSdqLNEDGSASQdgldkrnscRAKCAGDLNDM-MkttdsdGLihark 539
Cdd:TIGR03797 528 QLGVVLQNGRLMSGSIFENIAGG-------APLT--LDEAWEAAR---------MAGLAEDIRAMpM------GM----- 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 nyniiddsevvnvskkvliHdfvsalpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:TIGR03797 579 -------------------H-----------TVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVS 628
|
250 260 270
....*....|....*....|....*....|....*
gi 221056887 620 KTINNLKGNEnritIIIAHRLSTIRYANTIFVLSN 654
Cdd:TIGR03797 629 ESLERLKVTR----IVIAHRLSTIRNADRIYVLDA 659
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
384-654 |
1.09e-33 |
|
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: 129.51 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 384 QFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIG 463
Cdd:cd03225 1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-DLTKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 464 VVSQDPllfsnsiknnikyslyslkdleylSDQLnedgsasqdgldkrnscrakcagdlndMMKTTDSDgLIHARKNYNi 543
Cdd:cd03225 79 LVFQNP------------------------DDQF---------------------------FGPTVEEE-VAFGLENLG- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 544 IDDSEVVNVSKKVLIHDFVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
Cdd:cd03225 106 LPEEEIEERVEEALELVGLEGLRDR-------SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK 178
|
250 260 270
....*....|....*....|....*....|...
gi 221056887 624 NLKgnENRITIIIA-HRLSTIR-YANTIFVLSN 654
Cdd:cd03225 179 KLK--AEGKTIIIVtHDLDLLLeLADRVIVLED 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1164-1431 |
1.57e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.78 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgd 1243
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFG----KE 1319
Cdd:COG4619 53 -----------------------------TSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLPFPfqlrER 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 DATREDVKRAckFAAIDefiesLPNKY-DTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG4619 104 KFDRERALEL--LERLG-----LPPDIlDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEEL 172
|
250 260 270
....*....|....*....|....*....|....
gi 221056887 1399 IVDIKDKADRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:COG4619 173 LREYLAEEGRAVLWVSHDPEQIERvADRVLTLEA 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
383-637 |
2.93e-33 |
|
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: 128.84 E-value: 2.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIINDSH-NLKDINLK 456
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 457 WWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdleylsdQLNedGSASQDGLDKRnscrakcagdlndmmkttdsdglih 536
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGL-----------RLH--GIKLKEELDER------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 537 arknyniiddseVVNVSKKVLIHDFVSalpDKyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:cd03260 120 ------------VEEALRKAALWDEVK---DR------LHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTA 178
|
250 260
....*....|....*....|.
gi 221056887 617 LVQKTINNLKgneNRITIIIA 637
Cdd:cd03260 179 KIEELIAELK---KEYTIVIV 196
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
402-654 |
4.08e-33 |
|
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: 136.42 E-value: 4.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDinlkWWRSK----IGVVSQDPLLFSNSIK 477
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL-DGADLSQ----WDREElgrhIGYLPQDVELFDGTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 478 NNIkyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdglihARknYNIIDDSEVVNVSKKVL 557
Cdd:COG4618 424 ENI--------------------------------------------------------AR--FGDADPEKVVAAAKLAG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 558 IHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIA 637
Cdd:COG4618 446 VHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVIT 524
|
250
....*....|....*..
gi 221056887 638 HRLSTIRYANTIFVLSN 654
Cdd:COG4618 525 HRPSLLAAVDKLLVLRD 541
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1164-1431 |
1.02e-32 |
|
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: 125.41 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLI------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnVGMKNVNefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIkfgkedatr 1323
Cdd:cd03246 49 ----LGLLRPT-------------------SGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIAENI--------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 edvkrackfaaidefieslpnkydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:cd03246 97 ---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK 143
|
250 260
....*....|....*....|....*...
gi 221056887 1404 dKADRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03246 144 -AAGATRIVIAHRPETLASADRILVLED 170
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
404-727 |
1.55e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 135.36 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 404 LNFTLTEGKTYAFVGESGCGKSTILKLIerL-YDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIky 482
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNAL--LgFLPYQGSLKING-IELRELDPESWRKHLSWVGQNPQLPHGTLRDNV-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 483 slySLkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdglihARKNyniIDDSEVVNVSKKVLIHDFV 562
Cdd:PRK11174 444 ---LL-------------------------------------------------GNPD---ASDEQLQQALENAWVSEFL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 563 SALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLST 642
Cdd:PRK11174 469 PLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLED 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 643 IRYANTIFVLsnrekgnrstvdvdiigedptkdnkenkqKNGKkgdtnknekmsnagsyIIEQGTHDALMKNkNGIYYTM 722
Cdd:PRK11174 547 LAQWDQIWVM-----------------------------QDGQ----------------IVQQGDYAELSQA-GGLFATL 580
|
....*
gi 221056887 723 INNQK 727
Cdd:PRK11174 581 LAHRQ 585
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1164-1428 |
2.44e-32 |
|
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: 126.08 E-value: 2.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekkeqg 1242
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1243 deeqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYN---LKDLRNLFSIVSQEPIL-FN--MSIYENIKF 1316
Cdd:cd03257 57 -----------------------------PTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPMSsLNprMTIGEQIAE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1317 GKEDATREDVKRACKFAAIDEFI-----ESLPNKYdtnvgPYgkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:cd03257 108 PLRIHGKLSKKEARKEAVLLLLVgvglpEEVLNRY-----PH--ELSGGQRQRVAIARALALNPKLLIADEPTSALDVSV 180
|
250 260 270
....*....|....*....|....*....|....*...
gi 221056887 1392 EKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03257 181 QAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAV 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1164-1431 |
2.54e-32 |
|
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: 125.27 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNVPIY--KDLTFSCDSKKTTAIVGETGSGKStvmSLLMrfydlkndhhivfknehtddvnnekkeq 1241
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKS---SLLS---------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1242 gdeeqnvgmknvnefSLTKEgshgdnsaVFKNSGKILLDGVdicdynlkdlrnlFSIVSQEPILFNMSIYENIKFGKE-D 1320
Cdd:cd03250 50 ---------------ALLGE--------LEKLSGSVSVPGS-------------IAYVSQEPWIQNGTIRENILFGKPfD 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1321 ATR-EDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSN-SEKLIEKT 1398
Cdd:cd03250 94 EERyEKVIKAC---ALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENC 170
|
250 260 270
....*....|....*....|....*....|...
gi 221056887 1399 IVDIKdKADRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03250 171 ILGLL-LNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1182-1385 |
4.50e-32 |
|
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: 122.76 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1182 YKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtddvnnekkeQGDEeqnvgmknvnefsltke 1261
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL------------------------SPTE----------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1262 gshgdnsavfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPILFN-MSIYENIKFGKEDATREDVKRACKFAAIDEFIe 1340
Cdd:pfam00005 40 -------------GTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENLRLGLLLKGLSKREKDARAEEALEKL- 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221056887 1341 SLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATS 1385
Cdd:pfam00005 106 GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
383-659 |
1.73e-31 |
|
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: 121.94 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-DGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNSIKNNIkyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyn 542
Cdd:cd03246 79 GYLPQDDELFSGSIAENI-------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iiddsevvnvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03246 97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
250 260 270
....*....|....*....|....*....|....*..
gi 221056887 623 NNLKGnENRITIIIAHRLSTIRYANTIFVLsnrEKGN 659
Cdd:cd03246 140 AALKA-AGATRIVIAHRPETLASADRILVL---EDGR 172
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
383-655 |
2.16e-31 |
|
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: 123.77 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRS 460
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgeDISGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPLLFSN-SIKNNIKYSLYslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmMKTTDSDGLIHARk 539
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLR----------------------------------------EHTRLSEEEIREI- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 nyniiddsevvnVSKK---VLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:cd03261 117 ------------VLEKleaVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASG 173
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 221056887 617 LVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNR 655
Cdd:cd03261 174 VIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1165-1431 |
3.58e-31 |
|
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: 122.19 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1165 EIMDVNFTYMSRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtddvnnekkeqgde 1244
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL---------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1245 eqnvgmknvnefsltkegshgdnsavFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--ILFNMSIYENIKFG----- 1317
Cdd:cd03225 52 --------------------------GPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQFFGPTVEEEVAFGlenlg 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 -KEDATREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:cd03225 106 lPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
|
250 260 270
....*....|....*....|....*....|....*.
gi 221056887 1397 KTIVDIKDKaDRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03225 175 ELLKKLKAE-GKTIIIVTHDLDLLLElADRVIVLED 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
337-1463 |
5.10e-31 |
|
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: 133.53 E-value: 5.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 337 MLTIVLPNITEYMKSLEatnSLYEIINRKPLVENNNDGKKLKD--IKKIQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTY 414
Cdd:TIGR00957 592 ILPMVISSIVQASVSLK---RLRIFLSHEELEPDSIERRTIKPgeGNSITVHNATFTW-ARDLPPTLNGITFSIPEGALV 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 415 AFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskIGVVSQDPLLFSNSIKNNIKYSlyslkdleyls 494
Cdd:TIGR00957 668 AVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWIQNDSLRENILFG----------- 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 495 DQLNEDgsasqdgldKRNSCRAKCAgdlndmmkttdsdgliharknynIIDDSEVvnvskkvlihdfvsaLPDKYETLVG 574
Cdd:TIGR00957 723 KALNEK---------YYQQVLEACA-----------------------LLPDLEI---------------LPSGDRTEIG 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLS 653
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMS 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 654 nrekgnrstvdvdiigedptkdnkenkqkngkkgdtnknekmsnaGSYIIEQGTHDALMKnKNGIYYTMInnqkvsskts 733
Cdd:TIGR00957 836 ---------------------------------------------GGKISEMGSYQELLQ-RDGAFAEFL---------- 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 734 nnndndkdsdmkssvykdseRGYDPDEMNGNTKN---GNESASDKKSNKMSDE---------------NASSKNAGG--- 792
Cdd:TIGR00957 860 --------------------RTYAPDEQQGHLEDswtALVSGEGKEAKLIENGmlvtdvvgkqlqrqlSASSSDSGDqsr 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 793 KLSFLRNLFKRKPKAPNNLRMVyreifSYKKDVVIIALSI----IVAGGLYPMFA---LLYAKYVSTLFdfANL------ 859
Cdd:TIGR00957 920 HHGSSAELQKAEAKEETWKLME-----ADKAQTGQVELSVywdyMKAIGLFITFLsifLFVCNHVSALA--SNYwlslwt 992
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 860 --------EANSN-KYSLY--------ILVIAIAMFISetlknyynnVIGEKVEKTMKHRLFENILYQEISFFDQDchAP 922
Cdd:TIGR00957 993 ddpmvngtQNNTSlRLSVYgalgilqgFAVFGYSMAVS---------IGGIQASRVLHQDLLHNKLRSPMSFFERT--PS 1061
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 923 GLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCPIVAAV---LTGTYFIFMRVFAIRAR-LSANKDVEKK 998
Cdd:TIGR00957 1062 GNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIippLGLLYFFVQRFYVASSRqLKRLESVSRS 1141
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 999 GInqpgtvflYNNddeifkdpsflIQEAFYNMNTVIIYGLEDYFCKLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFI 1078
Cdd:TIGR00957 1142 PV--------YSH-----------FNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCI 1202
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1079 NSFAYWFGsfLIRRGTIEVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFE--KYYPLIMRKSNIDVRdngGIRIKN 1156
Cdd:TIGR00957 1203 VLFAALFA--VISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVErlKEYSETEKEAPWQIQ---ETAPPS 1277
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1157 TNDIDGKIEIMDVNFTYmsRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtddvn 1235
Cdd:TIGR00957 1278 GWPPRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRI-------------------- 1335
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1236 NEKKEqgdeeqnvgmknvnefsltkegshgdnsavfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIK 1315
Cdd:TIGR00957 1336 NESAE----------------------------------GEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD 1381
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1316 -FGKedATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKL 1394
Cdd:TIGR00957 1382 pFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 1459
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1395 IEKTIVDIKDkaDRTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAEGTHEELLSvQDGVYKKYVKLA 1463
Cdd:TIGR00957 1460 IQSTIRTQFE--DCTVLTIAHRLNTIMDYTRVIVLDKGE-----VAEFGAPSNLLQ-QRGIFYSMAKDA 1520
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1164-1416 |
5.57e-31 |
|
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: 129.79 E-value: 5.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekkeqgd 1243
Cdd:TIGR02868 335 LELRDLSAGY--PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-------------------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATR 1323
Cdd:TIGR02868 387 ----------------------------PLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:TIGR02868 439 EELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
|
250
....*....|...
gi 221056887 1404 DKadRTIITIAHR 1416
Cdd:TIGR02868 519 SG--RTVVLITHH 529
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1155-1431 |
6.72e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.84 E-value: 6.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1155 KNTNDIDGKIEIMDVNFTYMSRP-----NVPIYKdltfscdsKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkne 1229
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQalkdiNLDIPE--------NKVTALIGPSGCGKSTLLRCLNRMNDLIPGARV----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1230 htddvnnekkeqgdeeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDI--CDYNLKDLRNLFSIVSQEPILFN 1307
Cdd:COG1117 70 --------------------------------------------EGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1308 MSIYENIKFG--------KEDAtREDVKRACKFAAI-DEfiesLPNKYDTNvgpyGKSLSGGQKQRVAIARALLREPKIL 1378
Cdd:COG1117 106 KSIYDNVAYGlrlhgiksKSEL-DEIVEESLRKAALwDE----VKDRLKKS----ALGLSGGQQQRLCIARALAVEPEVL 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 221056887 1379 LLDEATSSLDSNSEKLIEKTIVDIKDkaDRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:COG1117 177 LMDEPTSALDPISTAKIEELILELKK--DYTIVIVTHNMQQAARvSDYTAFFYL 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
360-723 |
7.42e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 129.94 E-value: 7.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 360 EIINRKPLVENNNDGKKLKDIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
Cdd:PRK11160 316 EITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 440 GDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDlEYLSDQLNedgsasQDGLDKRnscrakca 519
Cdd:PRK11160 395 GEILLNG-QPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASD-EALIEVLQ------QVGLEKL-------- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 520 gdlndmmkTTDSDGLiharknyniiddsevvnvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPK 599
Cdd:PRK11160 459 --------LEDDKGL-----------------------------------NAWLGEGGRQLSGGEQRRLGIARALLHDAP 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 600 ILILDEATSSLDNKSEylvQKTINNL-KGNENRITIIIAHRLSTIRYANTIFVLSnrekgnrstvdvdiigedptkdnke 678
Cdd:PRK11160 496 LLLLDEPTEGLDAETE---RQILELLaEHAQNKTVLMITHRLTGLEQFDRICVMD------------------------- 547
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 221056887 679 nkqkNGKkgdtnknekmsnagsyIIEQGTHDALMKNKNGiYYTMI 723
Cdd:PRK11160 548 ----NGQ----------------IIEQGTHQELLAQQGR-YYQLK 571
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1164-1431 |
1.08e-30 |
|
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: 119.73 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfyDLKndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLK------------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYNlKDLRNLFSIVSQEPILFNMSIYENIkfgkedatr 1323
Cdd:cd03247 54 ----------------------------PQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNNL--------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 edvkrackfaaidefieslpnkydtnvgpyGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:cd03247 96 ------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL 145
|
250 260
....*....|....*....|....*...
gi 221056887 1404 DkaDRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03247 146 K--DKTLIWITHHLTGIEHMDKILFLEN 171
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1275-1464 |
1.11e-30 |
|
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: 122.32 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1275 GKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYG 1354
Cdd:cd03288 76 GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1355 KSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADRTIITIAHRIASIKRSDKIVVFNNpdr 1434
Cdd:cd03288 155 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSR--- 229
|
170 180 190
....*....|....*....|....*....|
gi 221056887 1435 tGSFVQAEgTHEELLSVQDGVYKKYVKLAK 1464
Cdd:cd03288 230 -GILVECD-TPENLLAQEDGVFASLVRTDK 257
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
383-654 |
1.59e-30 |
|
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: 119.21 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-SHNLKDINLKWWRSK 461
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGeDLTDLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIkyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharkn 540
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENI------------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddsevvnvskkvlihdfvsALPdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03229 98 -----------------------ALG-------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRA 141
|
250 260 270
....*....|....*....|....*....|....*
gi 221056887 621 TINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:cd03229 142 LLKSLQAQLGITVVLVTHDLDeAARLADRVVVLRD 176
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
320-640 |
1.67e-30 |
|
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: 128.25 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 320 HGGSVISILLGVLISMFMLTIVLPN----ITEYMKSLEATNSLYEIINRKPLVENNNDGKKLKDIKKIQFKNVRFHYDTr 395
Cdd:TIGR02868 268 LAPVTLAVLVLLPLAAFEAFAALPAaaqqLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPG- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 396 kDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLKWWRSKIGVVSQDPLLFSNS 475
Cdd:TIGR02868 347 -APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP-VSSLDQDEVRRRVSVCAQDAHLFDTT 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 476 IKNNIKYslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdglihARKNyniIDDSEVVNVSKK 555
Cdd:TIGR02868 425 VRENLRL------------------------------------------------------ARPD---ATDEELWAALER 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 556 VLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITII 635
Cdd:TIGR02868 448 VGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVL 525
|
....*
gi 221056887 636 IAHRL 640
Cdd:TIGR02868 526 ITHHL 530
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
383-654 |
2.55e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 120.55 E-value: 2.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDiNLKWWRSKI 462
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG-EDVAR-DPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSN-SIKNNIKY--SLYSLKDLEylsdqlnedgsasqdgLDKRnscrakcagdLNDMMKTTDsdglihark 539
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRFfaRLYGLPRKE----------------ARER----------IDELLELFG--------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 nyniiddsevvnvskkvlihdfvsaLPDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG1131 121 -------------------------LTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELW 171
|
250 260 270
....*....|....*....|....*....|....*..
gi 221056887 620 KTINNLKgnENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:COG1131 172 ELLRELA--AEGKTVLLStHYLEEAeRLCDRVAIIDK 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1164-1432 |
2.78e-30 |
|
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: 118.44 E-value: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL---------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 EEqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYN--LKDLRNLFSIVSQEPILF-NMSIYENIKFGked 1320
Cdd:cd03229 50 EE--------------------------PDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFpHLTVLENIALG--- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1321 atredvkrackfaaidefieslpnkydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03229 101 ------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
|
250 260 270
....*....|....*....|....*....|...
gi 221056887 1401 DIKDKADRTIITIAHRIASIKR-SDKIVVFNNP 1432
Cdd:cd03229 145 SLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
383-657 |
6.95e-30 |
|
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: 119.31 E-value: 6.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRS 460
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgqDITGLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPLLFSN-SIKNNIKYSLYslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmMKTTDSDGLIHARk 539
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPLR----------------------------------------EHTDLSEAEIREL- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 nyniiddsevvnVSKKVlihDFVSaLP---DKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:COG1127 122 ------------VLEKL---ELVG-LPgaaDKM-------PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSA 178
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 221056887 617 LVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNREK 657
Cdd:COG1127 179 VIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKI 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1164-1440 |
1.10e-29 |
|
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: 118.01 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtddvnnekkEQGD 1243
Cdd:cd03259 1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL------------------------ERPD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDlRNLfSIVSQEPILF-NMSIYENIKFG----- 1317
Cdd:cd03259 54 ------------------------------SGEILIDGRDVTGVPPER-RNI-GMVFQDYALFpHLTVAENIAFGlklrg 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 -KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:cd03259 102 vPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELR 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 221056887 1397 KTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQ 1440
Cdd:cd03259 171 EELKELQRELGITTIYVTHDQEEALAlADRIAVMNE----GRIVQ 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
384-654 |
1.53e-29 |
|
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: 115.80 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 384 QFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIG 463
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-KDIAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 464 VVSQdpllfsnsiknnikyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyni 543
Cdd:cd00267 77 YVPQ---------------------------------------------------------------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 544 iddsevvnvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
Cdd:cd00267 81 ------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
250 260 270
....*....|....*....|....*....|..
gi 221056887 624 NLKgNENRITIIIAHRLSTI-RYANTIFVLSN 654
Cdd:cd00267 125 ELA-EEGRTVIIVTHDPELAeLAADRVIVLKD 155
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
382-729 |
3.36e-29 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 124.83 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
Cdd:PRK10790 340 RIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL-DGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSNSIKNNIKyslyslkdleylsdqLNEDgsasqdgldkrnscrakcagdlndmmkttdsdgliharkny 541
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVT---------------LGRD----------------------------------------- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 niIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:PRK10790 441 --ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 622 INNLKgnENRITIIIAHRLSTIRYANTIFVLSNREkgnrstvdvdiigedptkdnkenkqkngkkgdtnknekmsnagsy 701
Cdd:PRK10790 519 LAAVR--EHTTLVVIAHRLSTIVEADTILVLHRGQ--------------------------------------------- 551
|
330 340
....*....|....*....|....*...
gi 221056887 702 IIEQGTHDALMKnKNGIYYTMINNQKVS 729
Cdd:PRK10790 552 AVEQGTHQQLLA-AQGRYWQMYQLQLAG 578
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1162-1461 |
8.74e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 126.01 E-value: 8.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1162 GKIEIMDVNFTYmsRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtddvnnekke 1240
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE--------------------- 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1241 qgdeeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIK-FGKE 1319
Cdd:PLN03130 1293 ---------------------------------RGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDpFNEH 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 -DAtreDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:PLN03130 1340 nDA---DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKT 1416
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 1399 IVDikDKADRTIITIAHRIASIKRSDKIVVFNnpdrTGSfVQAEGTHEELLSVQDGVYKKYVK 1461
Cdd:PLN03130 1417 IRE--EFKSCTMLIIAHRLNTIIDCDRILVLD----AGR-VVEFDTPENLLSNEGSAFSKMVQ 1472
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
383-656 |
1.02e-28 |
|
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: 115.28 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINL-KWW 458
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtDISKLSEKELaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 459 RSKIGVVSQDPLLFSN-SIKNNIKYSLYSLKDleylsdqlnedgsasqdgldKRNSCRAKCAGDLNDMmkttdsdGLIHA 537
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGV--------------------PKKERRERAEELLERV-------GLGDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 538 RKNYniiddsevvnvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:cd03255 134 LNHY-----------------------------------PSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKE 178
|
250 260 270
....*....|....*....|....*....|....*....
gi 221056887 618 VQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
Cdd:cd03255 179 VMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
383-654 |
1.08e-28 |
|
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: 116.44 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSK 461
Cdd:COG1124 2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG-RPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPllfsnsiknnikyslyslkdleYLSdqlnedgsasqdgLDKRNScrakcagdlndmMKTTDSDGL-IHARKN 540
Cdd:COG1124 81 VQMVFQDP----------------------YAS-------------LHPRHT------------VDRILAEPLrIHGLPD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiDDSEVVNVSKKV-LIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseYLVQ 619
Cdd:COG1124 114 ----REERIAELLEQVgLPPSFLDRYP-----------HQLSGGQRQRVAIARALILEPELLLLDEPTSALD----VSVQ 174
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 221056887 620 KTINNL----KGNENRITIIIAHRLSTIRY-ANTIFVLSN 654
Cdd:COG1124 175 AEILNLlkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQN 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1164-1450 |
1.17e-28 |
|
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: 122.32 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPN--VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeq 1241
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP----------------------- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1242 gdeeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNL---FSIVSQEPIL-FN--MSIYENIK 1315
Cdd:COG1123 318 -------------------------------TSGSILFDGKDLTKLSRRSLRELrrrVQMVFQDPYSsLNprMTVGDIIA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1316 FG---KEDATREDVKrackfAAIDEFIES--LP----NKYdtnvgPYgkSLSGGQKQRVAIARALLREPKILLLDEATSS 1386
Cdd:COG1123 367 EPlrlHGLLSRAERR-----ERVAELLERvgLPpdlaDRY-----PH--ELSGGQRQRVAIARALALEPKLLILDEPTSA 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1387 LDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAEGTHEELLS 1450
Cdd:COG1123 435 LDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYD----GRIV-EDGPTEEVFA 494
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
382-653 |
1.51e-28 |
|
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: 114.43 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYdtRKDV-EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS 460
Cdd:cd03369 6 EIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPLLFSNSIKNNikyslyslkdleylsdqlnedgsasqdgLDKrnscrakcagdlndmmkttdsdgliharkn 540
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSN----------------------------LDP------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 YNIIDDSEVvnvskkvlihdfvsalpdkYETL-VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:cd03369 105 FDEYSDEEI-------------------YGALrVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
250 260 270
....*....|....*....|....*....|....
gi 221056887 620 KTINNLKGNENriTIIIAHRLSTIRYANTIFVLS 653
Cdd:cd03369 166 KTIREEFTNST--ILTIAHRLRTIIDYDKILVMD 197
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1164-1453 |
1.58e-28 |
|
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: 115.46 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTvmslLMRfydlkndhHIVfknehtddvnnekkeqgd 1243
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSV----LLK--------LII------------------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvGmknvnefsLTKegshgdnsavfKNSGKILLDGVDICDYNLKDLRNL---FSIVSQEPILF-NMSIYENIKFG-- 1317
Cdd:COG1127 53 -----G--------LLR-----------PDSGEILVDGQDITGLSEKELYELrrrIGMLFQGGALFdSLTVFENVAFPlr 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 -----KEDATREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:COG1127 109 ehtdlSEAEIRELVLEKLELVGLPGAADKMPS-----------ELSGGMRKRVALARALALDPEILLYDEPTAGLDPITS 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 1393 KLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAEGTHEELLSVQD 1453
Cdd:COG1127 178 AVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLAD----GK-IIAEGTPEELLASDD 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1164-1453 |
2.04e-28 |
|
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: 114.91 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLI------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnVGMknvnefsLTKEgshgdnsavfknSGKILLDGVDICDYN---LKDLRNLFSIVSQEPILFN-MSIYENIKFGKE 1319
Cdd:cd03261 47 ----VGL-------LRPD------------SGEVLIDGEDISGLSeaeLYRLRRRMGMLFQSGALFDsLTVFENVAFPLR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 DATREDVKRACKFAAidEFIE--SLPNKYDTnvgpYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:cd03261 104 EHTRLSEEEIREIVL--EKLEavGLRGAEDL----YPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDD 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1398 TIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNNpdrtgSFVQAEGTHEELLSVQD 1453
Cdd:cd03261 178 LIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYD-----GKIVAEGTPEELRASDD 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
383-643 |
2.51e-28 |
|
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: 114.95 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlKDINLKWWRSKI 462
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED--VRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSN-SIKNNIKYslyslkdleylsdqlnedgsasqdgldkrnscrakcAGDLNDMMKttdsdglihaRKNY 541
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRY------------------------------------FAELYGLFD----------EELK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 NIIDDsevvnvskkvLIHDFvsALPDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:COG4555 111 KRIEE----------LIELL--GLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREI 174
|
250 260
....*....|....*....|..
gi 221056887 622 INNLKgNENRITIIIAHRLSTI 643
Cdd:COG4555 175 LRALK-KEGKTVLFSSHIMQEV 195
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
386-654 |
3.03e-28 |
|
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: 112.53 E-value: 3.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 386 KNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVV 465
Cdd:cd03214 3 ENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-KDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 466 SQdpllfsnsiknnikyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndMMKTTDSDGLIHarKNYNiid 545
Cdd:cd03214 79 PQ---------------------------------------------------------ALELLGLAHLAD--RPFN--- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 546 dsevvnvskkvlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:cd03214 97 ---------------------------------ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRL 143
|
250 260 270
....*....|....*....|....*....|
gi 221056887 626 KGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:cd03214 144 ARERGKTVVMVLHDLNlAARYADRVILLKD 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1164-1450 |
3.24e-28 |
|
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: 115.61 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPN--VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeq 1241
Cdd:TIGR04520 1 IEVENVSFSY---PEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLL----------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1242 gdeeqnvgmknvnefsltkegshgdnSAVFK-NSGKILLDGVDICD-YNLKDLRNLFSIVSQEP--ILFNMSIYENIKFG 1317
Cdd:TIGR04520 49 --------------------------NGLLLpTSGKVTVDGLDTLDeENLWEIRKKVGMVFQNPdnQFVGATVEDDVAFG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 KE------DATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:TIGR04520 103 LEnlgvprEEMRKRVDEALKLVGMEDFRDREPHL-----------LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKG 171
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1392 EKLIEKTIVDIKDKADRTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAEGTHEELLS 1450
Cdd:TIGR04520 172 RKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNK----GK-IVAEGTPREIFS 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
383-654 |
3.67e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.98 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINL-KWW 458
Cdd:COG1136 5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdiSSLSERELaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 459 RSKIGVVSQDPLLFSN-SIKNNIKYSLYslkdleyLSdqlnedgsasqdGLDKRNscrakcagdlndmmkttdsdgliha 537
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLL-------LA------------GVSRKE------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 538 rknyniiDDSEVVNVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG1136 121 -------RRERARELLERVGLGDRLDHRP-----------SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEE 182
|
250 260 270
....*....|....*....|....*....|....*..
gi 221056887 618 VQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:COG1136 183 VLELLRELNRELGTTIVMVTHDPELAARADRVIRLRD 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
400-654 |
4.18e-28 |
|
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: 120.92 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNN 479
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL-DGADLKQWDRETFGKHIGYLPQDVELFPGTVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 480 IkyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdglihARKNYNIiDDSEVVNVSKKVLIH 559
Cdd:TIGR01842 412 I--------------------------------------------------------ARFGENA-DPEKIIEAAKLAGVH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHR 639
Cdd:TIGR01842 435 ELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHR 513
|
250
....*....|....*
gi 221056887 640 LSTIRYANTIFVLSN 654
Cdd:TIGR01842 514 PSLLGCVDKILVLQD 528
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
383-644 |
6.13e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.22 E-value: 6.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLK---WWR 459
Cdd:COG2884 2 IRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG-QDLSRLKRReipYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlEYLsdqlnedgsasqdGLDKRNscrakcagdlndmmkttdsdglIHAR 538
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALPL------RVT-------------GKSRKE----------------------IRRR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 539 knyniiddseVVNVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDnksEYLV 618
Cdd:COG2884 118 ----------VREVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIARALVNRPELLLADEPTGNLD---PETS 173
|
250 260
....*....|....*....|....*...
gi 221056887 619 QKTINNLKG-NENRITIIIA-HRLSTIR 644
Cdd:COG2884 174 WEIMELLEEiNRRGTTVLIAtHDLELVD 201
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1164-1450 |
7.04e-28 |
|
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: 113.99 E-value: 7.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfknehtddvnnekkeqgd 1243
Cdd:COG1120 2 LEAENLSVGY---GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL--LKPS---------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPIL-FNMSIYENIKFG----- 1317
Cdd:COG1120 55 ------------------------------SGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRELVALGryphl 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 -------KEDatREDVKRACKFAAIDEFIESLpnkYDTnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLD-S 1389
Cdd:COG1120 105 glfgrpsAED--REAVEEALERTGLEHLADRP---VDE--------LSGGERQRVLIARALAQEPPLLLLDEPTSHLDlA 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1390 NSEKLIEkTIVDIKDKADRTII------TIAHRIAsikrsDKIVVFNNpdrtGSfVQAEGTHEELLS 1450
Cdd:COG1120 172 HQLEVLE-LLRRLARERGRTVVmvlhdlNLAARYA-----DRLVLLKD----GR-IVAQGPPEEVLT 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1274-1450 |
9.45e-28 |
|
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: 113.20 E-value: 9.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICdyNLKDLRNLFSIVSQEPILF-NMSIYENIKFGKEDATREDVKRACKFAAIDEF--IESLPNKYDtnv 1350
Cdd:cd03299 53 SGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMlgIDHLLNRKP--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1351 gpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNS-EKLIEKtIVDIKDKADRTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03299 128 ----ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKLREE-LKKIRKEFGVTVLHVTHDFEEAWAlADKVAI 202
|
170 180
....*....|....*....|..
gi 221056887 1429 FNNpdrtGSFVQAeGTHEELLS 1450
Cdd:cd03299 203 MLN----GKLIQV-GKPEEVFK 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1164-1431 |
1.06e-27 |
|
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: 113.41 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekkeqgd 1243
Cdd:COG4555 2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLK-------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYNLKDLRNLFsIVSQEPILF-NMSIYENIKFGKEDAt 1322
Cdd:COG4555 53 ----------------------------PDSGSILIDGEDVRKEPREARRQIG-VLPDERGLYdRLTVRENIRYFAELY- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1323 reDVKRACKFAAIDEFIES--LPNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:COG4555 103 --GLFDEELKKRIEELIELlgLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILR 176
|
250 260 270
....*....|....*....|....*....|..
gi 221056887 1401 DIKDKaDRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:COG4555 177 ALKKE-GKTVLFSSHIMQEVEAlCDRVVILHK 207
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
382-636 |
1.32e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.59 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD--P---TEGDIIINDsHNL--KDIN 454
Cdd:COG1117 11 KIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDG-EDIydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 455 LKWWRSKIGVVSQDPLLFSNSIKNNIkysLYSLKdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgl 534
Cdd:COG1117 87 VVELRRRVGMVFQKPNPFPKSIYDNV---AYGLR---------------------------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 535 IHARKNYNIIDdsEVVNVS-KKVLIHDFVSalpDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG1117 118 LHGIKSKSELD--EIVEESlRKAALWDEVK---DR----LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPI 188
|
250 260
....*....|....*....|...
gi 221056887 614 SEYLVQKTINNLKgneNRITIII 636
Cdd:COG1117 189 STAKIEELILELK---KDYTIVI 208
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
383-654 |
1.55e-27 |
|
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: 113.68 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-----DSHNLKDInlkw 457
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAL-KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgldtlDEENLWEI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 458 wRSKIGVVSQDPllfsnsiknnikyslyslkDleylsDQLNedGSASQD----GLDKRNSCRAKcagdlndmMKTtdsdg 533
Cdd:TIGR04520 76 -RKKVGMVFQNP-------------------D-----NQFV--GATVEDdvafGLENLGVPREE--------MRK----- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 534 liharknynIIDDsevvnVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:TIGR04520 116 ---------RVDE-----ALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPK 170
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 221056887 614 SEYLVQKTINNLKgNENRITII-IAHRLSTIRYANTIFVLSN 654
Cdd:TIGR04520 171 GRKEVLETIRKLN-KEEGITVIsITHDMEEAVLADRVIVMNK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1164-1429 |
1.72e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 112.06 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKST---VMSLLMRFydlkndhhivfknehtddvnnekk 1239
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDRP------------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1240 eqgdeeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDL----RNLFSIVSQEPILF-NMSIYENI 1314
Cdd:COG1136 61 ---------------------------------TSGEVLIDGQDISSLSERELarlrRRHIGFVFQFFNLLpELTALENV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1315 -------KFGKEDAtREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSL 1387
Cdd:COG1136 108 alplllaGVSRKER-RERARELLERVGLGDRLDHRPSQ-----------LSGGQQQRVAIARALVNRPKLILADEPTGNL 175
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 221056887 1388 DSNSEKLIEKTIVDIKDKADRTIITIAH--RIASikRSDKIVVF 1429
Cdd:COG1136 176 DSKTGEEVLELLRELNRELGTTIVMVTHdpELAA--RADRVIRL 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1164-1427 |
1.75e-27 |
|
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: 111.81 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTY-MSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLL--MRFYDlkndhhivfknehtddvnnekke 1240
Cdd:cd03255 1 IELKNLSKTYgGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggLDRPT----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1241 qgdeeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNL----FSIVSQEP-ILFNMSIYENIK 1315
Cdd:cd03255 58 ---------------------------------SGEVRVDGTDISKLSEKELAAFrrrhIGFVFQSFnLLPDLTALENVE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1316 FG------KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDS 1389
Cdd:cd03255 105 LPlllagvPKKERRERAEELLERVGLGDRLNHYPSE-----------LSGGQQQRVAIARALANDPKIILADEPTGNLDS 173
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 221056887 1390 NSEKLIEKTIVDIKDKADRTIITIAH--RIASikRSDKIV 1427
Cdd:cd03255 174 ETGKEVMELLRELNKEAGTTIVVVTHdpELAE--YADRII 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1164-1450 |
1.87e-27 |
|
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: 118.47 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPnVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALM------------------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkeGSHGDNSAVfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPI--LFNMSIYENIKFGKE-- 1319
Cdd:COG1123 54 ------------------GLLPHGGRI---SGEVLLDGRDLLELSEALRGRRIGMVFQDPMtqLNPVTVGDQIAEALEnl 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 ----DATREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:COG1123 113 glsrAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEI 181
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1396 EKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAEGTHEELLS 1450
Cdd:COG1123 182 LDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDD----GRIV-EDGPPEEILA 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
383-654 |
2.40e-27 |
|
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: 110.10 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKwwRSKI 462
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL--SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNSIKNNIkyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyn 542
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL-------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iiddsevvnvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03247 96 ----------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI 141
|
250 260 270
....*....|....*....|....*....|..
gi 221056887 623 nnLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03247 142 --FEVLKDKTLIWITHHLTGIEHMDKILFLEN 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1157-1431 |
2.84e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.78 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1157 TNDIDGKIEIMDVNFTYMSRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnn 1236
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKIL------------------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1237 ekkeqgdeeqnvgmknvnefsltkegshgdnSAVFK-NSGKILLDGVDICDYNLKDLRNLFSIVSQEP--ILFNMSIYEN 1313
Cdd:PRK13632 56 -------------------------------TGLLKpQSGEIKIDGITISKENLKEIRKKIGIIFQNPdnQFIGATVEDD 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1314 IKFGKEDA--TREDVKRACKFAA----IDEFIESLPnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSL 1387
Cdd:PRK13632 105 IAFGLENKkvPPKKMKDIIDDLAkkvgMEDYLDKEP-----------QNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 221056887 1388 DSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSE 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
383-667 |
4.60e-27 |
|
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: 110.64 E-value: 4.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKwwRSK 461
Cdd:cd03293 1 LEVRNVSKTYGGGGGaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGP--GPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFS-NSIKNNIKYslyslkdleylsdqlnedgsasqdGLDKRNSCRAKCAGDLNDMMKTTdsdGLIHARKN 540
Cdd:cd03293 75 RGYVFQQDALLPwLTVLDNVAL------------------------GLELQGVPKAEARERAEELLELV---GLSGFENA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 YniiddsevvnvskkvlihdfvsalPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03293 128 Y------------------------P-----------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQE 172
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 221056887 621 TINNLKgNENRITII-IAHRLS-TIRYANTIFVLSNREKGNRSTVDVDI 667
Cdd:cd03293 173 ELLDIW-RETGKTVLlVTHDIDeAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1165-1431 |
5.33e-27 |
|
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: 108.49 E-value: 5.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1165 EIMDVNFTYMSRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtddvnnekkeqgde 1244
Cdd:cd00267 1 EIENLSFRYGGRTAL---DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL---------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1245 eqnvgmknvnefsltkegshgdnsavFKNSGKILLDGVDICDYNLKDLRNLFSIVSQepilfnmsiyenikfgkedatre 1324
Cdd:cd00267 50 --------------------------KPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1325 dvkrackfaaidefieslpnkydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:cd00267 81 --------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE 128
|
250 260
....*....|....*....|....*...
gi 221056887 1405 KaDRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd00267 129 E-GRTVIIVTHDPELAELaADRVIVLKD 155
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
383-654 |
1.08e-26 |
|
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: 109.53 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI-NLKWWRSK 461
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG----RDVtGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIKYslyslkdleylsdqlnedgsasqdGLDKRNSCRAKCAGDLNDMMKTTDSDGLIHARkn 540
Cdd:cd03259 74 IGMVFQDYALFPHlTVAENIAF------------------------GLKLRGVPKAEIRARVRELLELVGLEGLLNRY-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddsevvnvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03259 128 ------------------------------------PHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELRE 171
|
250 260 270
....*....|....*....|....*....|....*
gi 221056887 621 TINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:cd03259 172 ELKELQRELGITTIYVTHDQEeALALADRIAVMNE 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
383-654 |
1.77e-26 |
|
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: 107.48 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDiNLKWWRSKI 462
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG-KDIKK-EPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNsiknnikyslysLKDLEYLsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyn 542
Cdd:cd03230 76 GYLPEEPSLYEN------------LTVRENL------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iiddsevvnvskkvlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03230 95 ------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELL 138
|
250 260 270
....*....|....*....|....*....|....
gi 221056887 623 NNLKgnENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:cd03230 139 RELK--KEGKTILLSsHILEEAeRLCDRVAILNN 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
383-654 |
1.79e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.47 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
Cdd:PRK13632 8 IKVENVSFSYPNSENNAL-KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-DGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPllfsnsiknnikyslyslkDLEYLsdqlnedGSASQD----GLDKRNSCRAKcagdlndmMKTtdsdglihar 538
Cdd:PRK13632 86 GIIFQNP-------------------DNQFI-------GATVEDdiafGLENKKVPPKK--------MKD---------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 539 knynIIDDsevvnVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:PRK13632 122 ----IIDD-----LAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
250 260 270
....*....|....*....|....*....|....*.
gi 221056887 619 QKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:PRK13632 182 KKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSE 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1164-1450 |
1.95e-26 |
|
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: 109.89 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTY-MSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneHTDDvnnekkeqg 1242
Cdd:COG1124 2 LEVRNLSVSYgQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL--------------ERPW--------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1243 deeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPIL-FN------MSIYENIK 1315
Cdd:COG1124 59 -------------------------------SGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAsLHprhtvdRILAEPLR 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1316 FGKEDATREDVKRACKFAAIDEfieSLPNKYdtnvgPYgkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:COG1124 108 IHGLPDREERIAELLEQVGLPP---SFLDRY-----PH--QLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEI 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1396 EKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAEGTHEELLS 1450
Cdd:COG1124 178 LNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQN----GRIV-EELTVADLLA 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
383-613 |
2.26e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 112.50 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI-NLKWWRSK 461
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVtGLPPEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdleylsdqlnedgsaSQDGLDKRNscRAKCAGDLNDMMkttdsdGLiharkn 540
Cdd:COG3842 79 VGMVFQDYALFPHlTVAENVAFGL-------------------RMRGVPKAE--IRARVAELLELV------GL------ 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 541 yniiddsevvnvskkvlihdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG3842 126 ----------------------EGLADRY-------PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAK 169
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1164-1450 |
2.55e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.00 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLL------------------------------ 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefSLTKegshgdnsavfKNSGKILLDGVDICDyNLKDLRNLFSIVSQEPILF-NMSIYENIKF-----G 1317
Cdd:COG1131 48 -------------GLLR-----------PTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYpDLTVRENLRFfarlyG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 KEDATREdvkrackfAAIDEFIE--SLPNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:COG1131 103 LPRKEAR--------ERIDELLElfGLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARREL 170
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1396 EKTIVDIKDKaDRTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAEGTHEELLS 1450
Cdd:COG1131 171 WELLRELAAE-GKTVLLSTHYLEEAERlCDRVAIIDK----GRIV-ADGTPDELKA 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
383-656 |
2.57e-26 |
|
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: 108.82 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHY-DTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWR 459
Cdd:cd03258 2 IELKNVSKVFgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQDPLLFSN-SIKNNIKYSLyslkdleylsdQLnedgsasqDGLDKRNscRAKCAGDLNDMMkttdsdGLIHAR 538
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPL-----------EI--------AGVPKAE--IEERVLELLELV------GLEDKA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 539 KNYniiddsevvnvskkvlihdfvsalPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS---- 614
Cdd:cd03258 135 DAY------------------------P-----------AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsi 179
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 221056887 615 -EYLvqKTINnlkgNENRITI-IIAHRLSTIR-YANTIFVLSNRE 656
Cdd:cd03258 180 lALL--RDIN----RELGLTIvLITHEMEVVKrICDRVAVMEKGE 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
383-654 |
8.43e-26 |
|
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: 108.21 E-value: 8.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKI 462
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-RDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLL-FSNSIKNNIKYSLYS-LKDLEYLSDqlnEDgsasqdgldkrnscRAKCAgdlnDMMKTTDSDGLihARKN 540
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGRYPhLGLFGRPSA---ED--------------REAVE----EALERTGLEHL--ADRP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 YNiiddsevvnvskkvlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:COG1120 135 VD------------------------------------ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLE 178
|
250 260 270
....*....|....*....|....*....|....*
gi 221056887 621 TINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:COG1120 179 LLRRLARERGRTVVMVLHDLNlAARYADRLVLLKD 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
383-654 |
1.02e-25 |
|
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: 106.40 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEIY--KDLNFTLTEGKTYAFVGESGCGKSTILKLI--ErlYDPTEGDIIINDShnlkdinlkww 458
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 459 rskIGVVSQDPLLFSNSIKNNIkyslysLKDLEYLSDQLNEDGSASQdgLDKrnscrakcagDLndmmkttdsdglihar 538
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENI------LFGKPFDEERYEKVIKACA--LEP----------DL---------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 539 knyniiddsevvnvskkvlihdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYL 617
Cdd:cd03250 111 ------------------------EILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHI 166
|
250 260 270
....*....|....*....|....*....|....*..
gi 221056887 618 VQKTINNLkGNENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03250 167 FENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
382-667 |
1.09e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 107.87 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKwwRS 460
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGP--GP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPLLFS-NSIKNNIKYSLyslkdleylsdqlnedgsaSQDGLDKRnSCRAKcAGDLNDMMkttdsdGLihark 539
Cdd:COG1116 81 DRGVVFQEPALLPwLTVLDNVALGL-------------------ELRGVPKA-ERRER-ARELLELV------GL----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 nyniiddsevvnvskkvliHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG1116 129 -------------------AGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQ 178
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 221056887 620 KTINNLKGNENRITIIIAH------RLstiryANTIFVLSNREKGNRSTVDVDI 667
Cdd:COG1116 179 DELLRLWQETGKTVLFVTHdvdeavFL-----ADRVVVLSARPGRIVEEIDVDL 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1164-1450 |
2.10e-25 |
|
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: 106.13 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTvmslLMRFYDLKndhhivfknehtddvnnekkEQG 1242
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCINGL--------------------ERP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1243 DeeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNL---FSIVSQEPILFN-MSIYENIKFGK 1318
Cdd:cd03258 58 T------------------------------SGSVLVDGTDLTLLSGKELRKArrrIGMIFQHFNLLSsRTVFENVALPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1319 EDATREDVKRACKfaaIDEFIE--SLPNKYDTnvgpYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:cd03258 108 EIAGVPKAEIEER---VLELLElvGLEDKADA----YPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSIL 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1397 KTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQaEGTHEELLS 1450
Cdd:cd03258 181 ALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEK----GEVVE-EGTVEEVFA 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
403-645 |
2.69e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 108.67 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQDPllFSnsiknni 480
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqDITGLSGRELRPLRRRMQMVFQDP--YA------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 481 kySL---YSLKDLeyLSDQLNEDGSASQDGLDKRnscrakcagdLNDMMKTTdsdGL--IHARKNyniiddsevvnvskk 555
Cdd:COG4608 107 --SLnprMTVGDI--IAEPLRIHGLASKAERRER----------VAELLELV---GLrpEHADRY--------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 556 vlIHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDnKSeylVQKTINNLKG---NENRI 632
Cdd:COG4608 155 --PHEF-------------------SGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQAQVLNLLEdlqDELGL 209
|
250
....*....|....
gi 221056887 633 T-IIIAHRLSTIRY 645
Cdd:COG4608 210 TyLFISHDLSVVRH 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
391-654 |
3.57e-25 |
|
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: 104.65 E-value: 3.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 391 HYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWRSKIGVVSQDP- 469
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERRKSIGYVMQDVd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 470 -LLFSNSIKNNIkysLYSLKDLeylsdqlnedgsasqdgldkrnscrAKCAGDLNDMMKTTDsdgliharknyniiddse 548
Cdd:cd03226 82 yQLFTDSVREEL---LLGLKEL-------------------------DAGNEQAETVLKDLD------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 549 vvnvskkvlIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGn 628
Cdd:cd03226 116 ---------LYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA- 174
|
250 260
....*....|....*....|....*..
gi 221056887 629 ENRITIIIAHRLSTI-RYANTIFVLSN 654
Cdd:cd03226 175 QGKAVIVITHDYEFLaKVCDRVLLLAN 201
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1165-1431 |
3.80e-25 |
|
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: 104.92 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1165 EIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfknehtddvnnekkeqgde 1244
Cdd:cd03235 1 EVEDLTVSY---GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGL--LKPT----------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1245 eqnvgmknvnefsltkegshgdnsavfknSGKILLDGvdicdYNLKDLRNLFSIVSQEPIL---FNMSIYENI------- 1314
Cdd:cd03235 53 -----------------------------SGSIRVFG-----KPLEKERKRIGYVPQRRSIdrdFPISVRDVVlmglygh 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1315 -----KFGKEDatREDVKRACKFAAIDEFIeslpnkyDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDS 1389
Cdd:cd03235 99 kglfrRLSKAD--KAKVDEALERVGLSELA-------DRQIG----ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 221056887 1390 NSEKLIEKTIVDIKDKaDRTIITIAHRI-ASIKRSDKIVVFNN 1431
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLgLVLEYFDRVLLLNR 207
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
383-613 |
4.80e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 108.24 E-value: 4.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN-LKWWRSK 461
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTdLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIkysLYSLKdleylsdqlnedgsasqdgldkrnscrakcagdlndMMKTTDSDglIHARkn 540
Cdd:COG3839 77 IAMVFQSYALYPHmTVYENI---AFPLK------------------------------------LRKVPKAE--IDRR-- 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 541 yniiddseVVNVSKKVLIHDFVsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG3839 114 --------VREAAELLGLEDLL----DRK-------PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1165-1431 |
5.36e-25 |
|
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: 103.28 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1165 EIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfknehtddvnnekkeqgde 1244
Cdd:cd03214 1 EVENLSVGY---GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL--LKPS----------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1245 eqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQepilfnmsiyenikfgkedatre 1324
Cdd:cd03214 53 -----------------------------SGEILLDGKDLASLSPKELARKIAYVPQ----------------------- 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1325 dvkrACKFAAIDEFIESLpnkYDTnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:cd03214 81 ----ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLAR 145
|
250 260
....*....|....*....|....*...
gi 221056887 1405 KADRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03214 146 ERGKTVVMVLHDLNLAARyADRVILLKD 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
383-652 |
9.54e-25 |
|
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: 110.38 E-value: 9.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT---EGDIIINDsHNLKDINLKWWR 459
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDG-RDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQDPLLFSNSIKnnikyslyslkdleyLSDQLNEdgsasqdGLDKRNSCRAKcagdlndmmkttdsdglIHARk 539
Cdd:COG1123 83 RRIGMVFQDPMTQLNPVT---------------VGDQIAE-------ALENLGLSRAE-----------------ARAR- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 nyniiddseVVNVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG1123 123 ---------VLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEIL 182
|
250 260 270
....*....|....*....|....*....|....
gi 221056887 620 KTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:COG1123 183 DLLRELQRERGTTVLLITHDLGVVaEIADRVVVM 216
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1273-1448 |
1.31e-24 |
|
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: 103.86 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 NSGKILLDGVDIcdYNLKDLRNLFSIVSQEPILF-NMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPNK 1345
Cdd:cd03300 53 TSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1346 ydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADR---TIITIAH-RIASIK 1421
Cdd:cd03300 131 -----------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDL---KLRKDMQLELKRLQKElgiTFVFVTHdQEEALT 196
|
170 180
....*....|....*....|....*..
gi 221056887 1422 RSDKIVVFNNpdrtGSFVQAeGTHEEL 1448
Cdd:cd03300 197 MSDRIAVMNK----GKIQQI-GTPEEI 218
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
64-361 |
2.69e-24 |
|
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: 105.44 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 64 VSFVCATISGGSLPFFVSVFG--------VIMKNMN---------------LGENVDDIIFSLVLIGIFQFVMSFISSFC 120
Cdd:cd18558 3 VGILCAIIHGGLLPAFMVIFGdmtdsftnGGMTNITgnssglnssagpfekLEEEMTLYAYYYLIIGAIVLITAYIQGSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 121 MDIVTTKILKTLKVEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLT 200
Cdd:cd18558 83 WGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 201 LCVTCVFPLIYICGVICNKKAKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEHTILKKFNLSEKLYSKYMLKANFME 280
Cdd:cd18558 163 LVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 281 SLHIGMINGFILASYAFGFWYGTRIIISdlsnaqsnNDFHGGSVISILLGVLISMFMLTIVLPNITEYMKsleATNSLYE 360
Cdd:cd18558 243 NISMGAAFLLIYASYALAFWYGTYLVTQ--------QEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFAN---ARGAAYH 311
|
.
gi 221056887 361 I 361
Cdd:cd18558 312 I 312
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1164-1432 |
2.90e-24 |
|
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: 102.55 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSR-PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtddvnnekkEQG 1242
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGL------------------------ERP 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1243 DeeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKdlrnlFSIVSQEPILFN-MSIYENIKFG---- 1317
Cdd:cd03293 57 T------------------------------SGEVLVDGEPVTGPGPD-----RGYVFQQDALLPwLTVLDNVALGlelq 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 --KEDATREDVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:cd03293 102 gvPKAEARERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQL 170
|
250 260 270
....*....|....*....|....*....|....*...
gi 221056887 1396 EKTIVDIKDKADRTIITIAHRIA-SIKRSDKIVVFNNP 1432
Cdd:cd03293 171 QEELLDIWRETGKTVLLVTHDIDeAVFLADRVVVLSAR 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
384-655 |
3.17e-24 |
|
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: 102.23 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 384 QFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinlkwwRSKIG 463
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 464 VVSQDPLL---FSNSIKNNIKYSLYSLKdleylsdqlnedgsasqdGLDKRNSCRAKCAGDlnDMMKTTDSDGLIHARkn 540
Cdd:cd03235 72 YVPQRRSIdrdFPISVRDVVLMGLYGHK------------------GLFRRLSKADKAKVD--EALERVGLSELADRQ-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddsevvnvskkvlIhdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03235 130 -----------------I-------------------GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYE 173
|
250 260 270
....*....|....*....|....*....|....*.
gi 221056887 621 TINNLKGnENRITIIIAHRLSTI-RYANTIFVLSNR 655
Cdd:cd03235 174 LLRELRR-EGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1164-1450 |
8.03e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 102.09 E-value: 8.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfknehtddvnnekkeqgd 1243
Cdd:COG1121 7 IELENLTVSY---GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGL--LPPT---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDIcdynlKDLRNLFSIVSQE-------PI----LFNMSIYE 1312
Cdd:COG1121 60 ------------------------------SGTVRLFGKPP-----RRARRRIGYVPQRaevdwdfPItvrdVVLMGRYG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1313 NIKF----GKEDatREDVKRACKFAAIDEFIeslpnkyDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:COG1121 105 RRGLfrrpSRAD--REAVDEALERVGLEDLA-------DRPIG----ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 1389 SNSEKLIEKTIVDIKdKADRTIITIAHRIASIKR-SDKIVVFNnpdRTgsfVQAEGTHEELLS 1450
Cdd:COG1121 172 AATEEALYELLRELR-REGKTILVVTHDLGAVREyFDRVLLLN---RG---LVAHGPPEEVLT 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
383-654 |
8.48e-24 |
|
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: 101.88 E-value: 8.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINLKWWRS 460
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdiNKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDpllfsnsiknnikyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharkn 540
Cdd:cd03256 79 QIGMIFQQ------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 YNIIDDSEVV-NV-SKKVLIHDFVSALP------DKYETL-----VG------SNASKLSGGQKQRISIARAIIRNPKIL 601
Cdd:cd03256 87 FNLIERLSVLeNVlSGRLGRRSTWRSLFglfpkeEKQRALaalerVGlldkayQRADQLSGGQQQRVAIARALMQQPKLI 166
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 602 ILDEATSSLDNKS-----EYLvqKTINNLKGnenrITIIIA-HRLSTIR-YANTIFVLSN 654
Cdd:cd03256 167 LADEPVASLDPASsrqvmDLL--KRINREEG----ITVIVSlHQVDLAReYADRIVGLKD 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
383-611 |
9.17e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.39 E-value: 9.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWR 459
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQDP-LLFSNSIKNNIKYSLYslkdleylsdqlnedgsasQDGLDKRNscRAKCAGDLNDMMkttdsdGLIHAR 538
Cdd:COG1135 82 RKIGMIFQHFnLLSSRTVAENVALPLE-------------------IAGVPKAE--IRKRVAELLELV------GLSDKA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 539 KNYniiddsevvnvskkvlihdfvsalPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG1135 135 DAY------------------------P-----------SQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
383-655 |
9.63e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 101.70 E-value: 9.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinlkwwRSKI 462
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQdpllfsnsiKNNIKYSLY-SLKDLEYLsdqlnedGSASQDGLDKRNScrakcagdlndmmkttdsdglihaRKNY 541
Cdd:COG1121 78 GYVPQ---------RAEVDWDFPiTVRDVVLM-------GRYGRRGLFRRPS------------------------RADR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 NIIDDS-EVVNVS--KKVLIhdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:COG1121 118 EAVDEAlERVGLEdlADRPI-------------------GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEAL 178
|
250 260 270
....*....|....*....|....*....|....*....
gi 221056887 619 QKTINNLkgNENRITIIIA-HRLSTIR-YANTIFVLSNR 655
Cdd:COG1121 179 YELLREL--RREGKTILVVtHDLGAVReYFDRVLLLNRG 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1274-1448 |
1.03e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 104.41 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDIcdynlKDL----RNlFSIVSQEPILF-NMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESL 1342
Cdd:COG3842 59 SGRILLDGRDV-----TGLppekRN-VGMVFQDYALFpHLTVAENVAFGlrmrgvPKAEIRARVAELLELVGLEGLADRY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1343 PNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKD---KADRTIITIAH---- 1415
Cdd:COG3842 133 PHQ-----------LSGGQQQRVALARALAPEPRVLLLDEPLSALDA---KLREEMREELRRlqrELGITFIYVTHdqee 198
|
170 180 190
....*....|....*....|....*....|....*
gi 221056887 1416 --RIasikrSDKIVVFNNpdrtGSFVQAeGTHEEL 1448
Cdd:COG3842 199 alAL-----ADRIAVMND----GRIEQV-GTPEEI 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
383-652 |
1.08e-23 |
|
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: 103.59 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDIIIN--DSHNLKDINLK 456
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgeDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 457 WWRSK-IGVVSQDPLlfsnsiknnikyslyslkdleylsdqlnedgsASqdgldkrnscrakcagdLNDMMKTTDSdgLI 535
Cdd:COG0444 82 KIRGReIQMIFQDPM--------------------------------TS-----------------LNPVMTVGDQ--IA 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 536 HARKNYNIIDDSE----VVNVSKKVLIHDFVSALpDKY--EtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSS 609
Cdd:COG0444 111 EPLRIHGGLSKAEarerAIELLERVGLPDPERRL-DRYphE---------LSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 221056887 610 LDnkseYLVQKTI----NNLKgNENRITII-IAHRLSTIRY-ANTIFVL 652
Cdd:COG0444 181 LD----VTIQAQIlnllKDLQ-RELGLAILfITHDLGVVAEiADRVAVM 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
399-1431 |
1.56e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 109.10 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlkdinlkWWRSKIGVVSQDPLLFSNSIKN 478
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 479 NIKYslyslkdleylsdqlnedgsasqdgLDKRNscrakcAGDLNDmmkttdsdgliharknyniiddseVVNVSKkvLI 558
Cdd:PTZ00243 740 NILF-------------------------FDEED------AARLAD------------------------AVRVSQ--LE 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 559 HDfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTI-NNLKGnenRITIII 636
Cdd:PTZ00243 763 AD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDaHVGERVVEECFlGALAG---KTRVLA 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 637 AHRLSTIRYANTIFVLsnrekgnrstvdvdiigedptkdnkenkqkngkkgdtnKNEKMSNAGSYI------IEQGTHDA 710
Cdd:PTZ00243 839 THQVHVVPRADYVVAL--------------------------------------GDGRVEFSGSSAdfmrtsLYATLAAE 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 711 LMKNKNGiyytminnqkvssktsnnndndkdsdmkssvykdSERGYDPDEMNGNTKNGNESASDKKSNKmSDENASSKNA 790
Cdd:PTZ00243 881 LKENKDS----------------------------------KEGDADAEVAEVDAAPGGAVDHEPPVAK-QEGNAEGGDG 925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 791 GGKLSFLRNLFKRKPKAPNNLRM-VYREIFSYkkdvviialsiivAGGLYPMFALLYAKYVSTLFDFAN----------- 858
Cdd:PTZ00243 926 AALDAAAGRLMTREEKASGSVPWsTYVAYLRF-------------CGGLHAAGFVLATFAVTELVTVSSgvwlsmwstrs 992
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 859 LEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLFENILYQEISFFDQdchAP-GLLSSHINRDVHLLK 937
Cdd:PTZ00243 993 FKLSAATYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDT---TPlGRILNRFSRDIDILD 1069
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 938 TGLVNNIVIFTHFIVLFIVSMIMSFYFCPIVAAVLTGTYFIFMRVFAIRArlSANKDVEKKGinqpgtvflynnddEIFK 1017
Cdd:PTZ00243 1070 NTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYN--SANREIRRIK--------------SVAK 1133
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1018 DPSF-LIQEAFYNMNTVIIYGLED-------------YFCKLIEKAidySNK--GQKRKTLVN-------------SMLW 1068
Cdd:PTZ00243 1134 SPVFtLLEEALQGSATITAYGKAHlvmqealrrldvvYSCSYLENV---ANRwlGVRVEFLSNivvtvialigvigTMLR 1210
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1069 GFSQSAQLFINSFAY---------WfgsfLIRR-GTIEVDdfMKSLFTFLFTGSYAGKLMSLKGDSENAKLSfekyypli 1138
Cdd:PTZ00243 1211 ATSQEIGLVSLSLTMamqttatlnW----LVRQvATVEAD--MNSVERLLYYTDEVPHEDMPELDEEVDALE-------- 1276
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1139 mRKSNIDVRDNGGIRIKNT--------NDIDGKIEIMDVNFTYmsRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVM 1209
Cdd:PTZ00243 1277 -RRTGMAADVTGTVVIEPAsptsaaphPVQAGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLL 1353
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1210 SLLMRFYDLkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNL 1289
Cdd:PTZ00243 1354 LTFMRMVEV------------------------------------------------------CGGEIRVNGREIGAYGL 1379
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1290 KDLRNLFSIVSQEPILFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIAR 1369
Cdd:PTZ00243 1380 RELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMAR 1458
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 1370 ALL-REPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:PTZ00243 1459 ALLkKGSGFILMDEATANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQYDKIIVMDH 1519
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1164-1449 |
1.96e-23 |
|
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: 100.84 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPnvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTddvnnekkeqgd 1243
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI------------EPT------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPILF-NMSIYENI----KFGK 1318
Cdd:cd03295 55 ------------------------------SGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFpHMTVEENIalvpKLLK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1319 EDATREDvKRAckfaaiDEFIESL---PNKYdtnVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:cd03295 105 WPKEKIR-ERA------DELLALVgldPAEF---ADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQL 174
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1396 EKTIVDIKDKADRTIITIAHRI-ASIKRSDKIVVFNNpdrtGSFVQaEGTHEELL 1449
Cdd:cd03295 175 QEEFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKN----GEIVQ-VGTPDEIL 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1164-1431 |
2.10e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.05 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMsrPNVPIYK----DLTFSCDSKKTTAIVGETGSGKSTVMsllmrfydlkndHHIvfknehtddvnnekk 1239
Cdd:PRK13637 3 IKIENLTHIYM--EGTPFEKkaldNVNIEIEDGEFVGLIGHTGSGKSTLI------------QHL--------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1240 eqgdeeqnvgmknvnefsltkegshgdNSAVFKNSGKILLDGVDICD--YNLKDLRNLFSIVSQEP--ILFNMSIYENIK 1315
Cdd:PRK13637 54 ---------------------------NGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEETIEKDIA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1316 FG------KEDATREDVKRACKFAAIDefIESLPNKydtnvGPYgkSLSGGQKQRVAIARALLREPKILLLDEATSSLDS 1389
Cdd:PRK13637 107 FGpinlglSEEEIENRVKRAMNIVGLD--YEDYKDK-----SPF--ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 221056887 1390 NSEKLIEKTIVDIKDKADRTIITIAHRIASI-KRSDKIVVFNN 1431
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNK 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1274-1431 |
3.27e-23 |
|
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: 99.25 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDlRNLfSIVSQEPILF-NMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPnky 1346
Cdd:cd03301 54 SGRIYIGGRDVTDLPPKD-RDI-AMVFQNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKP--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1347 dtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSnseKLIEKT---IVDIKDKADRTIITIAH-RIASIKR 1422
Cdd:cd03301 129 --------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA---KLRVQMraeLKRLQQRLGTTTIYVTHdQVEAMTM 197
|
....*....
gi 221056887 1423 SDKIVVFNN 1431
Cdd:cd03301 198 ADRIAVMND 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
383-611 |
3.40e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 100.07 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH-NLKDINLKWWRSK 461
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDlTDSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIkyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndMMkttdsdGLIHARKn 540
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENV--------------------------------------------TL------APIKVKK- 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 541 yniIDDSEVVNVSKKVL----IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG1126 108 ---MSKAEAEERAMELLervgLADKADAYP-----------AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1183-1442 |
3.44e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.62 E-value: 3.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1183 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgdeeqnvgmknVNEFSLTkeg 1262
Cdd:PRK14239 22 NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDL----------------------------------NPEVTIT--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1263 shgdnsavfknsGKILLDGVDIcdYNLK----DLRNLFSIVSQEPILFNMSIYENIKFG------KEDAT-REDVKRACK 1331
Cdd:PRK14239 65 ------------GSIVYNGHNI--YSPRtdtvDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVlDEAVEKSLK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1332 FAAI-DEFIESLpnkYDTNVGpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDRTI 1410
Cdd:PRK14239 131 GASIwDEVKDRL---HDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTM 200
|
250 260 270
....*....|....*....|....*....|..
gi 221056887 1411 ITIAHriaSIKRSDKIvvfnnPDRTGSFVQAE 1442
Cdd:PRK14239 201 LLVTR---SMQQASRI-----SDRTGFFLDGD 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
383-611 |
4.94e-23 |
|
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: 98.76 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDINLkwWR 459
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlklTDDKKNINE--LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQDPLLFSN-SIKNNIKYslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdGLIHAR 538
Cdd:cd03262 76 QKVGMVFQQFNLFPHlTVLENITL--------------------------------------------------APIKVK 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 539 KnyniIDDSEVVNVS----KKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:cd03262 106 G----MSKAEAEERAlellEKVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
398-652 |
1.21e-22 |
|
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: 97.75 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 398 VEIYKDL-NFTL-----TEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS---HNLKDINLKWWRSKIGVVSQD 468
Cdd:cd03297 4 VDIEKRLpDFTLkidfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKKINLPPQQRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 469 PLLFSN-SIKNNIkysLYSLKDLEYLSDQLNEDgsasqdgldkrnscrakcagdlndmmKTTDSDGLIHarknyniidds 547
Cdd:cd03297 84 YALFPHlNVRENL---AFGLKRKRNREDRISVD--------------------------ELLDLLGLDH----------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 548 evvnvskkvlihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
Cdd:cd03297 124 ------------------------LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
250 260
....*....|....*....|....*.
gi 221056887 628 NENRITIIIAHRLSTIRY-ANTIFVL 652
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYlADRIVVM 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1163-1450 |
1.38e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.32 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1163 KIEIMDVNFTY--MSRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekke 1240
Cdd:PRK13635 5 IIRVEHISFRYpdAATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLL---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1241 qgdeeqnvgmknvnefsltkegshgdNSAVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--ILFNMSIYENIKFGK 1318
Cdd:PRK13635 54 --------------------------NGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdnQFVGATVQDDVAFGL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1319 E------DATREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:PRK13635 108 EnigvprEEMVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 1393 KLIEKTIVDIKDKADRTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAEGTHEELLS 1450
Cdd:PRK13635 177 REVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGE-----ILEEGTPEEIFK 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1274-1449 |
2.86e-22 |
|
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: 98.10 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNL----FSIVSQEPILF-NMSIYENIKFGKE-----DATREDV-KRACKFAAIDEFIESL 1342
Cdd:cd03294 78 SGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENVAFGLEvqgvpRAEREERaAEALELVGLEGWEHKY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1343 PNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIA-SIK 1421
Cdd:cd03294 158 PDE-----------LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDeALR 226
|
170 180
....*....|....*....|....*...
gi 221056887 1422 RSDKIVVFnnpdRTGSFVQAeGTHEELL 1449
Cdd:cd03294 227 LGDRIAIM----KDGRLVQV-GTPEEIL 249
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
383-638 |
3.88e-22 |
|
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: 96.17 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN-LKWWRSK 461
Cdd:cd03301 1 VELENVTKRFGNVTAL---DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG----RDVTdLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKdleylsdqlnedgsASQDGLDKRnscrakcagdlndmmkttdsdgliharkn 540
Cdd:cd03301 74 IAMVFQNYALYPHmTVYDNIAFGLKLRK--------------VPKDEIDER----------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddseVVNVSKKVLIhdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03301 111 --------VREVAELLQI----EHLLDRK-------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRA 171
|
250
....*....|....*...
gi 221056887 621 TINNLKGNENRITIIIAH 638
Cdd:cd03301 172 ELKRLQQRLGTTTIYVTH 189
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1161-1431 |
4.38e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1161 DGKIEIMDVNFTYMSRPnVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekke 1240
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLI---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1241 qgdeeqnvgmknvNEFSLTKEgshgdnsavfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--ILFNMSIYENIKFGK 1318
Cdd:PRK13640 54 -------------NGLLLPDD----------NPNSKITVDGITLTAKTVWDIREKVGIVFQNPdnQFVGATVGDDVAFGL 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1319 ED--ATREDVKRACKFAAID----EFIESLPnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:PRK13640 111 ENraVPRPEMIKIVRDVLADvgmlDYIDSEP-----------ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
250 260 270
....*....|....*....|....*....|....*....
gi 221056887 1393 KLIEKTIVDIKDKADRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDD 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1164-1450 |
4.49e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 4.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLI------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdNSAVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--ILFNMSIYENIKFGKE-- 1319
Cdd:PRK13650 54 -----------------------DGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEDDVAFGLEnk 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 ----DATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK13650 111 giphEEMKERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1396 EKTIVDIKDKADRTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAEGTHEELLS 1450
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQ-----VESTSTPRELFS 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1184-1428 |
5.33e-22 |
|
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: 98.59 E-value: 5.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1184 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfKNEHTddvnnekkeqgdeeqnvgmknvnefsltkegs 1263
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLP---------PPGIT-------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1264 hgdnsavfknSGKILLDGVDICDYNLKDLRNL----FSIVSQEPIL-FN--MSIYENIkfgkEDATR--EDVKRAckfAA 1334
Cdd:COG0444 62 ----------SGEILFDGEDLLKLSEKELRKIrgreIQMIFQDPMTsLNpvMTVGDQI----AEPLRihGGLSKA---EA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1335 IDEFIESLpnkydTNVG-PYGKS--------LSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1405
Cdd:COG0444 125 RERAIELL-----ERVGlPDPERrldrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRE 199
|
250 260
....*....|....*....|....
gi 221056887 1406 ADRTIITIAHRIASIKR-SDKIVV 1428
Cdd:COG0444 200 LGLAILFITHDLGVVAEiADRVAV 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
383-662 |
6.26e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.49 E-value: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII-DGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPllfsnsiknnikyslyslkDLEYLSDQLnEDGSASqdGLDKRNScrakcagDLNDMMKTTDsdgliharknyn 542
Cdd:PRK13650 84 GMVFQNP-------------------DNQFVGATV-EDDVAF--GLENKGI-------PHEEMKERVN------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iiddsEVVNVskkVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK13650 123 -----EALEL---VGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTI 183
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 221056887 623 NNLKgNENRITII-IAHRLSTIRYANTIFVLSNREKGNRST 662
Cdd:PRK13650 184 KGIR-DDYQMTVIsITHDLDEVALSDRVLVMKNGQVESTST 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1164-1431 |
6.49e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.07 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfYDLkndhhivfknehtddvnnekkEQGD 1243
Cdd:COG1118 3 IEVRNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII---AGL---------------------ETPD 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDIcDYNL--KDlRNL-FsiVSQEPILF-NMSIYENIKFG-- 1317
Cdd:COG1118 56 ------------------------------SGRIVLNGRDL-FTNLppRE-RRVgF--VFQHYALFpHMTVAENIAFGlr 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 ----KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:COG1118 102 vrppSKAEIRARVEELLELVQLEGLADRYPSQ-----------LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRK 170
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 221056887 1394 LIEKTIVDIKDKADRTIITIAH------RIAsikrsDKIVVFNN 1431
Cdd:COG1118 171 ELRRWLRRLHDELGGTTVFVTHdqeealELA-----DRVVVMNQ 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1164-1431 |
7.29e-22 |
|
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: 94.00 E-value: 7.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfknehtddvnnekkeqgd 1243
Cdd:cd03230 1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL--LKPD---------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDyNLKDLRNLFSIVSQEPILF-NMSIYENIKfgkedat 1322
Cdd:cd03230 54 ------------------------------SGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYeNLTVRENLK------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1323 redvkrackfaaidefieslpnkydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:cd03230 96 ----------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL 141
|
250 260 270
....*....|....*....|....*....|
gi 221056887 1403 KDKaDRTIITIAHRIASI-KRSDKIVVFNN 1431
Cdd:cd03230 142 KKE-GKTILLSSHILEEAeRLCDRVAILNN 170
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
381-662 |
1.26e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 96.62 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 381 KKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN----DSHNLKDInlk 456
Cdd:PRK13635 4 EIIRVEHISFRYPDAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlSEETVWDV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 457 wwRSKIGVVSQDPllfsnsiknnikyslyslkdleylsdqlnedgsasqdgldkrnscrakcagDlNDMMKTTDSDGLIH 536
Cdd:PRK13635 80 --RRQVGMVFQNP---------------------------------------------------D-NQFVGATVQDDVAF 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 537 ARKNYNIIDDSEVVNVS---KKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK13635 106 GLENIGVPREEMVERVDqalRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 221056887 614 SEYLVQKTINNLKgNENRITII-IAHRLSTIRYANTIFVLSNREKGNRST 662
Cdd:PRK13635 175 GRREVLETVRQLK-EQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1274-1448 |
1.60e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 97.84 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDlRNLfSIVSQEPILF-NMSIYENIKFG----KEDatREDVKRACKFAA----IDEFIESLPn 1344
Cdd:COG3839 57 SGEILIGGRDVTDLPPKD-RNI-AMVFQSYALYpHMTVYENIAFPlklrKVP--KAEIDRRVREAAellgLEDLLDRKP- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1345 kydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKD---KADRTII---------- 1411
Cdd:COG3839 132 ----------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA---KLRVEMRAEIKRlhrRLGTTTIyvthdqveam 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 221056887 1412 TIAhriasikrsDKIVVFNNpdrtGSFVQAeGTHEEL 1448
Cdd:COG3839 199 TLA---------DRIAVMND----GRIQQV-GTPEEL 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
383-636 |
2.17e-21 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 95.12 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRS 460
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDgqDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPLLFSNS--IKN----NIKY--------SLYSLKD----LEYLsDQLnedgsasqdGLDKRnscrakcagdl 522
Cdd:COG3638 81 RIGMIFQQFNLVPRLsvLTNvlagRLGRtstwrsllGLFPPEDreraLEAL-ERV---------GLADK----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 523 ndmmkttdsdglIHARknyniiddsevvnvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILI 602
Cdd:COG3638 140 ------------AYQR--------------------------------------ADQLSGGQQQRVAIARALVQEPKLIL 169
|
250 260 270
....*....|....*....|....*....|....*....
gi 221056887 603 LDEATSSLDNKS-----EYLvqKTINnlkgNENRITIII 636
Cdd:COG3638 170 ADEPVASLDPKTarqvmDLL--RRIA----REDGITVVV 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
385-619 |
2.47e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 385 FKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlKDInlkwwrsKIGV 464
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----KGL-------RIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 465 VSQDPLLFSN-SIKNNIKYSLYSLKDLEYLSDQLNEDGSASQDGLDKrnscrakcAGDLNDMMktTDSDGliharknYNI 543
Cdd:COG0488 66 LPQEPPLDDDlTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLER--------LAELQEEF--EALGG-------WEA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 544 idDSEVvnvsKKVLihdfvSAL---PDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-----E 615
Cdd:COG0488 129 --EARA----EEIL-----SGLgfpEEDLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleE 193
|
....
gi 221056887 616 YLVQ 619
Cdd:COG0488 194 FLKN 197
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1161-1434 |
2.87e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 95.16 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1161 DGKIEIMDVNFTYMSRPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtddvnnekk 1239
Cdd:COG1116 5 APALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL------------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1240 EQGDeeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDIcdynlKDLRNLFSIVSQEPILFN-MSIYENIKFG- 1317
Cdd:COG1116 61 EKPT------------------------------SGEVLVDGKPV-----TGPGPDRGVVFQEPALLPwLTVLDNVALGl 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 --KEDATREDVKRACKFAAI---DEFIESLPnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:COG1116 106 elRGVPKAERRERARELLELvglAGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTR 174
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 221056887 1393 KLIEKTIVDIKDKADRTIITIAHRIA-SIKRSDKIVVF-NNPDR 1434
Cdd:COG1116 175 ERLQDELLRLWQETGKTVLFVTHDVDeAVFLADRVVVLsARPGR 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
383-637 |
3.73e-21 |
|
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: 93.63 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRS 460
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqDVSDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPLLFSN-SIKNNIKYSLyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdglihark 539
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFAL------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 nyniiddsEVVNVSKKvLIHDFVSA------LPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03292 104 --------EVTGVPPR-EIRKRVPAalelvgLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
250 260
....*....|....*....|....
gi 221056887 614 SEYLVQKTINnlKGNENRITIIIA 637
Cdd:cd03292 171 TTWEIMNLLK--KINKAGTTVVVA 192
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1164-1455 |
6.30e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.43 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLM------------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnVGMKNVNEfsltkegshgdnsavfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPI-LFNMSIYE-NIKFGKE-- 1319
Cdd:PRK13648 56 ----IGIEKVKS-------------------GEIFYNNQAITDDNFEKLRKHIGIVFQNPDnQFVGSIVKyDVAFGLEnh 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 ----DATREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK13648 113 avpyDEMHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1396 EKTIVDIKDKADRTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAEGTHEELLSVQDGV 1455
Cdd:PRK13648 182 LDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGT-----VYKEGTPTEIFDHAEEL 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
386-654 |
7.95e-21 |
|
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: 98.22 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 386 KNVRFHYDTRK--------DVEIYKDLNFTLTEGKTYAFVGESGCGKST----ILKLIerlydPTEGDIIINDS--HNLK 451
Cdd:COG4172 279 RDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQdlDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 452 DINLKWWRSKIGVVSQDPLlfsnsiknnikyslyslkdleylsdqlnedGSasqdgldkrnscrakcagdLNDMMKTTD- 530
Cdd:COG4172 354 RRALRPLRRRMQVVFQDPF------------------------------GS-------------------LSPRMTVGQi 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 531 -SDGL-IHARKnyniIDDSE----VVNVSKKVlihdfvsALP----DKY--EtlvgsnaskLSGGQKQRISIARAIIRNP 598
Cdd:COG4172 385 iAEGLrVHGPG----LSAAErrarVAEALEEV-------GLDpaarHRYphE---------FSGGQRQRIAIARALILEP 444
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 599 KILILDEATSSLDnKSeylVQKTINNLKGN---ENRIT-IIIAHRLSTIRY-ANTIFVLSN 654
Cdd:COG4172 445 KLLVLDEPTSALD-VS---VQAQILDLLRDlqrEHGLAyLFISHDLAVVRAlAHRVMVMKD 501
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1274-1447 |
8.52e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.53 E-value: 8.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNL---FSIVSQEpilFN-MS---IYENIKF-----GKEDATREdvKRackfaaIDEFIE- 1340
Cdd:COG1135 59 SGSVLVDGVDLTALSERELRAArrkIGMIFQH---FNlLSsrtVAENVALpleiaGVPKAEIR--KR------VAELLEl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1341 -SLPNKYDTnvgpYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTI--IT----- 1412
Cdd:COG1135 128 vGLSDKADA----YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIvlIThemdv 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 221056887 1413 ---IAHRIASIKRSdKIV-------VFNNP--DRTGSFVQAEGTHEE 1447
Cdd:COG1135 204 vrrICDRVAVLENG-RIVeqgpvldVFANPqsELTRRFLPTVLNDEL 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1165-1415 |
1.34e-20 |
|
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: 91.55 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1165 EIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqgde 1244
Cdd:cd03226 1 RIENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILA------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1245 eqnvgmknvnefSLTKEgshgdnsavfkNSGKILLDGVDICdynLKDLRNLFSIVSQEP--ILFNMSIYENIKFGKEDAT 1322
Cdd:cd03226 48 ------------GLIKE-----------SSGSILLNGKPIK---AKERRKSIGYVMQDVdyQLFTDSVREELLLGLKELD 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1323 R--EDVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03226 102 AgnEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIR 170
|
250
....*....|....*
gi 221056887 1401 DIKdKADRTIITIAH 1415
Cdd:cd03226 171 ELA-AQGKAVIVITH 184
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
383-613 |
1.50e-20 |
|
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: 92.30 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI-NLKWWRSK 461
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDItNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIKYSLySLKDLeylsdqlnedgsasqdgldKRNSCRAKCAgdlnDMMKTTDSDGliHARKn 540
Cdd:cd03300 74 VNTVFQNYALFPHlTVFENIAFGL-RLKKL-------------------PKAEIKERVA----EALDLVQLEG--YANR- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 541 yniiddsevvnvskkvlihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03300 127 -----------------------------------KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
850-1125 |
1.97e-20 |
|
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: 93.39 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 850 VSTLFDFANLeansNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHI 929
Cdd:cd18557 26 IIKGGDLDVL----NELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDK--HKTGELTSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 930 NRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCPIVAAVLtgtyFIFMRVFAIRARLSankdveKKGINQpgtvfLY 1009
Cdd:cd18557 100 SSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVL----LLVIPLLLIASKIY------GRYIRK-----LS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1010 NNDDEIFKDPSFLIQEAFYNMNTVIIYGLEDY----FCKLIEKAIDYSnkgqKRKTLVNSMLWGFSQSAQLFINSFAYWF 1085
Cdd:cd18557 165 KEVQDALAKAGQVAEESLSNIRTVRSFSAEEKeirrYSEALDRSYRLA----RKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 221056887 1086 GSFLIRRGTIEVDD---FMksLFTFLFTGSYAG------KLMSLKGDSE 1125
Cdd:cd18557 241 GGYLVLSGQLTVGEltsFI--LYTIMVASSVGGlssllaDIMKALGASE 287
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1164-1460 |
2.08e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtddvnnEKKEQGD 1243
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES----------------EVRVEGR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 EE---QNVGMKNVNefsltkegshgdnsavfknsgkilldgvdicdynLKDLRNLFSIVSQEPILFNMSIYENIKFG-KE 1319
Cdd:PRK14258 69 VEffnQNIYERRVN----------------------------------LNRLRRQVSMVHPKPNLFPMSVYDNVAYGvKI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 DATREDVKrackfaaIDEFIES------LPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:PRK14258 115 VGWRPKLE-------IDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASM 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1394 LIEKTIVDIKDKADRTIITIAHRIASIKRSDKIVVF--NNPDRTGSFVQAEGTHEELLSVQDGVYKKYV 1460
Cdd:PRK14258 188 KVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFfkGNENRIGQLVEFGLTKKIFNSPHDSRTREYV 256
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
383-653 |
2.15e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.70 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF-EGEDISTLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNSIKNNIKYSlyslkdleYLSDQLNEDGSASQDGLDKRNscrakcagdlndmmkttdsdgliharknyn 542
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFP--------WQIRNQQPDPAIFLDDLERFA------------------------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iiddsevvnvskkvlihdfvsaLPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK10247 126 ----------------------LP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEII 180
|
250 260 270
....*....|....*....|....*....|.
gi 221056887 623 NNLKGNENRITIIIAHRLSTIRYANTIFVLS 653
Cdd:PRK10247 181 HRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
383-656 |
3.19e-20 |
|
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: 91.59 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHY-DTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSK 461
Cdd:cd03295 1 IEFENVTKRYgGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIkySLYsLKDLEYLSDQLNEdgsasqdgldkrnscRAkcagdlndmmkttdsDGLIHarkn 540
Cdd:cd03295 77 IGYVIQQIGLFPHmTVEENI--ALV-PKLLKWPKEKIRE---------------RA---------------DELLA---- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddsevvnvskkvLIHdfvsaLPDkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03295 120 ----------------LVG-----LDP--AEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQE 176
|
250 260 270
....*....|....*....|....*....|....*..
gi 221056887 621 TINNLKGNENRITIIIAHRL-STIRYANTIFVLSNRE 656
Cdd:cd03295 177 EFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGE 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
100-653 |
3.64e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 97.74 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 100 IFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNNPGSKLtsdldfyLEQVNAGIGTKFLTIF 179
Cdd:PLN03232 953 IVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRV-------INRFSKDIGDIDRNVA 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 180 TYTSAFLGLyFWSLFKNARL-----TLCVTCVFPLI---YICGVICNKKAKINKKTSLLYNNNTMSIIEEALVGIRTVVS 251
Cdd:PLN03232 1026 NLMNMFMNQ-LWQLLSTFALigtvsTISLWAIMPLLilfYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRA 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 252 YcgehtilKKFNLSEKLYSKYMlkANFMEslhigmingFILASYAFGFWYGTRII------------ISDLSNAQSNNDF 319
Cdd:PLN03232 1105 Y-------KAYDRMAKINGKSM--DNNIR---------FTLANTSSNRWLTIRLEtlggvmiwltatFAVLRNGNAENQA 1166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 320 HGGSVISILLGVLISMF-MLTIVLPNITEYMKSLEATNSLYEIIN----RKPLVENNNDGKKLKDIKKIQFKNVRFHYdt 394
Cdd:PLN03232 1167 GFASTMGLLLSYTLNITtLLSGVLRQASKAENSLNSVERVGNYIDlpseATAIIENNRPVSGWPSRGSIKFEDVHLRY-- 1244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 395 RKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFS 473
Cdd:PLN03232 1245 RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD-CDVAKFGLTDLRRVLSIIPQSPVLFS 1323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 474 NSIKNNIkyslyslkdleylsDQLNEDgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyniiDDSEVVNVS 553
Cdd:PLN03232 1324 GTVRFNI--------------DPFSEH--------------------------------------------NDADLWEAL 1345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 554 KKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkgNENR-- 631
Cdd:PLN03232 1346 ERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR----EEFKsc 1421
|
570 580
....*....|....*....|..
gi 221056887 632 ITIIIAHRLSTIRYANTIFVLS 653
Cdd:PLN03232 1422 TMLVIAHRLNTIIDCDKILVLS 1443
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
383-613 |
3.77e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.67 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKD--INLKWWRS 460
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG----RDlfTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPLLFSN-SIKNNIKYslyslkdleylsdqlnedgsasqdGLDKRNSCRAKCAGDLNDMMKTTDSDGLIHARk 539
Cdd:COG1118 76 RVGFVFQHYALFPHmTVAENIAF------------------------GLRVRPPSKAEIRARVEELLELVQLEGLADRY- 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 540 nyniiddsevvnvskkvlihdfvsalPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG1118 131 --------------------------P-----------SQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1196-1448 |
3.89e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1196 AIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkeGSHGdnsavfKNSG 1275
Cdd:COG1129 34 ALLGENGAGKSTLMKILS------------------------------------------------GVYQ------PDSG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1276 KILLDGVDICDYNLKDLRNL-FSIVSQEPILF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL-----PnkyDT 1348
Cdd:COG1129 60 EILLDGEPVRFRSPRDAQAAgIAIIHQELNLVpNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLgldidP---DT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1349 NVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSN-SEKLIEkTIVDIKDKaDRTIITIAHRIASIKR-SDKI 1426
Cdd:COG1129 137 PVG----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLFR-IIRRLKAQ-GVAIIYISHRLDEVFEiADRV 210
|
250 260
....*....|....*....|....*.
gi 221056887 1427 VVFnnpdRTGSFVQ----AEGTHEEL 1448
Cdd:COG1129 211 TVL----RDGRLVGtgpvAELTEDEL 232
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
62-338 |
4.14e-20 |
|
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: 92.49 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 62 LGVSFVCATISGGSLPFFVSVFGVIMKNMNLGENVDDIIF-SLVLIGIF--QFVMSFISSFCMDIVTTKILKTLKVEFLK 138
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLvPLAIIGLFllRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 139 SVFYQDGQFHDNNPG----SKLTSDLdfylEQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYICG 214
Cdd:cd18552 81 KLLRLPLSFFDRNSSgdliSRITNDV----NQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 215 VICNKKAKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEHTILKKFN-LSEKLYsKYMLKANFMESLHIGMINgfILA 293
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRkANERLR-RLSMKIARARALSSPLME--LLG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 221056887 294 SYAFGF--WYGTRIIISDLSNAqsnndfhgGSVISIllgvLISMFML 338
Cdd:cd18552 234 AIAIALvlWYGGYQVISGELTP--------GEFISF----ITALLLL 268
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1265-1388 |
5.94e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 5.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1265 GDNSAVFKNSGKILLDGVDICDYNLkDLRNLfSIVSQEPILF-NMSIYENIKFgkedATREDVKRACKFAAIDEFIES-- 1341
Cdd:COG4136 49 GTLSPAFSASGEVLLNGRRLTALPA-EQRRI-GILFQDDLLFpHLSVGENLAF----ALPPTIGRAQRRARVEQALEEag 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 221056887 1342 LPNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:COG4136 123 LAGFADRDPA----TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
383-663 |
6.76e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.35 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND----SHNLKDInlkww 458
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaitDDNFEKL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 459 RSKIGVVSQDPL-LFSNSIknnIKYslyslkDLEYlsdqlnedgsasqdGLDkrnscrakcagdlNDMMKTTDsdglIHa 537
Cdd:PRK13648 82 RKHIGIVFQNPDnQFVGSI---VKY------DVAF--------------GLE-------------NHAVPYDE----MH- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 538 rknyniiddSEVVNVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:PRK13648 121 ---------RRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 221056887 618 VQKTINNLKGNENrITII-IAHRLSTIRYANTIFVLsnrekgNRSTV 663
Cdd:PRK13648 181 LLDLVRKVKSEHN-ITIIsITHDLSEAMEADHVIVM------NKGTV 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1164-1427 |
8.20e-20 |
|
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: 90.32 E-value: 8.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSrpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCL------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdNSAVFKNSGKILLDGVDICDYNLKDLRNLFS---IVSQEPILFN-MSIYENIKFGKE 1319
Cdd:cd03256 48 -----------------------NGLVEPTSGSVLIDGTDINKLKGKALRQLRRqigMIFQQFNLIErLSVLENVLSGRL 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 DA-----------TREDVKRAckFAAIDEF-IESLPNKY-DTnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSS 1386
Cdd:cd03256 105 GRrstwrslfglfPKEEKQRA--LAALERVgLLDKAYQRaDQ--------LSGGQQQRVAIARALMQQPKLILADEPVAS 174
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 221056887 1387 LDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIV 1427
Cdd:cd03256 175 LDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIV 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
402-654 |
9.75e-20 |
|
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: 90.09 E-value: 9.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI-NLKWWRSKIGVVSQDPLLFSN-SIKNN 479
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDItNLPPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 480 IKYslyslkdleylsdqlnedgsasqdGLDKRNSCRAKcagdlndmmkttdsdgliharknyniiDDSEVVNVSKKVLIh 559
Cdd:cd03299 92 IAY------------------------GLKKRKVDKKE---------------------------IERKVLEIAEMLGI- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 560 dfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLK--GNENRITII-I 636
Cdd:cd03299 120 ----------DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK---EKLREELKkiRKEFGVTVLhV 186
|
250
....*....|....*....
gi 221056887 637 AHRLSTIRY-ANTIFVLSN 654
Cdd:cd03299 187 THDFEEAWAlADKVAIMLN 205
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
389-611 |
9.83e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.67 E-value: 9.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 389 RFHYDT----RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWwRSK-IG 463
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING-HKLEYGDYKY-RCKhIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 464 VVSQDPllfSNSIknNIKYSLYSLKDlEYLSdqLNEDGSASQdgldkRNSCrakcagdlndmmkttdsdgliharknyni 543
Cdd:COG4167 91 MIFQDP---NTSL--NPRLNIGQILE-EPLR--LNTDLTAEE-----REER----------------------------- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 544 iddseVVNVSKKVlihdfvSALPDKYETlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4167 129 -----IFATLRLV------GLLPEHANF----YPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
382-653 |
1.08e-19 |
|
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: 90.35 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
Cdd:cd03288 19 EIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-DGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSNSIKNNikyslyslkdleylsdqlnedgsasqdgLDKRNSCrakcagdlndmmktTDsDGLIHArkny 541
Cdd:cd03288 97 LSIILQDPILFSGSIRFN----------------------------LDPECKC--------------TD-DRLWEA---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 niIDDSEVVNVskkvlihdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03288 130 --LEIAQLKNM---------VKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKV 198
|
250 260 270
....*....|....*....|....*....|..
gi 221056887 622 InnLKGNENRITIIIAHRLSTIRYANTIFVLS 653
Cdd:cd03288 199 V--MTAFADRTVVTIAHRVSTILDADLVLVLS 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1274-1448 |
1.30e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.17 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLR-------------NLFSivSQepilfnmSIYENIKFGKEDA--TREDVKrackfAAIDEF 1338
Cdd:PRK11153 59 SGRVLVDGQDLTALSEKELRkarrqigmifqhfNLLS--SR-------TVFDNVALPLELAgtPKAEIK-----ARVTEL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1339 IE--SLPNKYDTnvgpYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHR 1416
Cdd:PRK11153 125 LElvGLSDKADR----YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221056887 1417 IASIKR---------SDKIV-------VFNNP--DRTGSFVQaEGTHEEL 1448
Cdd:PRK11153 201 MDVVKRicdrvavidAGRLVeqgtvseVFSHPkhPLTREFIQ-STLHLDL 249
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
383-644 |
1.56e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.79 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDT-RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWR 459
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDgqDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQD-PLLFSNSIKNNIKYSLyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdglihar 538
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALPL------------------------------------------------------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 539 knyniiddsEVVNVSKKvLIHDFVSALPDkyetLVGSNA------SKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
Cdd:PRK11153 108 ---------ELAGTPKA-EIKARVTELLE----LVGLSDkadrypAQLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
|
250 260 270
....*....|....*....|....*....|....*.
gi 221056887 613 KSeylvQKTINNLKGNENR---ITII-IAHRLSTIR 644
Cdd:PRK11153 174 AT----TRSILELLKDINRelgLTIVlITHEMDVVK 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
382-652 |
1.58e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYD--TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDINLK 456
Cdd:PRK13646 2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 457 WWRSKIGVVSQDP--LLFSNSIKNNIkyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgl 534
Cdd:PRK13646 82 PVRKRIGMVFQFPesQLFEDTVEREI------------------------------------------------------ 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 535 IHARKNYNiIDDSEVVNVSKKVLIH-----DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSS 609
Cdd:PRK13646 108 IFGPKNFK-MNLDEVKNYAHRLLMDlgfsrDVMSQSP-----------FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 221056887 610 LDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVaRYADEVIVM 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1154-1460 |
1.71e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.84 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1154 IKNTNDIDGKIEIMDVNFTYMSRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDhhivfknehtdd 1233
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAV---KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1234 vnnekkeqgdeeqnvgmknvnefsltkegshgdnsavFKNSGKILLDGVDICDYNLK--DLRNLFSIVSQEPILFNMSIY 1311
Cdd:PRK14243 66 -------------------------------------FRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPKSIY 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1312 ENIKFG------KEDATrEDVKRACKFAAI-DEFIESLPNKydtnvgpyGKSLSGGQKQRVAIARALLREPKILLLDEAT 1384
Cdd:PRK14243 109 DNIAYGaringyKGDMD-ELVERSLRQAALwDEVKDKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1385 SSLDSNSEKLIEKTIVDIKDkaDRTIITIAHRIASIKR-SDKIVVFN-----NPDRTGSFVQAEGTHEELLSVQDGVYKK 1458
Cdd:PRK14243 180 SALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARvSDMTAFFNvelteGGGRYGYLVEFDRTEKIFNSPQQQATRD 257
|
..
gi 221056887 1459 YV 1460
Cdd:PRK14243 258 YV 259
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
383-652 |
3.99e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.47 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHY-DTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGD--IIINDSHNLKDINLKWWR 459
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPA--LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnsKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQDPllfsnsiknnikyslyslkDLEYLSDQLNEDGSAsqdGLDKRNSCRakcagdlNDMMKTtdsdglihark 539
Cdd:PRK13640 84 EKVGIVFQNP-------------------DNQFVGATVGDDVAF---GLENRAVPR-------PEMIKI----------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 nyniiddseVVNVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:PRK13640 124 ---------VRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQIL 183
|
250 260 270
....*....|....*....|....*....|....
gi 221056887 620 KTINNLKgNENRITII-IAHRLSTIRYANTIFVL 652
Cdd:PRK13640 184 KLIRKLK-KKNNLTVIsITHDIDEANMADQVLVL 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1163-1460 |
4.93e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1163 KIEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfknehtddvnnekkeqg 1242
Cdd:PRK14247 3 KIEIRDLKVSF---GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARV------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1243 deeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQEP-ILFNMSIYENIKFG---- 1317
Cdd:PRK14247 62 -------------------------------SGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPNLSIFENVALGlkln 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 ----KEDATREDVKRACKFAaidEFIESLPNKYDtnvGPYGKsLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:PRK14247 111 rlvkSKKELQERVRWALEKA---QLWDEVKDRLD---APAGK-LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTA 183
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1394 LIEKTIVDIKDkaDRTIITIAHRIASIKRSDKIVVFNnpdRTGSFVQAEGTHEELLSVQDGVYKKYV 1460
Cdd:PRK14247 184 KIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFL---YKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1164-1396 |
5.76e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 5.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:COG2884 2 IRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG----------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 EEQnvgmknvnefsLTkegshgdnsavfknSGKILLDGVDICDYNLKDLRNL---FSIVSQE-PILFNMSIYENIKF--- 1316
Cdd:COG2884 51 EER-----------PT--------------SGQVLVNGQDLSRLKRREIPYLrrrIGVVFQDfRLLPDRTVYENVALplr 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1317 --GKEDAT-REDVKrackfAAIDEFieSLPNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLD-SNSE 1392
Cdd:COG2884 106 vtGKSRKEiRRRVR-----EVLDLV--GLSDKAKALPH----ELSGGEQQRVAIARALVNRPELLLADEPTGNLDpETSW 174
|
....
gi 221056887 1393 KLIE 1396
Cdd:COG2884 175 EIME 178
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
351-653 |
5.82e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 94.03 E-value: 5.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 351 SLEATNSLYEIINRKPLV-ENNNDGKKLKDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTIL 428
Cdd:PLN03130 1205 AVERVGTYIDLPSEAPLViENNRPPPGWPSSGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSML 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 429 KLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleylsDQLNEDGSAS-QDG 507
Cdd:PLN03130 1283 NALFRIVELERGRILI-DGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL--------------DPFNEHNDADlWES 1347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 508 LDkrnscRAKcagdLNDMMKTtDSDGLiharknyniidDSEVvnvskkvlihdfvsalpdkyeTLVGSNaskLSGGQKQR 587
Cdd:PLN03130 1348 LE-----RAH----LKDVIRR-NSLGL-----------DAEV---------------------SEAGEN---FSVGQRQL 1382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 588 ISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkgNENR--ITIIIAHRLSTIRYANTIFVLS 653
Cdd:PLN03130 1383 LSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR----EEFKscTMLIIAHRLNTIIDCDRILVLD 1446
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
378-657 |
5.85e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.56 E-value: 5.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 378 KDIKKIQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDI-IINDSHNLK 451
Cdd:PRK14258 3 KLIPAIKVNNLSFYYDTQKILE---GVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVeFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 452 DINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdleylsdqlnedgsasqdgldKRNSCRAKCagDLNDMMKTTds 531
Cdd:PRK14258 80 RVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGV-------------------------KIVGWRPKL--EIDDIVESA-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 532 dgliharknyniIDDSEvvnvskkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK14258 131 ------------LKDAD----------------LWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 221056887 612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYAN-TIFVLSNREK 657
Cdd:PRK14258 183 PIASMKVESLIQSLRLRSELTMVIVSHNLHQVsRLSDfTAFFKGNENR 230
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
64-355 |
6.31e-19 |
|
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: 88.77 E-value: 6.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 64 VSFVCATISGGSLPFFVS-VFGVIMKNMNLgENVDDIIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFY 142
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGrLIDTIIKGGDL-DVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 143 QDGQFHD-NNPG---SKLTSDLdfylEQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYICGVICN 218
Cdd:cd18557 82 QEIAFFDkHKTGeltSRLSSDT----SVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 219 KKAKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEHTILKKFnlSEKLYSKYML--KANFMESLHIGMINGFILASYA 296
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRY--SEALDRSYRLarKKALANALFQGITSLLIYLSLL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 297 FGFWYGTRIIISdlsnaqsnNDFHGGSVISILLGVLISMFMLTIVLPNITEYMKSLEAT 355
Cdd:cd18557 236 LVLWYGGYLVLS--------GQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGAS 286
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1273-1388 |
6.70e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 87.74 E-value: 6.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 NSGKILLDGVDICD--YNLKDLRNLFSIVSQEPILF-NMSIYENI--------KFGKEDATredvKRAckfaaiDEFIES 1341
Cdd:COG1126 54 DSGTITVDGEDLTDskKDINKLRRKVGMVFQQFNLFpHLTVLENVtlapikvkKMSKAEAE----ERA------MELLER 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 221056887 1342 --LPNKYDTnvgpYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:COG1126 124 vgLADKADA----YPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1164-1442 |
1.03e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 86.73 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPnvpiykdLTFSCDSKK--TTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtddvnnekkeq 1241
Cdd:COG3840 2 LRLDDLTYRYGDFP-------LRFDLTIAAgeRVAILGPSGAGKSTLLNLIAGFLPPD---------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1242 gdeeqnvgmknvnefsltkegshgdnsavfknSGKILLDGVDICDYNlKDLRnLFSIVSQEPILFN-MSIYENIKFG--- 1317
Cdd:COG3840 53 --------------------------------SGRILWNGQDLTALP-PAER-PVSMLFQENNLFPhLTVAQNIGLGlrp 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 --KEDAT-REDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSN--SE 1392
Cdd:COG3840 99 glKLTAEqRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAlrQE 167
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1393 KLIEktIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNN-----PDRTGSFVQAE 1442
Cdd:COG3840 168 MLDL--VDELCRERGLTVLMVTHDPEDAARiADRVLLVADgriaaDGPTAALLDGE 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
383-637 |
1.10e-18 |
|
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: 86.40 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDiNLKWWRSKI 462
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-YSIRT-DRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNsiknnikyslysLKDLEYLsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgLIHAR-KNY 541
Cdd:cd03263 78 GYCPQFDALFDE------------LTVREHL----------------------------------------RFYARlKGL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 NIIDDSEVVNVSKKVLihdfvsALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03263 106 PKSEIKEEVELLLRVL------GLTDKANKR----ARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDL 175
|
250
....*....|....*.
gi 221056887 622 INNLKgnENRiTIIIA 637
Cdd:cd03263 176 ILEVR--KGR-SIILT 188
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
402-652 |
1.17e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.18 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNL--KDINLKWWRSKIGVVSQDP--LLFSNSIK 477
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGV-DItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 478 NNIKYSLYSLkdleylsdqlnedgsasqdGLdkrnscrakcagdlndmmkttdSDGLIHARknynIIDDSEVVNVSkkvl 557
Cdd:PRK13637 103 KDIAFGPINL-------------------GL----------------------SEEEIENR----VKRAMNIVGLD---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 558 ihdfvsalpdkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
Cdd:PRK13637 134 -----------YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVS 202
|
250
....*....|....*.
gi 221056887 638 HRLSTI-RYANTIFVL 652
Cdd:PRK13637 203 HSMEDVaKLADRIIVM 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1183-1450 |
1.95e-18 |
|
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: 85.95 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1183 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkeg 1262
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRP-------------------------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1263 shgdnsavfkNSGKILLDGVDICDYNLKDLRNL-----FSIVSqepILFNMSIYENIKFGKEDATREDVKRACKFAAIDE 1337
Cdd:cd03219 53 ----------TSGSVLFDGEDITGLPPHEIARLgigrtFQIPR---LFPELTVLENVMVAAQARTGSGLLLARARREERE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1338 FIES---------LPNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKDKaD 1407
Cdd:cd03219 120 ARERaeellervgLADLADRPAG----ELSYGQQRRLEIARALATDPKLLLLDEPAAGLnPEETEELAE-LIRELRER-G 193
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 221056887 1408 RTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAEGTHEELLS 1450
Cdd:cd03219 194 ITVLLVEHDMDVVMSlADRVTVLDQ----GR-VIAEGTPDEVRN 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1164-1431 |
2.03e-18 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 86.20 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSrpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTvmslLMRfydlkndhHIvfknehtddvnnekkeqgd 1243
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKST----LLR--------CI------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdNSAVFKNSGKILLDGVDICDYNLKDLRNL---FSIVSQE-PILFNMSIYENIKFGKE 1319
Cdd:TIGR02315 49 -----------------------NRLVEPSSGSILLEGTDITKLRGKKLRKLrrrIGMIFQHyNLIERLTVLENVLHGRL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 DA-----------TREDVKRAckFAAIDEFieSLPNKYDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:TIGR02315 106 GYkptwrsllgrfSEEDKERA--LSALERV--GLADKAYQRA----DQLSGGQQQRVAIARALAQQPDLILADEPIASLD 177
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 221056887 1389 SNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:TIGR02315 178 PKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKA 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1164-1429 |
2.95e-18 |
|
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: 84.85 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSrpnVPIYKDLTFScdSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03298 1 VRLDKIRFSYGE---QPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGF---------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsaVFKNSGKILLDGVDICdyNLKDLRNLFSIVSQEPILF-NMSIYENIKFGK---- 1318
Cdd:cd03298 48 --------------------------ETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFaHLTVEQNVGLGLspgl 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1319 ----EDatREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKL 1394
Cdd:cd03298 100 kltaED--RQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
250 260 270
....*....|....*....|....*....|....*
gi 221056887 1395 IEKTIVDIKDKADRTIITIAHRIASIKRSDKIVVF 1429
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVF 201
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1275-1429 |
3.11e-18 |
|
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: 85.04 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1275 GKILLDGVDICDYNLK-DL---RNLFSIVSQEPILF-NMSIYENIKFG-KEDATREDvkRACKFAAIDEF-IESLPNKYd 1347
Cdd:cd03297 52 GTIVLNGTVLFDSRKKiNLppqQRKIGLVFQQYALFpHLNVRENLAFGlKRKRNRED--RISVDELLDLLgLDHLLNRY- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1348 tnvgPYGksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKI 1426
Cdd:cd03297 129 ----PAQ--LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRI 202
|
...
gi 221056887 1427 VVF 1429
Cdd:cd03297 203 VVM 205
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
402-660 |
3.51e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.99 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD--PT---EGDIIINDsHNL--KDINLKWWRSKIGVVSQDPLLFSN 474
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHG-KNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 475 SIKNNIKYSlyslkdleylsdqlnedgsasqdgldkrnscrAKCAGDLNDMmkttdsdgliharknyniiddSEVVNVSK 554
Cdd:PRK14243 106 SIYDNIAYG--------------------------------ARINGYKGDM---------------------DELVERSL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 555 KvlihdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRITI 634
Cdd:PRK14243 133 R------QAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK---EQYTI 203
|
250 260 270
....*....|....*....|....*....|...
gi 221056887 635 II-------AHRLSTIryaNTIFVLSNREKGNR 660
Cdd:PRK14243 204 IIvthnmqqAARVSDM---TAFFNVELTEGGGR 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1273-1427 |
3.64e-18 |
|
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: 84.89 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 NSGKILLDGVDICD--YNLKDLRNLFSIVSQEPILF-NMSIYENIKFG--------KEDAtREDVKRACKFAAIDEFIES 1341
Cdd:cd03262 53 DSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFpHLTVLENITLApikvkgmsKAEA-EERALELLEKVGLADKADA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1342 LPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADRTIITIAHRIASIK 1421
Cdd:cd03262 132 YPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAR 199
|
....*..
gi 221056887 1422 R-SDKIV 1427
Cdd:cd03262 200 EvADRVI 206
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
390-611 |
4.81e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.00 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 390 FHYDT----RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVV 465
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD-HPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 466 SQDPllfSNSIknNIKYSLYSLKDLEYlsdQLNEDGSASQdgldkrnscRAKcagdlndmmkttdsdgliharknyNIID 545
Cdd:PRK15112 93 FQDP---STSL--NPRQRISQILDFPL---RLNTDLEPEQ---------REK------------------------QIIE 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 546 DSEVVNvskkvLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK15112 132 TLRQVG-----LLPDHASYYP-----------HMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
383-654 |
5.17e-18 |
|
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: 84.17 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGkTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINlkWWRSKI 462
Cdd:cd03264 1 LQLENLTKRYGKKRAL---DGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ--KLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNsiknnikyslysLKDLEYLsdqlneDGSASQDGLDKRNScrakcagdlndmmkttdsdgliharknyn 542
Cdd:cd03264 75 GYLPQEFGVYPN------------FTVREFL------DYIAWLKGIPSKEV----------------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iidDSEVVNVSKKVLIHDFVsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03264 108 ---KARVDEVLELVNLGDRA----KKK-------IGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLL 173
|
250 260 270
....*....|....*....|....*....|...
gi 221056887 623 NNLkgNENRITIIIAHRLSTIRY-ANTIFVLSN 654
Cdd:cd03264 174 SEL--GEDRIVILSTHIVEDVESlCNQVAVLNK 204
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1273-1431 |
6.93e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.31 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 NSGKILLDGVDICDYNLKDlRNLfSIVSQEPILF-NMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPnk 1345
Cdd:PRK09452 67 DSGRIMLDGQDITHVPAEN-RHV-NTVFQSYALFpHMTVFENVAFGlrmqktPAAEITPRVMEALRMVQLEEFAQRKP-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1346 ydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAH-RIASIKRSD 1424
Cdd:PRK09452 143 ---------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdQEEALTMSD 213
|
....*..
gi 221056887 1425 KIVVFNN 1431
Cdd:PRK09452 214 RIVVMRD 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1164-1419 |
9.83e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.29 E-value: 9.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSrpnVPIYKDLTFSCDSKKTTAIVGETGSGKST---VMSLLmrfyDLKNDHHIVFKNEHTDDVNNEKKE 1240
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLL----ETPDSGQLNIAGHQFDFSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1241 QGDE-EQNVGMknvnefsltkegshgdnsaVFKNsgkilldgvdicdYNL----KDLRNLFsivsQEPI-LFNMSiyeni 1314
Cdd:COG4161 76 AIRLlRQKVGM-------------------VFQQ-------------YNLwphlTVMENLI----EAPCkVLGLS----- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1315 kfgKEDAtredVKRACKFAA---IDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNs 1391
Cdd:COG4161 115 ---KEQA----REKAMKLLArlrLTDKADRFPLH-----------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE- 175
|
250 260 270
....*....|....*....|....*....|....*..
gi 221056887 1392 eklIEKTIVDIKDKADRTIIT---------IAHRIAS 1419
Cdd:COG4161 176 ---ITAQVVEIIRELSQTGITqvivtheveFARKVAS 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1274-1431 |
1.08e-17 |
|
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: 83.93 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDlRNLfSIVSQEPILF-NMSIYENIKFG----------KEDATREDVKRACKFAAIDEFIESL 1342
Cdd:cd03296 56 SGTILFGGEDATDVPVQE-RNV-GFVFQHYALFrHMTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRY 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1343 PNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIA-SIK 1421
Cdd:cd03296 134 PAQ-----------LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEeALE 202
|
170
....*....|
gi 221056887 1422 RSDKIVVFNN 1431
Cdd:cd03296 203 VADRVVVMNK 212
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1164-1415 |
1.33e-17 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 83.95 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSrpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtddvnnekkeqgd 1243
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEP------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsavfkNSGKILLDGVDICDYNLKDLRNLFS---IVSQEPILF-NMSIYENI----- 1314
Cdd:COG3638 56 -----------------------------TSGEILVDGQDVTALRGRALRRLRRrigMIFQQFNLVpRLSVLTNVlagrl 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1315 -----------KFgkedaTREDVKRAckFAAIDEFieSLPNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEA 1383
Cdd:COG3638 107 grtstwrsllgLF-----PPEDRERA--LEALERV--GLADKAYQRAD----QLSGGQQQRVAIARALVQEPKLILADEP 173
|
250 260 270
....*....|....*....|....*....|...
gi 221056887 1384 TSSLD-SNSEKLIEkTIVDIKDKADRTIITIAH 1415
Cdd:COG3638 174 VASLDpKTARQVMD-LLRRIAREDGITVVVNLH 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1274-1450 |
1.53e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYN-LKDLRNLFSIVSQEP--ILFNMSIYENIKFGKED------ATREDVKRACKFAAIDEFIESLPn 1344
Cdd:PRK13644 56 KGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPetQFVGRTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSP- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1345 kydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdRTIITIAHRIASIKRSD 1424
Cdd:PRK13644 135 ----------KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKG-KTIVYITHNLEELHDAD 203
|
170 180
....*....|....*....|....*.
gi 221056887 1425 KIVVFnnpDRtgSFVQAEGTHEELLS 1450
Cdd:PRK13644 204 RIIVM---DR--GKIVLEGEPENVLS 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
367-613 |
2.14e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.77 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 367 LVENNNDGKKLkdikkIQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND 446
Cdd:PRK09452 4 LNKQPSSLSPL-----VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 447 shnlKDIN-LKWWRSKIGVVSQDPLLFSN-SIKNNIKYSLyslkdleylsdqlnedgsasqdgldkrnscrakcagdlnD 524
Cdd:PRK09452 76 ----QDIThVPAENRHVNTVFQSYALFPHmTVFENVAFGL---------------------------------------R 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 525 MMKTTDSDglIHARknyniiddseVVNVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILD 604
Cdd:PRK09452 113 MQKTPAAE--ITPR----------VMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
....*....
gi 221056887 605 EATSSLDNK 613
Cdd:PRK09452 170 ESLSALDYK 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
402-652 |
2.34e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN----DSHNLKDInlkwWRSKIGVVSQDPLLFSN-SI 476
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvRFRSPRDA----QAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 477 KNNIkyslyslkdleYLSDQLnedgsaSQDGLDKRNSCRAKCAgdlnDMMKTTDSDgliharknyniIDdsevvnvskkv 556
Cdd:COG1129 97 AENI-----------FLGREP------RRGGLIDWRAMRRRAR----ELLARLGLD-----------ID----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 557 lihdfvsalPDkyeTLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVqKTINNLKgnENRITII 635
Cdd:COG1129 134 ---------PD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLF-RIIRRLK--AQGVAII 194
|
250
....*....|....*....
gi 221056887 636 -IAHRLSTIRY-ANTIFVL 652
Cdd:COG1129 195 yISHRLDEVFEiADRVTVL 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
383-643 |
2.57e-17 |
|
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: 83.21 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG-DIIINDsHNLKDINLKWWRSK 461
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFG-ERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSqdpllfsnsiknnikyslyslkdleylsdqlnedgSASQDGLDKRNSCRakcagdlnDMMKT--TDSDGLihark 539
Cdd:COG1119 80 IGLVS-----------------------------------PALQLRFPRDETVL--------DVVLSgfFDSIGL----- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 nYNIIDDSEVVNVskKVLIHDF-VSALPDK-YETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG1119 112 -YREPTDEQRERA--RELLELLgLAHLADRpFGTL--------SQGEQRRVLIARALVKDPELLILDEPTAGLDLGAREL 180
|
250 260
....*....|....*....|....*.
gi 221056887 618 VQKTINNLKGNENRITIIIAHRLSTI 643
Cdd:COG1119 181 LLALLDKLAAEGAPTLVLVTHHVEEI 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1267-1450 |
2.76e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.98 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1267 NSAVFKNSGKILLDGVDICDY-NLKDLRNLFSIVSQEP--ILFNMSIYENIKFGKE------DATREDVKRACKFAAIDE 1337
Cdd:PRK13633 57 NALLIPSEGKVYVDGLDTSDEeNLWDIRNKAGMVFQNPdnQIVATIVEEDVAFGPEnlgippEEIRERVDESLKKVGMYE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1338 FIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRI 1417
Cdd:PRK13633 137 YRRHAPHL-----------LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYM 205
|
170 180 190
....*....|....*....|....*....|...
gi 221056887 1418 ASIKRSDKIVVFNnpdrTGSFVQaEGTHEELLS 1450
Cdd:PRK13633 206 EEAVEADRIIVMD----SGKVVM-EGTPKEIFK 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
406-611 |
2.96e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 84.63 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 406 FTLTEGKTYAFVGESGCGKSTI---LKLIERlydPTEGDIIInDSHNLKDIN---LKWWRSKIGVVSQDPllfsnsiknn 479
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYY-QGQDLLKADpeaQKLLRQKIQIVFQNP---------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 480 ikYSlySLKDLEYLSDQL------NEDGSASQdgldkRnscRAKCAgdlnDMMKTTdsdGLI--HArKNYNiiddsevvn 551
Cdd:PRK11308 102 --YG--SLNPRKKVGQILeeplliNTSLSAAE-----R---REKAL----AMMAKV---GLRpeHY-DRYP--------- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 552 vskkvliHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11308 153 -------HMF-------------------SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
825-1119 |
3.44e-17 |
|
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: 83.75 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 825 VVIIALSIIVAGglypmFALLYAKYVSTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKH 901
Cdd:cd07346 2 LLALLLLLLATA-----LGLALPLLTKLLIDDVIPAGDLsllLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 902 RLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCPIVAAVLTGT---YFI 978
Cdd:cd07346 77 DLFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLlplYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 979 FMRVFAIRARlSANKDVEKKGinqpgtvflynndDEIFKdpsfLIQEAFYNMNTVIIYGLEDYFCKLIEKAidysNKGQK 1058
Cdd:cd07346 155 ILRYFRRRIR-KASREVRESL-------------AELSA----FLQESLSGIRVVKAFAAEEREIERFREA----NRDLR 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1059 RKTLVNSMLWGFSQSAQLFINSFA----YWFGSFLIRRGTIEVDDfmksLFTFLftgSYAGKLMS 1119
Cdd:cd07346 213 DANLRAARLSALFSPLIGLLTALGtalvLLYGGYLVLQGSLTIGE----LVAFL---AYLGMLFG 270
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1164-1415 |
3.60e-17 |
|
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: 82.07 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03292 1 IEFINVTKTY--PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYK----------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 EEQnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDYN---LKDLRNLFSIVSQE-PILFNMSIYENIKFGKE 1319
Cdd:cd03292 50 EEL-------------------------PTSGTIRVNGQDVSDLRgraIPYLRRKIGVVFQDfRLLPDRNVYENVAFALE 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 --DATREDVKRACKfAAIDEFieSLPNKYDTnvgpYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:cd03292 105 vtGVPPREIRKRVP-AALELV--GLSHKHRA----LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN 177
|
250
....*....|....*...
gi 221056887 1398 TIVDIkDKADRTIITIAH 1415
Cdd:cd03292 178 LLKKI-NKAGTTVVVATH 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
402-652 |
3.82e-17 |
|
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: 83.08 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSK-IGVVSQDPLLFSN-SIK 477
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqDIAAMSRKELRELRRKkISMVFQSFALLPHrTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 478 NNIKYslyslkdleylsdqlnedgsasqdGLDKRNSCRAKcagdlndmmkttdsdglIHARKnyniiddSEVVNvskKVL 557
Cdd:cd03294 121 ENVAF------------------------GLEVQGVPRAE-----------------REERA-------AEALE---LVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 558 IHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
Cdd:cd03294 150 LEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFIT 218
|
250
....*....|....*.
gi 221056887 638 HRLS-TIRYANTIFVL 652
Cdd:cd03294 219 HDLDeALRLGDRIAIM 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1179-1450 |
6.71e-17 |
|
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: 81.33 E-value: 6.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1179 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsl 1258
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR--------------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1259 tkegshgdnsavfknSGKILLDGVDICDYNLKDL-----------RNLFSivsqepilfNMSIYENIKFGKEDATREDVK 1327
Cdd:cd03224 54 ---------------SGSIRFDGRDITGLPPHERaragigyvpegRRIFP---------ELTVEENLLLGAYARRRAKRK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1328 RAckfaaIDEFIESLPNKYDtNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLdsnSEKLIE---KTIVDIKD 1404
Cdd:cd03224 110 AR-----LERVYELFPRLKE-RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL---APKIVEeifEAIRELRD 180
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 221056887 1405 KaDRTIITI---AHRIASIkrSDKIVVFnnpdRTGSFVqAEGTHEELLS 1450
Cdd:cd03224 181 E-GVTILLVeqnARFALEI--ADRAYVL----ERGRVV-LEGTAAELLA 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-1420 |
6.86e-17 |
|
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: 87.27 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 340 IVLPNITEYMKslEATNSLYEIINrkplvENNNDGKKLKDIKKIQFKNVRFHYdtrkdVEIYKDLNFTLTEGKTYAFVGE 419
Cdd:TIGR01271 393 VEMVNVTASWD--EGIGELFEKIK-----QNNKARKQPNGDDGLFFSNFSLYV-----TPVLKNISFKLEKGQLLAVAGS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 420 SGCGKSTILKLIERLYDPTEGDIiindSHNlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLySLKDLEYLSD---- 495
Cdd:TIGR01271 461 TGSGKSSLLMMIMGELEPSEGKI----KHS----------GRISFSPQTSWIMPGTIKDNIIFGL-SYDEYRYTSVikac 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 496 QLNEDgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyniiddsevvnvskkvlihdfVSALPDKYETLVGS 575
Cdd:TIGR01271 526 QLEED-------------------------------------------------------------IALFPEKDKTVLGE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 576 NASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY-LVQKTINNLKGNENRItiIIAHRLSTIRYANTIFVLSN 654
Cdd:TIGR01271 545 GGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRI--LVTSKLEHLKKADKILLLHE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 655 ----------REKGNRSTVDVDIIGEDpTKDNKENKQKNGKKGDTNKNEKMSNAGSYI---------IEQGTHDALMKNK 715
Cdd:TIGR01271 623 gvcyfygtfsELQAKRPDFSSLLLGLE-AFDNFSAERRNSILTETLRRVSIDGDSTVFsgpetikqsFKQPPPEFAEKRK 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 716 NGIYYTMINNQKVSSKTSNNNDNDKDSDMKSSVYKDSERGYD--PDE-------------------------------MN 762
Cdd:TIGR01271 702 QSIILNPIASARKFSFVQMGPQKAQATTIEDAVREPSERKFSlvPEDeqgeeslprgnqyhhglqhqaqrrqsvlqlmTH 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 763 GNTKNGNESASDKKSNKMS-----DENAS---------SKNAGGKLSF------LRNLF---KRKPKAPNNLRMVYREIF 819
Cdd:TIGR01271 782 SNRGENRREQLQTSFRKKSsitqqNELASeldiysrrlSKDSVYEISEeineedLKECFadeRENVFETTTWNTYLRYIT 861
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 820 SYKKDVVIIALSII-----VAGGLYPMFaLLYAKYVSTLFDFAN--------------LEANSNKYSLYILV------IA 874
Cdd:TIGR01271 862 TNRNLVFVLIFCLViflaeVAASLLGLW-LITDNPSAPNYVDQQhanasspdvqkpviITPTSAYYIFYIYVgtadsvLA 940
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 875 IAMF----ISETLKNyynnvigekVEKTMKHRLFENILYQEISFFDQdCHAPGLLSSHInRDVHLLKTGLVNNIVIFTHF 950
Cdd:TIGR01271 941 LGFFrglpLVHTLLT---------VSKRLHEQMLHSVLQAPMAVLNT-MKAGRILNRFT-KDMAIIDDMLPLTLFDFIQL 1009
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 951 IVL-----FIVSMIMSFYFcpiVAAVLTGTYFIFMRVFAIRARLSAnKDVEKKGiNQPgtvflynnddeIFkdpSFLIQe 1025
Cdd:TIGR01271 1010 TLIvlgaiFVVSVLQPYIF---IAAIPVAVIFIMLRAYFLRTSQQL-KQLESEA-RSP-----------IF---SHLIT- 1069
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1026 AFYNMNTVIIYGLEDYFCKLIEKAIDY--SNKGQKRKTLV-----NSMLWGFSQSAQLFINSFAYWFG----------SF 1088
Cdd:TIGR01271 1070 SLKGLWTIRAFGRQSYFETLFHKALNLhtANWFLYLSTLRwfqmrIDIIFVFFFIAVTFIAIGTNQDGegevgiiltlAM 1149
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1089 LIR-------RGTIEVDDFMKSLftflftgSYAGKLMSLKGDSENAKLSFEKYYPlimrkSNIDVRDNggiriKNTNDI- 1160
Cdd:TIGR01271 1150 NILstlqwavNSSIDVDGLMRSV-------SRVFKFIDLPQEEPRPSGGGGKYQL-----STVLVIEN-----PHAQKCw 1212
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1161 --DGKIEIMDVNFTYMSRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtddvnnek 1238
Cdd:TIGR01271 1213 psGGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR------------------------ 1267
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1239 keqgdeeqnvgmknvnefsltkegshgdnsaVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKfGK 1318
Cdd:TIGR01271 1268 -------------------------------LLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PY 1315
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1319 EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:TIGR01271 1316 EQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKT 1395
|
1210 1220
....*....|....*....|..
gi 221056887 1399 IVdiKDKADRTIITIAHRIASI 1420
Cdd:TIGR01271 1396 LK--QSFSNCTVILSEHRVEAL 1415
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
826-1116 |
7.87e-17 |
|
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: 83.09 E-value: 7.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 826 VIIALSIIVAGGLYPMFALLYAKYVSTLFD-------------------FANLEANSNKYSLYILVIAIAMFISETLKNY 886
Cdd:cd18558 2 VVGILCAIIHGGLLPAFMVIFGDMTDSFTNggmtnitgnssglnssagpFEKLEEEMTLYAYYYLIIGAIVLITAYIQGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 887 YNNVIGEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCP 966
Cdd:cd18558 82 FWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 967 IVAAVLTGTYFIFMRVFAIRAR-LSANKDVEKKGINQPGTVflynnddeifkdpsflIQEAFYNMNTVIIYGLEDYFCKL 1045
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKiLSGFTDKEKKAYAKAGAV----------------AEEVLEAFRTVIAFGGQQKEETR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 1046 IEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTIEVDDFMKSLFTFLFTGSYAGK 1116
Cdd:cd18558 224 YAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQ 294
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
403-654 |
8.46e-17 |
|
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: 83.62 E-value: 8.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS---HNLKDINLKWWRSKIGVVSQDPLLFSN-SIKN 478
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 479 NIKYslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdGLIHARKNYNIIDDSEVVNVSKkvli 558
Cdd:TIGR02142 95 NLRY--------------------------------------------------GMKRARPSERRISFERVIELLG---- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 559 hdfvsalpdkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITII-IA 637
Cdd:TIGR02142 121 ----------IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLH-AEFGIPILyVS 189
|
250
....*....|....*...
gi 221056887 638 HRLSTI-RYANTIFVLSN 654
Cdd:TIGR02142 190 HSLQEVlRLADRVVVLED 207
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
825-1109 |
9.92e-17 |
|
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: 82.47 E-value: 9.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 825 VVIIALSIIVAGglypmFALLYAKYVSTLFDfaNLEANSNKYSLYILVIAI-AMF----ISETLKNYYNNVIGEKVEKTM 899
Cdd:cd18552 2 ALAILGMILVAA-----TTAALAWLLKPLLD--DIFVEKDLEALLLVPLAIiGLFllrgLASYLQTYLMAYVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 900 KHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCP---IVAAVLTGTY 976
Cdd:cd18552 75 RNDLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWkltLIALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 977 FIFMRVFAIRARLSANKDVEKKG-INQpgtvflynnddeifkdpsfLIQEAFYNMNTVIIYGLEDY----FCKLIEKAID 1051
Cdd:cd18552 153 ALPIRRIGKRLRKISRRSQESMGdLTS-------------------VLQETLSGIRVVKAFGAEDYeikrFRKANERLRR 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 1052 YSNKGQKRKTLVNSMlwgfSQsaqlFINSFAY----WFGSFLIRRGTIEVDDFMkSLFTFLF 1109
Cdd:cd18552 214 LSMKIARARALSSPL----ME----LLGAIAIalvlWYGGYQVISGELTPGEFI-SFITALL 266
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
383-654 |
1.36e-16 |
|
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: 78.62 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN----DSHNLKDInlkwW 458
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgkevSFASPRDA----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 459 RSKIGVVSQdpllfsnsiknnikyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdglihar 538
Cdd:cd03216 74 RAGIAMVYQ----------------------------------------------------------------------- 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 539 knyniiddsevvnvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
|
250 260 270
....*....|....*....|....*....|....*...
gi 221056887 619 QKTINNLKgnENRITII-IAHRLSTI-RYANTIFVLSN 654
Cdd:cd03216 122 FKVIRRLR--AQGVAVIfISHRLDEVfEIADRVTVLRD 157
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1275-1450 |
1.47e-16 |
|
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: 83.24 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1275 GKILLDGVDICD----YNLKDLRNLFSIVSQEPILF-NMSIYENIKFGKEDATREDvkRACKFAAIDEF--IESLpnkyd 1347
Cdd:TIGR02142 52 GEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFpHLSVRGNLRYGMKRARPSE--RRISFERVIELlgIGHL----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1348 tnVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKI 1426
Cdd:TIGR02142 125 --LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRV 202
|
170 180
....*....|....*....|....
gi 221056887 1427 VVFNNpdrtGSfVQAEGTHEELLS 1450
Cdd:TIGR02142 203 VVLED----GR-VAAAGPIAEVWA 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
383-639 |
1.58e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 80.98 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIINdSHNL-----KD 452
Cdd:PRK14239 6 LQVSDLSVYYNKKKAL---NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYN-GHNIysprtDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 453 INLkwwRSKIGVVSQDPLLFSNSIKNNIKYSLY--SLKDLEYLsDQLNEDgsasqdgldkrnscrakcagdlndmmkttd 530
Cdd:PRK14239 82 VDL---RKEIGMVFQQPNPFPMSIYENVVYGLRlkGIKDKQVL-DEAVEK------------------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 531 sdglihARKNYNIIDdsEVvnvskKVLIHDfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:PRK14239 128 ------SLKGASIWD--EV-----KDRLHD---------------SALGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
250 260
....*....|....*....|....*....
gi 221056887 611 DNKSEYLVQKTINNLKgneNRITIIIAHR 639
Cdd:PRK14239 180 DPISAGKIEETLLGLK---DDYTMLLVTR 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
383-645 |
1.71e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.45 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTR----------KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKD 452
Cdd:PRK15079 9 LEVADLKVHFDIKdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL-GKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 453 INLKWW---RSKIGVVSQDPLlfsnsiknnikyslyslkdleylsdqlnedgsASqdgldkrnscrakcagdLNDMMKTT 529
Cdd:PRK15079 88 MKDDEWravRSDIQMIFQDPL--------------------------------AS-----------------LNPRMTIG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 530 DsdglIHA---RKNYNIIDDSEVVNVSKKVLIHdfVSALPDkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEA 606
Cdd:PRK15079 119 E----IIAeplRTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 221056887 607 TSSLDNKSEYLVqktINNLKG--NENRITII-IAHRLSTIRY 645
Cdd:PRK15079 189 VSALDVSIQAQV---VNLLQQlqREMGLSLIfIAHDLAVVKH 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1274-1430 |
1.89e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.85 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDlRNLfSIVSQEPILF-NMSIYENIKFG-------KEDaTREDVKRACKFAAIDEFIESlpnk 1345
Cdd:PRK11432 60 EGQIFIDGEDVTHRSIQQ-RDI-CMVFQSYALFpHMSLGENVGYGlkmlgvpKEE-RKQRVKEALELVDLAGFEDR---- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1346 ydtnvgpYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAH-RIASIKRSD 1424
Cdd:PRK11432 133 -------YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHdQSEAFAVSD 205
|
....*.
gi 221056887 1425 KIVVFN 1430
Cdd:PRK11432 206 TVIVMN 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1319-1416 |
2.16e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1319 EDATREDVKRACKFAAIDEFIESLpnkyDTnVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG4178 453 EAFSDAELREALEAVGLGHLAERL----DE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL 527
|
90
....*....|....*...
gi 221056887 1399 IVDIKDKAdrTIITIAHR 1416
Cdd:COG4178 528 LREELPGT--TVISVGHR 543
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1357-1431 |
2.65e-16 |
|
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: 77.85 E-value: 2.65e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLDSN-SEKLIeKTIVDIKDKaDRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERLF-KVIRRLRAQ-GVAVIFISHRLDEVFEiADRVTVLRD 157
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1275-1429 |
3.91e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.89 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1275 GKILLDGVDI--CDYNLKDLRNLFSIVSQEPILF-NMSIYENIKFG--------KEDATREDVKRACKFAAIDEFIESLP 1343
Cdd:PRK14267 64 GEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFpHLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1344 NKYDTNvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDRTIITIAHRIASIKRS 1423
Cdd:PRK14267 144 NDYPSN-------LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARV 214
|
....*.
gi 221056887 1424 DKIVVF 1429
Cdd:PRK14267 215 SDYVAF 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
61-307 |
3.92e-16 |
|
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: 80.67 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 61 LLGVSFVCATISGGSLPFFVSV---FGVIMKNMNLgenVDDIIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFL 137
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLlidDVIPAGDLSL---LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 138 KSVFYQDGQFHDNNP-G---SKLTSDLDfyleQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYIC 213
Cdd:cd07346 80 RHLQRLSLSFFDRNRtGdlmSRLTSDVD----AVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 214 GVICNKKAK-----INKKTSLLYNNntmsiIEEALVGIRTVVSYCGEHTILKKFNLSEKLYSKYMLKANFMESLHIGMIN 288
Cdd:cd07346 156 LRYFRRRIRkasreVRESLAELSAF-----LQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIG 230
|
250
....*....|....*....
gi 221056887 289 GFILASYAFGFWYGTRIII 307
Cdd:cd07346 231 LLTALGTALVLLYGGYLVL 249
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
381-656 |
4.05e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 4.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 381 KKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS 460
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPllfsnsiknnikyslyslkDLEYLSDQLNEDGSAsqdGLDKRNSCRakcagdlNDMMKTTDSDGLiharkn 540
Cdd:PRK13642 82 KIGMVFQNP-------------------DNQFVGATVEDDVAF---GMENQGIPR-------EEMIKRVDEALL------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddsevvnvskKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13642 127 --------------AVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
250 260 270
....*....|....*....|....*....|....*.
gi 221056887 621 TINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGE 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
403-614 |
4.85e-16 |
|
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: 81.69 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-----DSHnlKDINLKWWRSKIGVVSQDPLLFSN-SI 476
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqDSA--RGIFLPPHRRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 477 KNNIKYSLyslkdleylsdqlnedgsasqdgldkRNSCRAKCAGDLNDmmkttdsdgliharknynIIDdsevvnvskkV 556
Cdd:COG4148 95 RGNLLYGR--------------------------KRAPRAERRISFDE------------------VVE----------L 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 557 L-IhdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:COG4148 121 LgI-----------GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1291-1431 |
4.97e-16 |
|
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: 78.91 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1291 DLRNLFSIV--SQEPILFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIA 1368
Cdd:cd03290 74 RSRNRYSVAyaAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVA 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 1369 RALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKD 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1273-1459 |
5.05e-16 |
|
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: 79.12 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 NSGKILLDGVDICDYNLKDLRNL-FSIVSQEPILF-NMSIYENIKFGKEDATREDVKRACKFAA-IDEF-IESLPNKYdt 1348
Cdd:cd03218 53 DSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEElLEEFhITHLRKSK-- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1349 nvgpyGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK------AD---RTIITIAHRiAS 1419
Cdd:cd03218 131 -----ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRgigvliTDhnvRETLSITDR-AY 204
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 221056887 1420 IKRSDKIVvfnnpdrtgsfvqAEGTHEELLSVQDgVYKKY 1459
Cdd:cd03218 205 IIYEGKVL-------------AEGTPEEIAANEL-VRKVY 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
395-638 |
5.51e-16 |
|
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: 78.85 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDIIINDSHNLKDInlkwWRSKIGVVSQDPLL 471
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQ----FQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 472 FSN-SIKNNIKYSLYSLkdLEYLSDQLNEDGSASQDGLdkrnscrakcaGDLNDmmkttdsdgliharknyniiddsevv 550
Cdd:cd03234 93 LPGlTVRETLTYTAILR--LPRKSSDAIRKKRVEDVLL-----------RDLAL-------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 551 nvskKVLIHDFVSALpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNEN 630
Cdd:cd03234 134 ----TRIGGNLVKGI---------------SGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL-ARRN 193
|
....*...
gi 221056887 631 RITIIIAH 638
Cdd:cd03234 194 RIVILTIH 201
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
396-643 |
6.68e-16 |
|
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: 78.03 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLkwwRSKIGVVSQDPLLFSNs 475
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA---LRRIGALIEAPGFYPN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 476 iknnikysLYSLKDLEYLSDQLnedgsasqdGLDKRNscrakcagdlndMMKTTDSDGLIHARKnyniiddsevvnvsKK 555
Cdd:cd03268 87 --------LTARENLRLLARLL---------GIRKKR------------IDEVLDVVGLKDSAK--------------KK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 556 VlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnrITII 635
Cdd:cd03268 124 V---------------------KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQG--ITVL 180
|
....*....
gi 221056887 636 IA-HRLSTI 643
Cdd:cd03268 181 ISsHLLSEI 189
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1164-1428 |
9.70e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.49 E-value: 9.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsRPNVPIYK----DLTFSCDSKKTTAIVGETGSGKSTVMsllmrfydlkndhhivfknEHTDDVNNEKK 1239
Cdd:PRK13641 3 IKFENVDYIY--SPGTPMEKkgldNISFELEEGSFVALVGHTGSGKSTLM-------------------QHFNALLKPSS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1240 eqgdeeqnvGMKNVNEFSLTKEGShgdnsavfknsgkilldgvdicDYNLKDLRNLFSIVSQ--EPILFNMSIYENIKFG 1317
Cdd:PRK13641 62 ---------GTITIAGYHITPETG----------------------NKNLKKLRKKVSLVFQfpEAQLFENTVLKDVEFG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 ------KEDATREDVKRACKFAAIDEfieSLPNKydtnvGPYgkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:PRK13641 111 pknfgfSEDEAKEKALKWLKKVGLSE---DLISK-----SPF--ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
250 260 270
....*....|....*....|....*....|....*...
gi 221056887 1392 EKLIEKTIVDIKdKADRTIITIAHRIASI-KRSDKIVV 1428
Cdd:PRK13641 181 RKEMMQLFKDYQ-KAGHTVILVTHNMDDVaEYADDVLV 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1162-1420 |
1.04e-15 |
|
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: 79.13 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1162 GKIEIMDVNFTYMSRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtddvnnekkeq 1241
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1242 gdeeqnvgmknvnefsltkegshgdnsavfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIK-FGKEd 1320
Cdd:cd03289 58 ---------------------------------GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLDpYGKW- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1321 aTREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03289 104 -SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK 182
|
250 260
....*....|....*....|
gi 221056887 1401 diKDKADRTIITIAHRIASI 1420
Cdd:cd03289 183 --QAFADCTVILSEHRIEAM 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
402-626 |
1.18e-15 |
|
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: 77.86 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKD---------INLKwwRSKIGVVSQdpllF 472
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDlaqaspreiLALR--RRTIGYVSQ----F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 473 SNSIKNnikyslysLKDLEYLSDQLNEDGSASQDGLDKrnscrakcAGDLndmmkttdsdgLihARKNyniiddsevvnv 552
Cdd:COG4778 102 LRVIPR--------VSALDVVAEPLLERGVDREEARAR--------AREL-----------L--ARLN------------ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 553 skkvlihdfvsaLPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
Cdd:COG4778 141 ------------LP---ERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1165-1460 |
1.24e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.55 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1165 EIMDVNFTYMSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHhivfknehtddvnnekkeqgde 1244
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSK---------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1245 eqnvgmknvnefsltkegshgdnsavFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILF-NMSIYENIKFGKEDATR 1323
Cdd:PRK14246 67 --------------------------IKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpHLSIYDNIAYPLKSHGI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 EDvKRACKfAAIDEFIESL---PNKYDTNVGPyGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:PRK14246 121 KE-KREIK-KIVEECLRKVglwKEVYDRLNSP-ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIT 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1401 DIKDKAdrTIITIAHRIASIKRSDKIVVFNnpdRTGSFVQAEGTHEELLSVQDGVYKKYV 1460
Cdd:PRK14246 198 ELKNEI--AIVIVSHNPQQVARVADYVAFL---YNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1164-1450 |
1.27e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 79.29 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsRPNVPIYK----DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydLKNDHHIVFKNEHTddVNNEKK 1239
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPFERralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL--LQPTSGTVTIGERV--ITAGKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1240 EQgdeeqnvgmknvnefsltkegshgdnsavfknsgkilldgvdicdyNLKDLRNLFSIVSQ--EPILFNMSIYENIKFG 1317
Cdd:PRK13634 77 NK----------------------------------------------KLKPLRKKVGIVFQfpEHQLFEETVEKDICFG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 KED--ATREDVKRACKfaaidEFIE--SLPNKYDTNvGPYgkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:PRK13634 111 PMNfgVSEEDAKQKAR-----EMIElvGLPEELLAR-SPF--ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 1394 LIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAEGTHEELLS 1450
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHK----GT-VFLQGTPREIFA 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
402-644 |
1.30e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.68 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKST----ILKLIerlydPTEGDIIINDS--HNLKDINLKWWRSKIGVVSQDPllfsNS 475
Cdd:PRK15134 303 KNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQplHNLNRRQLLPVRHRIQVVFQDP----NS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 476 iknnikyslyslkdleYLSDQLNedgsasqdgldkrnscrakcagdlndmMKTTDSDGL-IHARKNYNIIDDSEVVNVSK 554
Cdd:PRK15134 374 ----------------SLNPRLN---------------------------VLQIIEEGLrVHQPTLSAAQREQQVIAVME 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 555 KVLIHdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseylVQKTI-NNLKG--NENR 631
Cdd:PRK15134 411 EVGLD---PETRHRY-------PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT----VQAQIlALLKSlqQKHQ 476
|
250
....*....|....
gi 221056887 632 IT-IIIAHRLSTIR 644
Cdd:PRK15134 477 LAyLFISHDLHVVR 490
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
383-611 |
1.67e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.49 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRkdveiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-SHNLKDINlkwwRSK 461
Cdd:COG3840 2 LRLDDLTYRYGDF-----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPPA----ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIkyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdGL-IHARK 539
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNI----------------------------------------------------GLgLRPGL 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 540 NYNIIDDSEVVNVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG3840 101 KLTAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
383-611 |
2.48e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.69 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLKwwRSKI 462
Cdd:PRK11000 4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR-MNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQdpllfsnsiknniKYSLYSlkdleYLSdqlnedgsasqdgldkrnscrakcagdLNDMMkttdSDGLIHARKNYN 542
Cdd:PRK11000 78 GMVFQ-------------SYALYP-----HLS---------------------------VAENM----SFGLKLAGAKKE 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 543 IIDDSevVNVSKKVLihdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11000 109 EINQR--VNQVAEVL----------QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1352-1416 |
2.49e-15 |
|
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: 75.27 E-value: 2.49e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1352 PYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikdkADRTIITIAHR 1416
Cdd:cd03223 87 PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE----LGITVISVGHR 147
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1299-1450 |
2.50e-15 |
|
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: 79.37 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1299 VSQEPILF-NMSIYENIKFGKEDATREDvkRACKFAAIDEF--IESLPNKYDTNvgpygksLSGGQKQRVAIARALLREP 1375
Cdd:COG4148 82 VFQEARLFpHLSVRGNLLYGRKRAPRAE--RRISFDEVVELlgIGHLLDRRPAT-------LSGGERQRVAIGRALLSSP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1376 KILLLDEATSSLD--SNSEKL--IEKtivdIKDKADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAEGTHEELLS 1450
Cdd:COG4148 153 RLLLMDEPLAALDlaRKAEILpyLER----LRDELDIPILYVSHSLDEVARlADHVVLLEQ----GR-VVASGPLAEVLS 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1164-1455 |
3.19e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.83 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekkeqgd 1243
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnEFSltkegshgdnsavfknsGKILLDGVDICDYNLKDLRNLFSIVSQEP--ILFNMSIYENIKFGKEDa 1321
Cdd:PRK13642 59 -----------EFE-----------------GKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDDVAFGMEN- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1322 trEDVKRACKFAAIDEFIESLpNKYDTNVGPYGKsLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PRK13642 110 --QGIPREEMIKRVDEALLAV-NMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 221056887 1402 IKDKADRTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAEGTHEELLSVQDGV 1455
Cdd:PRK13642 186 IKEKYQLTVLSITHDLDEAASSDRILVM----KAGEIIKEAAPSELFATSEDMV 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
383-649 |
3.49e-15 |
|
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: 75.98 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWwRSKI 462
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG-EPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSNsiknnikyslysLKDLEYLsdqlneDGSASQDGLDKRnscrakcAGDLNDMMKTTDSDGLIHARknyn 542
Cdd:COG4133 78 AYLGHADGLKPE------------LTVRENL------RFWAALYGLRAD-------REAIDEALEAVGLAGLADLP---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iiddsevvnvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:COG4133 129 ----------------------------------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
250 260
....*....|....*....|....*..
gi 221056887 623 NNLKGNeNRITIIIAHRLSTIRYANTI 649
Cdd:COG4133 175 AAHLAR-GGAVLLTTHQPLELAAARVL 200
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1175-1401 |
5.01e-15 |
|
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: 75.59 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1175 SRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqgdeeqnvgmknvn 1254
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA----------------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1255 efsltkegshGDNSAVfknSGKILLDGVDIcDYNLKDLRNLFSIVSQEPILF-NMSIYENIKF----GKEDATREDVKRA 1329
Cdd:COG4133 50 ----------GLLPPS---AGEVLWNGEPI-RDAREDYRRRLAYLGHADGLKpELTVRENLRFwaalYGLRADREAIDEA 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 1330 CKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:COG4133 116 LEAVGLAGLADLPV-----------RQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1274-1417 |
5.14e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.20 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDIcDYNLKDLRNL---FSIVSQEP--ILFNMSIYENIKFG------KEDATREDVKRACKFAAIdefiESL 1342
Cdd:PRK13636 60 SGRILFDGKPI-DYSRKGLMKLresVGMVFQDPdnQLFSASVYQDVSFGavnlklPEDEVRKRVDNALKRTGI----EHL 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1343 PNKydtnvgPyGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRI 1417
Cdd:PRK13636 135 KDK------P-THCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDI 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1274-1453 |
5.16e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.15 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNLFSIVSQEP--ILFNMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLPNK 1345
Cdd:PRK13652 58 SGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPHH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1346 ydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASI-KRSD 1424
Cdd:PRK13652 138 -----------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMAD 206
|
170 180
....*....|....*....|....*....
gi 221056887 1425 KIVVFNNpdrtGSFVqAEGTHEELLSVQD 1453
Cdd:PRK13652 207 YIYVMDK----GRIV-AYGTVEEIFLQPD 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1152-1448 |
5.78e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.34 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1152 IRIKN-TNDIDGKIEIMDVNFTymsrpnvpIYKDLTFscdskkttAIVGETGSGKSTVMSLLMRFydlkndhhivfkneh 1230
Cdd:PRK11607 20 LEIRNlTKSFDGQHAVDDVSLT--------IYKGEIF--------ALLGASGCGKSTLLRMLAGF--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1231 tddvnnekkeqgdeEQnvgmknvnefsltkegshgdnsavfKNSGKILLDGVDICDynLKDLRNLFSIVSQEPILF-NMS 1309
Cdd:PRK11607 69 --------------EQ-------------------------PTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFpHMT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1310 IYENIKFG-KEDATRED-----VKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEA 1383
Cdd:PRK11607 108 VEQNIAFGlKQDKLPKAeiasrVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEP 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1384 TSSLDSNSEKLIEKTIVDIKDKADRTIITIAH-RIASIKRSDKIVVFNNpdrtGSFVQAeGTHEEL 1448
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNR----GKFVQI-GEPEEI 237
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1274-1427 |
6.12e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEdaTREDVKRACKFAA-IDEFieSLPNK-YDTNVg 1351
Cdd:PRK10247 61 SGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFPWQ--IRNQQPDPAIFLDdLERF--ALPDTiLTKNI- 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1352 pygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKRSDKIV 1427
Cdd:PRK10247 136 ---AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
329-664 |
6.40e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.85 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 329 LGVLISMFmltivlPNITEYMKSLEATNSLYEIINRKPLVENNNDGKKLKDIKKIQFKNVRFHydTRKDVEIYKDLNFTL 408
Cdd:COG4178 315 LSWFVDNY------QSLAEWRATVDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTLR--TPDGRPLLEDLSLSL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 409 TEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwRSKIGVVSQDPllfsnsiknnikyslY--- 485
Cdd:COG4178 387 KPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA------------GARVLFLPQRP---------------Ylpl 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 486 -SLKDleylsdQLnedgsasqdgldkrnsCRAKCAGDlndmmkttdsdgliharknyniIDDSEVVNVSKKVLIHDFVSA 564
Cdd:COG4178 440 gTLRE------AL----------------LYPATAEA----------------------FSDAELREALEAVGLGHLAER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 565 LpDkyetlVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN-LKGnenrITII-IAHRLS 641
Cdd:COG4178 476 L-D-----EEADWDQvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPG----TTVIsVGHRST 545
|
330 340
....*....|....*....|...
gi 221056887 642 TIRYANTIFVLSNREKGNRSTVD 664
Cdd:COG4178 546 LAAFHDRVLELTGDGSWQLLPAE 568
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1168-1428 |
7.03e-15 |
|
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: 74.51 E-value: 7.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1168 DVNFTYMSRP---NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqgde 1244
Cdd:cd03213 8 NLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1245 eqnvgMKNVNEfsltkegshgdnsavfKNSGKILLDGVDIcdyNLKDLRNLFSIVSQEPILF-NMSIYENIKFGkedatr 1323
Cdd:cd03213 57 -----GRRTGL----------------GVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHpTLTVRETLMFA------ 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 edvkrackfAAIdefieslpnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:cd03213 107 ---------AKL-------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA 158
|
250 260
....*....|....*....|....*..
gi 221056887 1404 DKAdRTIITIAHRIAS--IKRSDKIVV 1428
Cdd:cd03213 159 DTG-RTIICSIHQPSSeiFELFDKLLL 184
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1273-1448 |
7.52e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.82 E-value: 7.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 NSGKILLDGVDICDYNLKDLRNLFsiVSQEPILF-NMSIYENIKFG------KEDATREDVKRacKFAAIDEFI--ESLP 1343
Cdd:PRK10851 55 TSGHIRFHGTDVSRLHARDRKVGF--VFQHYALFrHMTVFDNIAFGltvlprRERPNAAAIKA--KVTQLLEMVqlAHLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1344 NKYDTNvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAH-RIASIKR 1422
Cdd:PRK10851 131 DRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHdQEEAMEV 203
|
170 180
....*....|....*....|....*.
gi 221056887 1423 SDKIVVFNNpdrtGSFVQAeGTHEEL 1448
Cdd:PRK10851 204 ADRVVVMSQ----GNIEQA-GTPDQV 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1274-1447 |
8.60e-15 |
|
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: 75.85 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNL-----FSIVSqepiLF-NMSIYENIKFG---------------------KEDATREDV 1326
Cdd:COG0411 58 SGRILFDGRDITGLPPHRIARLgiartFQNPR----LFpELTVLENVLVAaharlgrgllaallrlprarrEEREARERA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1327 KRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSN-SEKLIEkTIVDIKDK 1405
Cdd:COG0411 134 EELLERVGLADRADEPA-----------GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELAE-LIRRLRDE 201
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 221056887 1406 ADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAEGTHEE 1447
Cdd:COG0411 202 RGITILLIEHDMDLVMGlADRIVVLDF----GR-VIAEGTPAE 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
383-613 |
8.86e-15 |
|
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: 75.45 E-value: 8.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND----SHNLKDINlkww 458
Cdd:cd03296 3 IEVRNVSKRFGDFVALD---DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatDVPVQERN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 459 rskIGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEylsdqlnedgSASQDGLDKRnscrakcAGDLNDMMKttdsdgliha 537
Cdd:cd03296 76 ---VGFVFQHYALFRHmTVFDNVAFGLRVKPRSE----------RPPEAEIRAK-------VHELLKLVQ---------- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 538 rknyniiddsevvnvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03296 126 ------------------------LDWLADRY-------PAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
385-654 |
8.93e-15 |
|
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: 74.51 E-value: 8.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 385 FKNVRF---HYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI--ERLYDPTEGDIIINDshnlKDINLKWWR 459
Cdd:cd03213 6 FRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING----RPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQDPLLFSN-SIKNNIKYSlyslkdleylsdqlnedgsasqdgldkrnscrAKCAGdlndmmkttdsdglihar 538
Cdd:cd03213 82 KIIGYVPQDDILHPTlTVRETLMFA--------------------------------AKLRG------------------ 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 539 knyniiddsevvnvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:cd03213 112 -----------------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
250 260 270
....*....|....*....|....*....|....*...
gi 221056887 619 QKTINNLkGNENRITIIIAHRLSTIRYA--NTIFVLSN 654
Cdd:cd03213 151 MSLLRRL-ADTGRTIICSIHQPSSEIFElfDKLLLLSQ 187
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1267-1450 |
9.46e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.15 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1267 NSAVFKNSGKILLDGVDICDYNLKDLRNL----FSIVSQE-PILFNMSIYENIKFGKEDA------TREDVKRACKFAAI 1335
Cdd:PRK10070 75 NRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSfALMPHMTVLDNTAFGMELAginaeeRREKALDALRQVGL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1336 DEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAH 1415
Cdd:PRK10070 155 ENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISH 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 221056887 1416 RIASIKR-SDKIVVFNNpdrtGSFVQAeGTHEELLS 1450
Cdd:PRK10070 224 DLDEAMRiGDRIAIMQN----GEVVQV-GTPDEILN 254
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
383-658 |
9.76e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.60 E-value: 9.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVE---IYkDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDINLK 456
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErraLY-DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErviTAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 457 WWRSKIGVVSQDP--LLFSNSIknnikyslysLKDLeylsdqlnedgsasqdgldkrnscrakCAGDLNDMMKttDSDGL 534
Cdd:PRK13634 82 PLRKKVGIVFQFPehQLFEETV----------EKDI---------------------------CFGPMNFGVS--EEDAK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 535 IHARKNYniiddsEVVNVSKKVLIHD-FvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK13634 123 QKAREMI------ELVGLPEELLARSpF-----------------ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 221056887 614 SEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLsnrEKG 658
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAaRYADQIVVM---HKG 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
383-644 |
1.09e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 75.43 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH-------NLKDINL 455
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkpSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 456 kwWRSKIGVVSQdpllfsnsiknniKYSLYS-LKDLEylsdqlnedgsasqdgldkrNSCRAKCagdlnDMMKTTDSDGL 534
Cdd:COG4161 80 --LRQKVGMVFQ-------------QYNLWPhLTVME--------------------NLIEAPC-----KVLGLSKEQAR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 535 IHARKnyniiddsevvnVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:COG4161 120 EKAMK------------LLARLRLTDKADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
250 260 270
....*....|....*....|....*....|.
gi 221056887 615 EYLVQKTINNLKGNEnrIT-IIIAHRLSTIR 644
Cdd:COG4161 177 TAQVVEIIRELSQTG--ITqVIVTHEVEFAR 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
383-658 |
1.18e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVE--IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND------SHNlKDIn 454
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstSKN-KDI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 455 lKWWRSKIGVVSQDP--LLFSNSIknnikyslysLKDLEYlsdqlnedgsasqdgldkrnscrakcaGDLNDMMKTTDSD 532
Cdd:PRK13649 81 -KQIRKKVGLVFQFPesQLFEETV----------LKDVAF---------------------------GPQNFGVSQEEAE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 533 GLihARKNYNIIDDSevvnvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
Cdd:PRK13649 123 AL--AREKLALVGIS----------------------ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 221056887 613 KSEYLVQKTINNLkgNENRITIIIAHRL--STIRYANTIFVLsnrEKG 658
Cdd:PRK13649 179 KGRKELMTLFKKL--HQSGMTIVLVTHLmdDVANYADFVYVL---EKG 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
383-613 |
1.27e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.57 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDInlKWWRSKI 462
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHV--PPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSN-SIKNNIKYSLyslkdleylsdqlnedgsaSQDGLDKrnscrAKCAGDLNDMMkttdsdGLIHarkny 541
Cdd:PRK11607 94 NMMFQSYALFPHmTVEQNIAFGL-------------------KQDKLPK-----AEIASRVNEML------GLVH----- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 542 niiddsevvnvskkvlIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK11607 139 ----------------MQEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
78-308 |
2.36e-14 |
|
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: 75.55 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 78 FFVSVFGVIMKNMnLGENVDDII------------FSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDG 145
Cdd:cd18542 9 LLATALNLLIPLL-IRRIIDSVIggglrellwllaLLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 146 QFHDNNP-G---SKLTSDLDfyleQVNAGIGTKFLTIFtYTSAFLGLYFWSLFK-NARLTLCVTCVFPLIYICGVICNKK 220
Cdd:cd18542 88 SFHDKARtGdlmSRCTSDVD----TIRRFLAFGLVELV-RAVLLFIGALIIMFSiNWKLTLISLAIIPFIALFSYVFFKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 221 A-----KINKKTSLLynnNTMsiIEEALVGIRTVVSYCGEHTILKKFNLSEKLYSKYMLKANFMESLHIGMINGFILASY 295
Cdd:cd18542 163 VrpafeEIREQEGEL---NTV--LQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQI 237
|
250
....*....|...
gi 221056887 296 AFGFWYGTRIIIS 308
Cdd:cd18542 238 VLVLWVGGYLVIN 250
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
383-652 |
2.77e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.12 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHY-DTRKDVEIY--KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWR 459
Cdd:PRK13633 5 IKCKNVSYKYeSNEESTEKLalDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQDPllfSNSIKNNIkyslyslkdleylsdqLNEDGSASQDGLdkrnscrakcaGDLNDMMKTTDSDGLihark 539
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVATI----------------VEEDVAFGPENL-----------GIPPEEIRERVDESL----- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 540 nyniiddsevvnvsKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:PRK13633 130 --------------KKVGMYEYRRHAP-----------HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVV 184
|
250 260 270
....*....|....*....|....*....|...
gi 221056887 620 KTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:PRK13633 185 NTIKELNKKYGITIILITHYMEEAVEADRIIVM 217
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
383-645 |
3.58e-14 |
|
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: 74.46 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDT------RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDIN 454
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 455 LKWWRSKIGVVSQDPLLFSN---SIKNNIKYSLYSLKDLEylsdqlnedgsasqdgldkrNSCRAKCAGDLNDMMKTTDS 531
Cdd:TIGR02769 83 RRAFRRDVQLVFQDSPSAVNprmTVRQIIGEPLRHLTSLD--------------------ESEQKARIAELLDMVGLRSE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 532 dgliHARKnyniiddsevvnvskkvlihdfvsaLPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:TIGR02769 143 ----DADK-------------------------LP-----------RQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
250 260 270
....*....|....*....|....*....|....
gi 221056887 612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAYLFITHDLRLVQS 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1171-1431 |
3.90e-14 |
|
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: 78.03 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1171 FTYMSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqGDEEQNVGM 1250
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM----------------------------GELEPSEGK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1251 knvnefsltkegshgdnsavFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPILFNMSIYENIKFG-KEDATR-EDVKR 1328
Cdd:TIGR01271 483 --------------------IKHSGRI-------------------SFSPQTSWIMPGTIKDNIIFGlSYDEYRyTSVIK 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1329 ACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdIKDKADR 1408
Cdd:TIGR01271 524 ACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCL-CKLMSNK 599
|
250 260
....*....|....*....|...
gi 221056887 1409 TIITIAHRIASIKRSDKIVVFNN 1431
Cdd:TIGR01271 600 TRILVTSKLEHLKKADKILLLHE 622
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
371-611 |
4.08e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.53 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 371 NNDGKKLKDIKKiqfknvRFHYDTRKDveiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNL 450
Cdd:PRK11432 3 QKNFVVLKNITK------RFGSNTVID-----NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-DGEDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 451 KDINLKwwRSKIGVVSQDPLLFSN-SIKNNIKyslYSLKDLEYLSDQLNEdgsasqdgldkrnscRAKCAGDLNDMmktt 529
Cdd:PRK11432 71 THRSIQ--QRDICMVFQSYALFPHmSLGENVG---YGLKMLGVPKEERKQ---------------RVKEALELVDL---- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 530 dsdgliharknyniiddsevvnvskkvlihdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSS 609
Cdd:PRK11432 127 ---------------------------------AGFEDRY-------VDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
..
gi 221056887 610 LD 611
Cdd:PRK11432 167 LD 168
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1164-1448 |
4.47e-14 |
|
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: 72.92 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnVGMknvnefsltkegshgdnsaVFKNSGKILLDGVDIcDYNLKDLRNLFSIVSQEPILF-NMSIYENIKF------ 1316
Cdd:cd03263 49 ----TGE-------------------LRPTSGTAYINGYSI-RTDRKAARQSLGYCPQFDALFdELTVREHLRFyarlkg 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1317 ---GKEDATREDVKRACKfaaidefiesLPNKYDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:cd03263 105 lpkSEIKEEVELLLRVLG----------LTDKANKRA----RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1394 LIEKTIVDIkdKADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAEGTHEEL 1448
Cdd:cd03263 171 AIWDLILEV--RKGRSIILTTHSMDEAEAlCDRIAIMSD----GK-LRCIGSPQEL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1196-1428 |
4.78e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.60 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1196 AIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtddvnnekkeQGDEeqnvgmknvnefsltkegshgdnsavfknsG 1275
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLY------------------------QPDS------------------------------G 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1276 KILLDG--VDIcdYNLKDLRNLfSI--VSQEPILF-NMSIYENIKFGKEDATREDVKRAckfAAIDEfIESLPNKYDTNV 1350
Cdd:COG3845 61 EILIDGkpVRI--RSPRDAIAL-GIgmVHQHFMLVpNLTVAENIVLGLEPTKGGRLDRK---AARAR-IRELSERYGLDV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1351 GPYGK--SLSGGQKQRVAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKDkADRTIITIAHRIASIKR-SDKI 1426
Cdd:COG3845 134 DPDAKveDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE-ILRRLAA-EGKSIIFITHKLREVMAiADRV 211
|
..
gi 221056887 1427 VV 1428
Cdd:COG3845 212 TV 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
383-664 |
5.59e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.20 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-SHNLKDINLKWWRSK 461
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSNsiknnikyslysLKDLEylsdqlnedgsasqdgldkrnscrakcagdlNDMMkttdsdGLIHARKny 541
Cdd:PRK09493 79 AGMVFQQFYLFPH------------LTALE-------------------------------NVMF------GPLRVRG-- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 niiddsevvnvSKKVLIHDFVSALPDKyetlVGSNA------SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK09493 108 -----------ASKEEAEKQARELLAK----VGLAErahhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 221056887 616 YLVQKTINNLkGNENRITIIIAHRLSTIRYANT--IFVlsnrEKGnRSTVD 664
Cdd:PRK09493 173 HEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASrlIFI----DKG-RIAED 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
383-652 |
8.00e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEI--YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH---NLKDINLKW 457
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 458 WRSKIGVVSQDP--LLFSNSIknnikyslysLKDLEYlsdqlnedgsasqdgldkrnscrakcaGDLNdmMKTTDSDGLI 535
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTV----------LKDVEF---------------------------GPKN--FGFSEDEAKE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 536 HARKNYniiddsevvnvsKKVlihdfvsALPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK13641 124 KALKWL------------KKV-------GLS---EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
250 260 270
....*....|....*....|....*....|....*...
gi 221056887 616 YLVQKTINNLKgNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK13641 182 KEMMQLFKDYQ-KAGHTVILVTHNMDDVaEYADDVLVL 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
383-656 |
8.20e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.57 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDIN--LKWWRS 460
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGEPIKYDKksLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDP--LLFSNSIKNNIKYSLYSLKdleylsdqlnedgsASQDGLDKRnscrakcagdlndmmkttdsdglihar 538
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGPLNLG--------------LSKEEVEKR--------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 539 knyniiddseVVNVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:PRK13639 118 ----------VKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQI 176
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 221056887 619 QKTINNLkgNENRITIIIA-HRLSTI-RYANTIFVLSNRE 656
Cdd:PRK13639 177 MKLLYDL--NKEGITIIIStHDVDLVpVYADKVYVMSDGK 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1164-1419 |
9.43e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 72.74 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPnvpIYKDLTFSCDSKKTTAIVGETGSGKST---VMSLLmrfyDLKNDHHIVFKNEHTDDVNNEKKE 1240
Cdd:PRK11124 3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLL----EMPRSGTLNIAGNHFDFSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1241 QGDE-EQNVGMknvnefsltkegshgdnsaVFKNsgkilldgvdicdYNLkdlrnlfsivsqEPilfNMSIYENI----- 1314
Cdd:PRK11124 76 AIRElRRNVGM-------------------VFQQ-------------YNL------------WP---HLTVQQNLieapc 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1315 ---KFGKEDAtredVKRACKFAA---IDEFIESLPnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11124 109 rvlGLSKDQA----LARAEKLLErlrLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 221056887 1389 SNseklIEKTIVDIKDKADRTIIT---------IAHRIAS 1419
Cdd:PRK11124 174 PE----ITAQIVSIIRELAETGITqvivtheveVARKTAS 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1164-1420 |
9.68e-14 |
|
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: 72.81 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlknDHHIVFKNEHTddvnnekkeqgd 1243
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG------DLPPTYGNDVR------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdnsaVFknsGKILlDGVDIcdynlKDLRNLFSIVS---QEPILFNMSIYENI---KFG 1317
Cdd:COG1119 63 --------------------------LF---GERR-GGEDV-----WELRKRIGLVSpalQLRFPRDETVLDVVlsgFFD 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 K----EDATREDVKRAckFAAIDEF-IESLPNKydtnvgPYGkSLSGGQKQRVAIARALLREPKILLLDEATSSLD-SNS 1391
Cdd:COG1119 108 SiglyREPTDEQRERA--RELLELLgLAHLADR------PFG-TLSQGEQRRVLIARALVKDPELLILDEPTAGLDlGAR 178
|
250 260
....*....|....*....|....*....
gi 221056887 1392 EKLIEkTIVDIKDKADRTIITIAHRIASI 1420
Cdd:COG1119 179 ELLLA-LLDKLAAEGAPTLVLVTHHVEEI 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1274-1431 |
1.01e-13 |
|
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: 71.84 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKdLRNLFSIVSQEPILF-NMSIYENIKF----GKEDATREDvkrackfAAIDEFIEslpnkyDT 1348
Cdd:cd03264 53 SGTIRIDGQDVLKQPQK-LRRRIGYLPQEFGVYpNFTVREFLDYiawlKGIPSKEVK-------ARVDEVLE------LV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1349 NVGPYGK----SLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADRTIITIAHRIASIKRS- 1423
Cdd:cd03264 119 NLGDRAKkkigSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLc 196
|
....*...
gi 221056887 1424 DKIVVFNN 1431
Cdd:cd03264 197 NQVAVLNK 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1274-1462 |
1.30e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.80 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDIcDYNLKDL---RNLFSIVSQEP--ILFNMSIYENIKFG------KEDATREDVKRACKFAAIDEFIESL 1342
Cdd:PRK13639 56 SGEVLIKGEPI-KYDKKSLlevRKTVGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1343 PNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdRTIITIAHRIASI-K 1421
Cdd:PRK13639 135 PHH-----------LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVpV 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 221056887 1422 RSDKIVVFNNpdrtGSFVqAEGTHEELLSVQDGVYKKYVKL 1462
Cdd:PRK13639 203 YADKVYVMSD----GKII-KEGTPKEVFSDIETIRKANLRL 238
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1273-1418 |
1.32e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.05 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 NSGKILLDGVDICDYNLKD--LRNLFSIVSQEPILF-NMSIYENIKFGKEDatredVKRACKFAAIDEFIESLpnkydTN 1349
Cdd:PRK09493 54 TSGDLIVDGLKVNDPKVDErlIRQEAGMVFQQFYLFpHLTALENVMFGPLR-----VRGASKEEAEKQARELL-----AK 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1350 VG------PYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADR--TIITIAHRIA 1418
Cdd:PRK09493 124 VGlaerahHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP---ELRHEVLKVMQDLAEEgmTMVIVTHEIG 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1266-1450 |
1.55e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.82 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1266 DNSAVFKNSGKILLDGVDICDY-NLKDLRNLFSIVSQEPILFNMSIYENIKFGKedatredvkRACKFAAIDEFiESLPN 1344
Cdd:PRK14271 72 DKVSGYRYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGV---------RAHKLVPRKEF-RGVAQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1345 KYDTNVGPYGK----------SLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdrTIITIA 1414
Cdd:PRK14271 142 ARLTEVGLWDAvkdrlsdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVT 219
|
170 180 190
....*....|....*....|....*....|....*..
gi 221056887 1415 HRIASIKR-SDKIVVFNNpdrtGSFVQaEGTHEELLS 1450
Cdd:PRK14271 220 HNLAQAARiSDRAALFFD----GRLVE-EGPTEQLFS 251
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1184-1417 |
1.56e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.35 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1184 DLTFSCDSKKTTAIVGETGSGKSTVMS----LLMRFY------DLKNDHHIVFKNEhtddvnnekkeqgdeeqnvgmknv 1253
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYgtiqvgDIYIGDKKNNHEL------------------------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1254 nefsltkegshgdnsAVFKNSGKIlldgvdicdYNLKDLRNLFSIVSQEP--ILFNMSIYENIKFG-------KEDATRE 1324
Cdd:PRK13631 100 ---------------ITNPYSKKI---------KNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1325 DVKRACKFAAIDEFIEslpnkydtnVGPYGksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKd 1404
Cdd:PRK13631 156 AKFYLNKMGLDDSYLE---------RSPFG--LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK- 223
|
250
....*....|...
gi 221056887 1405 KADRTIITIAHRI 1417
Cdd:PRK13631 224 ANNKTVFVITHTM 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1274-1398 |
1.61e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.43 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICdyNLKDLR--NLFSIVSQEPIL---FNMSIYENI----KFGKedatREDVKRACKFAAIDEFIES--- 1341
Cdd:COG1101 60 SGSILIDGKDVT--KLPEYKraKYIGRVFQDPMMgtaPSMTIEENLalayRRGK----RRGLRRGLTKKRRELFRELlat 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 1342 ----LPNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLD-SNSEKLIEKT 1398
Cdd:COG1101 134 lglgLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpKTAALVLELT 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1181-1431 |
1.71e-13 |
|
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: 71.53 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1181 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtddvnnekkeqgdEEQNVGMKnvnefsltk 1260
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-----------------------------RVEGGGTT--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1261 egshgdnsavfknSGKILLDGVDICDYNLKDLrnlFSIVSQEPILF-NMSIYENIKFGKEDATREDVKRACKfAAIDEfI 1339
Cdd:cd03234 64 -------------SGQILFNGQPRKPDQFQKC---VAYVRQDDILLpGLTVRETLTYTAILRLPRKSSDAIR-KKRVE-D 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1340 ESLPNKYDTNVG-PYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADRTIITIAHRia 1418
Cdd:cd03234 126 VLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLA-RRNRIVILTIHQ-- 202
|
250
....*....|...
gi 221056887 1419 siKRSDKIVVFNN 1431
Cdd:cd03234 203 --PRSDLFRLFDR 213
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1153-1431 |
2.05e-13 |
|
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: 72.58 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1153 RIKNTNDiDGKIEIMDVN--FTYMSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneh 1230
Cdd:cd03291 23 KAKQENN-DRKHSSDDNNlfFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLIL----------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1231 tddvnnekkeqGDEEQNVGmknvnefsltkegshgdnsaVFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPILFNMSI 1310
Cdd:cd03291 85 -----------GELEPSEG--------------------KIKHSGRI-------------------SFSSQFSWIMPGTI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1311 YENIKFG-KEDATR-EDVKRACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:cd03291 115 KENIIFGvSYDEYRyKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 221056887 1389 SNSEKLIEKTIVdIKDKADRTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03291 192 VFTEKEIFESCV-CKLMANKTRILVTSKMEHLKKADKILILHE 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1308-1430 |
2.73e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1308 MSIYENIKFG-------KEDATREdVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLL 1380
Cdd:PRK11000 90 LSVAENMSFGlklagakKEEINQR-VNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 221056887 1381 DEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAH-RIASIKRSDKIVVFN 1430
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLD 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
383-654 |
3.73e-13 |
|
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: 70.00 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDInlkwwRSKI 462
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLFSN-SIKNNIKYsLYSLKDLEylsdqlnedgsasqdgldkrnscRAKCAGDLNDMMKTTDsdglIHARKNy 541
Cdd:cd03269 73 GYLPEERGLYPKmKVIDQLVY-LAQLKGLK-----------------------KEEARRRIDEWLERLE----LSEYAN- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 542 niiddsevvnvsKKVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03269 124 ------------KRV---------------------EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDV 170
|
250 260 270
....*....|....*....|....*....|....
gi 221056887 622 INNLKGNENRItIIIAHRLSTI-RYANTIFVLSN 654
Cdd:cd03269 171 IRELARAGKTV-ILSTHQMELVeELCDRVLLLNK 203
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1164-1449 |
3.82e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.88 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:COG4604 2 IEIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR----------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsLTKegshgdnsavfKNSGKILLDGVDICDYNLKDL-RNLfSIVSQEPIlFNM--SIYENIKFG--- 1317
Cdd:COG4604 50 --------------LLP-----------PDSGEVLVDGLDVATTPSRELaKRL-AILRQENH-INSrlTVRELVAFGrfp 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 --KEDATREDVkrackfAAIDEFI-----ESLPNKY-DTnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDS 1389
Cdd:COG4604 103 ysKGRLTAEDR------EIIDEAIayldlEDLADRYlDE--------LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 1390 NSEKLIEKTIVDIKDKADRTIITIAHRI--ASiKRSDKIVVFNNpdrtGSfVQAEGTHEELL 1449
Cdd:COG4604 169 KHSVQMMKLLRRLADELGKTVVIVLHDInfAS-CYADHIVAMKD----GR-VVAQGTPEEII 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
580-654 |
4.94e-13 |
|
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: 68.33 E-value: 4.94e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnenrITII-IAHRLSTIRYANTIFVLSN 654
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG-----ITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1184-1428 |
4.96e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 72.07 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1184 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegs 1263
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE---------------------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1264 hgdnsavfKNSGKILLDGVDICDYNLKDLRNL---FSIVSQEPilF---N--MSIYENIKFG---KEDATREDVKrackf 1332
Cdd:COG4608 70 --------PTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--YaslNprMTVGDIIAEPlriHGLASKAERR----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1333 AAIDEFIESlpnkydtnVG--P-----YGKSLSGGQKQRVAIARALLREPKILLLDEATSSLD-SnseklIEKTIV---- 1400
Cdd:COG4608 135 ERVAELLEL--------VGlrPehadrYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvS-----IQAQVLnlle 201
|
250 260
....*....|....*....|....*....
gi 221056887 1401 DIKDKADRTIITIAHRIASIKR-SDKIVV 1428
Cdd:COG4608 202 DLQDELGLTYLFISHDLSVVRHiSDRVAV 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1358-1432 |
5.68e-13 |
|
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: 70.16 E-value: 5.68e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1358 SGGQKQRVAIARALLREPKILLLDEATSSLDS-NSEKLIEKtIVDIKDkADRTIITIAHRIASIKR-SDKIVVFNNP 1432
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAaNRAVVVEL-IEEAKA-RGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
400-643 |
6.50e-13 |
|
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: 70.65 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNN 479
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQI-DGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 480 ikyslyslkdleylsdqlnedgsasqdgLDKrnscrakcagdlndmmkttdsdgliharknYNIIDDSEVVNVSKKVLIH 559
Cdd:cd03289 97 ----------------------------LDP------------------------------YGKWSDEEIWKVAEEVGLK 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTinnLKGNENRITIIIA-H 638
Cdd:cd03289 119 SVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKT---LKQAFADCTVILSeH 195
|
....*
gi 221056887 639 RLSTI 643
Cdd:cd03289 196 RIEAM 200
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
402-656 |
7.02e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.37 E-value: 7.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKW-WRSKIGVVSQDPLLFSN-SIK 477
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIAKISDAELREvRRKKIAMVFQSFALMPHmTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 478 NNIKYSLyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttDSDGLIHARKNYNIIDdsevvnVSKKVL 557
Cdd:PRK10070 125 DNTAFGM---------------------------------------------ELAGINAEERREKALD------ALRQVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 558 IHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
Cdd:PRK10070 154 LENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFIS 222
|
250 260
....*....|....*....|
gi 221056887 638 HRL-STIRYANTIFVLSNRE 656
Cdd:PRK10070 223 HDLdEAMRIGDRIAIMQNGE 242
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
397-656 |
7.22e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS-----HNLKDINLKWWRSKIGVVSQDPLL 471
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 472 FSN-SIKNNIKYSLyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharKNYNIIDDSEVV 550
Cdd:PRK14246 102 FPHlSIYDNIAYPL------------------------------------------------------KSHGIKEKREIK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 551 NVSKKVLIHdfVSALPDKYETLvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNEN 630
Cdd:PRK14246 128 KIVEECLRK--VGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK-NEI 203
|
250 260
....*....|....*....|....*.
gi 221056887 631 RITIIIAHRLSTIRYANTIFVLSNRE 656
Cdd:PRK14246 204 AIVIVSHNPQQVARVADYVAFLYNGE 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
402-611 |
7.38e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINLKWWRSKIGVVSQDPLLFSN---SI 476
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplAKLNRAQRKAFRRDIQMVFQDSISAVNprkTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 477 KNNIKYSLYSLKDLeylsdqlnedgsasqdglDKRNscRAKCAGDLNDMMKTTDSdgliHARKnyniiddsevvnvskkv 556
Cdd:PRK10419 109 REIIREPLRHLLSL------------------DKAE--RLARASEMLRAVDLDDS----VLDK----------------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 557 lihdfvsaLPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10419 148 --------RP-----------PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
868-1448 |
9.09e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 868 LYILVIAIAMFISETLKN-YYNNV--IGEKVEKTMKHRLFENILyqEISFFDQDCHAPGLLSSHINRDVHLLKtglvnNI 944
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESqYFQNVgrVGFRLRSTLVAAIFHKSL--RLTHEARKNFASGKVTNMITTDANALQ-----QI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 945 VIFTH--FIVLFIVSMIMSFYFCPIVAAVLTGTYFIFMRVFAIRARLSANKDVEKKGinqpgtvfLYNNDDEIFkdpsfL 1022
Cdd:PLN03232 415 AEQLHglWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEG--------LQWTDKRVG-----I 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1023 IQEAFYNMNTVIIYGLEDYFCKLIEkaidysnkgqkrkTLVNSMLWGFsQSAQLF--INSF----------AYWFGSFLI 1090
Cdd:PLN03232 482 INEILASMDTVKCYAWEKSFESRIQ-------------GIRNEELSWF-RKAQLLsaFNSFilnsipvvvtLVSFGVFVL 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1091 RRGTIEVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIMRKSNIDVRD------NGGIRIKNTNdidgki 1164
Cdd:PLN03232 548 LGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNpplqpgAPAISIKNGY------ 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1165 eimdvnFTYMSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqgde 1244
Cdd:PLN03232 622 ------FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML------------------------------- 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1245 eqnvgmknvnefsltKEGSHGDNSAVfknsgkilldgvdicdynlkDLRNLFSIVSQEPILFNMSIYENIKFGkEDATRE 1324
Cdd:PLN03232 665 ---------------GELSHAETSSV--------------------VIRGSVAYVPQVSWIFNATVRENILFG-SDFESE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1325 DVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNseklIEKTIVD--I 1402
Cdd:PLN03232 709 RYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH----VAHQVFDscM 784
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 221056887 1403 KDK-ADRTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAEGTHEEL 1448
Cdd:PLN03232 785 KDElKGKTRVLVTNQLHFLPLMDRIILVSE-----GMIKEEGTFAEL 826
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
383-644 |
9.96e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 9.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH-------NLKDINL 455
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 456 kwWRSKIGVVSQdpllfsnsiknniKYSLYSlkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmKTTDSDGLI 535
Cdd:PRK11124 80 --LRRNVGMVFQ-------------QYNLWP----------------------------------------HLTVQQNLI 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 536 HARKNYNIIDDSEVVNVSKKVL----IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11124 105 EAPCRVLGLSKDQALARAEKLLerlrLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
250 260 270
....*....|....*....|....*....|....
gi 221056887 612 NKSEYLVQKTINNLKgnENRIT-IIIAHRLSTIR 644
Cdd:PRK11124 174 PEITAQIVSIIRELA--ETGITqVIVTHEVEVAR 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1274-1388 |
1.20e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDiCDYNLKDLRNLfSIVSQEPILFN-MSIYENIKFGKE------DATREDVKRACKFAAIDEFIESLPNKy 1346
Cdd:PRK10771 53 SGSLTLNGQD-HTTTPPSRRPV-SMLFQENNLFShLTVAQNIGLGLNpglklnAAQREKLHAIARQMGIEDLLARLPGQ- 129
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 221056887 1347 dtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK10771 130 ----------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1183-1458 |
1.21e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 69.87 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1183 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgdeeqnVGMknvnefsltkeg 1262
Cdd:COG4167 30 KPVSFTLEAGQTLAIIGENGSGKSTLAKML-----------------------------------AGI------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1263 shgdnsaVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPilfNMSIYENIKFGK--EDATR-----EDVKRACKFAAI 1335
Cdd:COG4167 63 -------IEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP---NTSLNPRLNIGQilEEPLRlntdlTAEEREERIFAT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1336 DEFIESLPNKYDTnvgpYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAH 1415
Cdd:COG4167 133 LRLVGLLPEHANF----YPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 221056887 1416 RIASIKR-SDKIVVFNNpdrtGSFVQAEGTHEELLSVQDGVYKK 1458
Cdd:COG4167 209 HLGIVKHiSDKVLVMHQ----GEVVEYGKTAEVFANPQHEVTKR 248
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1163-1448 |
1.37e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.11 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1163 KIEIMDVNFTYmsRPNVPIY----KDLTFSCDSKKTTAIVGETGSGKSTV---MSLLMrfydLKNDHHI--VFKNEHTDD 1233
Cdd:PRK13651 2 QIKVKNIVKIF--NKKLPTElkalDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALL----LPDTGTIewIFKDEKNKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1234 VNNEKKEQGDEeqnvgmknvNEFSLTKegshgdnsavFKNSGKIlldgvdicdynlKDLRNLFSIVSQ--EPILFNMSIY 1311
Cdd:PRK13651 76 KTKEKEKVLEK---------LVIQKTR----------FKKIKKI------------KEIRRRVGVVFQfaEYQLFEQTIE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1312 ENIKFG-------KEDATredvKRACKFAAIDEFIESLPNKydtnvGPYGksLSGGQKQRVAIARALLREPKILLLDEAT 1384
Cdd:PRK13651 125 KDIIFGpvsmgvsKEEAK----KRAAKYIELVGLDESYLQR-----SPFE--LSGGQKRRVALAGILAMEPDFLVFDEPT 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1385 SSLDSNSEKLIEKtIVDIKDKADRTIITIAHRIASI-KRSDKIVVFNNpdrtGSFVQAEGTHEEL 1448
Cdd:PRK13651 194 AGLDPQGVKEILE-IFDNLNKQGKTIILVTHDLDNVlEWTKRTIFFKD----GKIIKDGDTYDIL 253
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1274-1428 |
1.52e-12 |
|
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: 68.55 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGkedATREDVKRACKFAAIDEFIESLpnkydtNVGPY 1353
Cdd:cd03266 59 AGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTARENLEYF---AGLYGLKGDELTARLEELADRL------GMEEL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1354 ----GKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADRTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03266 130 ldrrVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERlCDRVVV 208
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1292-1450 |
1.56e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1292 LRNLFSIVSQEPILFNMSIYENIKFGKE-DATRedVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRVAIARA 1370
Cdd:PLN03130 677 IRGTVAYVPQVSWIFNATVRDNILFGSPfDPER--YERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARA 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1371 LLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADRTIITiaHRIASIKRSDKIVVFNNpdrtgSFVQAEGTHEELL 1449
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVT--NQLHFLSQVDRIILVHE-----GMIKEEGTYEELS 827
|
.
gi 221056887 1450 S 1450
Cdd:PLN03130 828 N 828
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1193-1432 |
1.79e-12 |
|
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: 71.64 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1193 KTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsLTKegshgdnsavfk 1272
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLR-------------------------------------------LIP------------ 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 NSGKILLDGVDICDYNLKDLRNL---FSIVSQEPilFN-----MSIYENI-------KFGKEDATREDvkRACkfAAIDE 1337
Cdd:COG4172 338 SEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDP--FGslsprMTVGQIIaeglrvhGPGLSAAERRA--RVA--EALEE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1338 fieslpnkydtnVG--P-----YGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDsnseKLIEKTIVDI-KDKADRT 1409
Cdd:COG4172 412 ------------VGldPaarhrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQILDLlRDLQREH 475
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 221056887 1410 -----IIT--------IAHRIASIKRSdKIV-------VFNNP 1432
Cdd:COG4172 476 glaylFIShdlavvraLAHRVMVMKDG-KVVeqgpteqVFDAP 517
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1274-1448 |
1.87e-12 |
|
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: 68.32 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDL-RNLFSIVSQEPILF-NMSIYENIKFGKEdaTREDVKRAckfaaIDEFIESLPNKYDTNVG 1351
Cdd:TIGR03410 54 SGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFpRLTVEENLLTGLA--ALPRRSRK-----IPDEIYELFPVLKEMLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1352 PYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTII----------TIAHRIASIK 1421
Cdd:TIGR03410 127 RRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILlveqyldfarELADRYYVME 206
|
170 180
....*....|....*....|....*..
gi 221056887 1422 RsdkivvfnnpdrtGSFVqAEGTHEEL 1448
Cdd:TIGR03410 207 R-------------GRVV-ASGAGDEL 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
382-613 |
2.06e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.26 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrsk 461
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 igVVSQ-DP------LLFSNsiknnikYSLY---SLKD-LEYlsdqlnedgsasqdGLDKRNSCRAKcagdlndmmkttd 530
Cdd:PRK11650 67 --VVNElEPadrdiaMVFQN-------YALYphmSVREnMAY--------------GLKIRGMPKAE------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 531 sdglIHARknyniiddseVVNVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:PRK11650 111 ----IEER----------VAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNL 165
|
...
gi 221056887 611 DNK 613
Cdd:PRK11650 166 DAK 168
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
376-652 |
2.35e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 68.96 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 376 KLKDIKKIqfknvrFHYDTRKDVEIYKDLNFTLTEGKtyaFV---GESGCGKSTILKLIERLYDPTEGDIIINDshnlKD 452
Cdd:COG1101 3 ELKNLSKT------FNPGTVNEKRALDGLNLTIEEGD---FVtviGSNGAGKSTLLNAIAGSLPPDSGSILIDG----KD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 453 I-NLK-WWRSK-IGVVSQDPLL---FSNSIKNNIkyslySLkdleylsdqlnedgsAsqdglDKRNSCRakcagdlndmm 526
Cdd:COG1101 70 VtKLPeYKRAKyIGRVFQDPMMgtaPSMTIEENL-----AL---------------A-----YRRGKRR----------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 527 kttdsdGLIHArknyniiddsevVNVSKKVLIHDFVSA----LPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILI 602
Cdd:COG1101 114 ------GLRRG------------LTKKRRELFRELLATlglgLENRLDTKVGL----LSGGQRQALSLLMATLTKPKLLL 171
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 221056887 603 LDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
Cdd:COG1101 172 LDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEqALDYGNRLIMM 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
404-612 |
2.59e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.98 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSKIGVVSQDP-LLFSNSIKNNI 480
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsgHDITRLKNREVPFLRRQIGMIFQDHhLLMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 481 KYSLYSlkdleylsdqlnedGSASQDGLDKRNSCrakcagdlndmmkTTDSDGLIHARKNYNIiddsevvnvskkvlihd 560
Cdd:PRK10908 101 AIPLII--------------AGASGDDIRRRVSA-------------ALDKVGLLDKAKNFPI----------------- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221056887 561 fvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
Cdd:PRK10908 137 ------------------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1177-1450 |
2.93e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.10 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1177 PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnef 1256
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKIL-------------------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1257 sltkegsHGDNSAvfkNSGKILLDGVDICDYNLKD-LRNLFSIVSQEPILF-NMSIYENI-------KFG--KEDATRED 1325
Cdd:PRK11288 51 -------SGNYQP---DAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVpEMTVAENLylgqlphKGGivNRRLLNYE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1326 VKRacKFAAIDEFIEslPnkyDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDS-NSEKLIeKTIVDIKD 1404
Cdd:PRK11288 121 ARE--QLEHLGVDID--P---DTPL----KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLF-RVIRELRA 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 221056887 1405 KAdRTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQ-----AEGTHEELLS 1450
Cdd:PRK11288 189 EG-RVILYVSHRMEEIFAlCDAITVF----KDGRYVAtfddmAQVDRDQLVQ 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1308-1431 |
3.64e-12 |
|
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: 67.49 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1308 MSIYENIKFGKeDATREDVKRACKFAAIDEFIE--SLPNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATS 1385
Cdd:TIGR01184 69 LTVRENIALAV-DRVLPDLSKSERRAIVEEHIAlvGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 221056887 1386 SLDSNSEKLIEKTIVDIKDKADRTIITIAHRI-ASIKRSDKIVVFNN 1431
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVTVLMVTHDVdEALLLSDRVVMLTN 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1160-1431 |
3.94e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.61 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1160 IDGKIEIMDVNFTYmsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTvmsLLMRFydlkndhhivfknehtddvnnekk 1239
Cdd:PRK13647 1 MDNIIEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKST---LLLHL------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1240 eqgdeeqnvgmknvnefsltkegshgdNSAVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--ILFNMSIYENIKFG 1317
Cdd:PRK13647 52 ---------------------------NGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAFG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 ------KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:PRK13647 105 pvnmglDKDEVERRVEEALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 221056887 1392 EKLIeKTIVDIKDKADRTIITIAHRI-ASIKRSDKIVVFNN 1431
Cdd:PRK13647 174 QETL-MEILDRLHNQGKTVIVATHDVdLAAEWADQVIVLKE 213
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1196-1415 |
4.34e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.85 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1196 AIVGETGSGKSTVMSLLMrFYDLKNdhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegshgdnsavFKNSG 1275
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNALA-FRSPKG--------------------------------------------------VKGSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1276 KILLDGVDIcdyNLKDLRNLFSIVSQEPILF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIE--SLPNKYDTNVGP 1352
Cdd:TIGR00955 84 SVLLNGMPI---DAKEMRAISAYVQQDDLFIpTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1353 YG--KSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdRTIITIAH 1415
Cdd:TIGR00955 161 PGrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKG-KTIICTIH 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
396-611 |
6.29e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWRSKIGVVSQDPLLfS 473
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidTLSPGKLQALRRDIQFIFQDPYA-S 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 474 NSIKNNIKYSLyslkdLEYLSDQLNEDGSASQdgldKRNSCRAKCAGDLNDmmkttdsdgliHARKnyniiddsevvnvs 553
Cdd:PRK10261 414 LDPRQTVGDSI-----MEPLRVHGLLPGKAAA----ARVAWLLERVGLLPE-----------HAWR-------------- 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 554 kkvLIHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10261 460 ---YPHEF-------------------SGGQRQRICIARALALNPKVIIADEAVSALD 495
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1356-1429 |
6.55e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.10 E-value: 6.55e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 1356 SLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADRTIITIAHRIASIKRSDKIVVF 1429
Cdd:NF040873 119 ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
383-670 |
7.38e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLKWWRSKI 462
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE-VNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDP--LLFSNSIKNNIKyslYSLKDLEYLSDQLNEdgsasqdgldkrnscRAKCAGDLNDMMKTTDsdgliharkn 540
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVA---FGPVNMGLDKDEVER---------------RVEEALKAVRMWDFRD---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddsevvnvskKVLIHdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13647 134 --------------KPPYH--------------------LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 621 TINNLkgNENRITIIIA-HRLS-TIRYANTIFVLSN----REKGNRSTVDVDIIGE 670
Cdd:PRK13647 180 ILDRL--HNQGKTVIVAtHDVDlAAEWADQVIVLKEgrvlAEGDKSLLTDEDIVEQ 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
383-636 |
7.84e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.17 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDI-IINDSHNLKDINLK 456
Cdd:PRK14267 5 IETVNLRVYYG---SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVrLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 457 WWRSKIGVVSQDPLLFSN-SIKNNIKYSLyslkdleylsdQLNedgsasqdgldkrnscrakcagdlndmmkttdsdGLI 535
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHlTIYDNVAIGV-----------KLN----------------------------------GLV 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 536 HARKNYniidDSEVVNVSKKvlihdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK14267 117 KSKKEL----DERVEWALKK-------AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
250 260
....*....|....*....|.
gi 221056887 616 YLVQKTINNLKgneNRITIII 636
Cdd:PRK14267 186 AKIEELLFELK---KEYTIVL 203
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
62-291 |
7.94e-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: 67.81 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 62 LGVSFVCATISGGS---LPFFVS-VFGVIMKNMNLGENVD-----DIIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTL 132
Cdd:cd18547 1 LILVIILAIISTLLsvlGPYLLGkAIDLIIEGLGGGGGVDfsgllRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 133 KVE-FLK----SVFYqdgqFHDNNPG---SKLTSDLDfyleQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVT 204
Cdd:cd18547 81 RKDlFEKlqrlPLSY----FDTHSHGdimSRVTNDVD----NISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 205 CVFPLIYICGvicnkkAKINKKTSLLYNNNTMSI------IEEALVGIRTVVSYCGEHTILKKFN-LSEKLYsKYMLKAN 277
Cdd:cd18547 153 VTVPLSLLVT------KFIAKRSQKYFRKQQKALgelngyIEEMISGQKVVKAFNREEEAIEEFDeINEELY-KASFKAQ 225
|
250
....*....|....
gi 221056887 278 FMESLhIGMINGFI 291
Cdd:cd18547 226 FYSGL-LMPIMNFI 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1274-1448 |
1.09e-11 |
|
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: 65.85 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDI-CDynLKDLRNLFSIVSQEPILFN-MSIYENIK-FG-----KEDATREDVKRACKFAAIDEFIESLPNK 1345
Cdd:cd03265 54 SGRATVAGHDVvRE--PREVRRRIGIVFQDLSVDDeLTGWENLYiHArlygvPGAERRERIDELLDFVGLLEAADRLVKT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1346 YdtnvgpygkslSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASI-KRSD 1424
Cdd:cd03265 132 Y-----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCD 200
|
170 180
....*....|....*....|....
gi 221056887 1425 KIVVFNNpdrtGSFVqAEGTHEEL 1448
Cdd:cd03265 201 RVAIIDH----GRII-AEGTPEEL 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1159-1430 |
1.23e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1159 DIDGKIEIMDVNFTYMSRPNVPIY----KDLTFScdSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfknehtddv 1234
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFEFKalnnTSLTFK--KNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1235 nnekkeqGDEEQNVGMKNVNEfsltkegshgdnsavfknsgkilldgvdicdynLKDLRNLFSIVSQEP--ILFNMSIYE 1312
Cdd:PRK13645 71 -------GDYAIPANLKKIKE---------------------------------VKRLRKEIGLVFQFPeyQLFQETIEK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1313 NIKFGKED--ATREDVkrackFAAIDEFIE--SLPNKYdTNVGPYgkSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK13645 111 DIAFGPVNlgENKQEA-----YKKVPELLKlvQLPEDY-VKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 221056887 1389 SNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFN 1430
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMH 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
383-625 |
1.29e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKwwRSKI 462
Cdd:PRK13536 42 IDLAGVSKSY---GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA--RARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQdpllFSNSiknnikyslyslkDLEYlsdqlnedgsasqdgldkrnscrakcagdlndmmkTTDSDGLIHARknYN 542
Cdd:PRK13536 117 GVVPQ----FDNL-------------DLEF-----------------------------------TVRENLLVFGR--YF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 IIDDSEVVNVSKKVLihDFvSALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK13536 143 GMSTREIEAVIPSLL--EF-ARLESKADARV----SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL 215
|
...
gi 221056887 623 NNL 625
Cdd:PRK13536 216 RSL 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
366-640 |
1.32e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.83 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 366 PLVENNNDGKKLKDIKkiqfkNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDP--TEGD 441
Cdd:PRK09473 1 TVPLAQQQADALLDVK-----DLRVTFSTPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 442 IIINDSH--NLKDINLKWWRS-KIGVVSQDPLLfsnsiknnikyslySLKDLEYLSDQLNEDGSASQdGLDKRNScrakc 518
Cdd:PRK09473 76 ATFNGREilNLPEKELNKLRAeQISMIFQDPMT--------------SLNPYMRVGEQLMEVLMLHK-GMSKAEA----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 519 agdLNDMMKTTDSDGLIHARKNYNIIDdsevvnvskkvliHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNP 598
Cdd:PRK09473 136 ---FEESVRMLDAVKMPEARKRMKMYP-------------HEF-------------------SGGMRQRVMIAMALLCRP 180
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 221056887 599 KILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
383-638 |
2.11e-11 |
|
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: 68.29 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL--YDPTEGDIIINDSH------------ 448
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 449 ----------NLKDINLKWWRSkigvvsQDPLLFSNSIKNNI----KYSLYSLKD-LEYLSDQLNEDGSASQDGLDKrns 513
Cdd:TIGR03269 78 vgepcpvcggTLEPEEVDFWNL------SDKLRRRIRKRIAImlqrTFALYGDDTvLDNVLEALEEIGYEGKEAVGR--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 514 crakcAGDLNDMmkttdsdgliharknyniiddsevVNVSKKVLiHdfvsalpdkyetlvgsNASKLSGGQKQRISIARA 593
Cdd:TIGR03269 149 -----AVDLIEM------------------------VQLSHRIT-H----------------IARDLSGGEKQRVVLARQ 182
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 221056887 594 IIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
Cdd:TIGR03269 183 LAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
390-636 |
2.15e-11 |
|
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: 65.43 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 390 FHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinLKWWRSKIGVVSQDP 469
Cdd:cd03267 27 FKRKYR-EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--------LVPWKRRKKFLRRIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 470 LLFSNsiKNNIKYSLYSLKDLEYLSDQLNEDGSASQDGLDKrnscrakcagdLNDMMKTTDsdgliharknyniiddsev 549
Cdd:cd03267 98 VVFGQ--KTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDE-----------LSELLDLEE------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 550 vnvskkvlihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNE 629
Cdd:cd03267 146 ----------------------LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY--NR 201
|
....*..
gi 221056887 630 NRITIII 636
Cdd:cd03267 202 ERGTTVL 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
383-653 |
2.29e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.41 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS---HNLKDI-NLkww 458
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidYSRKGLmKL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 459 RSKIGVVSQDP--LLFSNSIKNNIKYSLYSLkdleylsdQLNEDgsasqdgldkrnscrakcagdlndmmkttdsdglih 536
Cdd:PRK13636 81 RESVGMVFQDPdnQLFSASVYQDVSFGAVNL--------KLPED------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 537 arknyniiddsEVVNVSKKVLIHDFVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:PRK13636 117 -----------EVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
250 260 270
....*....|....*....|....*....|....*....
gi 221056887 617 LVQKTINNLKgNENRITIIIA-HRLSTIR-YANTIFVLS 653
Cdd:PRK13636 179 EIMKLLVEMQ-KELGLTIIIAtHDIDIVPlYCDNVFVMK 216
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
397-654 |
2.38e-11 |
|
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: 65.04 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWW---RSKIGVVSQDPLLFS 473
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 474 NSIKNNIKYslyslkdleylsdqlnedGSASqdgldkrNSCRAKCAGDLNDMMKTTDsdgliharknyniiddsevvnvs 553
Cdd:cd03290 93 ATVEENITF------------------GSPF-------NKQRYKAVTDACSLQPDID----------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 554 kkvlihdfvsALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRI 632
Cdd:cd03290 125 ----------LLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRT 194
|
250 260
....*....|....*....|..
gi 221056887 633 TIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03290 195 LVLVTHKLQYLPHADWIIAMKD 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1196-1428 |
2.63e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1196 AIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegSHGDNSavfknsG 1275
Cdd:PRK13549 35 SLCGENGAGKSTLMKVLSGVY----------------------------------------------PHGTYE------G 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1276 KILLDGVDICDYNLKDL-RNLFSIVSQEPILF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLpnKYDTNVGPY 1353
Cdd:PRK13549 63 EIIFEGEELQASNIRDTeRAGIAIIHQELALVkELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATP 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1354 GKSLSGGQKQRVAIARALLREPKILLLDEATSSLdSNSEKLIEKTIV-DIKDKaDRTIITIAHRIASIKR-SDKIVV 1428
Cdd:PRK13549 141 VGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIIrDLKAH-GIACIYISHKLNEVKAiSDTICV 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1164-1431 |
2.66e-11 |
|
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: 64.55 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:cd03268 1 LKTNDLTKTYGKKRVL---DDISLHVKKGEIYGFLGPNGAGKTTTMKIIL------------------------------ 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefSLTKegshgdnsavfKNSGKILLDGVDICDyNLKDLRNLFSIVSqEPILF-NMSIYENIKFGkedAT 1322
Cdd:cd03268 48 -------------GLIK-----------PDSGEITFDGKSYQK-NIEALRRIGALIE-APGFYpNLTARENLRLL---AR 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1323 REDVKRAckfaAIDEFIE--SLPNKYDTNVGPYgkSLsgGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03268 99 LLGIRKK----RIDEVLDvvGLKDSAKKKVKGF--SL--GMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELIL 170
|
250 260 270
....*....|....*....|....*....|..
gi 221056887 1401 DIKDKAdRTIITIAHRIASI-KRSDKIVVFNN 1431
Cdd:cd03268 171 SLRDQG-ITVLISSHLLSEIqKVADRIGIINK 201
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1353-1396 |
2.77e-11 |
|
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: 65.15 E-value: 2.77e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 221056887 1353 YGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDS-NSEKLIE 1396
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAaTGEQIID 187
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1274-1450 |
2.82e-11 |
|
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: 65.00 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDL-----------RNLFSivsqepilfNMSIYENIKFG-----KEDATREDVKRACK-FAAID 1336
Cdd:COG0410 57 SGSIRFDGEDITGLPPHRIarlgigyvpegRRIFP---------SLTVEENLLLGayarrDRAEVRADLERVYElFPRLK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1337 EFIESLpnkydtnvgpyGKSLSGGQKQRVAIARALLREPKILLLDEATSSLdsnSEKLIEK---TIVDIKDKAdrtiITI 1413
Cdd:COG0410 128 ERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL---APLIVEEifeIIRRLNREG----VTI 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 221056887 1414 ------AHRIASIkrSDKIVVFnnpdRTGSFVqAEGTHEELLS 1450
Cdd:COG0410 190 llveqnARFALEI--ADRAYVL----ERGRIV-LEGTAAELLA 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1339-1388 |
2.89e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.82 E-value: 2.89e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 221056887 1339 IESLPNKYdtnvgPYgkSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11144 118 IEPLLDRY-----PG--SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
383-611 |
2.98e-11 |
|
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: 65.15 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDIN----LKW 457
Cdd:COG4181 9 IELRGLTKTVGTGaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG-QDLFALDedarARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 458 WRSKIGVVSQDPLLfsnsiknnikysLYSLKDLEYLSDQLNEDGsasqdgldkRNSCRAKCAGDLNDMmkttdsdGLIHa 537
Cdd:COG4181 88 RARHVGFVFQSFQL------------LPTLTALENVMLPLELAG---------RRDARARARALLERV-------GLGH- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 538 RknyniiddsevvnvskkvlihdfVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4181 139 R-----------------------LDHYP-----------AQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
65-309 |
3.06e-11 |
|
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: 66.03 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 65 SFVCATISGGS---LPFFVS--VFGVIMKNmnlgeNVDDI---IFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEF 136
Cdd:cd18572 1 AFVFLVVAALSelaIPHYTGavIDAVVADG-----SREAFyraVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 137 LKSVFYQDGQFHD-NNPG---SKLTSDLDfyleQVNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYI 212
Cdd:cd18572 76 FRSLLRQDIAFFDaTKTGeltSRLTSDCQ----KVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 213 cgvICNKKAKINKKTSLLYNN---NTMSIIEEALVGIRTVVSYCGEHTILKKFN-LSEKLYSKYMLKAnFMESLHIGMIN 288
Cdd:cd18572 152 ---ITKVYGRYYRKLSKEIQDalaEANQVAEEALSNIRTVRSFATEEREARRYErALDKALKLSVRQA-LAYAGYVAVNT 227
|
250 260
....*....|....*....|.
gi 221056887 289 GFILASYAFGFWYGTRIIISD 309
Cdd:cd18572 228 LLQNGTQVLVLFYGGHLVLSG 248
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
383-636 |
3.79e-11 |
|
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: 64.31 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDInlKWWRSKI 462
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPLLfsnsiknnikyslyslkdleylsdqlnEDGSASQDGLdkrnscrakcagdlndmmkttdsdgLIHARKnYN 542
Cdd:cd03265 76 GIVFQDLSV---------------------------DDELTGWENL-------------------------YIHARL-YG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iIDDSEVVNVSKKVLihDFVsALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03265 103 -VPGAERRERIDELL--DFV-GLLEAADRLV----KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
250
....*....|....
gi 221056887 623 NNLKgNENRITIII 636
Cdd:cd03265 175 EKLK-EEFGMTILL 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
398-652 |
3.80e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSN-SI 476
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 477 KNNIKYSL----YSLKDLEYLSDQLNedgsasqdgldkrnscrakCAGDLNdmmkttdsdgliharknyniiddsevvnv 552
Cdd:PRK15439 104 KENILFGLpkrqASMQKMKQLLAALG-------------------CQLDLD----------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 553 skkvlihdfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKtINNLKGNENR 631
Cdd:PRK15439 136 ----------------------SSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSR-IRELLAQGVG 192
|
250 260
....*....|....*....|..
gi 221056887 632 ItIIIAHRLSTIR-YANTIFVL 652
Cdd:PRK15439 193 I-VFISHKLPEIRqLADRISVM 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1179-1388 |
3.88e-11 |
|
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: 67.40 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1179 VPIYKDLTFSCDSKKTTAIVGETGSGKS-TVMSLLmrfydlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefs 1257
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL--------------------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1258 ltkeGSHGDNSAvfKNSGKILLDGVDICDYNLKDLRNL----FSIVSQEPilfnMS-----------IYENIKFgKEDAT 1322
Cdd:COG4172 58 ----RLLPDPAA--HPSGSILFDGQDLLGLSERELRRIrgnrIAMIFQEP----MTslnplhtigkqIAEVLRL-HRGLS 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1323 REDVKRACkfaaidefIESLpnkydTNVG---P------YGKSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:COG4172 127 GAAARARA--------LELL-----ERVGipdPerrldaYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1273-1382 |
4.06e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.67 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 NSGKILLDGVDICDYNLkDLRNLFSI--VSQEPILF-NMSIYENIK-----FGKEDATREDvkracKFAA-IDEF-IESL 1342
Cdd:COG1137 56 DSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFrKLTVEDNILavlelRKLSKKEREE-----RLEElLEEFgITHL 129
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 221056887 1343 PNKYdtnvgpyGKSLSGGQKQRVAIARALLREPKILLLDE 1382
Cdd:COG1137 130 RKSK-------AYSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
383-659 |
4.64e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.53 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDV--EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE-----GDIIINDSHNLKDInl 455
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEgkvtvGDIVVSSTSKQKEI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 456 KWWRSKIGVVSQDP--LLFSNSIknnikyslysLKDLEYLSDQLnedgsasqdGLDKRNSCRakcagdlndmmkttdsdg 533
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETV----------LKDVAFGPQNF---------GIPKEKAEK------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 534 lIHARKnyniiddSEVVNVSKkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK13643 123 -IAAEK-------LEMVGLAD-----EFWEKSP-----------FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 221056887 614 SEYLVQKTINNLKgNENRITIIIAHRLSTIR-YANTIFVLsnrEKGN 659
Cdd:PRK13643 179 ARIEMMQLFESIH-QSGQTVVLVTHLMDDVAdYADYVYLL---EKGH 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
390-653 |
5.42e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.64 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 390 FHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND--------------SHNLKDI-N 454
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitNPYSKKIkN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 455 LKWWRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKDleylsdqlnedgsasqdgldKRNSCRAKCAGDLNDMmkttdsd 532
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGV--------------------KKSEAKKLAKFYLNKM------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 533 GLiharknyniiddsevvnvskkvlihdfvsalpdkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
Cdd:PRK13631 164 GL----------------------------------DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP 209
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 221056887 613 KSEYLVQKTINNLKGNeNRITIIIAHRLSTI-RYANTIFVLS 653
Cdd:PRK13631 210 KGEHEMMQLILDAKAN-NKTVFVITHTMEHVlEVADEVIVMD 250
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
864-1123 |
5.57e-11 |
|
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: 65.35 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 864 NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNN 943
Cdd:cd18780 42 NQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDV--TRTGELLNRLSSDTQVLQNAVTVN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 944 IVIFTHFIVLFIVSMIMSFYFCPivaaVLTGTYFIFMRVFAIRARLSA--NKDVEKKginqpgtvflynnddeiFKD--- 1018
Cdd:cd18780 120 LSMLLRYLVQIIGGLVFMFTTSW----KLTLVMLSVVPPLSIGAVIYGkyVRKLSKK-----------------FQDala 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1019 -PSFLIQEAFYNMNTVIIYGLEDYFCKLIEKAIDYSNKGQKRKTLVNSMLWGF-SQSAQLFInSFAYWFGSFLIRRGTIE 1096
Cdd:cd18780 179 aASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFmGAAAQLAI-VLVLWYGGRLVIDGELT 257
|
250 260 270
....*....|....*....|....*....|
gi 221056887 1097 VDD---FMksLFTFLFTGSYAGkLMSLKGD 1123
Cdd:cd18780 258 TGLltsFL--LYTLTVAMSFAF-LSSLYGD 284
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1356-1427 |
6.93e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.65 E-value: 6.93e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 1356 SLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRI-ASIKRSDKIV 1427
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVdYALRYCERIV 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1308-1388 |
7.30e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.63 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1308 MSIYENI-------KFGKEDaTREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLL 1380
Cdd:PRK11650 91 MSVRENMayglkirGMPKAE-IEERVAEAARILELEPLLDRKPRE-----------LSGGQRQRVAMGRAIVREPAVFLF 158
|
....*...
gi 221056887 1381 DEATSSLD 1388
Cdd:PRK11650 159 DEPLSNLD 166
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
403-654 |
7.89e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 403 DLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDP----TEGDIIINDSHNLK--DINLKWWR-SKIGVVSQDPLLfsn 474
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHasEQTLRGVRgNKIAMIFQEPMV--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 475 siknnikyslySLKDLEYLSDQLNEDGSASQdGLdKRNSCRAkcagdlnDMMKTTDSDGLIHARKNYNiiddsevvnvsk 554
Cdd:PRK15134 104 -----------SLNPLHTLEKQLYEVLSLHR-GM-RREAARG-------EILNCLDRVGIRQAAKRLT------------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 555 kvlihDFvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
Cdd:PRK15134 152 -----DY---------------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLL 211
|
250 260
....*....|....*....|.
gi 221056887 635 IIAHRLSTIR-YANTIFVLSN 654
Cdd:PRK15134 212 FITHNLSIVRkLADRVAVMQN 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
386-610 |
9.28e-11 |
|
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: 63.22 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 386 KNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI-NLKWW---RSK 461
Cdd:cd03224 4 ENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG----RDItGLPPHeraRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDleylsdqlnedgSASQDGLDKrnscrakcagdlndmmkttdsdgliharkn 540
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENLLLGAYARRR------------AKRKARLER------------------------------ 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddsevvnvskkvlIHDFVSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:cd03224 115 -----------------VYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1274-1450 |
1.08e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 65.63 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNLFSIVSQEPIL-FNMSIYENIKFGK----------EDATREDVKRACKFAAIDEFIesl 1342
Cdd:PRK09536 57 AGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQFA--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1343 pnkyDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKlieKTIVDIKDKAD--RTIITIAHRIASI 1420
Cdd:PRK09536 134 ----DRPV----TSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV---RTLELVRRLVDdgKTAVAAIHDLDLA 202
|
170 180 190
....*....|....*....|....*....|.
gi 221056887 1421 KR-SDKIVVFnnpdrTGSFVQAEGTHEELLS 1450
Cdd:PRK09536 203 ARyCDELVLL-----ADGRVRAAGPPADVLT 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
383-656 |
1.09e-10 |
|
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: 60.93 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwRSKI 462
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------TVKI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQdpllfsnsiknnikyslyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyn 542
Cdd:cd03221 66 GYFEQ--------------------------------------------------------------------------- 70
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 iiddsevvnvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
250 260 270
....*....|....*....|....*....|....*..
gi 221056887 623 NNLKGnenrITIIIAH-R--LSTIryANTIFVLSNRE 656
Cdd:cd03221 114 KEYPG----TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1178-1463 |
1.21e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.55 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1178 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqGDEEQNVgmknvnefs 1257
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM----------------------------GHPKYEV--------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1258 ltkegshgdnsavfkNSGKILLDGVDICDYNLKD--LRNLFsiVS-QEPI------LFN-MSIYENIKFGKEDATREDVK 1327
Cdd:COG0396 55 ---------------TSGSILLDGEDILELSPDEraRAGIF--LAfQYPVeipgvsVSNfLRTALNARRGEELSAREFLK 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1328 RACKFAAIDEFIESLPNKYdTNVGpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaD 1407
Cdd:COG0396 118 LLKEKMKELGLDEDFLDRY-VNEG-----FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-D 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 1408 RTIITIAH--RIASIKRSDKIVVFNNpdrtGSFVqAEGTHEELLSVQDGVYKKYVKLA 1463
Cdd:COG0396 191 RGILIITHyqRILDYIKPDFVHVLVD----GRIV-KSGGKELALELEEEGYDWLKEEA 243
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1353-1418 |
1.43e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.23 E-value: 1.43e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 1353 YGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--RTIITIAHRIA 1418
Cdd:PRK11264 141 YPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMS 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
402-652 |
1.44e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS----HNLKD-INLKwwrskIGVVSQDPLLFSNsi 476
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvriRSPRDaIALG-----IGMVHQHFMLVPN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 477 knnikyslysLKDLEylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyNII---DDSEVVNVS 553
Cdd:COG3845 95 ----------LTVAE--------------------------------------------------NIVlglEPTKGGRLD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 554 KKVLIHDfVSALPDKY------ETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVqKTINNLK 626
Cdd:COG3845 115 RKAARAR-IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELF-EILRRLA 188
|
250 260
....*....|....*....|....*...
gi 221056887 627 gnENRITII-IAHRLSTIR-YANTIFVL 652
Cdd:COG3845 189 --AEGKSIIfITHKLREVMaIADRVTVL 214
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
865-1109 |
1.67e-10 |
|
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: 63.72 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 865 KYSLYILVIAIAMF-ISETLKNYYNNVIGEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNN 943
Cdd:cd18572 36 YRAVLLLLLLSVLSgLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDA--TKTGELTSRLTSDCQKVSDPLSTN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 944 IVIFTHFIVLFIVSMIMSFYF-----------CPIVAAVlTGTYFIFMRVFA--IRARL-SANKDVEkkginqpgtvfly 1009
Cdd:cd18572 114 LNVFLRNLVQLVGGLAFMFSLswrltllafitVPVIALI-TKVYGRYYRKLSkeIQDALaEANQVAE------------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1010 nnddeifkdpsfliqEAFYNMNTVIIYGLEDYFCKLIEKAID-YSNKGQKRKTLVNSMLWgFSQSAQLFINSFAYWFGSF 1088
Cdd:cd18572 180 ---------------EALSNIRTVRSFATEEREARRYERALDkALKLSVRQALAYAGYVA-VNTLLQNGTQVLVLFYGGH 243
|
250 260
....*....|....*....|.
gi 221056887 1089 LIRRGTIEVDdfmkSLFTFLF 1109
Cdd:cd18572 244 LVLSGRMSAG----QLVTFML 260
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
393-611 |
2.25e-10 |
|
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: 62.00 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 393 DTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDInlkwwRSKIGVVSQDP 469
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvVKEPAEA-----RRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 470 LLFSN-SIKNNIKY--SLYSLKdleylsdqlnedgsasqdgldkrnscRAKCAGDLNDMMKTTDSDGLIHARknyniidd 546
Cdd:cd03266 88 GLYDRlTARENLEYfaGLYGLK--------------------------GDELTARLEELADRLGMEELLDRR-------- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 547 sevvnvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:cd03266 134 ------------------------------VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1176-1452 |
2.38e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1176 RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtddvnnekkEQGDEEQNVGMknvne 1255
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE----------------------QAGGLVQCDKM----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1256 fsltkegshgdnsaVFKNSGKILLDGVDICDYNLKDLRNL-FSIVSQEPI-----LFNM--SIYENIK----FGKEDATR 1323
Cdd:PRK10261 79 --------------LLRRRSRQVIELSEQSAAQMRHVRGAdMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREEAMV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1324 EdVKRACKFAAIDEfieslpnkYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:PRK10261 145 E-AKRMLDQVRIPE--------AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQ 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 221056887 1404 DKADRTIITIAHriasikrsDKIVVFNNPDRTgsFVQAEGTHEELLSVQ 1452
Cdd:PRK10261 216 KEMSMGVIFITH--------DMGVVAEIADRV--LVMYQGEAVETGSVE 254
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1269-1449 |
2.51e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1269 AVFKNSGKILLDGVDICDYNLKD-LRNLFSIVSQEP----ILFNMSIYENI------KFGKEDATredVKRACKFAAIDE 1337
Cdd:PRK10762 301 ALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSVKENMsltalrYFSRAGGS---LKHADEQQAVSD 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1338 FIESLPNKYDTNVGPYGKsLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADRTIITIAHRI 1417
Cdd:PRK10762 378 FIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSEM 455
|
170 180 190
....*....|....*....|....*....|...
gi 221056887 1418 ASI-KRSDKIVVFNNPDRTGSFVQAEGTHEELL 1449
Cdd:PRK10762 456 PEVlGMSDRILVMHEGRISGEFTREQATQEKLM 488
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1350-1446 |
2.66e-10 |
|
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: 61.05 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1350 VGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03222 65 YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYlSDRIHV 144
|
90
....*....|....*....
gi 221056887 1429 F-NNPDRTGSFVQAEGTHE 1446
Cdd:cd03222 145 FeGEPGVYGIASQPKGTRE 163
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
383-655 |
2.94e-10 |
|
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: 61.74 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-SHNLKDINlkwwRSK 461
Cdd:cd03298 1 VRLDKIRFSYG-----EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPA----DRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIKYSLY-SLKDLEylSDQLNEDGSASQ---DGLDKRnscrakcagdlndmmkttdsdglih 536
Cdd:cd03298 72 VSMLFQENNLFAHlTVEQNVGLGLSpGLKLTA--EDRQAIEVALARvglAGLEKR------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 537 arknyniiddsevvnvskkvlihdfvsaLPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:cd03298 125 ----------------------------LPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 221056887 617 LVQKTINNLKGNENRITIIIAHRLSTIR--YANTIFVLSNR 655
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKrlAQRVVFLDNGR 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
345-638 |
3.01e-10 |
|
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: 64.44 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 345 ITEYMKSLEATNSLYEIINRKPLVennndgkKLKDIKKiqfknvRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGK 424
Cdd:TIGR03269 257 VAVFMEGVSEVEKECEVEVGEPII-------KVRNVSK------RYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 425 STILKLIERLYDPTEGDIIINDSHNLKDINLKWW----RSK--IGVVSQDpllfsnsiknnikYSLYSLKD-LEYLSDQL 497
Cdd:TIGR03269 324 TTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPdgrgRAKryIGILHQE-------------YDLYPHRTvLDNLTEAI 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 498 nedgsasqdGLDkrnscrakcagdLND---MMKTtdsdglIHARKNYNIiDDSEVVNVSKKvlihdfvsaLPDKyetlvg 574
Cdd:TIGR03269 391 ---------GLE------------LPDelaRMKA------VITLKMVGF-DEEKAEEILDK---------YPDE------ 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 575 snaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
Cdd:TIGR03269 428 -----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSH 486
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-611 |
3.48e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 62.24 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIInDSHNLKDINLK 456
Cdd:PRK14247 3 KIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYL-DGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 457 WWRSKIGVVSQDPLLFSN-SIKNNIKYSLyslkdleylsdqlnedgsasqdgldkrnscrakcagDLNDMMKttdsdgli 535
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNlSIFENVALGL------------------------------------KLNRLVK-------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 536 harknyniiddsevvnvSKKVLIHDFVSALP-----DKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:PRK14247 115 -----------------SKKELQERVRWALEkaqlwDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
.
gi 221056887 611 D 611
Cdd:PRK14247 178 D 178
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
369-654 |
3.50e-10 |
|
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: 62.57 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 369 ENNNDGKKLKDIKKIQFKNVRFHYDTrkdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindSH 448
Cdd:cd03291 26 QENNDRKHSSDDNNLFFSNLCLVGAP-----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----KH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 449 NlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLySLKDLEYLSdqlnedgsasqdgldkrnscrakcagdlndmmkt 528
Cdd:cd03291 97 S----------GRISFSSQFSWIMPGTIKENIIFGV-SYDEYRYKS---------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 529 tdsdgliharknyniiddsevvnVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
Cdd:cd03291 132 -----------------------VVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 221056887 609 SLDNKSEYLV-QKTINNLKGNENRitIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03291 189 YLDVFTEKEIfESCVCKLMANKTR--ILVTSKMEHLKKADKILILHE 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1164-1393 |
3.70e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.45 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMSRPNV--PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeq 1241
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLL----------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1242 gdeeqnvgmknvnefsltkegshgdNSAVFKNSGKILLDGVDIC----DYNLKDLRNLFSIVSQ--EPILFNMSIYENIK 1315
Cdd:PRK13649 54 -------------------------NGLHVPTQGSVRVDDTLITstskNKDIKQIRKKVGLVFQfpESQLFEETVLKDVA 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1316 FGKED---ATREDVKRACKFAAIDEFIESLPNKydtnvGPYgkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:PRK13649 109 FGPQNfgvSQEEAEALAREKLALVGISESLFEK-----NPF--ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
.
gi 221056887 1393 K 1393
Cdd:PRK13649 182 K 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
387-611 |
3.77e-10 |
|
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: 64.32 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 387 NVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKS----TILKLIERLYDPTEGDIIINDsHNLKDINLKWWR--- 459
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG-QDLLGLSERELRrir 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 -SKIGVVSQDPLLfsnsiknnikySLYSLKDLEylsDQLNEDGSASQdGLDKRnscrakcagdlndmmkttdsdgliHAR 538
Cdd:COG4172 91 gNRIAMIFQEPMT-----------SLNPLHTIG---KQIAEVLRLHR-GLSGA------------------------AAR 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 539 KnyniiddsEVVNVSKKVLIHDfvsalPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4172 132 A--------RALELLERVGIPD-----P---ERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
374-611 |
3.89e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 374 GKKLkdikkIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndSHNLkdi 453
Cdd:COG0488 312 GKKV-----LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--GETV--- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 454 nlkwwrsKIGVVSQDpllfsnsiknnikyslyslkdleylSDQLNEDGSAsqdgldkrnscrakcagdLNDMMKTTDSDG 533
Cdd:COG0488 379 -------KIGYFDQH-------------------------QEELDPDKTV------------------LDELRDGAPGGT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 534 LIHARknyniiddsevvnvskkvlihDFVSAL---PDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:COG0488 409 EQEVR---------------------GYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
.
gi 221056887 611 D 611
Cdd:COG0488 464 D 464
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
398-644 |
3.89e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwrskigvVSQDPLLFSNSIK 477
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN------------------INYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 478 NNIKYSLYSLKDLEYLSDQLNEdgsasqdgLDKRNSCRAKCAgdlndmmkttdsdgliharknYNIIDDSEVVNVSKKVL 557
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENL--------YIGRHLTKKVCG---------------------VNIIDWREMRVRAAMML 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 558 IhdfVSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYLVQkTINNLKgNENRITIII 636
Cdd:PRK09700 131 L---RVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEvDYLFL-IMNQLR-KEGTAIVYI 201
|
....*...
gi 221056887 637 AHRLSTIR 644
Cdd:PRK09700 202 SHKLAEIR 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
381-652 |
4.15e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.72 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 381 KKIQFKNVRFHYDTRKDVEiYKDLN---FTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDIN 454
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFE-FKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaiPANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 455 -LKWWRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLkdleylsdqlnedgsasqdGLDKRNscrakcagdlndmmkttds 531
Cdd:PRK13645 84 eVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNL-------------------GENKQE------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 532 dgliharknyniiddsevvnVSKKV-LIHDFVSaLPDKYetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:PRK13645 126 --------------------AYKKVpELLKLVQ-LPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 221056887 611 DNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVM 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
392-636 |
4.27e-10 |
|
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: 61.40 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 392 YDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINL----KWWRSKIGVVSQ 467
Cdd:cd03218 10 YGKRKVV---NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG----QDITKlpmhKRARLGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 468 DPLLFSN-SIKNNIKYSLYSLKDL-EYLSDQLNEdgsasqdgldkrnscrakcagdlndmmkttdsdgliharknyniid 545
Cdd:cd03218 83 EASIFRKlTVEENILAVLEIRGLSkKEREEKLEE---------------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 546 dsevvnvskkvLIHDFvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:cd03218 117 -----------LLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL 179
|
250
....*....|.
gi 221056887 626 KgnENRITIII 636
Cdd:cd03218 180 K--DRGIGVLI 188
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
394-611 |
5.19e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.96 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDIIINDshnlKDIN-LKWWRSKIGVVSQDP 469
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNG----RRLTaLPAEQRRIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 470 LLFSN-SIKNNIKYSLyslkdleylsdqlnedgsasQDGLDKRnscrakcagdlndmmkttdsdglihARKNyniiddsE 548
Cdd:COG4136 86 LLFPHlSVGENLAFAL--------------------PPTIGRA-------------------------QRRA-------R 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 549 VVNVSKKVLIHDFVSALPDkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4136 114 VEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1181-1450 |
5.57e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.52 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1181 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmRFYDLKNDHHIVFKNEHTDDVNNEkkeqgDEEQNVGMKNvnefsltk 1260
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGQTINLVRDK-----DGQLKVADKN-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1261 egshgdnsavfknsgkilldgvdicdyNLKDLRNLFSIVSQEPILFN-MSIYENIK--------FGKEDAtREDVKRACK 1331
Cdd:PRK10619 86 ---------------------------QLRLLRTRLTMVFQHFNLWShMTVLENVMeapiqvlgLSKQEA-RERAVKYLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1332 FAAIDEFIEslpnkydtnvGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--RT 1409
Cdd:PRK10619 138 KVGIDERAQ----------GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRIMQQLAEegKT 204
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 221056887 1410 IITIAHRIASIKRSDKIVVFNNPDRtgsfVQAEGTHEELLS 1450
Cdd:PRK10619 205 MVVVTHEMGFARHVSSHVIFLHQGK----IEEEGAPEQLFG 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1187-1388 |
5.62e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.67 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1187 FSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefSLTKEGShgd 1266
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLL--------------------------------------------TMIETPT--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1267 nsavfknSGKILLDGVDICDYN---LKDLRNLFSIVSQ-----------------EPILFNMSIyenikfgkedaTREDv 1326
Cdd:PRK11308 69 -------GGELYYQGQDLLKADpeaQKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSL-----------SAAE- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 1327 kRACKFAAIDEFIESLPNKYDTnvgpYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11308 130 -RREKALAMMAKVGLRPEHYDR----YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1152-1451 |
6.53e-10 |
|
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: 63.67 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1152 IRIKN-TNDIDGKIEIMDVNFTYmsrpnvpiykdltfscDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDH-HIVFKNE 1229
Cdd:TIGR03269 1 IEVKNlTKKFDGKEVLKNISFTI----------------EEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSgRIIYHVA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1230 HTddvnnEKKEQGDEEQNVGMK-NVNEFSLTKEgshgdnsavfknsgkiLLDGVDICDYNLKDLRNLFSIVSQEPILF-- 1306
Cdd:TIGR03269 65 LC-----EKCGYVERPSKVGEPcPVCGGTLEPE----------------EVDFWNLSDKLRRRIRKRIAIMLQRTFALyg 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1307 NMSIYENIKFGKEDA---TREDVKRACkfaaidEFIESLpnKYDTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEA 1383
Cdd:TIGR03269 124 DDTVLDNVLEALEEIgyeGKEAVGRAV------DLIEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEP 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1384 TSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASI-KRSDKIVVFNNpdrtGSFVQaEGTHEELLSV 1451
Cdd:TIGR03269 196 TGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIeDLSDKAIWLEN----GEIKE-EGTPDEVVAV 259
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
402-638 |
6.87e-10 |
|
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: 60.94 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinlkwwrskiGVVSQDP-----LLFSNsi 476
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE-----------------GKQITEPgpdrmVVFQN-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 477 knnikyslYSLkdLEYLSDQLNEDGSASQDGLDKRNSCRAKCAGDLNDMMkttdsdGLIHARknyniiddsevvnvskkv 556
Cdd:TIGR01184 63 --------YSL--LPWLTVRENIALAVDRVLPDLSKSERRAIVEEHIALV------GLTEAA------------------ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 557 lihdfvsalpDKYETlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRIT-II 635
Cdd:TIGR01184 109 ----------DKRPG-------QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI-WEEHRVTvLM 170
|
...
gi 221056887 636 IAH 638
Cdd:TIGR01184 171 VTH 173
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
403-654 |
7.34e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 403 DLNFTL-TEGKTYAFvGESGCGKSTILKLIERLYDPTEGDIIINDsHNL----KDINLKWWRSKIGVVSQDPLLFSN-SI 476
Cdd:PRK11144 16 TVNLTLpAQGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLfdaeKGICLPPEKRRIGYVFQDARLFPHyKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 477 KNNIKYSlyslkdleylsdqlnedgsasqdgldkrnscrakcagdlndmMKTTDsdgliharknyniiddsevvnvskKV 556
Cdd:PRK11144 94 RGNLRYG------------------------------------------MAKSM------------------------VA 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 557 LIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD--NKSE---YL--VQKTINnlkgne 629
Cdd:PRK11144 108 QFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlpRKREllpYLerLAREIN------ 179
|
250 260
....*....|....*....|....*..
gi 221056887 630 nrITII-IAHRLSTI-RYANTIFVLSN 654
Cdd:PRK11144 180 --IPILyVSHSLDEIlRLADRVVVLEQ 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1270-1412 |
7.90e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.06 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1270 VFKNSGKILLDGVDICDYNLKD-LRNLFSIVSQEPILFN-MSIYENIKFG---KEDATREDVK-RACKFaaIDEF-IESL 1342
Cdd:PRK10895 53 VPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRrLSVYDNLMAVlqiRDDLSAEQREdRANEL--MEEFhIEHL 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1343 PNKYdtnvgpyGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIIT 1412
Cdd:PRK10895 131 RDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLIT 193
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
64-355 |
8.13e-10 |
|
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: 61.88 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 64 VSFVCATISGGSLPFFV-SVFGVIMKNMNLG-----ENVDDIIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFL 137
Cdd:cd18780 3 IALLVSSGTNLALPYFFgQVIDAVTNHSGSGgeealRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 138 KSVFYQDGQFHD-NNPG---SKLTSDldfylEQV--NAGIGTKFLTIFTYTSAFLGLYFwsLFK-NARLTLCVTCVFPLI 210
Cdd:cd18780 83 SAIIAQEIAFFDvTRTGellNRLSSD-----TQVlqNAVTVNLSMLLRYLVQIIGGLVF--MFTtSWKLTLVMLSVVPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 211 YICGVICNKKAKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEHTILKKFnlSEKLYSKYMLKANFmeSLHIGMINGF 290
Cdd:cd18780 156 SIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRY--SEKINESYLLGKKL--ARASGGFNGF 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 291 ILA----SYAFGFWYGTRIIISDlsnaqsnnDFHGGSVISILL---GVLISMFMLTIVlpnITEYMKSLEAT 355
Cdd:cd18780 232 MGAaaqlAIVLVLWYGGRLVIDG--------ELTTGLLTSFLLytlTVAMSFAFLSSL---YGDFMQAVGAS 292
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
402-652 |
8.14e-10 |
|
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: 60.91 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI-NLK---WWRSKIGVVSQDPLLFSN-SI 476
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG----EDItGLPpheIARLGIGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 477 KNNIKYSLYSLKDLEYLSDQLnedgSASQDGLDKRnscrakcAGDLNDMMKttdsdgliharknyniiddsevvnvskkv 556
Cdd:cd03219 93 LENVMVAAQARTGSGLLLARA----RREEREARER-------AEELLERVG----------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 557 lihdfvsaLPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLdNKSEylVQKTINNLKG-NENRITI- 634
Cdd:cd03219 133 --------LADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPAAGL-NPEE--TEELAELIRElRERGITVl 197
|
250
....*....|....*....
gi 221056887 635 IIAHRLSTI-RYANTIFVL 652
Cdd:cd03219 198 LVEHDMDVVmSLADRVTVL 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1184-1428 |
8.45e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.05 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1184 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqgdeeqnvGMknvnefsLTKEGs 1263
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALM-----------------------------------GL-------LAANG- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1264 hgdnsavfKNSGKILLDGVDICDYNLKDLRNL----FSIVSQEPIL-FN--MSIYENI--------KFGKEDATREDVKR 1328
Cdd:PRK09473 71 --------RIGGSATFNGREILNLPEKELNKLraeqISMIFQDPMTsLNpyMRVGEQLmevlmlhkGMSKAEAFEESVRM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1329 --ACKFAAIDEFIESLPNKYdtnvgpygkslSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1406
Cdd:PRK09473 143 ldAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREF 211
|
250 260
....*....|....*....|....*
gi 221056887 1407 DRTIITIAHR---IASIkrSDKIVV 1428
Cdd:PRK09473 212 NTAIIMITHDlgvVAGI--CDKVLV 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1174-1388 |
9.78e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1174 MSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqGDEEQNvgmknv 1253
Cdd:COG0488 6 KSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA----------------------------GELEPD------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1254 nefsltkegshgdnsavfknSGKILLDgvdicdynlKDLRnlFSIVSQEPILF-NMSIYENIKFG--------------- 1317
Cdd:COG0488 52 --------------------SGEVSIP---------KGLR--IGYLPQEPPLDdDLTVLDTVLDGdaelraleaeleele 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 -KEDATREDVKRA----CKFAAIDEF-----IESL-------PNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLL 1380
Cdd:COG0488 101 aKLAEPDEDLERLaelqEEFEALGGWeaearAEEIlsglgfpEEDLDRPVS----ELSGGWRRRVALARALLSEPDLLLL 176
|
....*...
gi 221056887 1381 DEATSSLD 1388
Cdd:COG0488 177 DEPTNHLD 184
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1183-1431 |
1.14e-09 |
|
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: 59.99 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1183 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtddvnnekkeQGDeeqnvgmknvnefsltkeg 1262
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII------------------------LPD------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1263 shgdnsavfknSGKILLDG--VDICDynlkdlRNLFSIVSQEPILF-NMSIYENIKF-------GKEDATREdvkrackf 1332
Cdd:cd03269 54 -----------SGEVLFDGkpLDIAA------RNRIGYLPEERGLYpKMKVIDQLVYlaqlkglKKEEARRR-------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1333 aaIDEFIESLpnkydtNVGPYGKS----LSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdR 1408
Cdd:cd03269 109 --IDEWLERL------ELSEYANKrveeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAG-K 179
|
250 260
....*....|....*....|....
gi 221056887 1409 TIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03269 180 TVILSTHQMELVEElCDRVLLLNK 203
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1357-1417 |
1.14e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 60.65 E-value: 1.14e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRI 1417
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSV 195
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
404-611 |
1.17e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 404 LNFTLT--EGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS-HNLKDINlkwwRSKIGVVSQDPLLFSN-SIKNN 479
Cdd:PRK10771 16 MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdHTTTPPS----RRPVSMLFQENNLFSHlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 480 IKYSLY-SLKdleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgLIHARKnyniiddSEVVNVSKKVLI 558
Cdd:PRK10771 92 IGLGLNpGLK---------------------------------------------LNAAQR-------EKLHAIARQMGI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 221056887 559 HDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10771 120 EDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1274-1384 |
1.17e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.73 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDIcdyNLKD----LRNLFSIVS----QEPILFNMSIYENI---------KFGKEDATREDvkrackfAAID 1336
Cdd:COG1129 306 SGEIRLDGKPV---RIRSprdaIRAGIAYVPedrkGEGLVLDLSIRENItlasldrlsRGGLLDRRRER-------ALAE 375
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 221056887 1337 EFIESL---PNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEAT 1384
Cdd:COG1129 376 EYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
405-652 |
1.39e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.46 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEgdIIINDSHNLKDINL---------KWWRSKIGVVSQDPllfsns 475
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW--HVTADRFRWNGIDLlklsprerrKIIGREIAMIFQEP------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 476 iknnikysLYSLKDLEYLSDQLNEdgsasqdgldkrnscrakcagdlndMMKTTDSDGLIHARKNYNIiddSEVVNVSKK 555
Cdd:COG4170 99 --------SSCLDPSAKIGDQLIE-------------------------AIPSWTFKGKWWQRFKWRK---KRAIELLHR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 556 VLIHDfvsalpdkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITII 635
Cdd:COG4170 143 VGIKD--------HKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARL--NQLQGTSI 212
|
250 260
....*....|....*....|
gi 221056887 636 --IAHRLSTI-RYANTIFVL 652
Cdd:COG4170 213 llISHDLESIsQWADTITVL 232
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
870-1115 |
1.47e-09 |
|
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: 60.99 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 870 ILVI-AIAMFisetLKNYYNNVIGEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFT 948
Cdd:cd18573 50 VFVVgAAANF----GRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDK--NKTGELVSRLSSDTSVVGKSLTQNLSDGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 949 HFIVLFIVSMIMSFYFCPIVAAVLTGT---YFIFMRVFAIRAR-LSanKDVEKK--GINQpgtvflynnddeifkdpsfL 1022
Cdd:cd18573 124 RSLVSGVGGIGMMLYISPKLTLVMLLVvppIAVGAVFYGRYVRkLS--KQVQDAlaDATK-------------------V 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1023 IQEAFYNMNTVIIYGLEDYFCKLIEKAIDYSNKGQKRKTLVNSMLWGfsqSAQLFINSFAY---WFGSFLIRRGTIEVDD 1099
Cdd:cd18573 183 AEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFG---STGFSGNLSLLsvlYYGGSLVASGELTVGD 259
|
250
....*....|....*.
gi 221056887 1100 fmksLFTFLFTGSYAG 1115
Cdd:cd18573 260 ----LTSFLMYAVYVG 271
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
579-644 |
1.85e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.15 E-value: 1.85e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLKG--NENRITIIIAHRLSTIR 644
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE---LVGEVLNTIRQlaQEKRTMVIVTHEMSFAR 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
578-652 |
1.87e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 1.87e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVAL 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
378-472 |
2.14e-09 |
|
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: 61.74 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 378 KDIKKIQFKNVRFHYDTRKDVEIYK--DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINL 455
Cdd:COG4615 323 ADFQTLELRGVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG-QPVTADNR 401
|
90
....*....|....*..
gi 221056887 456 KWWRSKIGVVSQDPLLF 472
Cdd:COG4615 402 EAYRQLFSAVFSDFHLF 418
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1346-1429 |
2.19e-09 |
|
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: 62.11 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1346 YDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SD 1424
Cdd:COG1245 449 LDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYiSD 524
|
....*
gi 221056887 1425 KIVVF 1429
Cdd:COG1245 525 RLMVF 529
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
383-654 |
2.23e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.51 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrski 462
Cdd:COG4152 2 LELKGLTKRFGDKTAV---DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 gvvsqdpllFSNSIKNNIKY-----SLY---SLKD-LEYLSdQLNedgsasqdGLDKRnscRAKCAGDlnDMMKTTDsdg 533
Cdd:COG4152 65 ---------LDPEDRRRIGYlpeerGLYpkmKVGEqLVYLA-RLK--------GLSKA---EAKRRAD--EWLERLG--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 534 lIHARKNyniiddsevvnvsKKVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD-- 611
Cdd:COG4152 119 -LGDRAN-------------KKV---------------------EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpv 163
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 221056887 612 NKSeyLVQKTINNLKgnENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:COG4152 164 NVE--LLKDVIRELA--AKGTTVIFSsHQMELVeELCDRIVIINK 204
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
397-638 |
2.56e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.31 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI---ERlYDPTEGDIIINDshnlKDInLKW---WRSK--IGVVSQD 468
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDG----EDI-LELspdERARagIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 469 PL--------LFSNSIKNNIKYSLYSLKDLEylsDQLNEdgSASQDGLDKrnscrakcagdlnDMMKttdsdglihaRKn 540
Cdd:COG0396 86 PVeipgvsvsNFLRTALNARRGEELSAREFL---KLLKE--KMKELGLDE-------------DFLD----------RY- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddsevVNVSkkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:COG0396 137 ---------VNEG--------------------------FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAE 181
|
250
....*....|....*...
gi 221056887 621 TINNLKgNENRITIIIAH 638
Cdd:COG0396 182 GVNKLR-SPDRGILIITH 198
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1178-1450 |
2.58e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 59.64 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1178 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefs 1257
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL------------------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1258 LTKEgshgdnsavfknSGKILLDGVDICDYNLKDLRNLFSIVSQEP-----------ILFNMSIYENI--KFGKEDatRE 1324
Cdd:PRK11231 52 LTPQ------------SGTVFLGDKPISMLSSRQLARRLALLPQHHltpegitvrelVAYGRSPWLSLwgRLSAED--NA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1325 DVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:PRK11231 118 RVNQAMEQTRINHLADRRLT-----------DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT 186
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 221056887 1405 KAdRTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAEGTHEELLS 1450
Cdd:PRK11231 187 QG-KTVVTVLHDLNQASRyCDHLVVLAN----GHVM-AQGTPEEVMT 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1357-1431 |
2.63e-09 |
|
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: 57.07 E-value: 2.63e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkadRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQvATKIIELED 142
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1353-1395 |
3.18e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 3.18e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 221056887 1353 YGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK15134 422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI 464
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1274-1428 |
3.22e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.49 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDI---CDYNLKDLRNLFSIVSQEPIL-FN--MS----IYENIKFGKEDATREDVKRACKfaAIDEFIESLP 1343
Cdd:PRK15079 75 DGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPLAsLNprMTigeiIAEPLRTYHPKLSRQEVKDRVK--AMMLKVGLLP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1344 NKydtnVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADR----TIITIAHRIAS 1419
Cdd:PRK15079 153 NL----INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS----IQAQVVNLLQQLQRemglSLIFIAHDLAV 224
|
170
....*....|
gi 221056887 1420 IKR-SDKIVV 1428
Cdd:PRK15079 225 VKHiSDRVLV 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1355-1431 |
3.23e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.74 E-value: 3.23e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1355 KSLSGGQKQRVAIARALLREPKILLLDEATSSLDS-NSEkLIEKTIVDIKDKaDRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:COG4152 128 EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPvNVE-LLKDVIRELAAK-GTTVIFSSHQMELVEElCDRIVIINK 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1337-1429 |
3.41e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1337 EFIE--SLPNKYDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIA 1414
Cdd:PRK13409 436 EIIKplQLERLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVD 511
|
90
....*....|....*.
gi 221056887 1415 HRIASIKR-SDKIVVF 1429
Cdd:PRK13409 512 HDIYMIDYiSDRLMVF 527
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
388-445 |
3.63e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 58.94 E-value: 3.63e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 388 VRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN 445
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1274-1431 |
3.67e-09 |
|
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: 57.83 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNL-FSIVSQEP----ILFNMSIYENIkfgkedatredvkrackfaaidefieSLPNkydt 1348
Cdd:cd03215 54 SGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLSVAENI--------------------------ALSS---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1349 nvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADRTIITIAHRIASIKR-SDKIV 1427
Cdd:cd03215 104 -------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGlCDRIL 175
|
....
gi 221056887 1428 VFNN 1431
Cdd:cd03215 176 VMYE 179
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1356-1389 |
4.60e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.92 E-value: 4.60e-09
10 20 30
....*....|....*....|....*....|....
gi 221056887 1356 SLSGGQKQRVAIARALLREPKILLLDEATSSLDS 1389
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1176-1460 |
5.04e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.03 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1176 RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgdeeqnVGMknvne 1255
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKML-----------------------------------AGM----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1256 fsltkegshgdnsaVFKNSGKILLDGVDIC--DYNLKDLRnlFSIVSQEPI-----------LFNMSIYENIKFGKEDat 1322
Cdd:PRK15112 63 --------------IEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQ-- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1323 REDvkrackfaAIDEFIES---LPNkydtNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PRK15112 125 REK--------QIIETLRQvglLPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLM 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 1400 VDIKDKADRTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAEGTHEELLSVQDGVYKKYV 1460
Cdd:PRK15112 193 LELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQ----GEVVERGSTADVLASPLHELTKRLI 250
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
399-651 |
5.19e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.83 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKwwRSKIGvvsqdpllfsnsikn 478
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG----QTINLV--RDKDG--------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 479 niKYSLYSLKDLEYLSDQLNedgsasqdgldkrnscrakcagdlndmMKTTDSDGLIHARKNYNIIDDS-EVVNVSKKVL 557
Cdd:PRK10619 78 --QLKVADKNQLRLLRTRLT---------------------------MVFQHFNLWSHMTVLENVMEAPiQVLGLSKQEA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 558 IHDFVSALpDKY---ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITI 634
Cdd:PRK10619 129 RERAVKYL-AKVgidERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMV 206
|
250
....*....|....*....
gi 221056887 635 IIAHRLSTIRYANT--IFV 651
Cdd:PRK10619 207 VVTHEMGFARHVSShvIFL 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1356-1388 |
5.68e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.93 E-value: 5.68e-09
10 20 30
....*....|....*....|....*....|...
gi 221056887 1356 SLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1164-1415 |
5.95e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsRPNVPIYKDLTFSCDSK----KTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekk 1239
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPFASRALFDIDLEvkkgSYTALIGHTGSGKSTLLQHL--------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1240 eQGDEEQNVGMKNVNEFSLTKEGSHGDnsavfknsgkilldgvdicdynLKDLRNLFSIVSQEP--ILFNMSIYENIKFG 1317
Cdd:PRK13643 53 -NGLLQPTEGKVTVGDIVVSSTSKQKE----------------------IKPVRKKVGVVFQFPesQLFEETVLKDVAFG 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1318 -------KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSN 1390
Cdd:PRK13643 110 pqnfgipKEKAEKIAAEKLEMVGLADEFWEKSPFE-----------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
250 260
....*....|....*....|....*
gi 221056887 1391 SEKLIEKTIVDIKdKADRTIITIAH 1415
Cdd:PRK13643 179 ARIEMMQLFESIH-QSGQTVVLVTH 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
400-654 |
6.02e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.49 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLlfsnsIKNN 479
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK-PISMLSSRQLARRLALLPQHHL-----TPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 480 IkyslySLKDL-EY-LSDQLNEDGSASQDglDKRNSCRAkcagdlndMMKTTdsdgliharknyniiddsevvnvskkvl 557
Cdd:PRK11231 91 I-----TVRELvAYgRSPWLSLWGRLSAE--DNARVNQA--------MEQTR---------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 558 ihdfVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIA 637
Cdd:PRK11231 128 ----INHLADR-------RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVL 195
|
250
....*....|....*...
gi 221056887 638 HRLS-TIRYANTIFVLSN 654
Cdd:PRK11231 196 HDLNqASRYCDHLVVLAN 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1174-1388 |
6.02e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.63 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1174 MSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqgdeeqnvgmknv 1253
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS---------------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1254 nefsltkegshGDNSAvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPIL-FNMSIYENIKFGKEDATREDVKRAckf 1332
Cdd:PRK13548 50 -----------GELSP---DSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDD--- 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1333 AAIDEFIESlpnkydTNVGPYGK----SLSGGQKQRVAIARALLR------EPKILLLDEATSSLD 1388
Cdd:PRK13548 113 ALVAAALAQ------VDLAHLAGrdypQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD 172
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
65-308 |
6.06e-09 |
|
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: 59.06 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 65 SFVCATISGG---SLPFFV-----SVFGVIMKNMNLGENVDdiIFSLVLIGIFQF--VMSFISSFCMDIVTTKILKTLKV 134
Cdd:cd18573 1 ALALLLVSSAvtmSVPFAIgklidVASKESGDIEIFGLSLK--TFALALLGVFVVgaAANFGRVYLLRIAGERIVARLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 135 EFLKSVFYQDGQFHDNNP---------------GSKLTSDLDFYLEQVNAGIGTkfLTIFTYTSaflglyfwslfknARL 199
Cdd:cd18573 79 RLFKSILRQDAAFFDKNKtgelvsrlssdtsvvGKSLTQNLSDGLRSLVSGVGG--IGMMLYIS-------------PKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 200 TLCVTCVFPLIYICGVICNKKAKinKKTSLLYNN--NTMSIIEEALVGIRTVVSYCGEHTILKKFNlsEKLYSKYML--- 274
Cdd:cd18573 144 TLVMLLVVPPIAVGAVFYGRYVR--KLSKQVQDAlaDATKVAEERLSNIRTVRAFAAERKEVERYA--KKVDEVFDLakk 219
|
250 260 270
....*....|....*....|....*....|....*...
gi 221056887 275 ----KANFMESLHIgMINGFILAsyafGFWYGTRIIIS 308
Cdd:cd18573 220 ealaSGLFFGSTGF-SGNLSLLS----VLYYGGSLVAS 252
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1272-1449 |
6.15e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1272 KNSGKILLDGVDICDYN-LKDLRNLFSIVSQE----------PILFNmSIYENI-----KFGKEDATRedVKRACKFAaI 1335
Cdd:PRK10982 300 KSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyaylDIGFN-SLISNIrnyknKVGLLDNSR--MKSDTQWV-I 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1336 DEFIESLPNkYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDRTIITIAH 1415
Cdd:PRK10982 376 DSMRVKTPG-HRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISS 449
|
170 180 190
....*....|....*....|....*....|....*
gi 221056887 1416 RIAS-IKRSDKIVVFNNPDRTGSFVQAEGTHEELL 1449
Cdd:PRK10982 450 EMPElLGITDRILVMSNGLVAGIVDTKTTTQNEIL 484
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1339-1429 |
6.45e-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: 58.19 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1339 IESLpnkYDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIA 1418
Cdd:cd03237 105 IEQI---LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDII 177
|
90
....*....|..
gi 221056887 1419 SIKR-SDKIVVF 1429
Cdd:cd03237 178 MIDYlADRLIVF 189
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
396-638 |
7.18e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI--ERLYDPTEGDIIINDShNLKDINLKWwRSKIGVVsqdpLLFS 473
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGE-SILDLEPEE-RAHLGIF----LAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 474 NSIKNNikyslyslkdleylsdqlnedGSASQDGLdkRNSCRAKcagdlndmmkttdsdglihaRKNYNiidDSEVVNVS 553
Cdd:CHL00131 92 YPIEIP---------------------GVSNADFL--RLAYNSK--------------------RKFQG---LPELDPLE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 554 kkvlihdFVSALPDKYEtLVGSNASKL--------SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:CHL00131 126 -------FLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL 197
|
250
....*....|...
gi 221056887 626 KGNENRItIIIAH 638
Cdd:CHL00131 198 MTSENSI-ILITH 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1199-1428 |
8.00e-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: 59.84 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1199 GETGSGKSTVMSLLMRFYdlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegSHGDNSavfknsGKIL 1278
Cdd:TIGR02633 34 GENGAGKSTLMKILSGVY----------------------------------------------PHGTWD------GEIY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1279 LDGVDICDYNLKDL-RNLFSIVSQEPILF-NMSIYENIKFGKE-------DATREDVKRACKFAA---IDEFIESLPnky 1346
Cdd:TIGR02633 62 WSGSPLKASNIRDTeRAGIVIIHQELTLVpELSVAENIFLGNEitlpggrMAYNAMYLRAKNLLRelqLDADNVTRP--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1347 dtnVGPYGkslsGGQKQRVAIARALLREPKILLLDEATSSLdsnSEKLIEKTIVDIKDKADRTI--ITIAHRIASIKR-S 1423
Cdd:TIGR02633 139 ---VGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL---TEKETEILLDIIRDLKAHGVacVYISHKLNEVKAvC 208
|
....*
gi 221056887 1424 DKIVV 1428
Cdd:TIGR02633 209 DTICV 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
389-445 |
9.23e-09 |
|
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: 57.54 E-value: 9.23e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 389 RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN 445
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
825-1110 |
9.30e-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: 58.61 E-value: 9.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 825 VVIIALSIIVAgglypMFALLYAKYVSTLFDF---ANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKH 901
Cdd:cd18570 5 ILILLLSLLIT-----LLGIAGSFFFQILIDDiipSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 902 RLFENILYQEISFFDQdcHAPGLLSSHIN-----RDV--HLLKTGLVNNIVIFTHFIVLFIVSMIMsFYFCPIVAAVLTG 974
Cdd:cd18570 80 GYFKHLLKLPLSFFET--RKTGEIISRFNdankiREAisSTTISLFLDLLMVIISGIILFFYNWKL-FLITLLIIPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 975 TYFIFMRVF--AIRARLSANKDVEkkginqpgtvflynnddeifkdpSFLIqEAFYNMNTVIIYGLEDYFCKLIEKA-ID 1051
Cdd:cd18570 157 IILLFNKPFkkKNREVMESNAELN-----------------------SYLI-ESLKGIETIKSLNAEEQFLKKIEKKfSK 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 1052 YSNKGQKRKTLVNSMLwGFSQSAQLFINSFAYWFGSFLIRRGTIEVDDFM--KSLFTFLFT 1110
Cdd:cd18570 213 LLKKSFKLGKLSNLQS-SIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIafNALLGYFLG 272
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
386-625 |
1.02e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 386 KNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDInlkwwRSKIGVV 465
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-TAPLAEA-----REDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 466 SQDP-LLFSNSIKNNIkyslyslkdleylsdqlnedgsasqdGLDKRNSCRAKCAGDLndmmkttdsdgliharknynii 544
Cdd:PRK11247 87 FQDArLLPWKKVIDNV--------------------------GLGLKGQWRDAALQAL---------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 545 ddsEVVNVSKKVliHDFVSALpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
Cdd:PRK11247 119 ---AAVGLADRA--NEWPAAL---------------SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIES 178
|
.
gi 221056887 625 L 625
Cdd:PRK11247 179 L 179
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
59-347 |
1.05e-08 |
|
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: 58.23 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 59 KKLLGVSFVCATISGG---SLPFFVSVF---GVIMKNMNLGenvddIIFSLVLIGIF--QFVMSFISSFCMDIVTTKILK 130
Cdd:cd18549 1 KKLFFLDLFCAVLIAAldlVFPLIVRYIiddLLPSKNLRLI-----LIIGAILLALYilRTLLNYFVTYWGHVMGARIET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 131 TLKVEFLKSVFYQDGQFHDNNP-G---SKLTSDLdFYL-EQVNAGIGTKFLTIFTYTSAFLGLyfwsLFKNARLTLCVTC 205
Cdd:cd18549 76 DMRRDLFEHLQKLSFSFFDNNKtGqlmSRITNDL-FDIsELAHHGPEDLFISIITIIGSFIIL----LTINVPLTLIVFA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 206 VFPLIYICGVICNKK-----AKINKKTSLLYnnntmSIIEEALVGIRTVVSYCGEHTILKKFNLSEKLYSK-----YMLK 275
Cdd:cd18549 151 LLPLMIIFTIYFNKKmkkafRRVREKIGEIN-----AQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLEskkkaYKAM 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 276 ANFMESLH--IGMINGFILASYAFgFWYGTRIIISDLsnaqsnndfhggsvISILLgvLISMFMLTI-VLPNITE 347
Cdd:cd18549 226 AYFFSGMNffTNLLNLVVLVAGGY-FIIKGEITLGDL--------------VAFLL--YVNVFIKPIrRLVNFTE 283
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1338-1443 |
1.20e-08 |
|
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: 56.18 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1338 FIESLPNKYDTNVG--PYGK---SLSGGQKQRVAIARALLREPK--ILLLDEATSSLDSNS-EKLIE--KTIVDIKDkad 1407
Cdd:cd03238 64 FIDQLQFLIDVGLGylTLGQklsTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDiNQLLEviKGLIDLGN--- 140
|
90 100 110
....*....|....*....|....*....|....*..
gi 221056887 1408 rTIITIAHRIASIKRSDKIVVFN-NPDRTGSFVQAEG 1443
Cdd:cd03238 141 -TVILIEHNLDVLSSADWIIDFGpGSGKSGGKVVFSG 176
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
825-1109 |
1.30e-08 |
|
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: 57.83 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 825 VVIIALSIIVAGglypmFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLF 904
Cdd:cd18551 2 ILALLLSLLGTA-----ASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 905 ENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCP----IVAAVLTGTYFIFM 980
Cdd:cd18551 77 RRLLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWvltlVTLAVVPLAFLIIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 981 RVFAIRARLSANKDVEKKGINQpgtvflynnddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCKLIEKAIDYSNKGQKRK 1060
Cdd:cd18551 155 PLGRRIRKASKRAQDALGELSA-------------------ALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 221056887 1061 TLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTIEVDDFMkSLFTFLF 1109
Cdd:cd18551 216 AKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLV-AFLLYLF 263
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
394-622 |
1.37e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.42 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWRSKIGVVSQdpllfs 473
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG----GDIDDPDVAEACHYLGH------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 474 nsiKNNIKYSLYSLKDLEYLSDQLNEDGSASQDGLdkrnscrakCAGDLndmmkttdsDGLIHarknyniiddsevvnvs 553
Cdd:PRK13539 81 ---RNAMKPALTVAENLEFWAAFLGGEELDIAAAL---------EAVGL---------APLAH----------------- 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 554 kkvlihdfvsaLPDKYetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK13539 123 -----------LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
99-309 |
1.61e-08 |
|
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: 57.78 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 99 IIFSLVLIG--IFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIG 172
Cdd:cd18544 41 LLLALLYLGllLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVgrlvTRVTNDTEALNELFTSGLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 173 TKFLTIFTytsaFLGLYFWSLFKNARLTLCVTCVFPLIYICGVICNKKAK-----INKKTSLLynnNTMsiIEEALVGIR 247
Cdd:cd18544 121 TLIGDLLL----LIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRkayreVREKLSRL---NAF--LQESISGMS 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 248 TVVSYCGEHTILKKFN-LSEKLYsKYMLKANFMESLHIGMINGFILASYAFGFWYGTRIIISD 309
Cdd:cd18544 192 VIQLFNREKREFEEFDeINQEYR-KANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSG 253
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1330-1433 |
1.75e-08 |
|
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: 55.07 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1330 CKFAAIDEFIESLPNKY-DTNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD-----IK 1403
Cdd:smart00382 33 VIYIDGEDILEEVLDQLlLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLK 112
|
90 100 110
....*....|....*....|....*....|....*.
gi 221056887 1404 DKADRTIITIAHRIASIK------RSDKIVVFNNPD 1433
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGpallrrRFDRRIVLLLIL 148
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
829-1120 |
1.76e-08 |
|
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: 57.49 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 829 ALSIIVAGGLypmfALLYAKYVSTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLFE 905
Cdd:cd18576 2 LILLLLSSAI----GLVFPLLAGQLIDAALGGGDTaslNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 906 NILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCPIVAAVLTGT---YFIFMRV 982
Cdd:cd18576 78 HLQRLPLSFFHE--RRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATvpvVVLVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 983 F--AIRaRLSanKDVEkkginqpgtvflynndDEIfKDPSFLIQEAFYNMNTVIIYGLEDY----FCKLIEKAIDYSNKG 1056
Cdd:cd18576 156 FgrRIR-KLS--KKVQ----------------DEL-AEANTIVEETLQGIRVVKAFTREDYeierYRKALERVVKLALKR 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1057 QKRKTLVNS--MLWGFSQSAQLFinsfayWFGSFLIRRGTIEVDDfmksLFTFLF-TGSYAGKLMSL 1120
Cdd:cd18576 216 ARIRALFSSfiIFLLFGAIVAVL------WYGGRLVLAGELTAGD----LVAFLLyTLFIAGSIGSL 272
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
383-611 |
1.93e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 57.18 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYD-TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrsK 461
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-------------P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 I-------GVVSQ-DPLLFSNSIKNNIKYSLyslkdleylsdQLNedgsasqdGLDKRNScrakcagdlndmmkttdsdg 533
Cdd:COG4525 71 VtgpgadrGVVFQkDALLPWLNVLDNVAFGL-----------RLR--------GVPKAER-------------------- 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 534 liHARKNYNIiddsevvnvsKKVLIHDFVSALPdkYEtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4525 112 --RARAEELL----------ALVGLADFARRRI--WQ---------LSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
399-631 |
1.99e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.75 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindshnlkdinlkwwrskigvvsqdpllfsnsikn 478
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI----------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 479 nikyslyslkdleYLSDQLNEDGSASQDGLDKRNScrakcagdlndmmkttdsdGLIHaRKNYNIIDDSEVVNVSKKVLI 558
Cdd:PRK11629 68 -------------FNGQPMSKLSSAAKAELRNQKL-------------------GFIY-QFHHLLPDFTALENVAMPLLI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 559 ------------HDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylvQKTINNLK 626
Cdd:PRK11629 115 gkkkpaeinsraLEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN----ADSIFQLL 188
|
....*
gi 221056887 627 GNENR 631
Cdd:PRK11629 189 GELNR 193
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1353-1431 |
2.86e-08 |
|
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: 56.74 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1353 YGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:TIGR02769 147 LPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDK 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
403-671 |
3.55e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPT---EGDIIINDSH-NLKDINLKwwrSKIGVV--SQD----PLLf 472
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVcRFKDIRDS---EALGIViiHQElaliPYL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 473 snSIKNNIkyslyslkdleYLSdqlNEdgsasqdgldkrnscRAKcagdlndmmkttdsdgliharknYNIIDDSEVVNV 552
Cdd:NF040905 94 --SIAENI-----------FLG---NE---------------RAK-----------------------RGVIDWNETNRR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 553 SKKVLihDFVsALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVQkTINNLKgnENR 631
Cdd:NF040905 120 ARELL--AKV-GLDESPDTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LLLELK--AQG 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 221056887 632 IT-IIIAHRLSTIRY-ANTIFVLsnREKGNRSTVDV--DIIGED 671
Cdd:NF040905 190 ITsIIISHKLNEIRRvADSITVL--RDGRTIETLDCraDEVTED 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
384-635 |
3.81e-08 |
|
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: 55.61 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 384 QFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINlKW---WRS 460
Cdd:TIGR03410 2 EVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDG----EDIT-KLpphERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 K--IGVVSQDPLLFSN-SIKNNIkyslyslkdleylsdqlnedgsasQDGLDKRnscrakcagdlndmmkttdsdglihA 537
Cdd:TIGR03410 74 RagIAYVPQGREIFPRlTVEENL------------------------LTGLAAL-------------------------P 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 538 RKNYNIIDDsevvnvskkvlIHDFVSALPDkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:TIGR03410 105 RRSRKIPDE-----------IYELFPVLKE----MLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKD 169
|
250
....*....|....*...
gi 221056887 618 VQKTINNLKgNENRITII 635
Cdd:TIGR03410 170 IGRVIRRLR-AEGGMAIL 186
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1273-1436 |
4.41e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 NSGKILLDGVDICDYNLKDL----RNLFSIVSQEPILFNMSIYENIKFGK--EDATREDVKRACKfAAIDEFieSLPNKY 1346
Cdd:PRK10908 55 SAGKIWFSGHDITRLKNREVpflrRQIGMIFQDHHLLMDRTVYDNVAIPLiiAGASGDDIRRRVS-AALDKV--GLLDKA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1347 DTnvgpYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDsnsEKLIEKtIVDIKDKADR---TIITIAHRIASI-KR 1422
Cdd:PRK10908 132 KN----FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD---DALSEG-ILRLFEEFNRvgvTVLMATHDIGLIsRR 203
|
170
....*....|....
gi 221056887 1423 SDKIVVFNNPDRTG 1436
Cdd:PRK10908 204 SYRMLTLSDGHLHG 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1298-1433 |
4.51e-08 |
|
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: 57.50 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1298 IVSQEPILF-NMSIYEN------IKFGKEDATREDVkRACKFAAIDE-FIESLPNKYDTnvgpygkSLSGGQKQRVAIAR 1369
Cdd:TIGR03269 369 ILHQEYDLYpHRTVLDNlteaigLELPDELARMKAV-ITLKMVGFDEeKAEEILDKYPD-------ELSEGERHRVALAQ 440
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 1370 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRI---------ASIKRSDKIVVFNNPD 1433
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMdfvldvcdrAALMRDGKIVKIGDPE 513
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1274-1418 |
4.58e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.34 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNL-FSIVSQEP-----ILfNMSIYENIKFGKEDatREDVKRAC--KFAAIDEFIESLPNK 1345
Cdd:COG3845 312 SGSIRLDGEDITGLSPRERRRLgVAYIPEDRlgrglVP-DMSVAENLILGRYR--RPPFSRGGflDRKAIRAFAEELIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1346 YD---TNVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK--------AD-RTIITI 1413
Cdd:COG3845 389 FDvrtPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgaavllisEDlDEILAL 468
|
....*
gi 221056887 1414 AHRIA 1418
Cdd:COG3845 469 SDRIA 473
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1274-1387 |
5.24e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.27 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNL-KDLRNLFSIVSQEPILFN-MSIYENIKFGKEDATREDVKRAckfaaIDEFIESLPNKYDTNVG 1351
Cdd:PRK11614 59 SGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQER-----IKWVYELFPRLHERRIQ 133
|
90 100 110
....*....|....*....|....*....|....*.
gi 221056887 1352 PYGkSLSGGQKQRVAIARALLREPKILLLDEATSSL 1387
Cdd:PRK11614 134 RAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
390-656 |
6.50e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.78 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 390 FHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-DSHNLKDINLKWWRSKIGVVSQD 468
Cdd:PRK13638 9 FRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgKPLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 469 P--LLFSNSIKNNIKYSLYSLkdleylsdqlnedgSASQDGLDKRnscrakcagdLNDMMKTTDSDGLIHarknyniidd 546
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNL--------------GVPEAEITRR----------VDEALTLVDAQHFRH---------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 547 sevvnvskkvlihdfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
Cdd:PRK13638 132 ----------------------------QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
250 260 270
....*....|....*....|....*....|.
gi 221056887 627 GNENRItIIIAHRLSTI-RYANTIFVLSNRE 656
Cdd:PRK13638 184 AQGNHV-IISSHDIDLIyEISDAVYVLRQGQ 213
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
99-307 |
6.84e-08 |
|
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: 55.88 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 99 IIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNNP-G---SKLTSDLDFyLEQVnAGIGTK 174
Cdd:cd18541 42 YALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRtGdlmARATNDLNA-VRMA-LGPGIL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 175 FL--TIFTYTSAFlglyFWSLFKNARLTLCVTCVFPLIYICGVicnkkaKINKKTSLLYNNN-----TMS-IIEEALVGI 246
Cdd:cd18541 120 YLvdALFLGVLVL----VMMFTISPKLTLIALLPLPLLALLVY------RLGKKIHKRFRKVqeafsDLSdRVQESFSGI 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 247 RTVVSYCGEHTILKKF-NLSEKLYSKYMlKANFMESLHIGMINGFILASYAFGFWYGTRIII 307
Cdd:cd18541 190 RVIKAFVQEEAEIERFdKLNEEYVEKNL-RLARVDALFFPLIGLLIGLSFLIVLWYGGRLVI 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1272-1450 |
7.57e-08 |
|
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: 56.76 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1272 KNSGKILLDGVDICDYN-LKDLRNLFSIVSQEP----ILFNMSIYENIKFG--KEDATREDVKRACKFAAIDEFIESLPN 1344
Cdd:TIGR02633 313 KFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgIVPILGVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1345 KYDTNVGPYGkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdRTIITIAHRIASI-KRS 1423
Cdd:TIGR02633 393 KTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVlGLS 470
|
170 180
....*....|....*....|....*..
gi 221056887 1424 DKIVVFNNPDRTGSFVQAEGTHEELLS 1450
Cdd:TIGR02633 471 DRVLVIGEGKLKGDFVNHALTQEQVLA 497
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1298-1446 |
7.96e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1298 IVSQEPILF-NMSIYENIKFG--KEDATREDVKrackfAAIDEFIESLpnKYDTNVGpygkSLSGGQKQRVAIARALLRE 1374
Cdd:PRK15439 90 LVPQEPLLFpNLSVKENILFGlpKRQASMQKMK-----QLLAALGCQL--DLDSSAG----SLEVADRQIVEILRGLMRD 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 1375 PKILLLDEATSSLD-SNSEKLIEKtIVDIKDKaDRTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQAEGTHE 1446
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSR-IRELLAQ-GVGIVFISHKLPEIRQlADRISVM----RDGTIALSGKTAD 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1356-1388 |
9.55e-08 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 55.12 E-value: 9.55e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 221056887 1356 SLSGGQKQRVAIARALL-------REPKILLLDEATSSLD 1388
Cdd:COG4559 133 TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD 172
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
383-625 |
9.76e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.58 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKwwRSKI 462
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVD---GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA--RQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQ-DPLLFSNSIKNNIK-YSLYSlkdleylsdqlnedGSASQdgldkrnSCRAKCAGDLNdmmkttdsdgliHARkn 540
Cdd:PRK13537 83 GVVPQfDNLDPDFTVRENLLvFGRYF--------------GLSAA-------AARALVPPLLE------------FAK-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddsevvnvskkvlihdfvsaLPDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13537 128 ------------------------LENKADAKVG----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
....*
gi 221056887 621 TINNL 625
Cdd:PRK13537 180 RLRSL 184
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
827-1100 |
1.04e-07 |
|
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: 55.11 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 827 IIALSIIVAGGLYPmfALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLFEN 906
Cdd:cd18541 5 ILFLILVDLLQLLI--PRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 907 ILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFY---------FCPIVAAVLTGTYF 977
Cdd:cd18541 83 LLTLSPSFYQK--NRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTispkltliaLLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 978 ---IFMRVFAIRARLSAnkdvekkgINQpgtvflynnddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCKLIEKAidysN 1054
Cdd:cd18541 161 gkkIHKRFRKVQEAFSD--------LSD-------------------RVQESFSGIRVIKAFVQEEAEIERFDKL----N 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 221056887 1055 KGQKRKTLVNSMLWGFSQSAQLFINSFAY----WFGSFLIRRGTIEVDDF 1100
Cdd:cd18541 210 EEYVEKNLRLARVDALFFPLIGLLIGLSFlivlWYGGRLVIRGTITLGDL 259
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
825-1118 |
1.11e-07 |
|
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: 55.13 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 825 VVIIALSIIVAGglypmFALLYAKYVSTLFDFANLEANSN---KYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKH 901
Cdd:cd18542 2 LLAILALLLATA-----LNLLIPLLIRRIIDSVIGGGLREllwLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 902 RLFENILYQEISFFDqdcHAP-GLLSSHINRDV----HLLKTGL---VNNIVIFT-HFIVLFIVSMIMSFY---FCPIVa 969
Cdd:cd18542 77 DLYDHLQRLSFSFHD---KARtGDLMSRCTSDVdtirRFLAFGLvelVRAVLLFIgALIIMFSINWKLTLIslaIIPFI- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 970 avltgtyFIFMRVFAIRARlsankdvekkginqpgtvflynnddEIFKDpsflIQEAFYNMNTVI---IYG--------L 1038
Cdd:cd18542 153 -------ALFSYVFFKKVR-------------------------PAFEE----IREQEGELNTVLqenLTGvrvvkafaR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1039 EDYfckLIEKaIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFA----YWFGSFLIRRGTIEVDDfmksLFTFLftgSYA 1114
Cdd:cd18542 197 EDY---EIEK-FDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQivlvLWVGGYLVINGEITLGE----LVAFI---SYL 265
|
....
gi 221056887 1115 GKLM 1118
Cdd:cd18542 266 WMLI 269
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
399-611 |
1.11e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.86 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindSHNLKDINLKWWRS-KIGVVSQDPLLFSN-SI 476
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI----RFHGTDVSRLHARDrKVGFVFQHYALFRHmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 477 KNNIKYSLYSLKDleylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdgliHARKNYNIIDdsevvnvsKKV 556
Cdd:PRK10851 92 FDNIAFGLTVLPR----------------------------------------------RERPNAAAIK--------AKV 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 557 L-IHDFV--SALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10851 118 TqLLEMVqlAHLADRY-------PAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1272-1396 |
1.12e-07 |
|
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: 53.65 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1272 KNSGKILLDGVDICDYNLKDLRNLFSIVSQEPILFNMSIYENIKFGKEDATREDVKRACKFAAIDEFiESLPNKYdtnvg 1351
Cdd:cd03231 52 PLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----- 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 221056887 1352 pygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:cd03231 126 -----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1184-1431 |
1.12e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1184 DLTFSCDSKKTTAIVGETGSGKS----TVMSLLmrfydlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefslt 1259
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLL----------------------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1260 kegshgDNSAVFKNSGKILLDGVDICDYNLKDLR----NLFSIVSQEPI-----LFNM--SIYENIKFGKedATREDVKR 1328
Cdd:PRK15134 60 ------PSPPVVYPSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMvslnpLHTLekQLYEVLSLHR--GMRREAAR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1329 ACKFAAIDEF-IESLPNKydtnVGPYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAD 1407
Cdd:PRK15134 132 GEILNCLDRVgIRQAAKR----LTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELN 207
|
250 260
....*....|....*....|....*
gi 221056887 1408 RTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:PRK15134 208 MGLLFITHNLSIVRKlADRVAVMQN 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
403-652 |
1.19e-07 |
|
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: 54.66 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN-LK-WWRSKIGVVS--QDPLLFSN-SIK 477
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG----RDITgLPpHRIARLGIARtfQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 478 NNIKYSLYSLKDLEYLSDQLNEDGSASQDGldkrnSCRAKcAGDLNDMMkttdsdGLIHARknyniiddsevvnvskkvl 557
Cdd:COG0411 98 ENVLVAAHARLGRGLLAALLRLPRARREER-----EARER-AEELLERV------GLADRA------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 558 ihdfvsalpdkyETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQkTINNLKGNENrITI-I 635
Cdd:COG0411 147 ------------DEPAGN----LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELAE-LIRRLRDERG-ITIlL 208
|
250
....*....|....*...
gi 221056887 636 IAHRLSTI-RYANTIFVL 652
Cdd:COG0411 209 IEHDMDLVmGLADRIVVL 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1164-1434 |
1.19e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYMS-RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqg 1242
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILG----------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1243 deeqnvgmknvnefSLTKegshgdnsavfKNSGKILLDGVDICDYNLKDL----RNLFSIVSQE-PILFNMSIYENIKF- 1316
Cdd:PRK10535 56 --------------CLDK-----------PTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLSHLTAAQNVEVp 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1317 ----GKEDATREdvKRACKFAA---IDEFIESLPNKydtnvgpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDS 1389
Cdd:PRK10535 111 avyaGLERKQRL--LRAQELLQrlgLEDRVEYQPSQ-----------LSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 221056887 1390 NSEKLIEKTIVDIKDKAdRTIITIAH---------RIASIKrsDKIVVFNNPDR 1434
Cdd:PRK10535 178 HSGEEVMAILHQLRDRG-HTVIIVTHdpqvaaqaeRVIEIR--DGEIVRNPPAQ 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1274-1450 |
1.24e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.79 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDIC----DYNLKDLRNLFSIVSQ--EPILFNMSIYENIKFGKEDaTREDVKRAcKFAAIDEFIESLPNKYD 1347
Cdd:PRK13646 61 TGTVTVDDITIThktkDKYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKN-FKMNLDEV-KNYAHRLLMDLGFSRDV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1348 TNVGPYgkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKI 1426
Cdd:PRK13646 139 MSQSPF--QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEV 216
|
170 180
....*....|....*....|....
gi 221056887 1427 VVFNNpdrtGSFVQaEGTHEELLS 1450
Cdd:PRK13646 217 IVMKE----GSIVS-QTSPKELFK 235
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
890-1101 |
1.30e-07 |
|
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: 54.86 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 890 VIGEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKT--------GLVNNIVIFTHFIVLFIVSMIMS 961
Cdd:cd18574 68 VVGERVAARLRNDLFSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSsfkqcvsqGLRSVTQTVGCVVSLYLISPKLT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 962 FYFCPIV-AAVLTGTYF-IFMRVFAIRArlsanKDVEKKGINqpgtvflynnddeifkdpsfLIQEAFYNMNTVIIYGLE 1039
Cdd:cd18574 146 LLLLVIVpVVVLVGTLYgSFLRKLSRRA-----QAQVAKATG--------------------VADEALGNIRTVRAFAME 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1040 DYFCKLiekaidYSNKGQKRKTLvNSML---WGFSQS-AQLFINSFA---YWFGSFLIRRGTIEVDDFM 1101
Cdd:cd18574 201 DRELEL------YEEEVEKAAKL-NEKLglgIGIFQGlSNLALNGIVlgvLYYGGSLVSRGELTAGDLM 262
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
94-308 |
1.37e-07 |
|
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: 54.80 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 94 ENVDDIIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNN-PG---SKLTSDLDFyLEQVna 169
Cdd:cd18575 33 ALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTrTGevlSRLTTDTTL-IQTV-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 170 gIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYICGVICNKKAKINKKTSLLYNNNTMSIIEEALVGIRTV 249
Cdd:cd18575 110 -VGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTV 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 250 VSYCGEHTILKKFN-LSEKLYSKYmLKANFMESLHIGMINGFILASYAFGFWYGTRIIIS 308
Cdd:cd18575 189 QAFTREDAERQRFAtAVEAAFAAA-LRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLA 247
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
571-641 |
1.40e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.21 E-value: 1.40e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 571 TLVGSNASK--LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLS 641
Cdd:TIGR00955 156 TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQPS 227
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
569-649 |
1.41e-07 |
|
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: 53.10 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 569 YETLvGSNASKLSGGQKQRISIARAIIRNPK--ILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRYA 646
Cdd:cd03238 78 YLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTV-ILIEHNLDVLSSA 155
|
...
gi 221056887 647 NTI 649
Cdd:cd03238 156 DWI 158
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
377-473 |
1.46e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 377 LKDIKKIQFKNVRFHYDTRK-DVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINL 455
Cdd:PRK10522 317 FPDWQTLELRNVTFAYQDNGfSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVTAEQP 392
|
90
....*....|....*...
gi 221056887 456 KWWRSKIGVVSQDPLLFS 473
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFD 410
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1274-1428 |
1.56e-07 |
|
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: 53.30 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDynlkdlrnlfsivsqepilfnMSIYENIKFG-----KEDATREDVKrackfaaIDEFIESLpnkydt 1348
Cdd:cd03217 56 EGEILFKGEDITD---------------------LPPEERARLGiflafQYPPEIPGVK-------NADFLRYV------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1349 NVGpygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDRTIITIAH--RIASIKRSDKI 1426
Cdd:cd03217 102 NEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHyqRLLDYIKPDRV 175
|
..
gi 221056887 1427 VV 1428
Cdd:cd03217 176 HV 177
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1274-1388 |
1.58e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.08 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNLFSIVSQE-PILFNMSIYENIKFGKEDATREDVKRAckfaAIDEFIE--SLPNKYDTNV 1350
Cdd:COG4138 49 QGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYLALHQPAGASSEAVEQ----LLAQLAEalGLEDKLSRPL 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 221056887 1351 GpygkSLSGGQKQRVAIARALLR-------EPKILLLDEATSSLD 1388
Cdd:COG4138 125 T----QLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1357-1417 |
1.59e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.32 E-value: 1.59e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRI 1417
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
91-309 |
1.64e-07 |
|
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: 54.41 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 91 NLGENVDDIIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNN-PG---SKLTSDldfyLEQ 166
Cdd:cd18576 30 GDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERrVGeltSRLSND----VTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 167 VNAGIGTKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYICGVICNKK-AKINKKT--SLlynNNTMSIIEEAL 243
Cdd:cd18576 106 IQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRiRKLSKKVqdEL---AEANTIVEETL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 244 VGIRTVVSYCGEHTILKKFNLS-EKLYSKYMLKANFMeslhiGMINGFILASyAFG-----FWYGTRIIISD 309
Cdd:cd18576 183 QGIRVVKAFTREDYEIERYRKAlERVVKLALKRARIR-----ALFSSFIIFL-LFGaivavLWYGGRLVLAG 248
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
392-664 |
1.66e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.42 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 392 YDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDiNLKWWRSKIGVVSQDP-- 469
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE-NIREVRKFVGLVFQNPdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 470 LLFSNSIKNNIKYSLYSLkdleylsdqlnedgsasqdGLDKrnscrakcagdlndmmkttdsDGLIHarknyniiddsEV 549
Cdd:PRK13652 90 QIFSPTVEQDIAFGPINL-------------------GLDE---------------------ETVAH-----------RV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 550 VNVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 629
Cdd:PRK13652 119 SSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETY 187
|
250 260 270
....*....|....*....|....*....|....*.
gi 221056887 630 NRITIIIAHRLSTI-RYANTIFVLSNREKGNRSTVD 664
Cdd:PRK13652 188 GMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVE 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1185-1449 |
1.68e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1185 LTFScdSKKTTAIVGETGSGKSTVMSLLMRfydlkndHHIvfknehtddvnnekkeqgdeeqnvgmknvnefsltkegsh 1264
Cdd:PRK10575 32 LTFP--AGKVTGLIGHNGSGKSTLLKMLGR-------HQP---------------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1265 gdnsavfKNSGKILLDGVDICDYNLKDL-RNLFSIVSQEPILFNMSIYENI------------KFGKEDatREDVKRACK 1331
Cdd:PRK10575 63 -------PSEGEILLDAQPLESWSSKAFaRKVAYLPQQLPAAEGMTVRELVaigrypwhgalgRFGAAD--REKVEEAIS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1332 FAAIDEFIESLPNkydtnvgpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTII 1411
Cdd:PRK10575 134 LVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVI 202
|
250 260 270
....*....|....*....|....*....|....*....
gi 221056887 1412 TIAHRIASIKR-SDKIVVFnnpdRTGSFVqAEGTHEELL 1449
Cdd:PRK10575 203 AVLHDINMAARyCDYLVAL----RGGEMI-AQGTPAELM 236
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1193-1439 |
1.68e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1193 KTTAIVGETGSGKSTVMSLLMRFYDlKNDHHIVFKNEHTDdVNNEKkeqgdEEQNVGMknvnefsltkegshgdnsavfk 1272
Cdd:PRK10762 31 RVMALVGENGAGKSTMMKVLTGIYT-RDAGSILYLGKEVT-FNGPK-----SSQEAGI---------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1273 nsgkilldgvdicdynlkdlrnlfSIVSQE-PILFNMSIYENIKFGKEDAT---REDVKRAckFAAIDEFIESLPNKY-- 1346
Cdd:PRK10762 82 ------------------------GIIHQElNLIPQLTIAENIFLGREFVNrfgRIDWKKM--YAEADKLLARLNLRFss 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1347 DTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSL-DSNSEKLIeKTIVDIKDKaDRTIITIAHRIASI-KRSD 1424
Cdd:PRK10762 136 DKLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELKSQ-GRGIVYISHRLKEIfEICD 209
|
250
....*....|....*
gi 221056887 1425 KIVVFnnpdRTGSFV 1439
Cdd:PRK10762 210 DVTVF----RDGQFI 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1196-1428 |
1.68e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1196 AIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtddvnnekkeqgdeeqnvgmknvnefsltkegSHGDNSavfknsG 1275
Cdd:NF040905 31 ALCGENGAGKSTLMKVLSGVY----------------------------------------------PHGSYE------G 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1276 KILLDGvDICDYnlKDLRNlfS------IVSQEPILF-NMSIYENIKFGKEDATR------EDVKRACKFAAIDEFIESl 1342
Cdd:NF040905 59 EILFDG-EVCRF--KDIRD--SealgivIIHQELALIpYLSIAENIFLGNERAKRgvidwnETNRRARELLAKVGLDES- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1343 PnkyDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKDKADRTIItIAHRIASIK 1421
Cdd:NF040905 133 P---DTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LLLELKAQGITSII-ISHKLNEIR 203
|
....*...
gi 221056887 1422 R-SDKIVV 1428
Cdd:NF040905 204 RvADSITV 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1347-1415 |
1.85e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.71 E-value: 1.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1347 DTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadrTIITIAH 1415
Cdd:TIGR03719 156 DADVT----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTH 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
403-611 |
1.89e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.94 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshNLKDINLKWWRSKIGVVSQ-DPLLFSNSIKNNIK 481
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI------TLDGKPVEGPGAERGVVFQnEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 482 YSLyslkdleylsdQLNedgsasqdGLDKRNscRAKCAGDlndMMKTTDSDGLiHARKNYniiddsevvnvskkvlihdf 561
Cdd:PRK11248 93 FGL-----------QLA--------GVEKMQ--RLEIAHQ---MLKKVGLEGA-EKRYIW-------------------- 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 221056887 562 vsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11248 128 -----------------QLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
397-654 |
2.19e-07 |
|
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: 52.91 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI---ERlYDPTEGDIIInDSHNLKDINLKWwRSK--IGVVSQDPLL 471
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPK-YEVTEGEILF-KGEDITDLPPEE-RARlgIFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 472 FSnsiknnikyslySLKDLEYLsdqlnedgsasqdgldkRNscrakcagdlndmmkttdsdgliharknyniiddsevVN 551
Cdd:cd03217 89 IP------------GVKNADFL-----------------RY-------------------------------------VN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 552 VSkkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENR 631
Cdd:cd03217 103 EG--------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLR-EEGK 155
|
250 260
....*....|....*....|....*
gi 221056887 632 ITIIIAHRLSTIRY--ANTIFVLSN 654
Cdd:cd03217 156 SVLIITHYQRLLDYikPDRVHVLYD 180
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
386-607 |
2.29e-07 |
|
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: 53.45 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 386 KNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI-NLKWW---RSK 461
Cdd:COG0410 7 ENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDItGLPPHriaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDleylsdqlnedgsasqdgldkrnscRAKCAGDLndmmkttdsdgliharkn 540
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLLLGAYARRD-------------------------RAEVRADL------------------ 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 541 yniiddsevvnvskkvlihDFVSAL-PDKYETLvGSNASKLSGGQKQRISIARAIIRNPKILILDEAT 607
Cdd:COG0410 117 -------------------ERVYELfPRLKERR-RQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
570-655 |
2.43e-07 |
|
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: 51.61 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN-----NLKGNENRITIIIAHRLSTIR 644
Cdd:smart00382 51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNLTVILTTNDEKDLG 130
|
90
....*....|.
gi 221056887 645 YANTIFVLSNR 655
Cdd:smart00382 131 PALLRRRFDRR 141
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
404-611 |
2.93e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.64 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdiNLKWWRSKigvvsqdplLFSnsiknnikys 483
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ------PLESWSSK---------AFA---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 484 lyslKDLEYLSDQLnedgsASQDGLDKRNSC---RAKCAGDLNdmmkttdsdgliharkNYNIIDDSEVVNVSKKVLIHD 560
Cdd:PRK10575 85 ----RKVAYLPQQL-----PAAEGMTVRELVaigRYPWHGALG----------------RFGAADREKVEEAISLVGLKP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 221056887 561 FVSALPDkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10575 140 LAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1347-1415 |
2.99e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 2.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1347 DTNVGPygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadrTIITIAH 1415
Cdd:PRK11819 158 DAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG----TVVAVTH 218
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
827-1095 |
3.17e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 53.67 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 827 IIALSIIVAGglypmFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAM---FISETLKNYYNNVIGEKVEKTMKHRL 903
Cdd:cd18555 7 ILLLSLLLQL-----LTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFllyGLFSFLRGYIIIKLQTKLDKSLMSDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 904 FENILYQEISFFDQdcHAPGLLSSHINRDVHL-------LKTGLVNNIVIFTHFIVLFIVSMIMSFYfcpivaaVLTGTY 976
Cdd:cd18555 82 FEHLLKLPYSFFEN--RSSGDLLFRANSNVYIrqilsnqVISLIIDLLLLVIYLIYMLYYSPLLTLI-------VLLLGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 977 FIFMRVFairarLSANKdVEKKginqpgtvflynNDDEIF---KDPSFLIqEAFYNMNTVIIYGLEDYFCK----LIEKA 1049
Cdd:cd18555 153 LIVLLLL-----LTRKK-IKKL------------NQEEIVaqtKVQSYLT-ETLYGIETIKSLGSEKNIYKkwenLFKKQ 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 221056887 1050 IDYSnkgqKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTI 1095
Cdd:cd18555 214 LKAF----KKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1307-1399 |
3.22e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.57 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1307 NMSIYENIKFGKE--DATREDVKRACKFAAIDEfIESLPNKYdtnvgpygksLSGGQKQRVAIARALLREPKILLLDEAT 1384
Cdd:PRK13539 87 ALTVAENLEFWAAflGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
90
....*....|....*
gi 221056887 1385 SSLDSNSEKLIEKTI 1399
Cdd:PRK13539 156 AALDAAAVALFAELI 170
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
99-309 |
3.35e-07 |
|
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: 53.72 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 99 IIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVF---------YQDG----QFHDNNpgsKLTSDLdfyle 165
Cdd:cd18568 44 ILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLslplsffasRKVGdiitRFQENQ---KIRRFL----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 166 qVNAGIGT--KFLTIFTYtsafLGLYFWslfKNARLTLCVTCVFPLIYICGVICNKKAKINKKTSLLYNNNTMSIIEEAL 243
Cdd:cd18568 116 -TRSALTTilDLLMVFIY----LGLMFY---YNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 244 VGIRTVVSYCGEHTILKKFnlsEKLYSKyMLKANF-MESLHI--GMINGFI-LASYAFGFWYGTRIIISD 309
Cdd:cd18568 188 TGIATIKALAAERPIRWRW---ENKFAK-ALNTRFrGQKLSIvlQLISSLInHLGTIAVLWYGAYLVISG 253
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
399-614 |
3.67e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.56 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLydptegdiiinDshnlKDINLKWWRS---KIGVVSQDPLLFSN- 474
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------D----KDFNGEARPQpgiKVGYLPQEPQLDPTk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 475 SIKNNIKYSLYSLKDLeylsdqlnedgsasqdgLDKRNSCRAKCAGDLNDMMKTTDSDGLIHarknyNIIDDSEVVNVSK 554
Cdd:TIGR03719 84 TVRENVEEGVAEIKDA-----------------LDRFNEISAKYAEPDADFDKLAAEQAELQ-----EIIDAADAWDLDS 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 555 KVLIHDFVSALPDKyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:TIGR03719 142 QLEIAMDALRCPPW-----DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1355-1430 |
3.74e-07 |
|
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: 52.72 E-value: 3.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1355 KSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFN 1430
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVID 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1353-1430 |
3.92e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 3.92e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1353 YGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFN 1430
Cdd:PRK10261 460 YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMY 538
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
404-640 |
4.01e-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: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI--NLKWWRSKIGVVSQDPLLFSN-SIKNNI 480
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----KDIetNLDAVRQSLGMCPQHNILFHHlTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 481 KYsLYSLKDLEYLSDQLnedgsasqdgldkrnscrakcagDLNDMMKTTdsdGLIHARKnyniiddsevvnvskkvlihd 560
Cdd:TIGR01257 1025 LF-YAQLKGRSWEEAQL-----------------------EMEAMLEDT---GLHHKRN--------------------- 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 561 fvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRL 640
Cdd:TIGR01257 1057 --------------EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
403-652 |
4.64e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPT---EGDIIINDS----HNLKDINlkwwRSKIGVVSQDPLLFSN- 474
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEelqaSNIRDTE----RAGIAIIHQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 475 SIKNNIkyslyslkdleYLSDQLNEdgsasqdgldkrnscrakcAGDLNDMMKTTDSDGLIHARKnyniIDdsevVNVSK 554
Cdd:PRK13549 98 SVLENI-----------FLGNEITP-------------------GGIMDYDAMYLRAQKLLAQLK----LD----INPAT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 555 KVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITI 634
Cdd:PRK13549 140 PV---------------------GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACI 197
|
250
....*....|....*....
gi 221056887 635 IIAHRLSTI-RYANTIFVL 652
Cdd:PRK13549 198 YISHKLNEVkAISDTICVI 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1307-1454 |
4.71e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.27 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1307 NMSIYENIK-----FGKEDAT-REDVKRACKFAaidefieSLPNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLL 1380
Cdd:PRK13537 94 DFTVRENLLvfgryFGLSAAAaRALVPPLLEFA-------KLENKADAKVG----ELSGGMKRRLTLARALVNDPDVLVL 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1381 DEATSSLDSNSEKLIEKTIVDIKdKADRTIITIAHRIASIKR-SDKIVVFNNPDRTgsfvqAEGTHEELLSVQDG 1454
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERlCDRLCVIEEGRKI-----AEGAPHALIESEIG 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1333-1395 |
4.97e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 53.68 E-value: 4.97e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1333 AAIDEFIE--SLPNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK13536 151 AVIPSLLEfaRLESKADARVS----DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
387-643 |
5.62e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 387 NVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIeRLYDPTEGDiiindshnlkdinlkwwrskigvV 465
Cdd:PRK10261 19 NIAFMQE-QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGL-----------------------V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 466 SQDPLLFSNSIKNNIKyslyslkdleyLSDQlnedgSASQdgldKRNSCRAKCAGDLNDMMKT-----TDSDGLIHARKN 540
Cdd:PRK10261 74 QCDKMLLRRRSRQVIE-----------LSEQ-----SAAQ----MRHVRGADMAMIFQEPMTSlnpvfTVGEQIAESIRL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 YNIIDDSEVVNVSKKVLihDFVSaLPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK10261 134 HQGASREEAMVEAKRML--DQVR-IPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ 209
|
250 260
....*....|....*....|...
gi 221056887 621 TINNLKGNENRITIIIAHRLSTI 643
Cdd:PRK10261 210 LIKVLQKEMSMGVIFITHDMGVV 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1164-1453 |
6.04e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.85 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTymsRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtddvnnekkeqgd 1243
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI------------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 eeqnvgmknvnefsltkegshgdNSAVFKNSGKILLDGVDI---CDYNLKDLRNLFSIVSQEPILF-NMSIYENIKFGKE 1319
Cdd:PRK11831 54 -----------------------GGQIAPDHGEILFDGENIpamSRSRLYTVRKRMSMLFQSGALFtDMNVFDNVAYPLR 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1320 DATR--EDVKRACKFAAidefIESLPNKYDTNVGPygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:PRK11831 111 EHTQlpAPLLHSTVMMK----LEAVGLRGAAKLMP--SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1398 TIVDIKDKADRTIITIAH---RIASIKRSDKIVvfnnpdrTGSFVQAEGTHEELLSVQD 1453
Cdd:PRK11831 185 LISELNSALGVTCVVVSHdvpEVLSIADHAYIV-------ADKKIVAHGSAQALQANPD 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1357-1388 |
6.15e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.13 E-value: 6.15e-07
10 20 30
....*....|....*....|....*....|..
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
386-626 |
6.73e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.20 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 386 KNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINL----KWWRSK 461
Cdd:PRK10895 7 KNLAKAYKGRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD----EDISLlplhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEylSDQLNEdgsasqdgldkrnscRAkcagdlNDMMKTTDsdgLIHARKN 540
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLQIRDDLS--AEQRED---------------RA------NELMEEFH---IEHLRDS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 YniiddsevvnvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK10895 134 M-----------------------------------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
....*.
gi 221056887 621 TINNLK 626
Cdd:PRK10895 179 IIEHLR 184
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
580-652 |
6.85e-07 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 51.47 E-value: 6.85e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRLSTIRYANTIFVL 652
Cdd:NF040873 120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
415-641 |
7.51e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.41 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 415 AFVGESGCGKSTILKLIERLYDPTEG-----DIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKd 489
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHK- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 490 leylsdqlnedgsasqdgldkrnscrakcagdlndmmkttdsdglIHARKNYNIIDDSEVVNVSKKVLIHDFVSALPdky 569
Cdd:PRK14271 130 ---------------------------------------------LVPRKEFRGVAQARLTEVGLWDAVKDRLSDSP--- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221056887 570 etlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRIT-IIIAHRLS 641
Cdd:PRK14271 162 --------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA---DRLTvIIVTHNLA 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1272-1450 |
7.57e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1272 KNSGKILLDG--VDI--CdynLKDLRNLFSIVSQEP----ILFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIES 1341
Cdd:PRK13549 315 RWEGEIFIDGkpVKIrnP---QQAIAQGIAMVPEDRkrdgIVPVMGVGKNITLAALDrfTGGSRIDDAAELKTILESIQR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1342 LPNKYDTNVGPYGkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADRTIITIAHRIASI- 1420
Cdd:PRK13549 392 LKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVl 469
|
170 180 190
....*....|....*....|....*....|
gi 221056887 1421 KRSDKIVVFNNPDRTGSFVQAEGTHEELLS 1450
Cdd:PRK13549 470 GLSDRVLVMHEGKLKGDLINHNLTQEQVME 499
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
865-1117 |
7.81e-07 |
|
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: 52.39 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 865 KYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNI 944
Cdd:cd18544 42 LLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR--TPVGRLVTRVTNDTEALNELFTSGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 945 VIFTHFIVLFIVSMIMSFYFCPIVAAVLTGT---YFIFMRVFAIRARlSANKDVEKK--GINqpgtvflynnddeifkdp 1019
Cdd:cd18544 120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVlplLLLATYLFRKKSR-KAYREVREKlsRLN------------------ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1020 SFLiQEAFYNMNTVIIYGLEDYFCKLIEKAidysNKGQKRKTLVNSMLWGFSQSAQLFINSFAY----WFGSFLIRRGTI 1095
Cdd:cd18544 181 AFL-QESISGMSVIQLFNREKREFEEFDEI----NQEYRKANLKSIKLFALFRPLVELLSSLALalvlWYGGGQVLSGAV 255
|
250 260
....*....|....*....|..
gi 221056887 1096 EVDdfmkSLFTFLftgSYAGKL 1117
Cdd:cd18544 256 TLG----VLYAFI---QYIQRF 270
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1356-1422 |
8.02e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 8.02e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1356 SLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadrTIITIAHRIASIKR 1422
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRN 218
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
866-1097 |
8.03e-07 |
|
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: 52.47 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 866 YSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLFENILYQEISFFDQdcHAPG-LLSSHINrDVH----LLKTGL 940
Cdd:cd18545 42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDS--RPVGkILSRVIN-DVNslsdLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 941 VNnivIFTHFIVLFIVSMIMsFYF-------CPIVAAVLtgtyFIFMRVFAIRARlSANKDVEKK--GINqpgtvflynn 1011
Cdd:cd18545 119 IN---LIPDLLTLVGIVIIM-FSLnvrlalvTLAVLPLL----VLVVFLLRRRAR-KAWQRVRKKisNLN---------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1012 ddeifkdpSFLiQEAFYNMNTVIIYGLEDYFCKLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIR 1091
Cdd:cd18545 180 --------AYL-HESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVL 250
|
....*.
gi 221056887 1092 RGTIEV 1097
Cdd:cd18545 251 GGAITV 256
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
400-652 |
1.07e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSN-SIKN 478
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-DGEHIQHYASKEVARRIGLLAQNATTPGDiTVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 479 NIKYSLYSLKDLeyLSDQLNEDGSAsqdgldkrnscrakcagdLNDMMKTTdsdGLIHarknyniiddsevvnvskkvli 558
Cdd:PRK10253 101 LVARGRYPHQPL--FTRWRKEDEEA------------------VTKAMQAT---GITH---------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 559 hdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
Cdd:PRK10253 136 -------------LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLH 202
|
250
....*....|....*
gi 221056887 639 RLS-TIRYANTIFVL 652
Cdd:PRK10253 203 DLNqACRYASHLIAL 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
383-638 |
1.08e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.19 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDT-RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG-------DIIINDSHNLKDIN 454
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 455 lkwwRSKIGVVSQdpllfsnsiknniKYSLyslkdLEYLSDQLNEDGSASQDGLDKRNscRAKCAGDLNDMMkttdsdGL 534
Cdd:PRK10535 85 ----REHFGFIFQ-------------RYHL-----LSHLTAAQNVEVPAVYAGLERKQ--RLLRAQELLQRL------GL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 535 iHARKNYNiiddsevvnvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK10535 135 -EDRVEYQ----------------------------------PSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
250 260
....*....|....*....|....
gi 221056887 615 EYLVQKTINNLKgNENRITIIIAH 638
Cdd:PRK10535 180 GEEVMAILHQLR-DRGHTVIIVTH 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
385-654 |
1.16e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 385 FKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI---NLKWWRS 460
Cdd:PTZ00243 1311 FEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG----REIgayGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 461 KIGVVSQDPLLFSNSIKNNIkyslyslkdleylsDQLNEDGSAsqdgldkrnscrakcagdlndmmkttdsdgliharkn 540
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNV--------------DPFLEASSA------------------------------------- 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 541 yniiddsEVVNVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILIL-DEATSSLDNKSEYLVQ 619
Cdd:PTZ00243 1414 -------EVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQ 1486
|
250 260 270
....*....|....*....|....*....|....*
gi 221056887 620 KTINNLKGNENRITiiIAHRLSTIRYANTIFVLSN 654
Cdd:PTZ00243 1487 ATVMSAFSAYTVIT--IAHRLHTVAQYDKIIVMDH 1519
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
398-643 |
1.18e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKwwRSK------IGVVSQD-PL 470
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG----KEIDFK--SSKealengISMVHQElNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 471 LFSNSIKNNIKYSLYSLKDLEYLSDQLNEDGSASQDGLDkrnscrakcagdlndmmkttdsdgliharknyniIDdsevV 550
Cdd:PRK10982 85 VLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELD----------------------------------ID----I 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 551 NVSKKVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 630
Cdd:PRK10982 127 DPRAKV---------------------ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGC 185
|
250
....*....|...
gi 221056887 631 RItIIIAHRLSTI 643
Cdd:PRK10982 186 GI-VYISHKMEEI 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
580-655 |
1.32e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 1.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVqKTINNLKgNENRITIIIAHRLstiryaNTIFVLSNR 655
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAReIEQLF-RVIRELR-AEGRVILYVSHRM------EEIFALCDA 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1193-1415 |
1.39e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.93 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1193 KTTAIVGETGSGKSTVMSLLMRFYD-LKNDHHIVFKNEHTDDvnnEKKEQGDEEQNVGMknvnefsltkegshgdnsaVF 1271
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDgSSGEVSLVGQPLHQMD---EEARAKLRAKHVGF-------------------VF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1272 KNsgkilldgvdicdynlkdlrnlFSIVSQEPILFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKydtnvg 1351
Cdd:PRK10584 95 QS----------------------FMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ------ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 1352 pygksLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAH 1415
Cdd:PRK10584 147 -----LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
400-639 |
1.47e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.73 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY--DPTEGDIIINDshnlkdinLKWWRSKIGVvsqdpllfsnsik 477
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD--------NQFGREASLI------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 478 nnikyslyslkdleylsdqlnedgsasqDGLDKRnscrakcaGDLNDMMKTTDSDGLiharknyniiddSEVVNVSKKVl 557
Cdd:COG2401 104 ----------------------------DAIGRK--------GDFKDAVELLNAVGL------------SDAVLWLRRF- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 558 ihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIA 637
Cdd:COG2401 135 --------------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL-ARRAGITLVVA 193
|
...
gi 221056887 638 -HR 639
Cdd:COG2401 194 tHH 196
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1274-1419 |
1.55e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKdlRNLFsiVSQEPILF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNV 1350
Cdd:PLN03211 124 TGTILANNRKPTKQILK--RTGF--VTQDDILYpHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTII 199
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1351 G-PYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdRTIITIAHRIAS 1419
Cdd:PLN03211 200 GnSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKG-KTIVTSMHQPSS 268
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
830-1071 |
1.76e-06 |
|
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: 51.33 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 830 LSIIVAGGLypMFALLYAkyVSTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLFEN 906
Cdd:cd18575 3 IALLIAAAA--TLALGQG--LRLLIDQGFAAGNTallNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 907 ILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCP--------IVAAVLtgtyfI 978
Cdd:cd18575 79 LLRLSPSFFET--TRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltllvllVIPLVV-----L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 979 FMRVFAIRAR-LSANkdvekkgiNQpgtvflynndDEIfKDPSFLIQEAFYNMNTVIIYGLEDY----FCKLIEKAIDYS 1053
Cdd:cd18575 152 PIILFGRRVRrLSRA--------SQ----------DRL-ADLSAFAEETLSAIKTVQAFTREDAerqrFATAVEAAFAAA 212
|
250
....*....|....*...
gi 221056887 1054 nkgqKRKTLVNSMLWGFS 1071
Cdd:cd18575 213 ----LRRIRARALLTALV 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1274-1388 |
1.78e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.09 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDL---RNLFSivSQEPILFNMSIYENIKFGKEDATREDVKRAckfaAIDEFIES--LPNKYDT 1348
Cdd:PRK03695 49 SGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPFAMPVFQYLTLHQPDKTRTEAVAS----ALNEVAEAlgLDDKLGR 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 221056887 1349 NVGpygkSLSGGQKQRVAIARALLR-------EPKILLLDEATSSLD 1388
Cdd:PRK03695 123 SVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1355-1416 |
1.78e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.73 E-value: 1.78e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 1355 KSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHR 1416
Cdd:COG2401 135 KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHH 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1274-1454 |
1.81e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDICDYNLKDLRNL-FSIVSQEPILFN-MSIYENIKFGKEdATRE-------DVKRACKFAAIDEFIESLPN 1344
Cdd:PRK09700 59 KGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDeLTVLENLYIGRH-LTKKvcgvniiDWREMRVRAAMMLLRVGLKV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1345 KYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSL-DSNSEKLIekTIVDIKDKADRTIITIAHRIASIKR- 1422
Cdd:PRK09700 138 DLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLRKEGTAIVYISHKLAEIRRi 211
|
170 180 190
....*....|....*....|....*....|..
gi 221056887 1423 SDKIVVFNNPDRTGSFVQAEGTHEELLSVQDG 1454
Cdd:PRK09700 212 CDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
382-651 |
1.89e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.63 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 382 KIQFKNVRFHYDTRKDVEI--YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI--IINDSHNLKDINLKW 457
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 458 W---------------------RSKIGVVSQ--DPLLFSNSIKNNIKYSLYSlkdleylsdqlnedgsasqdgldkrnsc 514
Cdd:PRK13651 82 KvleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQTIEKDIIFGPVS---------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 515 rakcagdlndmMKTTDSDGLIHARKNYNIIDdsevvnvskkvlihdfvsaLPDKYetlVGSNASKLSGGQKQRISIARAI 594
Cdd:PRK13651 134 -----------MGVSKEEAKKRAAKYIELVG-------------------LDESY---LQRSPFELSGGQKRRVALAGIL 180
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 595 IRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIA-HRL-STIRYAN-TIFV 651
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNL--NKQGKTIILVtHDLdNVLEWTKrTIFF 238
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
579-652 |
2.32e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 2.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVM 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1335-1431 |
2.40e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.24 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1335 IDEFIE--SLPNKYDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIIT 1412
Cdd:COG4586 135 LDELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILL 210
|
90 100
....*....|....*....|
gi 221056887 1413 IAHRIASIKR-SDKIVVFNN 1431
Cdd:COG4586 211 TSHDMDDIEAlCDRVIVIDH 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
407-645 |
2.66e-06 |
|
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: 50.48 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 407 TLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnLKDINLKwwrskigvvsqdPllfsnsiknnikyslys 486
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE----LDTVSYK------------P----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 487 lkdlEYLSdqlnedgsasqdgldkrnscrAKCAGDLNDMMKTTDSDGLIHARKNYNIIDdsevvnvskkvlihdfvsalP 566
Cdd:cd03237 68 ----QYIK---------------------ADYEGTVRDLLSSITKDFYTHPYFKTEIAK--------------------P 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 567 DKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
Cdd:cd03237 103 LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDY 181
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
397-671 |
3.16e-06 |
|
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: 51.75 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY--DPTEGDIIINDS----HNLKDINlkwwRSKIGVVSQDPL 470
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSplkaSNIRDTE----RAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 471 LFSN-SIKNNIkyslyslkdleYLSDQLNEDGSasqdgldkrnscrakcagdlndmmkttdsdgliharknynIIDDSEV 549
Cdd:TIGR02633 89 LVPElSVAENI-----------FLGNEITLPGG----------------------------------------RMAYNAM 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 550 VNVSKKVLIHDFVSALPdkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNe 629
Cdd:TIGR02633 118 YLRAKNLLRELQLDADN------VTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH- 190
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 221056887 630 NRITIIIAHRLSTIR-YANTIFVLsnREKGNRSTVDVDIIGED 671
Cdd:TIGR02633 191 GVACVYISHKLNEVKaVCDTICVI--RDGQHVATKDMSTMSED 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1164-1447 |
3.21e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.60 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1164 IEIMDVNFTYmsrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtddvnnekkeqGD 1243
Cdd:COG0488 316 LELEGLSKSY---GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA----------------------------GE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1244 EEQNvgmknvnefsltkegshgdnsavfknSGKILLdGVdicdyNLKdlrnlFSIVSQEPILF--NMSIYENIKFGKEDA 1321
Cdd:COG0488 365 LEPD--------------------------SGTVKL-GE-----TVK-----IGYFDQHQEELdpDKTVLDELRDGAPGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1322 TREDVkRAckfaaideFIESL---PNKYDTNVGpygkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG0488 408 TEQEV-RG--------YLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1399 IVDIKDkadrTIITIAH------RIAsikrsDKIVVFNNpdrtGSFVQAEGTHEE 1447
Cdd:COG0488 475 LDDFPG----TVLLVSHdryfldRVA-----TRILEFED----GGVREYPGGYDD 516
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1353-1428 |
3.46e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.90 E-value: 3.46e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1353 YGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKRS-DKIVV 1428
Cdd:PRK11022 150 YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAaHKIIV 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1357-1415 |
3.50e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 50.11 E-value: 3.50e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAH 1415
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
571-653 |
3.52e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.80 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 571 TLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRYA--N 647
Cdd:PLN03211 197 TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSRVYQmfD 275
|
....*.
gi 221056887 648 TIFVLS 653
Cdd:PLN03211 276 SVLVLS 281
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
825-1109 |
4.84e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 50.23 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 825 VVIIALSIIVAGGLYPMFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLF 904
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 905 ENILYQEISFFDQdcHAPGLLSSHINRDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCPIVAAV-LTGTYFI--FMR 981
Cdd:cd18778 81 DKLQRLSLRYFDD--RQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLtLIPIPFLalGAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 982 VFAIRARlsankdvekkginqPgtvfLYNNDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYfckliEKAiDYSNKGQK-RK 1060
Cdd:cd18778 159 LYSKKVR--------------P----RYRKVREALGELNALLQDNLSGIREIQAFGREEE-----EAK-RFEALSRRyRK 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 221056887 1061 TLVNSM-LWGFSQSAQLFINSFAY----WFGSFLIRRGTIEVDDfmksLFTFLF 1109
Cdd:cd18778 215 AQLRAMkLWAIFHPLMEFLTSLGTvlvlGFGGRLVLAGELTIGD----LVAFLL 264
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
386-611 |
4.99e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.54 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 386 KNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDII-------INDSHNLKDINLKW- 457
Cdd:PRK11701 10 RGLTKLYGPRKGCR---DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqLRDLYALSEAERRRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 458 WRSKIGVVSQDP---LLFSNSIKNNIKYSLYSLKDLEYlsdqlnedgsasqdgldkrnscrakcaGDLNDmmktTDSDGL 534
Cdd:PRK11701 87 LRTEWGFVHQHPrdgLRMQVSAGGNIGERLMAVGARHY---------------------------GDIRA----TAGDWL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 535 IHARKNYNIIDDsevvnvskkvlihdfvsaLPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11701 136 ERVEIDAARIDD------------------LPTTF-----------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1322-1388 |
5.67e-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: 50.94 E-value: 5.67e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1322 TREDVKRACKFAAIDEFIE--SLPNKYDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:COG1245 180 VRELLEKVDERGKLDELAEklGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1355-1415 |
6.01e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 6.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 1355 KSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdikdKADRTIITIAH 1415
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSH 399
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1274-1417 |
6.73e-06 |
|
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: 51.17 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1274 SGKILLDGVDIcDYNLKDLRNLFSIVSQEPILFN-MSIYENIKFGKEDATREDVKRACKFAAIDEfIESLPNKYDTNvgp 1352
Cdd:TIGR01257 984 SGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEEAQLEMEAMLE-DTGLHHKRNEE--- 1058
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 1353 yGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADRTIITIAHRI 1417
Cdd:TIGR01257 1059 -AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1322-1388 |
6.89e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 6.89e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 1322 TREDVKRACKFAAIDEFIE--SLPNKYDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK13409 180 VRELLKKVDERGKLDEVVErlGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
579-640 |
6.98e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 6.98e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PRK09544 120 KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
406-611 |
8.66e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 406 FTLTEGKTYAFVGESGCGKSTILKLI--ERLYDptEGDIIINdshnlKDInlkwwrskigVVS---QDPllfsnsiKNNI 480
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILngEVLLD--DGRIIYE-----QDL----------IVArlqQDP-------PRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 481 KYSLYS------------LKDLEYLSDQLNEDGSasqdgldKRNscrakcagdLNDMMKTTDsdgliharknynIID--- 545
Cdd:PRK11147 80 EGTVYDfvaegieeqaeyLKRYHDISHLVETDPS-------EKN---------LNELAKLQE------------QLDhhn 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 546 ----DSEVVNVSKKVLIHdfvsalPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11147 132 lwqlENRINEVLAQLGLD------PDA-------ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
580-654 |
9.82e-06 |
|
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: 47.81 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIahrLST-----IRYANTIFVLSN 654
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA--DAGKAVLL---ISSeldelLGLCDRILVMYE 179
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
570-645 |
1.22e-05 |
|
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: 48.52 E-value: 1.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRY 645
Cdd:cd03236 130 RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV-LVVEHDLAVLDY 204
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
99-337 |
1.26e-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: 48.62 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 99 IIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNNP-G---SKLTSDLDFYLEQVNAGIGTK 174
Cdd:cd18545 42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPvGkilSRVINDVNSLSDLLSNGLINL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 175 FLTIFTytsaFLGLYFWSLFKNARLTLCVTCVFPLIYICGVICNKKA-----KINKKTSLLYnnntmSIIEEALVGIRTV 249
Cdd:cd18545 122 IPDLLT----LVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRArkawqRVRKKISNLN-----AYLHESISGIRVI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 250 VSYCGEHTILKKF-NLSEKLYSKYMlKANFMESLH---IGMINGFilaSYAFGFWYGTRIIISDlsnaqsnndfhggsvi 325
Cdd:cd18545 193 QSFAREDENEEIFdELNRENRKANM-RAVRLNALFwplVELISAL---GTALVYWYGGKLVLGG---------------- 252
|
250
....*....|..
gi 221056887 326 SILLGVLISMFM 337
Cdd:cd18545 253 AITVGVLVAFIG 264
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
411-614 |
1.37e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 411 GKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSK-IGVVSQDPLLFS--NSIKNnikYSLY 485
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgQPLHQMDEEARAKLRAKhVGFVFQSFMLIPtlNALEN---VELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 486 SLkdLEYLSDQLNEDGSAS---QDGLDKRnscrakcagdlndmmkttdsdgliharknyniiddsevvnvskkvLIHdfv 562
Cdd:PRK10584 113 AL--LRGESSRQSRNGAKAlleQLGLGKR---------------------------------------------LDH--- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221056887 563 saLPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK10584 143 --LP-----------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
578-652 |
1.44e-05 |
|
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: 49.40 E-value: 1.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRY-ANTIFVL 652
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
580-658 |
1.45e-05 |
|
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: 47.60 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 580 LSGGQKQ------RISIARAIIRNPKILILDEATSSLD--NKSEYLVQkTINNLKGNENRITIIIAHRLSTIRYANTIFV 651
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeeNIEESLAE-IIEERKSQKNFQLIVITHDEELVDAADHIYR 194
|
....*..
gi 221056887 652 LSNREKG 658
Cdd:cd03240 195 VEKDGRQ 201
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
383-484 |
1.47e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.61 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFhydTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWRS 460
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipAMSRSRLYTVRK 84
|
90 100
....*....|....*....|....*
gi 221056887 461 KIGVVSQDPLLFSN-SIKNNIKYSL 484
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPL 109
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
580-647 |
1.74e-05 |
|
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: 49.36 E-value: 1.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKgnENRITII-IAHRLSTIRYAN 647
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE---GYMYRLCR--EFGITLFsVSHRKSLWKYHE 646
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1357-1459 |
2.08e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 47.68 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHR---IASIkrSDKIVVFNNpd 1433
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDmklVMGI--SDRIYVVNQ-- 229
|
90 100
....*....|....*....|....*.
gi 221056887 1434 rtGSFVqAEGTHEELLSVQDgVYKKY 1459
Cdd:PRK11300 230 --GTPL-ANGTPEEIRNNPD-VIKAY 251
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
394-654 |
2.18e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 48.68 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKwwrSKIGVVSQDPLL 471
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagDDVEALSARAAS---RRVASVPQDTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 472 fsnsiknnikyslyslkDLEYLSDQLNEDGsasqdgldkRNSCRAKCAGdlndmMKTTDSDGLIHArknyniIDDSEVvn 551
Cdd:PRK09536 89 -----------------SFEFDVRQVVEMG---------RTPHRSRFDT-----WTETDRAAVERA------MERTGV-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 552 vskkvlihdfvSALPDKYETlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseylVQKTINNLK----- 626
Cdd:PRK09536 130 -----------AQFADRPVT-------SLSGGERQRVLLARALAQATPVLLLDEPTASLD------INHQVRTLElvrrl 185
|
250 260
....*....|....*....|....*....
gi 221056887 627 GNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:PRK09536 186 VDDGKTAVAAIHDLDlAARYCDELVLLAD 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1357-1420 |
2.18e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 2.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdRTIITIAHRIASI 1420
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEG-KTMLVSTHNLGSV 205
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
856-991 |
2.45e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 47.89 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 856 FANLEANSNKYSLYILVIA-----IAMFISETLKNYYNNVIGEKVEKTMKHRLFENILYQEISFFDQdcHAPGLLSSHIN 930
Cdd:cd18563 30 LIQLGPGGNTSLLLLLVLGlagayVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDK--RQTGSLMSRVT 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 931 RDVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFY-----------FCPIVAAvltGTYFI-------FMRVFAIRARLSA 991
Cdd:cd18563 108 SDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSlnwklallvliPVPLVVW---GSYFFwkkirrlFHRQWRRWSRLNS 183
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
580-625 |
2.62e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 2.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 221056887 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL 451
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
580-654 |
2.78e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 47.46 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 580 LSGGQKQRISIARAIIR------NPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
Cdd:PRK13548 135 LSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLL 214
|
..
gi 221056887 653 SN 654
Cdd:PRK13548 215 HQ 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1272-1428 |
3.30e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1272 KNSGKILLDGVDICDYNLKD-LRNLFSIVSQE-PILFNMSIYENIKFGK---------EDATREDVKrackfAAIDEFie 1340
Cdd:PRK10982 50 KDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQRSVMDNMWLGRyptkgmfvdQDKMYRDTK-----AIFDEL-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1341 slpnkyDTNVGPYGK--SLSGGQKQRVAIARALLREPKILLLDEATSSLdsnSEKLIEKTIVDIKDKADR--TIITIAHR 1416
Cdd:PRK10982 123 ------DIDIDPRAKvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNHLFTIIRKLKERgcGIVYISHK 193
|
170
....*....|...
gi 221056887 1417 IASIKR-SDKIVV 1428
Cdd:PRK10982 194 MEEIFQlCDEITI 206
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1355-1429 |
4.07e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.92 E-value: 4.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1355 KSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITiAHRIASIKR-SDKIVVF 1429
Cdd:PRK13638 135 QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEiSDAVYVL 209
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1322-1446 |
4.59e-05 |
|
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: 46.59 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1322 TREDVKRACKFAAIDEFIE--SLPNKYDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLDS----NSEKLI 1395
Cdd:cd03236 107 VGELLKKKDERGKLDELVDqlELRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrlNAARLI 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 221056887 1396 EKTIVDikdkaDRTIITIAHRIASIKR-SDKI-VVFNNPDRTGSFVQAEGTHE 1446
Cdd:cd03236 183 RELAED-----DNYVLVVEHDLAVLDYlSDYIhCLYGEPGAYGVVTLPKSVRE 230
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
579-658 |
5.11e-05 |
|
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: 45.64 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNREKG 658
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
570-607 |
5.24e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.71 E-value: 5.24e-05
10 20 30
....*....|....*....|....*....|....*...
gi 221056887 570 ETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEAT 607
Cdd:COG1129 389 EQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
99-360 |
5.50e-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: 46.73 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 99 IIFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNNPgsklTSDLDF------YLEQVnagIG 172
Cdd:cd18555 44 LGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRS----SGDLLFransnvYIRQI---LS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 173 TKFLTIFTYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYICGVICNKKAKINKKTSLLYNNNTMSIIEEALVGIRTVVSY 252
Cdd:cd18555 117 NQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 253 CGEHTILKKFnlsEKLYSKYMLK-------ANFMESLHIG---MINGFILasyafgfWYGTRIIIsdlsnaqsNNDFHGG 322
Cdd:cd18555 197 GSEKNIYKKW---ENLFKKQLKAfkkkerlSNILNSISSSiqfIAPLLIL-------WIGAYLVI--------NGELTLG 258
|
250 260 270
....*....|....*....|....*....|....*...
gi 221056887 323 SVISILlgVLISMFMLTIVlpNITEYMKSLEATNSLYE 360
Cdd:cd18555 259 ELIAFS--SLAGSFLTPIV--SLINSYNQFILLKSYLE 292
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
402-611 |
5.59e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLK----WWRSKIGVVSQDP----LLFS 473
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG----HEVVTRspqdGLANGIVYISEDRkrdgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 474 NSIKNNIkyslySLKDLEYLSdqlnedgsasqdgldkrnscraKCAGDLNdmmkttdsdgliHARknyniiddsEVVNVS 553
Cdd:PRK10762 345 MSVKENM-----SLTALRYFS----------------------RAGGSLK------------HAD---------EQQAVS 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 554 kkvlihDFVSALPDK---YETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10762 377 ------DFIRLFNIKtpsMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1357-1421 |
5.68e-05 |
|
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: 47.82 E-value: 5.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATS--SLDsnseklIEKTIVDIKDKADRTIITIAHRIASIK 1421
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSavSVD------VEGYMYRLCREFGITLFSVSHRKSLWK 643
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
575-636 |
5.88e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 46.18 E-value: 5.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII 636
Cdd:COG1137 132 SKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLK--ERGIGVLI 191
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
578-625 |
6.59e-05 |
|
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: 47.13 E-value: 6.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 221056887 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL 449
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
383-652 |
7.33e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.13 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKI 462
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 463 GVVSQDPllfsnsiknnikyslyslkDLEYLSDQLNEDGSasqdgLDKRNSCRAKcagdlndmmkttdsdglIHARKNYN 542
Cdd:PRK13644 80 GIVFQNP-------------------ETQFVGRTVEEDLA-----FGPENLCLPP-----------------IEIRKRVD 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 543 IiddsevvnvskkvlihdfvsALPD-KYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:PRK13644 119 R--------------------ALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLER 178
|
250 260 270
....*....|....*....|....*....|.
gi 221056887 622 INNLKgNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:PRK13644 179 IKKLH-EKGKTIVYITHNLEELHDADRIIVM 208
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
825-1055 |
7.54e-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: 46.34 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 825 VVIIALSIIVAGGLYpMFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLF 904
Cdd:cd18580 1 VLLLLLLLLLLAFLS-QFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 905 ENILYQEISFFDQdcHAPGLLsshINR---DVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCP---IVAAVLTGTYFI 978
Cdd:cd18580 80 RSVLRAPMSFFDT--TPSGRI---LNRfskDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPyflIVLPPLLVVYYL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 979 FMRVFairarLSANKDVEkkginqpgtvFLynndDEIFKDPSF-LIQEAFYNMNTVIIYGLEDYFCKLIEKAIDYSNK 1055
Cdd:cd18580 155 LQRYY-----LRTSRQLR----------RL----ESESRSPLYsHFSETLSGLSTIRAFGWQERFIEENLRLLDASQR 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
570-655 |
8.06e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYanti 649
Cdd:PRK13409 444 ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDY---- 519
|
....*.
gi 221056887 650 fvLSNR 655
Cdd:PRK13409 520 --ISDR 523
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
403-611 |
9.64e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IINDSHNLKDINLkwwRSKIGVVSQdpllfsnsiknniK 481
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFGQPVDAGDIAT---RRRVGYMSQ-------------A 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 482 YSLYSlkdlEyLSDQLNedgsasqdgLDkrnscrakcagdlndmmkttdsdglIHARKnYNIIDDSevvnVSKKV--LIH 559
Cdd:NF033858 348 FSLYG----E-LTVRQN---------LE-------------------------LHARL-FHLPAAE----IAARVaeMLE 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 221056887 560 DFvsALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:NF033858 384 RF--DLADVADAL----PDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
579-643 |
9.91e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 9.91e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTI 643
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELR-DEGKTMLVSTHNLGSV 205
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
575-651 |
1.02e-04 |
|
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: 46.70 E-value: 1.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFV 651
Cdd:COG1245 451 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
569-654 |
1.20e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 569 YETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANT 648
Cdd:PRK10982 385 HRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDR 460
|
....*.
gi 221056887 649 IFVLSN 654
Cdd:PRK10982 461 ILVMSN 466
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
379-638 |
1.22e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 379 DIKKIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIErlydpteGDiiindsHnlkdinlkww 458
Cdd:PRK10938 257 NEPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT-------GD------H---------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 459 rskigvvsqdPLLFSNS----------------IKNNIKYslyslkdleyLSDQLNedgsasqdgLDKRNSCRAK---CA 519
Cdd:PRK10938 311 ----------PQGYSNDltlfgrrrgsgetiwdIKKHIGY----------VSSSLH---------LDYRVSTSVRnviLS 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 520 GDLndmmkttDSDGLIHArknyniiddsevvnVSkkvlihDFVSALPDKYETLVGSNASK-------LSGGQKQRISIAR 592
Cdd:PRK10938 362 GFF-------DSIGIYQA--------------VS------DRQQKLAQQWLDILGIDKRTadapfhsLSWGQQRLALIVR 414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 221056887 593 AIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1356-1396 |
1.25e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 221056887 1356 SLSGGQKQRVAIARALLREPKILLLDEATSSLDSNS-EKLIE 1396
Cdd:PLN03073 627 TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
380-509 |
1.25e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 46.15 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 380 IKKIQFKNVRfhydtrkdveIYKDLNFTLTEGKTyAFVGESGCGKSTILKLIERLYDPTEGDII-INDSHNLKDINLK-- 456
Cdd:COG3593 3 LEKIKIKNFR----------SIKDLSIELSDDLT-VLVGENNSGKSSILEALRLLLGPSSSRKFdEEDFYLGDDPDLPei 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 457 ----WWRSKIGVVSQDplLFSNSIKNNIKYSLYSLKD-----LEYLSDQLNEDGSASQDGLD 509
Cdd:COG3593 72 eielTFGSLLSRLLRL--LLKEEDKEELEEALEELNEelkeaLKALNELLSEYLKELLDGLD 131
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1356-1396 |
1.53e-04 |
|
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: 44.27 E-value: 1.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 221056887 1356 SLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:TIGR01189 127 QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
400-615 |
1.77e-04 |
|
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: 44.41 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskiGVVSQDPLLFSNSI--- 476
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---------------PLDFQRDSIARGLLylg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 477 -KNNIKYSLYSLKDLEYLSDqlneDGSASQdgldkrnscrakcagdLNDMMKTTDSDGLIHARKNYniiddsevvnvskk 555
Cdd:cd03231 80 hAPGIKTTLSVLENLRFWHA----DHSDEQ----------------VEEALARVGLNGFEDRPVAQ-------------- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 556 vlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:cd03231 126 ------------------------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1356-1448 |
1.78e-04 |
|
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: 46.16 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1356 SLSGGQKQRVAIARALLRE---PKILLLDEATSSL---DSNseKLIEkTIVDIKDKADrTIITIAHRIASIKRSDKIVVF 1429
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIK--KLLE-VLQRLVDKGN-TVVVIEHNLDVIKTADYIIDL 904
|
90 100
....*....|....*....|.
gi 221056887 1430 nNPD--RTGSFVQAEGTHEEL 1448
Cdd:TIGR00630 905 -GPEggDGGGTVVASGTPEEV 924
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
840-1054 |
1.88e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p 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.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 45.16 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 840 PMFALLYAkyvstLFDFANLEAN-------SNKYSL----YILV---IAIAMFISETLKNYYNNVIGEKVEKTMKHRLFE 905
Cdd:cd18606 2 PLLLLLLI-----LSQFAQVFTNlwlsfwtEDFFGLsqgfYIGIyagLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 906 NILYQEISFFDQdchAPglLSSHINR---DVHLLKTGLVNNIVIFTHFIVLFIVSMIMSFYFCPIVAAVLTGTYFIFMRV 982
Cdd:cd18606 77 RVLRAPMSFFDT---TP--LGRILNRfskDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221056887 983 FAI-RA------RLSANKDVekkginqpgtvFLYNNddeifkdpsflIQEAFYNMNTVIIYGLEDYFCKLIEKAIDYSN 1054
Cdd:cd18606 152 ANYyRAssrelkRLESILRS-----------FVYAN-----------FSESLSGLSTIRAYGAQDRFIKKNEKLIDNMN 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
411-679 |
2.02e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 411 GKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWRSK----IGVVSQDPLLFSN-SIKNNIkysly 485
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG----KEVTFNGPKSSqeagIGIIHQELNLIPQlTIAENI----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 486 slkdleYLSdqlnedgsasqdgldkRNSCRAKCAGDLNDMMKttDSDGLIhARKNyniiddsevvnvskkvlihdfvsaL 565
Cdd:PRK10762 101 ------FLG----------------REFVNRFGRIDWKKMYA--EADKLL-ARLN------------------------L 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 566 PDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVqKTINNLKgNENRITIIIAHRLstir 644
Cdd:PRK10762 132 RFSSDKLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELK-SQGRGIVYISHRL---- 201
|
250 260 270
....*....|....*....|....*....|....*..
gi 221056887 645 yaNTIFvlsnrEKGNRSTV--DVDIIGEDPTKDNKEN 679
Cdd:PRK10762 202 --KEIF-----EICDDVTVfrDGQFIAEREVADLTED 231
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
580-625 |
2.33e-04 |
|
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: 43.77 E-value: 2.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 221056887 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1346-1389 |
2.48e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 2.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 221056887 1346 YDTNVG-PYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDS 1389
Cdd:TIGR00956 198 RNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1360-1415 |
2.86e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.86e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1360 GQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKADRTIITIAH 1415
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLE----DVLNERNSTMIIISH 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
395-611 |
3.02e-04 |
|
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: 43.50 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrskigVVSQDPLLFSN 474
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP---------------LAEQRDEPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 475 SI----KNNIKYSLYSLKDLEYLsdqlNEDGSASQDgldkrnscrakcagDLNDMMKTTDSDGLIHarknyniiddsevv 550
Cdd:TIGR01189 75 ILylghLPGLKPELSALENLHFW----AAIHGGAQR--------------TIEDALAAVGLTGFED-------------- 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 551 nvskkvlihdfvsaLPdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:TIGR01189 123 --------------LP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
577-643 |
3.02e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.21 E-value: 3.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
570-652 |
3.05e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRY-ANT 648
Cdd:PRK13409 203 ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL--AEGKYVLVVEHDLAVLDYlADN 280
|
....
gi 221056887 649 IFVL 652
Cdd:PRK13409 281 VHIA 284
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
559-649 |
3.50e-04 |
|
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: 45.39 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 559 HDFVSALPD---KYETLV---------GSNASKLSGGQKQRISIARAIIR---NPKILILDEATSSLD----NKSEYLVQ 619
Cdd:TIGR00630 797 YEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHfddiKKLLEVLQ 876
|
90 100 110
....*....|....*....|....*....|
gi 221056887 620 KTINnlKGNEnriTIIIAHRLSTIRYANTI 649
Cdd:TIGR00630 877 RLVD--KGNT---VVVIEHNLDVIKTADYI 901
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
557-654 |
3.69e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.77 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 557 LIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIR-----NP--KILILDEATSSLDNKSEYLVQKTINNL--KG 627
Cdd:PRK03695 106 ALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDVAQQAALDRLLSELcqQG 183
|
90 100
....*....|....*....|....*....
gi 221056887 628 nenrITIIIA-HRLS-TIRYANTIFVLSN 654
Cdd:PRK03695 184 ----IAVVMSsHDLNhTLRHADRVWLLKQ 208
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
59-309 |
4.54e-04 |
|
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: 43.97 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 59 KKLLGVSFVCAtisggslpFFVSVFGVIMkNMNLGENVDDII------------FSLVLIGIFQFVMSFISSFCMDIVTT 126
Cdd:cd18570 1 KKLLILILLLS--------LLITLLGIAG-SFFFQILIDDIIpsgdinllniisIGLILLYLFQSLLSYIRSYLLLKLSQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 127 KILKTLKVEFLKSVFYQDGQFHDNNPGSKLTS---DLDFYLEQVNAGIGTKFLTIFTYTSAFLGLYfwslFKNARLTLCV 203
Cdd:cd18570 72 KLDIRLILGYFKHLLKLPLSFFETRKTGEIISrfnDANKIREAISSTTISLFLDLLMVIISGIILF----FYNWKLFLIT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 204 TCVFPLIYICGVICNKK-AKINKKTSLLYNNNTMSIIeEALVGIRTVVSYCGEHTILKKFnlsEKLYSKYmLKANFMESL 282
Cdd:cd18570 148 LLIIPLYILIILLFNKPfKKKNREVMESNAELNSYLI-ESLKGIETIKSLNAEEQFLKKI---EKKFSKL-LKKSFKLGK 222
|
250 260 270
....*....|....*....|....*....|..
gi 221056887 283 hIGMINGFI--LASYAFG---FWYGTRIIISD 309
Cdd:cd18570 223 -LSNLQSSIkgLISLIGSlliLWIGSYLVIKG 253
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1357-1391 |
4.88e-04 |
|
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: 43.02 E-value: 4.88e-04
10 20 30
....*....|....*....|....*....|....*
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
577-611 |
5.16e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 5.16e-04
10 20 30
....*....|....*....|....*....|....*
gi 221056887 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:NF033858 134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1325-1416 |
5.61e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1325 DVKRACKFAAIDEFIE--SLPNKYDTNVG-PYGKSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PLN03140 985 EVSKEEKMMFVDEVMElvELDNLKDAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
|
90
....*....|....*
gi 221056887 1402 IKDKAdRTIITIAHR 1416
Cdd:PLN03140 1065 TVDTG-RTVVCTIHQ 1078
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
570-654 |
5.98e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 43.28 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 570 ETLVGSNASKLSGGQKQRISIARAI---------IRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PRK13547 136 TALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDP 215
|
90
....*....|....*
gi 221056887 641 S-TIRYANTIFVLSN 654
Cdd:PRK13547 216 NlAARHADRIAMLAD 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1358-1388 |
6.04e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.38 E-value: 6.04e-04
10 20 30
....*....|....*....|....*....|.
gi 221056887 1358 SGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
580-624 |
6.64e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 6.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 221056887 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1356-1450 |
7.04e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.05 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1356 SLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASIKR-SDKIVVFnnpdR 1434
Cdd:PRK10253 143 TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIAL----R 218
|
90
....*....|....*.
gi 221056887 1435 TGSFVqAEGTHEELLS 1450
Cdd:PRK10253 219 EGKIV-AQGAPKEIVT 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1355-1401 |
7.14e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 7.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 221056887 1355 KSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS 485
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1306-1422 |
7.71e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 42.76 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1306 FNMSI--YENIKF-----GkedATREDVKRacKFAAIDEFIEsLPNKYDTNVgpygKSLSGGQKQRVAIARALLREPKIL 1378
Cdd:COG1134 99 FHPELtgRENIYLngrllG---LSRKEIDE--KFDEIVEFAE-LGDFIDQPV----KTYSSGMRARLAFAVATAVDPDIL 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 221056887 1379 LLDEATSSLDSN-SEKLIEKtIVDIKDKAdRTIITIAHRIASIKR 1422
Cdd:COG1134 169 LVDEVLAVGDAAfQKKCLAR-IRELRESG-RTVIFVSHSMGAVRR 211
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
579-652 |
7.95e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 7.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221056887 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINVL 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1355-1399 |
8.38e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.48 E-value: 8.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 221056887 1355 KSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PRK13538 128 RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1356-1402 |
9.28e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 9.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 221056887 1356 SLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIeKTIVDI 1402
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLV-RRFVDV 446
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1307-1429 |
9.69e-04 |
|
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: 42.52 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1307 NMSIYENIKFgkeDATREDVKRACKFAAIDEFIE--SLPNKYDTNVgpygKSLSGGQKQRVAIARALLREPKILLLDEAT 1384
Cdd:cd03220 98 ELTGRENIYL---NGRLLGLSRKEIDEKIDEIIEfsELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVL 170
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 221056887 1385 SSLDSN-SEKLIEKtIVDIKDKAdRTIITIAHRIASIKR-SDKIVVF 1429
Cdd:cd03220 171 AVGDAAfQEKCQRR-LRELLKQG-KTVILVSHDPSSIKRlCDRALVL 215
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
555-649 |
9.80e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 555 KVLIHDFVSALPdkyetlVGSNASKLSGGQKQRISIARAIIRNPK---ILILDEATSSLDNKSEYLVQKTINNLKgNENR 631
Cdd:PRK00635 1681 QALIDNGLGYLP------LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLV-SLGH 1753
|
90
....*....|....*...
gi 221056887 632 ITIIIAHRLSTIRYANTI 649
Cdd:PRK00635 1754 SVIYIDHDPALLKQADYL 1771
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
865-1101 |
1.03e-03 |
|
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: 42.77 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 865 KYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKHRLFENIL---YQEISFFDQdchapgllSSHINR---DVHLLKT 938
Cdd:cd18548 40 RTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQsfsFAEIDKFGT--------SSLITRltnDVTQVQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 939 GLVNNIVIFTHFIVLFIVSMIMSFY--------FCPIVAAVLTGTYFIFMRVFAIRARLSANKDvekkGINQpgtvflyn 1010
Cdd:cd18548 112 FVMMLLRMLVRAPIMLIGAIIMAFRinpklaliLLVAIPILALVVFLIMKKAIPLFKKVQKKLD----RLNR-------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1011 nddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCKLIEKA-IDYSNKGQKrktlVNSMLWGFSQSAQLFINS---FAYWFG 1086
Cdd:cd18548 180 -----------VVRENLTGIRVIRAFNREDYEEERFDKAnDDLTDTSLK----AGRLMALLNPLMMLIMNLaivAILWFG 244
|
250
....*....|....*
gi 221056887 1087 SFLIRRGTIEVDDFM 1101
Cdd:cd18548 245 GHLINAGSLQVGDLV 259
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
382-442 |
1.13e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 382 KIQF--KNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKL-IERLyDPTEGDI 442
Cdd:PRK11147 317 KIVFemENVNYQIDGKQLV---KDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSGRI 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1310-1460 |
1.33e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1310 IYENIKFGKEDATR-EDVkrACKFAAIDEFIESLPNKYDTNVG--PYGK---SLSGGQKQRVAIARALL---REPKILLL 1380
Cdd:PRK00635 1649 VYEGKHFGQLLQTPiEEV--AETFPFLKKIQKPLQALIDNGLGylPLGQnlsSLSLSEKIAIKIAKFLYlppKHPTLFLL 1726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1381 DEATSSLDSNSEKLIEK---TIVDIkdkaDRTIITIAHRIASIKRSDKIVVFN-NPDRTGSFVQAEGTHEELLSVQDGVY 1456
Cdd:PRK00635 1727 DEIATSLDNQQKSALLVqlrTLVSL----GHSVIYIDHDPALLKQADYLIEMGpGSGKTGGKILFSGPPKDISASKDSLL 1802
|
....
gi 221056887 1457 KKYV 1460
Cdd:PRK00635 1803 KTYM 1806
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
570-625 |
1.33e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 1.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 221056887 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILI-LDEATSSLDNKSEYLVQKTINNL 625
Cdd:TIGR00956 892 DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1352-1428 |
1.33e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.87 E-value: 1.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 1352 PYgkSLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADRTIITIAHRIASI-KRSDKIVV 1428
Cdd:PRK15093 156 PY--ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINV 231
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
99-311 |
1.38e-03 |
|
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: 42.53 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 99 IIFSLVLIGIFQFV-MSFISSFCMDIVTTkilktLKVEFLKSVFYQDGQFHDNNPG----SKLTSDL-DF--YLEQ-VNA 169
Cdd:cd18574 48 LLGLYLLQSLLTFAyISLLSVVGERVAAR-----LRNDLFSSLLRQDIAFFDTHRTgelvNRLTADVqEFksSFKQcVSQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 170 GIGTKFLTIftytSAFLGLYFWSlfknARLTLCVTCVFPLIYICGVICNKKAKINKKTSLLYNNNTMSIIEEALVGIRTV 249
Cdd:cd18574 123 GLRSVTQTV----GCVVSLYLIS----PKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTV 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 250 VSYCGEHTILKKFNL----SEKLYSKYmlkanfmeSLHIGM--------INGFILASYAFGfwyGTRIIISDLS 311
Cdd:cd18574 195 RAFAMEDRELELYEEevekAAKLNEKL--------GLGIGIfqglsnlaLNGIVLGVLYYG---GSLVSRGELT 257
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1307-1459 |
1.57e-03 |
|
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: 43.08 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1307 NMSIYENIKFgKEDATREDVKRACKFAAIDEFIESLpnKYDTNVG-PY------GKSLSGGQKQRVAIARAL-------- 1371
Cdd:TIGR00630 435 ELSIREAHEF-FNQLTLTPEEKKIAEEVLKEIRERL--GFLIDVGlDYlslsraAGTLSGGEAQRIRLATQIgsgltgvl 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1372 --LREPKILLLDEATssldsnsEKLIEkTIVDIKDKADrTIITIAHRIASIKRSDKIVvfnnpD------RTGSFVQAEG 1443
Cdd:TIGR00630 512 yvLDEPSIGLHQRDN-------RRLIN-TLKRLRDLGN-TLIVVEHDEDTIRAADYVI-----DigpgagEHGGEVVASG 577
|
170
....*....|....*.
gi 221056887 1444 THEELLSVQDGVYKKY 1459
Cdd:TIGR00630 578 TPEEILANPDSLTGQY 593
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1356-1417 |
1.59e-03 |
|
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: 43.46 E-value: 1.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221056887 1356 SLSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADRTIITIAHRI 1417
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII-REGRAVVLTSHSM 2130
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1357-1413 |
1.62e-03 |
|
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: 41.46 E-value: 1.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 1357 LSGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADRTII-TI 1413
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILcTI 165
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1335-1427 |
1.71e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 41.30 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1335 IDEFIESlPNKYDTNVgpygKSLSGGQKQRVAIAR--ALLRE---PkILLLDEATSSLD-SNSEKLIEKtivdIKDKADR 1408
Cdd:cd03278 97 VSEIIEA-PGKKVQRL----SLLSGGEKALTALALlfAIFRVrpsP-FCVLDEVDAALDdANVERFARL----LKEFSKE 166
|
90 100
....*....|....*....|
gi 221056887 1409 T-IITIAHRIASIKRSDKIV 1427
Cdd:cd03278 167 TqFIVITHRKGTMEAADRLY 186
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
387-614 |
2.24e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.09 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 387 NVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindshnlkdinlkwwrskigvvs 466
Cdd:PRK13540 6 ELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 467 qdpLLFSNSIKnnikyslyslKDLEYLSDQLNEDGSASqdGLDKRNSCRAKCAGDLNdmmktTDSDGLiharknyniiDD 546
Cdd:PRK13540 59 ---LFERQSIK----------KDLCTYQKQLCFVGHRS--GINPYLTLRENCLYDIH-----FSPGAV----------GI 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 547 SEVVNVSKKVLIHDFVSALpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK13540 109 TELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
581-651 |
2.40e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 2.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221056887 581 SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRYANTIFV 651
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLR-DGKRSFIIVTHYQRILDYIKPDYV 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
394-635 |
2.46e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 41.61 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKwwrsKIGVV----SQ 467
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyVPFKRRKEFAR----RIGVVfgqrSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 468 ---D-PLLFSNSIKNNIkyslYSLKD------LEYLSDQLnedgsasqdgldkrnscrakcagDLNDMMKTtdsdgliHA 537
Cdd:COG4586 107 lwwDlPAIDSFRLLKAI----YRIPDaeykkrLDELVELL-----------------------DLGELLDT-------PV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 538 RKnyniiddsevvnvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG4586 153 RQ----------------------------------------LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEA 192
|
250
....*....|....*...
gi 221056887 618 VQKTINNLKgNENRITII 635
Cdd:COG4586 193 IREFLKEYN-RERGTTIL 209
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
380-639 |
2.75e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 41.82 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 380 IKKIQFKNVRFHydtrKDVEIYKDLNFTLtegktyaFVGESGCGKSTILKLIERLYDPTEgdiiindSHNLKDINLKWWR 459
Cdd:pfam13175 3 IKSIIIKNFRCL----KDTEIDLDEDLTV-------LIGKNNSGKSSILEALDIFLNNKE-------KFFEDDFLVLYLK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 460 SKIGVVSQD-----PLLFSNSIKNNIKYSLYSLKDLEYLSDQLNEDGSASQDGLDKRNSCRAKCAGDLNDMMKTTDsdgl 534
Cdd:pfam13175 65 DVIKIDKEDlnifeNISFSIDIEIDVEFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISD---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 535 IHARKNYNIIDDSEVVNVSKKVLIHDFVSALPDKYETLVGSNASKlsggqkqrisiaraiirnPKILILDEATSSLDNKS 614
Cdd:pfam13175 141 LKKYLKQFKIYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEK------------------EEIKVDKEDLKKLINEL 202
|
250 260
....*....|....*....|....*
gi 221056887 615 EYLVQKTINNLKGNENRITIIIAHR 639
Cdd:pfam13175 203 EKSINYHENVLENLQIKKLLISADR 227
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
1174-1402 |
2.85e-03 |
|
Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.
Pssm-ID: 376671 [Multi-domain] Cd Length: 220 Bit Score: 40.81 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1174 MSRPNVPIY----KDLTFSCdskkttAIVGETGSGKSTVMSLLM-RFYDLKNDHHIVFknehtdDVNnekkeqgdeeqnv 1248
Cdd:pfam01935 7 LDGSEVPVYldvnKLVSRHF------AILGSTGSGKSNTVAVLLeELLEKKGATVLIF------DPH------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1249 gmknvNEFSLTKEGSHGDNSAVFKNSGKILLDGVDIcdyNLKDLRNLFsivsqepILFNMSIYENIKFGKEDATREDVKR 1328
Cdd:pfam01935 62 -----GEYGTLFRDLGAENVNVITPDPELKINPWLL---SPEDLADLL-------EELNLPNAEVQRSILEEALDQLKSE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1329 ACKFAAIDEFIESLPNKYDTNVGPYGKSlsggqkqRVAIARALLREPKILLLDEATSSLDSNSEKLIEK--------TIV 1400
Cdd:pfam01935 127 ELGKLSIDELIEKILEELLTEAAELNKL-------SNDAIRRVLDKLERLLRSGGLILTSTDIIKLILDilskggkvNII 199
|
..
gi 221056887 1401 DI 1402
Cdd:pfam01935 200 DL 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
374-447 |
2.96e-03 |
|
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: 41.84 E-value: 2.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221056887 374 GKKLKDiKKIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS 447
Cdd:TIGR03719 315 GPRLGD-KVIEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET 384
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
569-616 |
3.44e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 3.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 221056887 569 YETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:TIGR00956 198 RNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAL 246
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
578-614 |
3.48e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 3.48e-03
10 20 30
....*....|....*....|....*....|....*..
gi 221056887 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1272-1388 |
4.38e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.58 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1272 KNSGKILLDGVDICDYNLKDL-----------RNLFSIVSQEPILFNMS--IYENIKF----GKEDATREDVKRA--CKF 1332
Cdd:PRK15439 315 ARGGRIMLNGKEINALSTAQRlarglvylpedRQSSGLYLDAPLAWNVCalTHNRRGFwikpARENAVLERYRRAlnIKF 394
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 221056887 1333 AAIDEFIeslpnkydtnvgpygKSLSGGQKQRVAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK15439 395 NHAEQAA---------------RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1358-1415 |
4.53e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 4.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 221056887 1358 SGGQKQRVAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDRTIITIAH 1415
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH 209
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1326-1415 |
4.71e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1326 VKRACKFAAIDEFIESLP-NKY-DTNVGPYGKSLSGGQKQRVAIARALLREPKILL-LDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:TIGR00956 869 VSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
90
....*....|...
gi 221056887 1403 KDkADRTIITIAH 1415
Cdd:TIGR00956 949 AD-HGQAILCTIH 960
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1293-1388 |
4.95e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 1293 RNLFsivsqePILfnmSIYENIKF-----GKEDATREdvkrackfAAIDEFIESlpnkydTNVGPY-----GKsLSGGQK 1362
Cdd:NF033858 87 KNLY------PTL---SVFENLDFfgrlfGQDAAERR--------RRIDELLRA------TGLAPFadrpaGK-LSGGMK 142
|
90 100
....*....|....*....|....*.
gi 221056887 1363 QRVAIARALLREPKILLLDEATSSLD 1388
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
580-619 |
5.34e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 5.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 221056887 580 LSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQ 619
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQ 668
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
100-212 |
5.44e-03 |
|
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: 40.53 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221056887 100 IFSLVLIGIFQFVMSFISSFCMDIVTTKILKTLKVEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFLTIF 179
Cdd:cd18589 39 ITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLM 118
|
90 100 110
....*....|....*....|....*....|...
gi 221056887 180 TYTSAFLGLYFWSLFKNARLTLCVTCVFPLIYI 212
Cdd:cd18589 119 WYLARGLFLFIFMLWLSPKLALLTALGLPLLLL 151
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
578-611 |
5.90e-03 |
|
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: 39.55 E-value: 5.90e-03
10 20 30
....*....|....*....|....*....|....
gi 221056887 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:cd03233 117 RGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
400-442 |
6.12e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 6.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 221056887 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI 442
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
580-611 |
7.38e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 7.38e-03
10 20 30
....*....|....*....|....*....|..
gi 221056887 580 LSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
574-614 |
7.51e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 7.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 221056887 574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
|
| |
