|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-732 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 936.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 1 MKTYVLLYGKLIMTTMILNTGRFEEWYKVciIALKEKEIYVPSSPIAMLNGRLPLLRLGICRNMLSRPRLAKLPSIRFRS 80
Cdd:TIGR00958 2 ALAYLLPWFSLLLVDWALLRDLLQGIFGL--LLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAGGLLAAVKPLVAALC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 81 LVTPSSSQLIPLSRLCLRSPAVGKSLILQS-FRCNSSKTVPETSLPSASPiSKGSARSAHAKEQSKTDDykDIIRLFMLA 159
Cdd:TIGR00958 80 LATPSLSSLRALAFWEALDPAVRVALGLWSwFVWSYGAALPAAALWAVLS-SAGASEKEAEQGQSETAD--LLFRLLGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 160 KRDWKLLLTAILLLTISCSIGMSIPKVIGIVLDTLKTSSgsDFFDLKIPIFSLPLYEFLSFFTVALLIGCaanfgrfilL 239
Cdd:TIGR00958 157 GRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDK--GPPALASAIFFMCLLSIASSVSAGLRGGS---------F 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 240 RILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSI 319
Cdd:TIGR00958 226 NYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 320 LLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNA 399
Cdd:TIGR00958 306 VTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 400 KFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRLFELTDRKPSIS 479
Cdd:TIGR00958 386 GYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 480 PTVGHKYKPDRGVIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDI 559
Cdd:TIGR00958 466 LTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 560 SKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPtKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQ 639
Cdd:TIGR00958 546 VQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQ 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 640 RIAIARALIKKPTILILDEATSALDVESEgainYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHdGSVVEMGKFKE 719
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVERADQILVLKK-GSVVEMGTHKQ 699
|
730
....*....|...
gi 1370557 720 LYANPTsALSQLL 732
Cdd:TIGR00958 700 LMEDQG-CYKHLV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
154-723 |
1.52e-180 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 530.51 E-value: 1.52e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 154 RLFMLAKRDWKLLLTAILLLTISCSIGMSIPKVIGIVLDTLktSSGSDFfdlkipifsLPLYEFLSFFTVALLIGCAANF 233
Cdd:COG1132 11 RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDAL--LAGGDL---------SALLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 234 GRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSL 313
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 314 SPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKT 393
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 394 AAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRLFELTD 473
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 474 RKPSI-SPTVGHKYKPDRGVIEFKDVSFSYPtrPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTI 552
Cdd:COG1132 320 EPPEIpDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 553 TIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTyTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTL 632
Cdd:COG1132 398 LIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP-DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLgHDGSVV 712
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRNADRILVL-DDGRIV 553
|
570
....*....|.
gi 1370557 713 EMGKFKELYAN 723
Cdd:COG1132 554 EQGTHEELLAR 564
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
179-722 |
7.47e-136 |
|
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: 420.01 E-value: 7.47e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 179 IGMSIPKVIGIVLDTLKTSSGSDFfdlkipifslpLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKT 258
Cdd:COG2274 171 LALATPLFTQVVIDRVLPNQDLST-----------LWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 259 LHQDAEFFDNHKVGDLISRLgSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQ 338
Cdd:COG2274 240 LRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 339 IRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLA 418
Cdd:COG2274 319 LRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLW 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 419 YGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRLFELTDRKPSISPTVGHKYKPD-RGVIEFKD 497
Cdd:COG2274 399 LGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRlKGDIELEN 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 498 VSFSYPTRpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQE 577
Cdd:COG2274 479 VSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 578 PVLMSGTIRDNITYGLTyTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILD 657
Cdd:COG2274 558 VFLFSGTIRENITLGDP-DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILD 636
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 658 EATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:COG2274 637 EATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVL-DKGRIVEDGTHEELLA 698
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
176-468 |
1.71e-129 |
|
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: 388.41 E-value: 1.71e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 176 SCSIGMSIPKVIGIVLDTLKTSSGSdffdlkIPIFSLPLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVI 255
Cdd:cd18573 8 SSAVTMSVPFAIGKLIDVASKESGD------IEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 256 KKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVF 335
Cdd:cd18573 82 KSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 336 GKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLT 415
Cdd:cd18573 162 GRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1370557 416 VLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRL 468
Cdd:cd18573 242 VLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
493-723 |
9.82e-126 |
|
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: 376.49 E-value: 9.82e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIG 572
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSGTIRDNITYGLTYtPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPT 652
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPD-ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370557 653 ILILDEATSALDVESEGAINYTFGQLMksKSMTIVSIAHRLSTIRRSENVIVLGHdGSVVEMGKFKELYAN 723
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRNADLIAVLQN-GQVVEQGTHDELMAQ 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
217-722 |
1.23e-123 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 383.67 E-value: 1.23e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 217 FLSFFTVALLIGCAAnFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDG 296
Cdd:TIGR02204 61 FAFLLVVALVLALGT-AARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 297 VKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNE 376
Cdd:TIGR02204 140 LRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 377 LSRYNVAIRDIFQVGKTAAFTNAkffTTTSLLGDLSF---LTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLST 453
Cdd:TIGR02204 220 RSRFGGAVEKAYEAARQRIRTRA---LLTAIVIVLVFgaiVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 454 FYSEIMQGAGAASRLFELTDRKPSISPTVGHKYKPD--RGVIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSG 531
Cdd:TIGR02204 297 VWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVplRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 532 RGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTpTKEEIRSVAKQCFC 611
Cdd:TIGR02204 377 AGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDA-TDEEVEAAARAAHA 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 612 HNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSmTIVsIAH 691
Cdd:TIGR02204 456 HEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRT-TLI-IAH 533
|
490 500 510
....*....|....*....|....*....|.
gi 1370557 692 RLSTIRRSENVIVLGHdGSVVEMGKFKELYA 722
Cdd:TIGR02204 534 RLATVLKADRIVVMDQ-GRIVAQGTHAELIA 563
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
224-722 |
5.61e-107 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 340.16 E-value: 5.61e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 224 ALLIGCA-----ANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVsrsmTQKVSDGVK 298
Cdd:TIGR02203 58 LVVIGLAvlrgiCSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQV----ASAATDAFI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 299 ALI---CGVVGV-GMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEG 374
Cdd:TIGR02203 134 VLVretLTVIGLfIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 375 NELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTF 454
Cdd:TIGR02203 214 YETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 455 YSEIMQGAGAASRLFELTDRKPSisPTVGHKYKPD-RGVIEFKDVSFSYPTRpSVQIFKNLNFKIAPGSSVCIVGPSGRG 533
Cdd:TIGR02203 294 NAPMQRGLAAAESLFTLLDSPPE--KDTGTRAIERaRGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSG 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 534 KSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTKEEIRSVAKQCFCHN 613
Cdd:TIGR02203 371 KSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQD 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 614 FITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSmTIVsIAHRL 693
Cdd:TIGR02203 451 FVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT-TLV-IAHRL 528
|
490 500
....*....|....*....|....*....
gi 1370557 694 STIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:TIGR02203 529 STIEKADRIVVM-DDGRIVERGTHNELLA 556
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
366-722 |
6.25e-93 |
|
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: 304.05 E-value: 6.25e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 366 TVQSFVAEGNELSRYNVAIrdifqvgktAAFTNAKFFTTTSLlgdlSFL-------------TVLAYGSYLVLQSQLSIG 432
Cdd:COG5265 230 TVKYFGNEAREARRYDEAL---------ARYERAAVKSQTSL----ALLnfgqaliialgltAMMLMAAQGVVAGTMTVG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 433 DLT---AFM--LYTeytgnAVFGLSTFYSEIMQGAGAASRLFELTDRKPSISPTVGHK-YKPDRGVIEFKDVSFSY-PTR 505
Cdd:COG5265 297 DFVlvnAYLiqLYI-----PLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPpLVVGGGEVRFENVSFGYdPER 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 506 PsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTI 585
Cdd:COG5265 372 P---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTI 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 586 RDNITYGltyTP--TKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSAL 663
Cdd:COG5265 449 AYNIAYG---RPdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 664 DVESEGAINYTFGQLMKSKSmTIVsIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:COG5265 526 DSRTERAIQAALREVARGRT-TLV-IAHRLSTIVDADEILVL-EAGRIVERGTHAELLA 581
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
243-731 |
1.51e-92 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 302.32 E-value: 1.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 243 SERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVK--ALICGVVGvgMMCSLSPQLSIL 320
Cdd:PRK11176 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRegASIIGLFI--MMFYYSWQLSLI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 321 LLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAK 400
Cdd:PRK11176 171 LIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 401 FFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAfmlyteytgnaVF-----------GLSTFYSEIMQGAGAASRLF 469
Cdd:PRK11176 251 SDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITV-----------VFssmialmrplkSLTNVNAQFQRGMAACQTLF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 470 ELTDRKPSISpTVGHKYKPDRGVIEFKDVSFSYPTR--PSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNP 547
Cdd:PRK11176 320 AILDLEQEKD-EGKRVIERAKGDIEFRNVTFTYPGKevPAL---RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 548 TTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIG 627
Cdd:PRK11176 396 DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 628 PHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLgH 707
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEKADEILVV-E 552
|
490 500
....*....|....*....|....
gi 1370557 708 DGSVVEMGKFKELYANpTSALSQL 731
Cdd:PRK11176 553 DGEIVERGTHAELLAQ-NGVYAQL 575
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
493-722 |
1.39e-91 |
|
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: 287.59 E-value: 1.39e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIG 572
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSGTIRDNITYGlTYTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPT 652
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370557 653 ILILDEATSALDVESEGAInytFGQLMK-SKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:cd03253 158 ILLLDEATSALDTHTEREI---QAALRDvSKGRTTIVIAHRLSTIVNADKIIVL-KDGRIVERGTHEELLA 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
493-722 |
1.72e-88 |
|
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: 279.50 E-value: 1.72e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIG 572
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSGTIRDNITYGlTYTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPT 652
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 653 ILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIENADRIVVL-EDGKIVERGTHEELLA 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
491-720 |
7.69e-87 |
|
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: 274.87 E-value: 7.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 491 GVIEFKDVSFSYptRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRH 570
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQEPVLMSGTIRDNITYGlTYTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKK 650
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 651 PTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKEL 720
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKNADKILVL-DDGKIIEEGTHDEL 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
245-724 |
2.19e-85 |
|
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: 282.81 E-value: 2.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 245 RVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSD------AYVvsRSmtqkVSDGVKALICGVVGVGMMCSLSPQLS 318
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADvdaldnLYL--RV----LLPLLVALLVILAAVAFLAFFSPALA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 319 -ILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQV----GKT 393
Cdd:COG4987 159 lVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAqrrlARL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 394 AAFTNAkfftTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYT----EytgnAVFGLSTFYSEIMQGAGAASRLF 469
Cdd:COG4987 239 SALAQA----LLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAlalfE----ALAPLPAAAQHLGRVRAAARRLN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 470 ELTDRKPSISPTVGHKYKPDRGVIEFKDVSFSYPTRPSvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTT 549
Cdd:COG4987 311 ELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 550 GTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTyTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPH 629
Cdd:COG4987 390 GSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP-DATDEELWAALERVGLGDWLAALPDGLDTWLGEG 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 630 GTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLGhDG 709
Cdd:COG4987 469 GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLE-DG 545
|
490
....*....|....*
gi 1370557 710 SVVEMGKFKELYANP 724
Cdd:COG4987 546 RIVEQGTHEELLAQN 560
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
451-723 |
5.97e-84 |
|
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: 278.56 E-value: 5.97e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 451 LSTFYSEIMQGAGAASRLFELTDRKPSISPTVGHKYKPDRGV-IEFKDVSFSYPTRPsvQIFKNLNFKIAPGSSVCIVGP 529
Cdd:COG4988 294 LGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPsIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 530 SGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTyTPTKEEIRSVAKQC 609
Cdd:COG4988 372 SGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRP-DASDEELEAALEAA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 610 FCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSI 689
Cdd:COG4988 451 GLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILI 528
|
250 260 270
....*....|....*....|....*....|....
gi 1370557 690 AHRLSTIRRSENVIVLgHDGSVVEMGKFKELYAN 723
Cdd:COG4988 529 THRLALLAQADRILVL-DDGRIVEQGTHEELLAK 561
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
411-722 |
1.20e-82 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 276.07 E-value: 1.20e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 411 LSFLTVLAYGSYLVLQSQLSIGDLTAFMLYteytGNAVFG----LSTFYSEIMQGAGAASRLFELTDRKPSISPTVGHKY 486
Cdd:PRK13657 252 ITMLAILVLGAALVQKGQLRVGEVVAFVGF----ATLLIGrldqVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAID 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 487 KPD-RGVIEFKDVSFSYP-TRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNC 564
Cdd:PRK13657 328 LGRvKGAVEFDDVSFSYDnSRQGV---EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 565 KSLRRHIGIVQQEPVLMSGTIRDNITYGLTyTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIA 644
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIA 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 645 RALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIvsIAHRLSTIRRSENVIVLGHdGSVVEMGKFKELYA 722
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRNADRILVFDN-GRVVESGSFDELVA 558
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
235-722 |
1.60e-77 |
|
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: 265.07 E-value: 1.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 235 RFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDA----YVVSRSMTQKVSdgvkaLICGVVGVGMM 310
Cdd:TIGR01846 199 RTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRELEqirnFLTGSALTVVLD-----LLFVVVFLAVM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 311 CSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGN-------ELSRYNVA 383
Cdd:TIGR01846 274 FFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQfqnrwdrQLAAYVAA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 384 IRDIFQVGKTAAftnakffTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAG 463
Cdd:TIGR01846 354 SFRVTNLGNIAG-------QAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGI 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 464 AASRLFELTDrKPSISPTVGHKYKPD-RGVIEFKDVSFSY-PTRPSVqiFKNLNFKIAPGSSVCIVGPSGRGKSTIALLL 541
Cdd:TIGR01846 427 ALERLGDILN-SPTEPRSAGLAALPElRGAITFENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLL 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 542 LRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTkEEIRSVAKQCFCHNFITKFPNT 621
Cdd:TIGR01846 504 QRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPF-EHVIHAAKLAGAHDFISELPQG 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 622 YDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLmkSKSMTIVSIAHRLSTIRRSEN 701
Cdd:TIGR01846 583 YNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREI--CRGRTVIIIAHRLSTVRACDR 660
|
490 500
....*....|....*....|.
gi 1370557 702 VIVLgHDGSVVEMGKFKELYA 722
Cdd:TIGR01846 661 IIVL-EKGQIAESGRHEELLA 680
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
179-468 |
1.68e-77 |
|
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: 252.48 E-value: 1.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 179 IGMSIPKVIGIVLDTLktSSGSDFFDLKipifslplyEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKT 258
Cdd:cd18557 11 AQLLLPYLIGRLIDTI--IKGGDLDVLN---------ELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 259 LHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQ 338
Cdd:cd18557 80 LRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 339 IRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLA 418
Cdd:cd18557 160 IRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1370557 419 YGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRL 468
Cdd:cd18557 240 YGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
493-707 |
4.23e-75 |
|
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: 241.52 E-value: 4.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPsVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIG 572
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSGTIRDNItygltytptkeeirsvakqcfchnfitkfpntydtvigphgtlLSGGQKQRIAIARALIKKPT 652
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 653 ILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLGH 707
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDD 169
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
490-705 |
2.45e-73 |
|
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: 238.91 E-value: 2.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 490 RGVIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRR 569
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 570 HIGIVQQEPVLMSGTIRDNITYGLTYTPTkEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIK 649
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSF-ECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 650 KPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVL 705
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVL 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
184-724 |
5.69e-70 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 241.16 E-value: 5.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 184 PKVIGIVLDTLKTSSGSDffdlkipifslplYEFLSFFTVALLIGCAANFGRFILlRIL----SERVVARLRANVIKKTL 259
Cdd:PRK10789 15 PKVVGIIVDGVTEQHMTT-------------GQILMWIGTMVLIAVVVYLLRYVW-RVLlfgaSYQLAVELREDFYRQLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 260 HQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCS-LSPQLSILLLFFTPPVLFSASVFGKQ 338
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMIKRYGDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 339 IRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLA 418
Cdd:PRK10789 161 LHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 419 YGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRLFELTDRKPSISPtvGHKYKPD-RGVIEFKD 497
Cdd:PRK10789 241 GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKD--GSEPVPEgRGELDVNI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 498 VSFSYPTRpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQE 577
Cdd:PRK10789 319 RQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 578 PVLMSGTIRDNITYGLTyTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILD 657
Cdd:PRK10789 398 PFLFSDTVANNIALGRP-DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 658 EATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLGHdGSVVEMGKFKELYANP 724
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTEASEILVMQH-GHIAQRGNHDQLAQQS 540
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
493-722 |
8.51e-69 |
|
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: 227.37 E-value: 8.51e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYptRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHI 571
Cdd:cd03252 1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVLMSGTIRDNITYGLTyTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKP 651
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADP-GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 652 TILILDEATSALDVESEGAINytfgQLMK--SKSMTIVSIAHRLSTIRRSENVIVLGHdGSVVEMGKFKELYA 722
Cdd:cd03252 158 RILIFDEATSALDYESEHAIM----RNMHdiCAGRTVIIIAHRLSTVKNADRIIVMEK-GRIVEQGSHDELLA 225
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
179-722 |
8.22e-67 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 235.24 E-value: 8.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 179 IGMSIPKVIGIVLDTLktssgsdffdlkIPIFSLPLYEFLSFFTVALLIGCAA-NFGR-FILLRILSeRVVARLRANVIK 256
Cdd:TIGR03797 151 LGMLVPIATGILIGTA------------IPDADRSLLVQIALALLAAAVGAAAfQLAQsLAVLRLET-RMDASLQAAVWD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 257 KTLHQDAEFFDNHKVGDLISRlgsdAYVVSRsMTQKVSD-GVKALICGVVGV---GMMCSLSPQL---SILLLFFTPPVL 329
Cdd:TIGR03797 218 RLLRLPVSFFRQYSTGDLASR----AMGISQ-IRRILSGsTLTTLLSGIFALlnlGLMFYYSWKLalvAVALALVAIAVT 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 330 FSASVFgkQIRNTSKdLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSR----YNVAIRDIFQVGKTAAFTNakffTTT 405
Cdd:TIGR03797 293 LVLGLL--QVRKERR-LLELSGKISGLTVQLINGISKLRVAGAENRAFARwaklFSRQRKLELSAQRIENLLT----VFN 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 406 SLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRLFELTDRKPSISptvGHK 485
Cdd:TIGR03797 366 AVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVD---EAK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 486 YKPDR--GVIEFKDVSFSYptRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKL 562
Cdd:TIGR03797 443 TDPGKlsGAIEVDRVTFRY--RPdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 563 NCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPtkEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIA 642
Cdd:TIGR03797 521 DVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTL--DEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 643 IARALIKKPTILILDEATSALDVESEGAINYTFGQLmkskSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRNADRIYVL-DAGRVVQQGTYDELMA 673
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
235-722 |
2.75e-66 |
|
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: 234.45 E-value: 2.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 235 RFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSD---AYVVSRSMTQKVSDGVKALICGVVgvgMMC 311
Cdd:TIGR03796 214 QLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNdqvAEFLSGQLATTALDAVMLVFYALL---MLL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 312 sLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAeeqLSGIKTVQSFVAEGNE---LSR----YNVAI 384
Cdd:TIGR03796 291 -YDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVA---ISGLQSIETLKASGLEsdfFSRwagyQAKLL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 385 RDIFQVGKTaaftNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGA 464
Cdd:TIGR03796 367 NAQQELGVL----TQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGD 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 465 ASRL-------FELTDRKPSISPTVGHKYKPDRGVIEFKDVSFSY-PTRPSVqiFKNLNFKIAPGSSVCIVGPSGRGKST 536
Cdd:TIGR03796 443 LNRLddvlrnpVDPLLEEPEGSAATSEPPRRLSGYVELRNITFGYsPLEPPL--IENFSLTLQPGQRVALVGGSGSGKST 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 537 IALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTKEEIRSVAKQCFcHNFIT 616
Cdd:TIGR03796 521 IAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAI-HDVIT 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 617 KFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINytfgQLMKSKSMTIVSIAHRLSTI 696
Cdd:TIGR03796 600 SRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIID----DNLRRRGCTCIIVAHRLSTI 675
|
490 500
....*....|....*....|....*.
gi 1370557 697 RRSENVIVLGHdGSVVEMGKFKELYA 722
Cdd:TIGR03796 676 RDCDEIIVLER-GKVVQRGTHEELWA 700
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
491-715 |
2.39e-62 |
|
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: 209.27 E-value: 2.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 491 GVIEFKDVSFSYptRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRR 569
Cdd:cd03244 1 GDIEFKNVSLRY--RPnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 570 HIGIVQQEPVLMSGTIRDNITYGLTYTPtkEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIK 649
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDPFGEYSD--EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 650 KPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLgHDGSVVEMG 715
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHRLDTIIDSDRILVL-DKGRVVEFD 219
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
181-467 |
2.80e-61 |
|
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: 209.03 E-value: 2.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 181 MSIPKVIGIVLDTLKTSSGSDFFDLKIPIFSLPLYeflsfFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLH 260
Cdd:cd18780 13 LALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLI-----LLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 261 QDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIR 340
Cdd:cd18780 88 QEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 341 NTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYG 420
Cdd:cd18780 168 KLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370557 421 SYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASR 467
Cdd:cd18780 248 GRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVR 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
180-705 |
1.09e-60 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 224.14 E-value: 1.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 180 GMSIP---KVIGIVLDTLKTssGSDFFDLKIPIFSLPLYEFLSFFTVALligCaanfgrfilLRILSERVVARLRANVIK 256
Cdd:PTZ00265 73 GGTLPffvSVFGVIMKNMNL--GENVNDIIFSLVLIGIFQFILSFISSF---C---------MDVVTTKILKTLKLEFLK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 257 KTLHQDAEFFDNHKVGDLISRLgsDAYVvsrsmtQKVSDGVKALICGVVG-----VGM-MCSL--SPQLSILLLFFTPPV 328
Cdd:PTZ00265 139 SVFYQDGQFHDNNPGSKLTSDL--DFYL------EQVNAGIGTKFITIFTyasafLGLyIWSLfkNARLTLCITCVFPLI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 329 LFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFftttslL 408
Cdd:PTZ00265 211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLH------I 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 409 GDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGL------STFY--------SEIMQGAGAASRLFELTDR 474
Cdd:PTZ00265 285 GMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFHGGSVISIllgvliSMFMltiilpniTEYMKSLEATNSLYEIINR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 475 KPSISPTVGHKYKPDRGVIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITI 554
Cdd:PTZ00265 365 KPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 555 -DNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGL---------------------------------------- 593
Cdd:PTZ00265 445 nDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlnd 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 594 ---------------TYTPTKE-EIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILD 657
Cdd:PTZ00265 525 msnttdsneliemrkNYQTIKDsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILD 604
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1370557 658 EATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVL 705
Cdd:PTZ00265 605 EATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
491-712 |
4.06e-60 |
|
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: 203.20 E-value: 4.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 491 GVIEFKDVSFSYPTRPSVQIfKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRH 570
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQEPVLMSGTIRDNITYGLTYTpTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKK 650
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLA-DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370557 651 PTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLgHDGSVV 712
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVM-DSGRIV 217
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
176-468 |
2.11e-58 |
|
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: 200.79 E-value: 2.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 176 SCSIGMSIPKVIGIVLDTLKTSSgsdffdlkipiFSLPLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVI 255
Cdd:cd18576 8 SSAIGLVFPLLAGQLIDAALGGG-----------DTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 256 KKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVF 335
Cdd:cd18576 77 RHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 336 GKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLT 415
Cdd:cd18576 157 GRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1370557 416 VLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRL 468
Cdd:cd18576 237 VLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
451-705 |
2.36e-58 |
|
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: 207.91 E-value: 2.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 451 LSTFYSEIMQGAGAASRLFELTDRKPSISPTVGHKYKPDRGVIEFKDVSFSYPTRPSVqiFKNLNFKIAPGSSVCIVGPS 530
Cdd:TIGR02857 280 LGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 531 GRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTpTKEEIRSVAKQCF 610
Cdd:TIGR02857 358 GAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDA-SDAEIREALERAG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 611 CHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIA 690
Cdd:TIGR02857 437 LDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVT 514
|
250
....*....|....*
gi 1370557 691 HRLSTIRRSENVIVL 705
Cdd:TIGR02857 515 HRLALAALADRIVVL 529
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
176-448 |
6.81e-58 |
|
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: 199.02 E-value: 6.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 176 SCSIGMSIPKVIGIVLDTLKTSSGSDFFDLKIpifslplyeFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVI 255
Cdd:pfam00664 11 SGAISPAFPLVLGRILDVLLPDGDPETQALNV---------YSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 256 KKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVF 335
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 336 GKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLT 415
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1370557 416 VLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAV 448
Cdd:pfam00664 242 ALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
186-720 |
7.95e-58 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 210.37 E-value: 7.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 186 VIGIVLDTLKTSSGSDFFDLKIPIFsLP--LYEFLSFFTVALLIGCA----ANFGRFILLRILSERVVARLRANVIKKTL 259
Cdd:TIGR01193 162 VIAAIIVTLISIAGSYYLQKIIDTY-IPhkMMGTLGIISIGLIIAYIiqqiLSYIQIFLLNVLGQRLSIDIILSYIKHLF 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 260 HQDAEFFDNHKVGDLISRLgSDAyvvsrsmtQKVSDGVKALICGV-------VGVGM----------MCSLS--PQLSIL 320
Cdd:TIGR01193 241 ELPMSFFSTRRTGEIVSRF-TDA--------SSIIDALASTILSLfldmwilVIVGLflvrqnmllfLLSLLsiPVYAVI 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 321 LLFFTPPvlfsasvFGKQirntSKDLQEATGQLTRVAEEQLSGIKTVQSFvaeGNELSRYNvAIRDIFQVGKTAAFTNAK 400
Cdd:TIGR01193 312 IILFKRT-------FNKL----NHDAMQANAVLNSSIIEDLNGIETIKSL---TSEAERYS-KIDSEFGDYLNKSFKYQK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 401 FFTTTSLLGDLSFLT----VLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRLFE--LTDR 474
Cdd:TIGR01193 377 ADQGQQAIKAVTKLIlnvvILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 475 KPSISPTVGHKYKPDrGVIEFKDVSFSYPTrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITI 554
Cdd:TIGR01193 457 EFINKKKRTELNNLN-GDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 555 DNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLS 634
Cdd:TIGR01193 534 NGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSIS 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 635 GGQKQRIAIARALIKKPTILILDEATSALDVESEGAInytFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHdGSVVEM 714
Cdd:TIGR01193 614 GGQKQRIALARALLTDSKVLILDESTSNLDTITEKKI---VNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDH-GKIIEQ 689
|
....*.
gi 1370557 715 GKFKEL 720
Cdd:TIGR01193 690 GSHDEL 695
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
200-722 |
8.50e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 208.03 E-value: 8.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 200 SDFFDLKIPIFSLPLyeflsfftvALLIGCAANFgrfILLRILSER---------------VVARLRANVIKKTLHQDAE 264
Cdd:PRK10790 47 SYFIDNMVAKGNLPL---------GLVAGLAAAY---VGLQLLAAGlhyaqsllfnraavgVVQQLRTDVMDAALRQPLS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 265 FFDNHKVGDLISRLGSDAYVVsRSMTQKVSDGV---KALIcGVVGVGMMcSLSPQLSILLLFFTPPVL--------FSAS 333
Cdd:PRK10790 115 AFDTQPVGQLISRVTNDTEVI-RDLYVTVVATVlrsAALI-GAMLVAMF-SLDWRMALVAIMIFPAVLvvmviyqrYSTP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 334 VFgKQIRNTSKDLQEATgqltrvaEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQvGKTAAFTNAKFFtttsLLGDLSF 413
Cdd:PRK10790 192 IV-RRVRAYLADINDGF-------NEVINGMSVIQQFRQQARFGERMGEASRSHYM-ARMQTLRLDGFL----LRPLLSL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 414 LTVLAYGSYLVL-----QSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRLFELTDRKpsiSPTVGHKYKP 488
Cdd:PRK10790 259 FSALILCGLLMLfgfsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGP---RQQYGNDDRP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 489 -DRGVIEFKDVSFSYptRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL 567
Cdd:PRK10790 336 lQSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEPVLMSGTIRDNITYGLTYtpTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARAL 647
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLGRDI--SEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVL 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 648 IKKPTILILDEATSALDVESEGAINYTFgQLMKSKSmTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQAL-AAVREHT-TLVVIAHRLSTIVEADTILVL-HRGQAVEQGTHQQLLA 563
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
179-468 |
1.10e-55 |
|
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: 193.54 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 179 IGMSIPKVIGIVLDTLktssgsdffdLKIPIFSLpLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKT 258
Cdd:cd07346 14 LGLALPLLTKLLIDDV----------IPAGDLSL-LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 259 LHQDAEFFDNHKVGDLISRLGSDA----YVVSRSMTQKVSDGVKAlicgVVGVGMMCSLSPQLSILLLFFTPPVLFSASV 334
Cdd:cd07346 83 QRLSLSFFDRNRTGDLMSRLTSDVdavqNLVSSGLLQLLSDVLTL----IGALVILFYLNWKLTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 335 FGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFL 414
Cdd:cd07346 159 FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1370557 415 TVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRL 468
Cdd:cd07346 239 LVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
181-467 |
4.11e-55 |
|
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: 191.99 E-value: 4.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 181 MSIPKVIGIVLDTLkTSSGsDFFDLKIPIFSLplyeFLSFFTVALLIGCaanfgRFILLRILSERVVARLRANVIKKTLH 260
Cdd:cd18572 13 LAIPHYTGAVIDAV-VADG-SREAFYRAVLLL----LLLSVLSGLFSGL-----RGGCFSYAGTRLVRRLRRDLFRSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 261 QDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIR 340
Cdd:cd18572 82 QDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 341 NTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYG 420
Cdd:cd18572 162 KLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370557 421 SYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASR 467
Cdd:cd18572 242 GHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEK 288
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
245-693 |
5.29e-55 |
|
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: 198.74 E-value: 5.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 245 RVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLL-- 322
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAag 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 323 ----FFTPPVLFSASVfgkqiRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTN 398
Cdd:TIGR02868 163 lllaGFVAPLVSLRAA-----RAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 399 AKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRLFELTDRKPSI 478
Cdd:TIGR02868 238 ALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 479 SPTVGHK---YKPDRGVIEFKDVSFSYPTRPSVqiFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITID 555
Cdd:TIGR02868 318 AEGSAPAagaVGLGKPTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 556 NQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTyTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSG 635
Cdd:TIGR02868 396 GVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARP-DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSG 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 636 GQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRL 693
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
416-715 |
5.12e-54 |
|
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: 196.51 E-value: 5.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 416 VLAYGSYLVLQSQLSIGDLTA--FMLyteytGNAvfgLSTFYSEI-----MQGAGAA-SRLFELTDRKPSISPTVghKYK 487
Cdd:COG4618 256 VLGLGAYLVIQGEITPGAMIAasILM-----GRA---LAPIEQAIggwkqFVSARQAyRRLNELLAAVPAEPERM--PLP 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 488 PDRGVIEFKDVSFSYPTRPSVqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL 567
Cdd:COG4618 326 RPKGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEPVLMSGTIRDNIT-YGltyTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARA 646
Cdd:COG4618 405 GRHIGYLPQDVELFDGTIAENIArFG---DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARA 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFgQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMG 715
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKARGATVVVITHRPSLLAAVDKLLVL-RDGRVQAFG 548
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
493-711 |
4.02e-51 |
|
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: 176.64 E-value: 4.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYP--TRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRH 570
Cdd:cd03246 1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQEPVLMSGTIRDNItygltytptkeeirsvakqcfchnfitkfpntydtvigphgtlLSGGQKQRIAIARALIKK 650
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370557 651 PTILILDEATSALDVESEGAINYTFGQlMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSV 711
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLASADRILVL-EDGRV 173
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
179-468 |
5.26e-51 |
|
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: 180.32 E-value: 5.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 179 IGMSIPKVIGIVLDTLKTSSgsdffdlkipifslPLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKT 258
Cdd:cd18551 14 ASLAQPLLVKNLIDALSAGG--------------SSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 259 LHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQ 338
Cdd:cd18551 80 LRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 339 IRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLA 418
Cdd:cd18551 160 IRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1370557 419 YGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRL 468
Cdd:cd18551 240 VGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
413-720 |
9.49e-51 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 193.71 E-value: 9.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 413 FLTVLAY--GSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRLFELTDRKPSI----SPTVGHKY 486
Cdd:PTZ00265 1079 FINSFAYwfGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIdvrdNGGIRIKN 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 487 KPD-RGVIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYN------------------- 546
Cdd:PTZ00265 1159 KNDiKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtn 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 547 -----------------------------------PTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITY 591
Cdd:PTZ00265 1239 eqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKF 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 592 GlTYTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAI 671
Cdd:PTZ00265 1319 G-KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1370557 672 NYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGH---DGSVVEM-GKFKEL 720
Cdd:PTZ00265 1398 EKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrTGSFVQAhGTHEEL 1450
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
492-740 |
1.17e-50 |
|
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: 185.88 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPS--VQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS--- 566
Cdd:COG1123 260 LLEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEPVLM---SGTIRDNITYGLTY--TPTKEEIRSVAKQCF-----CHNFITKFPNTydtvigphgtlLSGG 636
Cdd:COG1123 340 LRRRVQMVFQDPYSSlnpRMTVGDIIAEPLRLhgLLSRAERRERVAELLervglPPDLADRYPHE-----------LSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 637 QKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMG 715
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVM-YDGRIVEDG 487
|
250 260
....*....|....*....|....*.
gi 1370557 716 KFKELYANPTSALSQ-LLneKAAPGP 740
Cdd:COG1123 488 PTEEVFANPQHPYTRaLL--AAVPSL 511
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
488-724 |
1.90e-49 |
|
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: 173.37 E-value: 1.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 488 PDRGVIEFKDVSFSY-PTRPSVqiFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS 566
Cdd:cd03369 2 PEHGEIEVENLSVRYaPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEPVLMSGTIRDNITYGLTYtpTKEEIRSVAKqcfchnfitkfpntydtvIGPHGTLLSGGQKQRIAIARA 646
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNLDPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLghdgsvvEMGKFKElYANP 724
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVM-------DAGEVKE-YDHP 207
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
205-716 |
9.79e-49 |
|
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: 181.01 E-value: 9.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 205 LKIPIFSLPLYEFL----SFFT-VALLIGCAANFGRFILLRILSERVVARLRANvIKKTLHQ---DAEFFDNhkvgdlIS 276
Cdd:TIGR01842 23 LAPPLYMLQVYDRVltsgSVPTlLMLTVLALGLYLFLGLLDALRSFVLVRIGEK-LDGALNQpifAASFSAT------LR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 277 RLGSDAYVVSRSMTQkvsdgVKALICG------------VVGVGMMCSLSPQLSILLLFFTPpVLFSASVFGKqiRNTSK 344
Cdd:TIGR01842 96 RGSGDGLQALRDLDQ-----LRQFLTGpglfaffdapwmPIYLLVCFLLHPWIGILALGGAV-VLVGLALLNN--RATKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 345 DLQEATGQL---TRVAEEQLSGIKTVQSFVAEGNELSRY---NVAIRDIFQVgktAAFTNAKFFTTTSLLGDLSFLTVLA 418
Cdd:TIGR01842 168 PLKEATEASiraNNLADSALRNAEVIEAMGMMGNLTKRWgrfHSKYLSAQSA---ASDRAGMLSNLSKYFRIVLQSLVLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 419 YGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRLFELTDRKPSISPTVghKYKPDRGVIEFKDV 498
Cdd:TIGR01842 245 LGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAM--PLPEPEGHLSVENV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 499 SFSyPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEP 578
Cdd:TIGR01842 323 TIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 579 VLMSGTIRDNITYgLTYTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDE 658
Cdd:TIGR01842 402 ELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDE 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 659 ATSALDVESEGAINYTFGQLmKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGK 716
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVL-QDGRIARFGE 536
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
492-715 |
2.62e-48 |
|
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: 170.76 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL--- 567
Cdd:cd03257 1 LLEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEPV-----LMsgTIRDNITYGLTY---TPTKEEIRSVAKQCFCH-----NFITKFPNTydtvigphgtlLS 634
Cdd:cd03257 81 RKEIQMVFQDPMsslnpRM--TIGEQIAEPLRIhgkLSKKEARKEAVLLLLVGvglpeEVLNRYPHE-----------LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 635 GGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVE 713
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVM-YAGKIVE 226
|
..
gi 1370557 714 MG 715
Cdd:cd03257 227 EG 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
451-735 |
2.86e-48 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 180.81 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 451 LSTFYSEIMQGAGAASRLFELTDRKPSISPTVGHKYKPDRGV-IEFKDVSFSYPTrpSVQIFKNLNFKIAPGSSVCIVGP 529
Cdd:PRK11174 307 LGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDPVtIEAEDLEILSPD--GKTLAGPLNFTLPAGQRIALVGP 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 530 SGRGKSTIALLLLRYYnPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGlTYTPTKEEIRSVAKQC 609
Cdd:PRK11174 385 SGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-NPDASDEQLQQALENA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 610 FCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSI 689
Cdd:PRK11174 463 WVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMV 540
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370557 690 AHRLSTIRRSENVIVLgHDGSVVEMGKFKELYANPtSALSQLLNEK 735
Cdd:PRK11174 541 THQLEDLAQWDQIWVM-QDGQIVQQGDYAELSQAG-GLFATLLAHR 584
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
493-724 |
3.21e-47 |
|
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: 167.89 E-value: 3.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIG 572
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPV--LMSGTIRDNITYGLTYTP-TKEEIRSVAKQCF----CHNFITKFPNTydtvigphgtlLSGGQKQRIAIAR 645
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLGlPREEIRERVEEALelvgLEHLADRPPHE-----------LSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 646 ALIKKPTILILDEATSALDVESEGAINYTFGQLmKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKFKELYANP 724
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAElADRVIVL-DDGRIVADGTPREVFSDY 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
464-723 |
8.72e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 176.17 E-value: 8.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 464 AASRLFELTDRKPSISPTVGHKYKPDRGVIEFKDVSFSYPTRPSvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLR 543
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 544 YYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTyTPTKEEIRSVAKQCFCHNFITKfPNTYD 623
Cdd:PRK11160 389 AWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEVLQQVGLEKLLED-DKGLN 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 624 TVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVI 703
Cdd:PRK11160 467 AWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDRIC 544
|
250 260
....*....|....*....|
gi 1370557 704 VLGhDGSVVEMGKFKELYAN 723
Cdd:PRK11160 545 VMD-NGQIIEQGTHQELLAQ 563
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
217-468 |
3.02e-46 |
|
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: 166.89 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 217 FLSFFTVALLIGCAAnFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDG 296
Cdd:cd18575 39 FLLLLAVALVLALAS-ALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 297 VKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNE 376
Cdd:cd18575 118 LRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 377 LSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYS 456
Cdd:cd18575 198 RQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWG 277
|
250
....*....|..
gi 1370557 457 EIMQGAGAASRL 468
Cdd:cd18575 278 DLQRAAGAAERL 289
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
493-707 |
2.42e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 161.52 E-value: 2.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIG 572
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSGTIRDNITYGLTY---TPTKEEIRSVAKQ-CFCHNFITKfpntydTVigphgTLLSGGQKQRIAIARALI 648
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLrerKFDRERALELLERlGLPPDILDK------PV-----ERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 649 KKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLGH 707
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEA 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
493-732 |
4.54e-45 |
|
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: 162.28 E-value: 4.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHI 571
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPvlMS-----GTIRDNITYGLT---YTPTKEEIRSVAKQC-FCHNFITKFPNTydtvigphgtlLSGGQKQRIA 642
Cdd:COG1124 82 QMVFQDP--YAslhprHTVDRILAEPLRihgLPDREERIAELLEQVgLPPSFLDRYPHQ-----------LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 643 IARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKFKELY 721
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVM-QNGRIVEELTVADLL 227
|
250
....*....|.
gi 1370557 722 ANPTSALSQLL 732
Cdd:COG1124 228 AGPKHPYTREL 238
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
494-709 |
7.73e-45 |
|
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: 160.33 E-value: 7.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 494 EFKDVSFSYPTRPSvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGI 573
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 574 VQQEP---VLMSgTIRDNITYGL-TYTPTKEEIR----SVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIAR 645
Cdd:cd03225 80 VFQNPddqFFGP-TVEEEVAFGLeNLGLPEEEIEerveEALELVGLEGLRDRSPFT-----------LSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 646 ALIKKPTILILDEATSALDVESEGAINYTFGQLmKSKSMTIVSIAHRLSTIRR-SENVIVLgHDG 709
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLElADRVIVL-EDG 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
493-753 |
8.77e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 162.21 E-value: 8.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQD-ISKLNCKSLRRHI 571
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEP--VLMSGTIRDNITYGLTY--TPTkEEIRS----VAKQCFCHNFITKfpntydtviGPHgtLLSGGQKQRIAI 643
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPR-EEMRKrvdeALKLVGMEDFRDR---------EPH--LLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 644 ARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYAN 723
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVM-NKGKIVAEGTPREIFSQ 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1370557 724 ------------PTSALSQLLNEKAAPGPSDqQLQIEKVIEK 753
Cdd:TIGR04520 227 vellkeigldvpFITELAKALKKRGIPLPPD-ILTEEELVDE 267
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
492-756 |
2.05e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 168.16 E-value: 2.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPsVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPT---TGTITIDNQDISKLNCKSLR 568
Cdd:COG1123 4 LLEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIVQQEP--VLMSGTIRDNITYGL-TYTPTKEEIRSVAKQCFCHNFITKFPNTYdtvigPHgtLLSGGQKQRIAIAR 645
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALeNLGLSRAEARARVLELLEAVGLERRLDRY-----PH--QLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 646 ALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANPT 725
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
250 260 270
....*....|....*....|....*....|.
gi 1370557 726 SALSQLLNEKAAPGPSDQQLQIEKVIEKEDL 756
Cdd:COG1123 236 ALAAVPRLGAARGRAAPAAAAAEPLLEVRNL 266
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
176-441 |
1.58e-43 |
|
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: 159.52 E-value: 1.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 176 SCSIGMSIPKVIGIVLDTlktssgsdffdlkipIFSLPLYEFLSFFTVAL----LIGCAANFGRFILLRILSERVVARLR 251
Cdd:cd18542 11 ATALNLLIPLLIRRIIDS---------------VIGGGLRELLWLLALLIlgvaLLRGVFRYLQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 252 ANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFS 331
Cdd:cd18542 76 NDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 332 ASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDL 411
Cdd:cd18542 156 SYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGL 235
|
250 260 270
....*....|....*....|....*....|
gi 1370557 412 SFLTVLAYGSYLVLQSQLSIGDLTAFMLYT 441
Cdd:cd18542 236 QIVLVLWVGGYLVINGEITLGELVAFISYL 265
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
217-468 |
1.86e-43 |
|
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: 159.12 E-value: 1.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 217 FLSFFTVAL-LIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSD 295
Cdd:cd18552 40 LVPLAIIGLfLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 296 GVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGN 375
Cdd:cd18552 120 LVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 376 ELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAF-----MLYteytgNAVFG 450
Cdd:cd18552 200 EIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFitallLLY-----QPIKR 274
|
250
....*....|....*...
gi 1370557 451 LSTFYSEIMQGAGAASRL 468
Cdd:cd18552 275 LSNVNANLQRGLAAAERI 292
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
493-746 |
8.40e-43 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 158.70 E-value: 8.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDISKLNCKSL 567
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINllerPTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 ---RRHIGIV-QQEPVLMSGTIRDNITYGLTYTPT-KEEIRS-VA----------KqcfchnfITKFPNTydtvigphgt 631
Cdd:COG1135 78 raaRRKIGMIfQHFNLLSSRTVAENVALPLEIAGVpKAEIRKrVAellelvglsdK-------ADAYPSQ---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 632 lLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAI-------NYTFGqlmksksMTIVSIAHRLSTIRR-SENVI 703
Cdd:COG1135 141 -LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSIldllkdiNRELG-------LTIVLITHEMDVVRRiCDRVA 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1370557 704 VLgHDGSVVEMGKFKELYANPTSALSQ-LLNEKAAPGPSDQQLQ 746
Cdd:COG1135 213 VL-ENGRIVEQGPVLDVFANPQSELTRrFLPTVLNDELPEELLA 255
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
493-709 |
1.08e-42 |
|
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: 154.57 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPT-RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKST---IALLLLRyynPTTGTITIDNQDISKLNCKSL- 567
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 ---RRHIGIVQQEPVLMSG-TIRDNITYGLTYTPT-KEEIRSVAKQCFCH----NFITKFPNTydtvigphgtlLSGGQK 638
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELPLLLAGVpKKERRERAEELLERvglgDRLNHYPSE-----------LSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370557 639 QRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDG 709
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIEL-RDG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
492-713 |
1.20e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.82 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPT-RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKST----IALLLlryyNPTTGTITIDNQDISKLNCKS 566
Cdd:COG1136 4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllniLGGLD----RPTSGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 L----RRHIGIVQQEPVLMSG-TIRDNITYGLTYTPT-KEEIRSVAKQCFCH----NFITKFPNTydtvigphgtlLSGG 636
Cdd:COG1136 80 LarlrRRHIGFVFQFFNLLPElTALENVALPLLLAGVsRKERRERARELLERvglgDRLDHRPSQ-----------LSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 637 QKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVE 713
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRL-RDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
492-724 |
4.08e-42 |
|
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: 153.51 E-value: 4.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDISKLNCKS 566
Cdd:cd03258 1 MIELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKST----LIRCINglerPTSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 L---RRHIG-IVQQEPVLMSGTIRDNITYGL--TYTPTKEEIRSVA---KQCFCHNFITKFPNTydtvigphgtlLSGGQ 637
Cdd:cd03258 77 LrkaRRRIGmIFQHFNLLSSRTVFENVALPLeiAGVPKAEIEERVLellELVGLEDKADAYPAQ-----------LSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 638 KQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKF 717
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
....*..
gi 1370557 718 KELYANP 724
Cdd:cd03258 226 EEVFANP 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
493-720 |
6.95e-42 |
|
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: 152.72 E-value: 6.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN---------PTTGTITIDNQDISKLN 563
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKST----LLRLLNrlndlipgaPDEGEVLLDGKDIYDLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 564 CK--SLRRHIGIVQQEPVLMSGTIRDNITYGLTY--TPTKEEIRSVAKQCfchnfITK---FPNTYDTvigPHGTLLSGG 636
Cdd:cd03260 74 VDvlELRRRVGMVFQKPNPFPGSIYDNVAYGLRLhgIKLKEELDERVEEA-----LRKaalWDEVKDR---LHALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 637 QKQRIAIARALIKKPTILILDEATSALDVESEGAINytfgQLMKS--KSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVE 713
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIE----ELIAElkKEYTIVIVTHNMQQAARvADRTAFL-LNGRLVE 220
|
....*..
gi 1370557 714 MGKFKEL 720
Cdd:cd03260 221 FGPTEQI 227
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
179-440 |
1.58e-41 |
|
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: 153.72 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 179 IGMSIPKVIGIVLDTLkTSSGSDFFDLKIPIfslplyefLSFFTVALLIGCAANFGRFILLRIlSERVVARLRANVIKKT 258
Cdd:cd18541 14 LQLLIPRIIGRAIDAL-TAGTLTASQLLRYA--------LLILLLALLIGIFRFLWRYLIFGA-SRRIEYDLRNDLFAHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 259 LHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQ 338
Cdd:cd18541 84 LTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 339 IRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLA 418
Cdd:cd18541 164 IHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLW 243
|
250 260
....*....|....*....|..
gi 1370557 419 YGSYLVLQSQLSIGDLTAFMLY 440
Cdd:cd18541 244 YGGRLVIRGTITLGDLVAFNSY 265
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
511-661 |
7.51e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.02 E-value: 7.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 511 FKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSG-TIRDNI 589
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 590 TYGLT-YTPTKEEIRSVAkqcfcHNFITKFPNTY--DTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATS 661
Cdd:pfam00005 81 RLGLLlKGLSKREKDARA-----EEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
492-723 |
1.04e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 150.91 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHI 571
Cdd:PRK13632 7 MIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEP--VLMSGTIRDNITYGL---TYTPT--KEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIA 644
Cdd:PRK13632 86 GIIFQNPdnQFIGATVEDDIAFGLenkKVPPKkmKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 645 RALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHdGSVVEMGKFKELYAN 723
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSE-GKLIAQGKPKEILNN 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
494-709 |
3.71e-40 |
|
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: 145.08 E-value: 3.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 494 EFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGI 573
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 574 VQQepvlmsgtirdnitygltytptkeeirsvakqcfchnfitkfpntydtvigphgtlLSGGQKQRIAIARALIKKPTI 653
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 654 LILDEATSALDVESEGAINYTFGQLMKSKsMTIVSIAHRLSTIRRSENVIVLGHDG 709
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
493-710 |
5.80e-40 |
|
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: 146.46 E-value: 5.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVQ--IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIdnqdisklnckslRRH 570
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQEPVLMSGTIRDNITYGLTYTPtkEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKK 650
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDE--ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370557 651 PTILILDEATSALDVESEGAI--NYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLgHDGS 710
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNK--TRILVTHQLQLLPHADQIVVL-DNGR 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
492-724 |
7.01e-40 |
|
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: 147.43 E-value: 7.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTI---ALLLLRyynPTTGTITIDNQDISKLNCK--- 565
Cdd:COG1127 5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLlklIIGLLR---PDSGEILVDGQDITGLSEKely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 566 SLRRHIGIVQQEPVLMSG-TIRDNITYGLTYTP--TKEEIRSVAKQCFC----HNFITKFPNTydtvigphgtlLSGGQK 638
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVAFPLREHTdlSEAEIRELVLEKLElvglPGAADKMPSE-----------LSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 639 QRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKF 717
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVL-ADGKIIAEGTP 226
|
....*..
gi 1370557 718 KELYANP 724
Cdd:COG1127 227 EELLASD 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
493-715 |
9.79e-40 |
|
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: 144.76 E-value: 9.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCkSLRRHIG 572
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSGTIRDNItygltytptkeeirsvakqcfchnfitkfpntydtvigphGTLLSGGQKQRIAIARALIKKPT 652
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 653 ILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLgHDGSVVEMG 715
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFL-ENGKIIMQG 178
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
492-728 |
1.62e-39 |
|
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: 149.05 E-value: 1.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNP---TTGTITIDNQDISKLNCKSL 567
Cdd:COG0444 1 LLEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 R----RHIGIVQQEPvlMSG-----TIRDNITYGLTY--TPTKEEIRSVAKQCFC-------HNFITKFPNTydtvigph 629
Cdd:COG0444 81 RkirgREIQMIFQDP--MTSlnpvmTVGDQIAEPLRIhgGLSKAEARERAIELLErvglpdpERRLDRYPHE-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 630 gtlLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIV--LG 706
Cdd:COG0444 151 ---LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVAVmyAG 227
|
250 260
....*....|....*....|....*.
gi 1370557 707 HdgsVVEMGKFKELYANP----TSAL 728
Cdd:COG0444 228 R---IVEEGPVEELFENPrhpyTRAL 250
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
183-467 |
2.36e-39 |
|
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: 147.69 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 183 IPKVIGIVLDTLKTS---SGSDFF-DLKIPIFSLplyeFLSFFTVALLigcaaNFGRFILLRILSERVVARLRANVIKKT 258
Cdd:cd18574 15 IPLLLGDLVNVISRSlkeTNGDFIeDLKKPALKL----LGLYLLQSLL-----TFAYISLLSVVGERVAARLRNDLFSSL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 259 LHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQ 338
Cdd:cd18574 86 LRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 339 IRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRD-------------IFQvgktaAFTNakFFttt 405
Cdd:cd18574 166 LRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKaaklneklglgigIFQ-----GLSN--LA--- 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370557 406 slLGDLSfLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASR 467
Cdd:cd18574 236 --LNGIV-LGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGAR 294
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
492-713 |
4.22e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.42 E-value: 4.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPtrPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS---LR 568
Cdd:COG2884 1 MIRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIVQQE-PVLMSGTIRDNITYGLTYTPTKE-EIRSVAKQCFCH----NFITKFPNTydtvigphgtlLSGGQKQRIA 642
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALPLRVTGKSRkEIRRRVREVLDLvglsDKAKALPHE-----------LSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370557 643 IARALIKKPTILILDEATSALDVE-SEGAINYtFGQLMKSKsMTIVsIA-HRLSTIRRSEN-VIVLgHDGSVVE 713
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPEtSWEIMEL-LEEINRRG-TTVL-IAtHDLELVDRMPKrVLEL-EDGRLVR 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
493-713 |
1.29e-38 |
|
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: 143.00 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTR-PSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNckslrRHI 571
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVLMS-GTIRDNITYGLTYT-PTKEEIRSVAKQCF--CHnfITKFPNTYdtvigPHGtlLSGGQKQRIAIARAL 647
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQgVPKAEARERAEELLelVG--LSGFENAY-----PHQ--LSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 648 IKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLS-TIRRSENVIVL-GHDGSVVE 713
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDeAVFLADRVVVLsARPGRIVA 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
208-755 |
1.36e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 155.52 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 208 PIFSLPLYEFLSFFTVALligcaaNFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSR 287
Cdd:PLN03232 949 PGFYIVVYALLGFGQVAV------TFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDR 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 288 SMTQKVSDGVKAL-----ICGVVGVGMMCSLSPQLSILLLFFTPPVLFsasvfgkqiRNTSKDLQEaTGQLTRVA----- 357
Cdd:PLN03232 1023 NVANLMNMFMNQLwqllsTFALIGTVSTISLWAIMPLLILFYAAYLYY---------QSTSREVRR-LDSVTRSPiyaqf 1092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 358 EEQLSGIKTVQSFVAEgNELSRYNVAIRDiFQVGKTAAFTNAKFFTT---TSLLGDLSFLT----VLAYGSylvLQSQLS 430
Cdd:PLN03232 1093 GEALNGLSSIRAYKAY-DRMAKINGKSMD-NNIRFTLANTSSNRWLTirlETLGGVMIWLTatfaVLRNGN---AENQAG 1167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 431 IGDLTAFMLytEYTGNavfgLSTFYSEIMQGAGAASRLFELTDRK------PSISPTVGHKYKP-----DRGVIEFKDVS 499
Cdd:PLN03232 1168 FASTMGLLL--SYTLN----ITTLLSGVLRQASKAENSLNSVERVgnyidlPSEATAIIENNRPvsgwpSRGSIKFEDVH 1241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 500 FSY-PTRPSVqiFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEP 578
Cdd:PLN03232 1242 LRYrPGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSP 1319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 579 VLMSGTIRDNItygltyTPTKE----EIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTIL 654
Cdd:PLN03232 1320 VLFSGTVRFNI------DPFSEhndaDLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKIL 1393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 655 ILDEATSALDVESEGAINYTFGQLMKSKSMTIvsIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYANPTSALSQLLNe 734
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIREEFKSCTMLV--IAHRLNTIIDCDKILVL-SSGQVLEYDSPQELLSRDTSAFFRMVH- 1469
|
570 580
....*....|....*....|.
gi 1370557 735 kaAPGPSDQQLQIEKVIEKED 755
Cdd:PLN03232 1470 --STGPANAQYLSNLVFERRE 1488
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
225-468 |
1.52e-38 |
|
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: 145.31 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 225 LLIGCA---ANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALI 301
Cdd:cd18577 54 VYLGIGsfvLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 302 CGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYN 381
Cdd:cd18577 134 TFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 382 VAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFltVLA--YGSYLVLQSQLSIGD-LTAFMLYTeYTGNAVFGLSTFYSEI 458
Cdd:cd18577 214 KALEKARKAGIKKGLVSGLGLGLLFFIIFAMY--ALAfwYGSRLVRDGEISPGDvLTVFFAVL-IGAFSLGQIAPNLQAF 290
|
250
....*....|
gi 1370557 459 MQGAGAASRL 468
Cdd:cd18577 291 AKARAAAAKI 300
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
493-707 |
1.99e-38 |
|
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: 141.17 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLN--CKSLRRH 570
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQEPVLMSG-TIRDNITYGltytptkeeirsvakqcfchnfitkfpntydtvigphgtlLSGGQKQRIAIARALIK 649
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 650 KPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLGH 707
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRD 176
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
493-720 |
2.37e-38 |
|
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: 142.64 E-value: 2.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCK---SLRR 569
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 570 HIGIVQQEPVLMSG-TIRDNITYGL--TYTPTKEEIRSVAKQCF----CHNFITKFPNTydtvigphgtlLSGGQKQRIA 642
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLreHTRLSEEEIREIVLEKLeavgLRGAEDLYPAE-----------LSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 643 IARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKFKEL 720
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVL-YDGKIVAEGTPEEL 224
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
183-468 |
2.38e-38 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 144.76 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 183 IPKVIGIVLDTLKTSSGSDFFDLKIPIFSLplyeflsfftVALLIGCAANFgRFILLRILSERVVARLRANVIKKTLHQD 262
Cdd:cd18784 15 IPYYTGQVIDGIVIEKSQDKFSRAIIIMGL----------LAIASSVAAGI-RGGLFTLAMARLNIRIRNLLFRSIVSQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 263 AEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNT 342
Cdd:cd18784 84 IGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 343 SKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSY 422
Cdd:cd18784 164 SKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGH 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370557 423 LVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRL 468
Cdd:cd18784 244 LVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
492-721 |
1.56e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 141.81 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPSVQIfKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHI 571
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEP--VLMSGTIRDNITYGLT--YTPTKEEIRSVAKQCFCHNFITKFPNTydtvigPHGtlLSGGQKQRIAIARAL 647
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGLEnhAVPYDEMHRRVSEALKQVDMLERADYE------PNA--LSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370557 648 IKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELY 721
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVM-NKGTVYKEGTPTEIF 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
492-727 |
1.95e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 140.13 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDI--SKLNCK 565
Cdd:COG1126 1 MIEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKST----LLRCINlleePDSGTITVDGEDLtdSKKDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 566 SLRRHIGIVQQE----PVLmsgTIRDNITYGLTYTP--TKEEIRSVAKQCFCH----NFITKFPNTydtvigphgtlLSG 635
Cdd:COG1126 74 KLRRKVGMVFQQfnlfPHL---TVLENVTLAPIKVKkmSKAEAEERAMELLERvglaDKADAYPAQ-----------LSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 636 GQKQRIAIARALIKKPTILILDEATSALDVESEGAInytfGQLMKS---KSMTIVSIAHRLSTIRR-SENVIVLgHDGSV 711
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEV----LDVMRDlakEGMTMVVVTHEMGFAREvADRVVFM-DGGRI 214
|
250
....*....|....*.
gi 1370557 712 VEMGKFKELYANPTSA 727
Cdd:COG1126 215 VEEGPPEEFFENPQHE 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
488-744 |
7.59e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 150.27 E-value: 7.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 488 PDRGVIEFKDVSFSY-PTRPSVqiFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS 566
Cdd:PLN03130 1233 PSSGSIKFEDVVLRYrPELPPV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEPVLMSGTIRDNItygltyTPTKE----EIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIA 642
Cdd:PLN03130 1311 LRKVLGIIPQAPVLFSGTVRFNL------DPFNEhndaDLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLS 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 643 IARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIvsIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:PLN03130 1385 LARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLI--IAHRLNTIIDCDRILVL-DAGRVVEFDTPENLLS 1461
|
250 260
....*....|....*....|..
gi 1370557 723 NPTSALSQLLNekaAPGPSDQQ 744
Cdd:PLN03130 1462 NEGSAFSKMVQ---STGAANAQ 1480
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
492-715 |
1.19e-36 |
|
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: 138.64 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHI 571
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVLMSG-TIRDNITYGLT------YTPTKEEIRSVAK---QCFCHNFITKfpnTYDTvigphgtlLSGGQKQRI 641
Cdd:COG1120 78 AYVPQEPPAPFGlTVRELVALGRYphlglfGRPSAEDREAVEEaleRTGLEHLADR---PVDE--------LSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 642 AIARALIKKPTILILDEATSALDvesegaINY------TFGQLMKSKSMTIVSIAHRLS-TIRRSENVIVLgHDGSVVEM 714
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLD------LAHqlevleLLRRLARERGRTVVMVLHDLNlAARYADRLVLL-KDGRIVAQ 219
|
.
gi 1370557 715 G 715
Cdd:COG1120 220 G 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
494-715 |
1.86e-36 |
|
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: 135.26 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 494 EFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGI 573
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 574 VQQepvlmsgtirdnitygltytptkeeirsVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKKPTI 653
Cdd:cd03214 78 VPQ----------------------------ALELLGLAHLADRPFNE-----------LSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 654 LILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLS-TIRRSENVIVLgHDGSVVEMG 715
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNlAARYADRVILL-KDGRIVAQG 180
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
183-467 |
4.10e-36 |
|
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: 138.31 E-value: 4.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 183 IPKVIGIVLDTLKTSSGSDF-FDLKipifslPLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQ 261
Cdd:cd18547 18 GPYLLGKAIDLIIEGLGGGGgVDFS------GLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 262 DAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRN 341
Cdd:cd18547 92 PLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 342 TSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGS 421
Cdd:cd18547 172 YFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGG 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370557 422 YLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASR 467
Cdd:cd18547 252 LLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
493-727 |
9.19e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.08 E-value: 9.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTiallLLR----YYNPTTGTITIDNQDISKL--Ncks 566
Cdd:COG3842 6 LELENVSKRYGDVTAL---DDVSLSIEPGEFVALLGPSGCGKTT----LLRmiagFETPDSGRILLDGRDVTGLppE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 lRRHIGIVQQEPVL---MsgTIRDNITYGLTY--TPtKEEIRSVAKQC--FCHnfITKFPNTYdtvigPHgtLLSGGQKQ 639
Cdd:COG3842 76 -KRNVGMVFQDYALfphL--TVAENVAFGLRMrgVP-KAEIRARVAELleLVG--LEGLADRY-----PH--QLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 640 RIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIV----------SIAHRlstirrsenVIVLgHDG 709
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIyvthdqeealALADR---------IAVM-NDG 212
|
250
....*....|....*...
gi 1370557 710 SVVEMGKFKELYANPTSA 727
Cdd:COG3842 213 RIEQVGTPEEIYERPATR 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
488-722 |
9.54e-36 |
|
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: 146.63 E-value: 9.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 488 PDRGVIEFKDVSFSYptRPSVQ-IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS 566
Cdd:TIGR00957 1280 PPRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEPVLMSGTIRDNITYGLTYtpTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARA 646
Cdd:TIGR00957 1358 LRFKITIIPQDPVLFSGSLRMNLDPFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFgqLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTI--RTQFEDCTVLTIAHRLNTIMDYTRVIVL-DKGEVAEFGAPSNLLQ 1508
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
493-720 |
2.11e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 134.42 E-value: 2.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlNCKSLRRHIG 572
Cdd:COG1131 1 IEVRGLTKRYGDKTAL---DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSG-TIRDNIT-----YGLTYTPTKEEIRSVAKQCFCHNFITKFPNTYdtvigphgtllSGGQKQRIAIARA 646
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLmKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKFKEL 720
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERlCDRVAII-DKGRIVADGTPDEL 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
492-723 |
3.00e-35 |
|
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: 134.21 E-value: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNcKSLRRHI 571
Cdd:COG4555 1 MIEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVLMSG-TIRDNITY-GLTYTPTKEEIRSVAKQcFCHNFitKFPNTYDTVIGPhgtlLSGGQKQRIAIARALIK 649
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYfAELYGLFDEELKKRIEE-LIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 650 KPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSiAHRLSTIRR-SENVIVLgHDGSVVEMGKFKELYAN 723
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFS-SHIMQEVEAlCDRVVIL-HKGKVVAQGSLDELREE 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
488-665 |
3.34e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.45 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 488 PDRGVIEFKDVSFSYPTRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLR----YYNPTTGTITIDNQDISKL 562
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKST----LLRliagLEKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 563 nckslRRHIGIVQQEPVLMs-gTIRDNITYGLTYTP-TKEEIRSVAKQCFCH----NFITKFPNTydtvigphgtlLSGG 636
Cdd:COG1116 79 -----GPDRGVVFQEPALLpwlTVLDNVALGLELRGvPKAERRERARELLELvglaGFEDAYPHQ-----------LSGG 142
|
170 180
....*....|....*....|....*....
gi 1370557 637 QKQRIAIARALIKKPTILILDEATSALDV 665
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDA 171
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
176-440 |
5.25e-35 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 134.92 E-value: 5.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 176 SCSIGMSIPKVIGIVLDTlktssgsdffdlkiPIFSLPLYEFLSFFTVALLIGCA---ANFGRFILLRILSERVVARLRA 252
Cdd:cd18543 11 ATLAGLAIPLLTRRAIDG--------------PIAHGDRSALWPLVLLLLALGVAeavLSFLRRYLAGRLSLGVEHDLRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 253 NVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMT---QKVSDGVKAlicgVVGVGMMCSLSPQLSILLLFFTPPVL 329
Cdd:cd18543 77 DLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAfgpFLLGNLLTL----VVGLVVMLVLSPPLALVALASLPPLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 330 FSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLG 409
Cdd:cd18543 153 LVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALP 232
|
250 260 270
....*....|....*....|....*....|.
gi 1370557 410 DLSFLTVLAYGSYLVLQSQLSIGDLTAFMLY 440
Cdd:cd18543 233 ELGLAAVLALGGWLVANGSLTLGTLVAFSAY 263
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
516-728 |
5.36e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.01 E-value: 5.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 516 FKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLN---CKSLRRHIGIVQQEP--VL---MsgTIRD 587
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPyaSLnprM--TVGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 588 NITYGLTY--TPTKEEIRSVAKQCFchnfitkfpntyDTViG---------PHgtLLSGGQKQRIAIARALIKKPTILIL 656
Cdd:COG4608 117 IIAEPLRIhgLASKAERRERVAELL------------ELV-GlrpehadryPH--EFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 657 DEATSALDVeSEGA--INyTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIV--LGHdgsVVEMGKFKELYANP----TSA 727
Cdd:COG4608 182 DEPVSALDV-SIQAqvLN-LLEDLQDELGLTYLFISHDLSVVRHiSDRVAVmyLGK---IVEIAPRDELYARPlhpyTQA 256
|
.
gi 1370557 728 L 728
Cdd:COG4608 257 L 257
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
512-724 |
1.15e-34 |
|
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: 133.54 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 512 KNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL---RRH-IGIVQQEPVLMSG-TIR 586
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelRRKkISMVFQSFALLPHrTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 587 DNITYGLTYTPTKEEIR-----SVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKKPTILILDEATS 661
Cdd:cd03294 121 ENVAFGLEVQGVPRAEReeraaEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 662 ALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANP 724
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
492-722 |
1.47e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.22 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYP--TRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRR 569
Cdd:PRK13635 5 IIRVEHISFRYPdaATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 570 HIGIVQQEP--VLMSGTIRDNITYGLTY--TPTKEEIRSV---AKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIA 642
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDDVAFGLENigVPREEMVERVdqaLRQVGMEDFLNREPHR-----------LSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 643 IARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVM-NKGEILEEGTPEEIFK 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
492-740 |
1.69e-34 |
|
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: 139.05 E-value: 1.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPT-----RPSVQIFK---NLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYyNPTTGTITIDNQDISKLN 563
Cdd:COG4172 275 LLEARDLKVWFPIkrglfRRTVGHVKavdGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 564 CK---SLRRHIGIVQQEPV--L---MsgTIRDNITYGLT---YTPTKEEIRSVAKQCFC-----HNFITKFPNTydtvig 627
Cdd:COG4172 354 RRalrPLRRRMQVVFQDPFgsLsprM--TVGQIIAEGLRvhgPGLSAAERRARVAEALEevgldPAARHRYPHE------ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 628 phgtlLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLg 706
Cdd:COG4172 426 -----FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRAlAHRVMVM- 499
|
250 260 270
....*....|....*....|....*....|....*
gi 1370557 707 HDGSVVEMGKFKELYANPTSALSQ-LLneKAAPGP 740
Cdd:COG4172 500 KDGKVVEQGPTEQVFDAPQHPYTRaLL--AAAPLL 532
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
493-724 |
1.74e-34 |
|
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: 132.04 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYP-TRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHI 571
Cdd:cd03295 1 IEFENVTKRYGgGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVLMSG-TIRDNItyglTYTPT-----KEEIRSVAKQCF--CHNFITKFPNTYdtvigPHGtlLSGGQKQRIAI 643
Cdd:cd03295 78 GYVIQQIGLFPHmTVEENI----ALVPKllkwpKEKIRERADELLalVGLDPAEFADRY-----PHE--LSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 644 ARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYAN 723
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
.
gi 1370557 724 P 724
Cdd:cd03295 227 P 227
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
179-466 |
1.94e-34 |
|
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: 133.28 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 179 IGMSIPKVIGIVLDTLKTSSGSDFfdlkipifsLPLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKT 258
Cdd:cd18544 14 LELLGPLLIKRAIDDYIVPGQGDL---------QGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 259 LHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKAL--ICGVVGVgmMCSLSPQLSILLLFFTPPVLFSASVFG 336
Cdd:cd18544 85 QRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLllLIGILIA--MFLLNWRLALISLLVLPLLLLATYLFR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 337 KQIRNTSKDLQEATGQL-TRVAEeQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLT 415
Cdd:cd18544 163 KKSRKAYREVREKLSRLnAFLQE-SISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALAL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1370557 416 VLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSeIMQGAGAAS 466
Cdd:cd18544 242 VLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFN-ILQSAMASA 291
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
493-715 |
2.76e-34 |
|
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: 130.33 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLncKSLRRHIG 572
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSG-TIRDNITYGLT--YTPTKEEIRSV---AKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARA 646
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKlrGVPKAEIRARVrelLELVGLEGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMG 715
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
492-730 |
2.86e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 134.16 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPT-RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDISKLNCKS 566
Cdd:PRK11153 1 MIELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKST----LIRCINllerPTSGRVLVDGQDLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 L---RRHIG-IVQQEPVLMSGTIRDNITYGLTYTPT-KEEIRS-----------VAKqcfcHNfitKFPNTydtvigphg 630
Cdd:PRK11153 77 LrkaRRQIGmIFQHFNLLSSRTVFDNVALPLELAGTpKAEIKArvtellelvglSDK----AD---RYPAQ--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 631 tlLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAI-------NYTFGqlmksksMTIVSIAHRLSTIRR-SENV 702
Cdd:PRK11153 141 --LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIlellkdiNRELG-------LTIVLITHEMDVVKRiCDRV 211
|
250 260
....*....|....*....|....*...
gi 1370557 703 IVLGhDGSVVEMGKFKELYANPTSALSQ 730
Cdd:PRK11153 212 AVID-AGRLVEQGTVSEVFSHPKHPLTR 238
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
372-710 |
5.24e-34 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 138.02 E-value: 5.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 372 AEGNELSRYNVAIRDIF--QVGKTAAFTnakFFTTTSllgdlSFLTVLAygSYLV-----LQSQLSIGDLT----AFmly 440
Cdd:COG4178 242 AERRRLRRRFDAVIANWrrLIRRQRNLT---FFTTGY-----GQLAVIF--PILVaapryFAGEITLGGLMqaasAF--- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 441 teytgNAVFG-LSTF---YSEIMQGAGAASRLFEL------TDRKPSISPTVGHkykPDRGVIEFKDVSFSYPT-RPsvq 509
Cdd:COG4178 309 -----GQVQGaLSWFvdnYQSLAEWRATVDRLAGFeealeaADALPEAASRIET---SEDGALALEDLTLRTPDgRP--- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLR----YYNPTTGTITI-DNQDISklnckslrrhigIVQQEPVLMSGT 584
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKST----LLRaiagLWPYGSGRIARpAGARVL------------FLPQRPYLPLGT 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 585 IRDNITY-GLTYTPTKEEIRSVAKQCFCHNFITKFpntyDTViGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSAL 663
Cdd:COG4178 442 LREALLYpATAEAFSDAELREALEAVGLGHLAERL----DEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1370557 664 DVESEGAInYtfgQLMKS--KSMTIVSIAHRLSTIRRSENVIVLGHDGS 710
Cdd:COG4178 517 DEENEAAL-Y---QLLREelPGTTVISVGHRSTLAAFHDRVLELTGDGS 561
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
492-724 |
6.73e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 130.93 E-value: 6.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN------P---TTGTITIDNQDI--S 560
Cdd:COG1117 11 KIEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKST----LLRCLNrmndliPgarVEGEILLDGEDIydP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 561 KLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTK-----EEI-----RSVA---------KQcfchnfitkfpnt 621
Cdd:COG1117 84 DVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKskselDEIveeslRKAAlwdevkdrlKK------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 622 ydtvigpHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLmkSKSMTIVSIAHRLSTIRR-SE 700
Cdd:COG1117 151 -------SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARvSD 221
|
250 260
....*....|....*....|....
gi 1370557 701 NVIVLgHDGSVVEMGKFKELYANP 724
Cdd:COG1117 222 YTAFF-YLGELVEFGPTEQIFTNP 244
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
492-725 |
7.66e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 131.46 E-value: 7.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPsVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALL----LLRYYNPTTgTITIDNQDISKLNCKSL 567
Cdd:PRK13640 5 IVEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLinglLLPDDNPNS-KITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEP--VLMSGTIRDNITYGLT--YTPTKEEIRSVAK---QCFCHNFITKFPNTydtvigphgtlLSGGQKQR 640
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAFGLEnrAVPRPEMIKIVRDvlaDVGMLDYIDSEPAN-----------LSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 641 IAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKEL 720
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVL-DDGKLLAQGSPVEI 230
|
....*
gi 1370557 721 YANPT 725
Cdd:PRK13640 231 FSKVE 235
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
218-478 |
7.67e-34 |
|
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: 132.19 E-value: 7.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 218 LSFFTVALLIGcAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFD--NHKVGDLISRLGSDAYVVSRSMTQKVSD 295
Cdd:cd18578 56 LMFLVLAIVAG-IAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 296 GVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGN 375
Cdd:cd18578 135 ILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDY 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 376 ELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGD-LTAFMLYTeYTGNAVFGLSTF 454
Cdd:cd18578 215 FLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQfFIVFMALI-FGAQSAGQAFSF 293
|
250 260
....*....|....*....|....
gi 1370557 455 YSEIMQGAGAASRLFELTDRKPSI 478
Cdd:cd18578 294 APDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
218-469 |
1.86e-33 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 131.09 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 218 LSFFTVALLIGCAANFGRFILLRIlSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGV 297
Cdd:cd18564 58 AALVGIALLRGLASYAGTYLTALV-GQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 298 KALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNEL 377
Cdd:cd18564 137 TNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 378 SRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYteytgnavfgLSTFYSE 457
Cdd:cd18564 217 RRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY----------LKNLYKP 286
|
250
....*....|..
gi 1370557 458 IMQGAGAASRLF 469
Cdd:cd18564 287 VRDLAKLTGRIA 298
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
181-467 |
3.12e-33 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 129.77 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 181 MSIPKVIGIVLDTLKTSSGSDFFdlKIPIFSLPLYEFLSfftvALLIGCAANFGRFILLRIlservVARLRANVIKKTLH 260
Cdd:cd18590 13 TFIPYYTGRVIDILGGEYQHNAF--TSAIGLMCLFSLGS----SLSAGLRGGLFMCTLSRL-----NLRLRHQLFSSLVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 261 QDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALI--CGVVGVgmMCSLSPQLSILLLFFTPPVLFSASVFGKQ 338
Cdd:cd18590 82 QDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVktLGMLGF--MLSLSWQLTLLTLIEMPLTAIAQKVYNTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 339 IRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLA 418
Cdd:cd18590 160 HQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1370557 419 YGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASR 467
Cdd:cd18590 240 CGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAK 288
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
493-709 |
4.68e-33 |
|
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: 126.88 E-value: 4.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDI--SKLNCKS 566
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKST----LLRCINlleePDSGTIIIDGLKLtdDKKNINE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQE----PVLmsgTIRDNITYGLTYTP--TKEEIRSVAKQCF----CHNFITKFPNTydtvigphgtlLSGG 636
Cdd:cd03262 74 LRQKVGMVFQQfnlfPHL---TVLENITLAPIKVKgmSKAEAEERALELLekvgLADKADAYPAQ-----------LSGG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 637 QKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsMTIVSIAHRLSTIRRSENVIVLGHDG 709
Cdd:cd03262 140 QQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
492-719 |
5.56e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.51 E-value: 5.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTI--ALL-LLRyynPTTGTITIDNQDISKLnckslR 568
Cdd:COG1121 6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLlkAILgLLP---PTSGTVRLFGKPPRRA-----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIV-QQEP-----------VLMSGTIRDNityGLTYTPTKEEiRSVAKQCFchnfitkfpntyDTV---------IG 627
Cdd:COG1121 75 RRIGYVpQRAEvdwdfpitvrdVVLMGRYGRR---GLFRRPSRAD-REAVDEAL------------ERVgledladrpIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 628 phgtLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLmKSKSMTIVSIAHRLSTIRR-SENVIVLg 706
Cdd:COG1121 139 ----ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREyFDRVLLL- 212
|
250
....*....|...
gi 1370557 707 hDGSVVEMGKFKE 719
Cdd:COG1121 213 -NRGLVAHGPPEE 224
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
183-467 |
8.45e-33 |
|
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: 128.81 E-value: 8.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 183 IPKVIGIVLDTLKTSSGSdffdlKIPIFSLPLYEFLSFFTVALLigcaaNFGRFILLRILSERVVARLRANVIKKTLHQD 262
Cdd:cd18778 18 PPWLIRELVDLVTIGSKS-----LGLLLGLALLLLGAYLLRALL-----NFLRIYLNHVAEQKVVADLRSDLYDKLQRLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 263 AEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNT 342
Cdd:cd18778 88 LRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 343 SKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSY 422
Cdd:cd18778 168 YRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGR 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1370557 423 LVLQSQLSIGDLTAFMLYteytgnavfgLSTFY---------SEIMQGAGAASR 467
Cdd:cd18778 248 LVLAGELTIGDLVAFLLY----------LGLFYepitslhglNEMLQRALAGAE 291
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
493-711 |
2.03e-32 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 123.66 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlNCKSLRRHIG 572
Cdd:cd03230 1 IEVRNLSKRYGKKTAL---DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSG-TIRDNITYgltytptkeeirsvakqcfchnfitkfpntydtvigphgtllSGGQKQRIAIARALIKKP 651
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL------------------------------------------SGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370557 652 TILILDEATSALDVESEgainYTFGQLMKS---KSMTIVSIAHRLSTI-RRSENVIVLgHDGSV 711
Cdd:cd03230 115 ELLILDEPTSGLDPESR----REFWELLRElkkEGKTILLSSHILEEAeRLCDRVAIL-NNGRI 173
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
491-732 |
7.57e-32 |
|
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: 125.02 E-value: 7.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 491 GVIEFKDVSFSYPT--RPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLR 568
Cdd:cd03288 18 GEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIVQQEPVLMSGTIRDNITYGLTYT-PTKEEIRSVAKqcfCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARAL 647
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECKCTdDRLWEALEIAQ---LKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 648 IKKPTILILDEATSALDVESEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLGhDGSVVEMGKFKELYANPTSA 727
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILDADLVLVLS-RGILVECDTPENLLAQEDGV 248
|
....*
gi 1370557 728 LSQLL 732
Cdd:cd03288 249 FASLV 253
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-441 |
1.20e-31 |
|
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: 125.31 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 179 IGMSIPKVIGIVLD-TLKTSSGSDFFDLkipifslpLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKK 257
Cdd:cd18563 14 LGLVPPYLTKILIDdVLIQLGPGGNTSL--------LLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 258 TLHQDAEFFDNHKVGDLISRLGSDayvvSRSMTQKVSDGVKALICGV---VGVG-MMCSLSPQLSILLLFFTPPVLFSAS 333
Cdd:cd18563 86 LQRLSLSFFDKRQTGSLMSRVTSD----TDRLQDFLSDGLPDFLTNIlmiIGIGvVLFSLNWKLALLVLIPVPLVVWGSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 334 VFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSF 413
Cdd:cd18563 162 FFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGT 241
|
250 260
....*....|....*....|....*...
gi 1370557 414 LTVLAYGSYLVLQSQLSIGDLTAFMLYT 441
Cdd:cd18563 242 LIVWYFGGRQVLSGTMTLGTLVAFLSYL 269
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
492-712 |
1.21e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.01 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRpsVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDISKLNCKSL 567
Cdd:COG3638 2 MLELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKST----LLRCLNglvePTSGEILVDGQDVTALRGRAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 ---RRHIGIVQQEP-----------VLMS-----GTIRdnityGLTYTPTKEEIRsVAKQCFchnfitkfpntyDTV-IG 627
Cdd:COG3638 76 rrlRRRIGMIFQQFnlvprlsvltnVLAGrlgrtSTWR-----SLLGLFPPEDRE-RALEAL------------ERVgLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 628 PH-----GTLlSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SEN 701
Cdd:COG3638 138 DKayqraDQL-SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADR 216
|
250
....*....|.
gi 1370557 702 VIVLgHDGSVV 712
Cdd:COG3638 217 IIGL-RDGRVV 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
512-726 |
1.27e-31 |
|
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: 123.60 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 512 KNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKslRRHIGIVQQEPVLMSG-TIRDNIT 590
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 591 YGLTY-TPTKEEIRSVAKQcfchnfITKFPNTyDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEG 669
Cdd:cd03299 94 YGLKKrKVDKKEIERKVLE------IAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 670 AINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANPTS 726
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
184-441 |
1.67e-31 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 125.37 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 184 PKVIGIVLDTLKTSSGS-DFFDLKIPIFSLPLYEFLsfFTVALLIGCAA-----NFGRFILLRILSERVVARLRANVIKK 257
Cdd:cd18565 19 PLLIGVAIDAVFNGEASfLPLVPASLGPADPRGQLW--LLGGLTVAAFLleslfQYLSGVLWRRFAQRVQHDLRTDTYDH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 258 TLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGK 337
Cdd:cd18565 97 VQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 338 QIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVL 417
Cdd:cd18565 177 RIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATF 256
|
250 260 270
....*....|....*....|....*....|
gi 1370557 418 AYGSYLVLQ------SQLSIGDLTAFMLYT 441
Cdd:cd18565 257 VVGGYWVLDgpplftGTLTVGTLVTFLFYT 286
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
493-724 |
4.40e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 4.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKST----IALLLlryyNPTTGTITIDNQDISKLNCKslR 568
Cdd:COG3839 4 LELENVSKSYGGVEAL---KDIDLDIEDGEFLVLLGPSGCGKSTllrmIAGLE----DPTSGEILIGGRDVTDLPPK--D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIVQQEPVL---MsgTIRDNITYGLTY--TPtKEEI----RSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQ 639
Cdd:COG3839 75 RNIAMVFQSYALyphM--TVYENIAFPLKLrkVP-KAEIdrrvREAAELLGLEDLLDRKPKQ-----------LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 640 RIAIARALIKKPTILILDEATSALD----VESEGAINytfgQLMKSKSMTIV----------SIAHRlstirrsenVIVL 705
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIK----RLHRRLGTTTIyvthdqveamTLADR---------IAVM 207
|
250
....*....|....*....
gi 1370557 706 gHDGSVVEMGKFKELYANP 724
Cdd:COG3839 208 -NDGRIQQVGTPEELYDRP 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
493-707 |
8.85e-31 |
|
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: 120.21 E-value: 8.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS---LRR 569
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 570 HIGIVQQEPVLMSG-TIRDNITYGL--TYTPTKEEIRSVA---KQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAI 643
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALevTGVPPREIRKRVPaalELVGLSHKHRALPAE-----------LSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 644 ARALIKKPTILILDEATSALDVESEGAINYTFGQLMKsKSMTIVSIAHRLSTIRR-SENVIVLGH 707
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTtRHRVIALER 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
493-722 |
2.38e-30 |
|
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: 119.98 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDISKLNCKSL- 567
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKST----LLRCLNglvePTSGSVLIDGTDINKLKGKALr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 --RRHIGIVQQEPVLMSG-TIRDNITYG-LTYTPT---------KEEIRsVAKQCFCH-NFITKFPNTYDTvigphgtlL 633
Cdd:cd03256 75 qlRRQIGMIFQQFNLIERlSVLENVLSGrLGRRSTwrslfglfpKEEKQ-RALAALERvGLLDKAYQRADQ--------L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 634 SGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVE 713
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVF 225
|
....*....
gi 1370557 714 MGKFKELYA 722
Cdd:cd03256 226 DGPPAELTD 234
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
214-466 |
4.08e-30 |
|
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: 121.04 E-value: 4.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 214 LYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDayvVSrSMTQKV 293
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVIND---VN-SLSDLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 294 SDGVKALICGVVG----VGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQS 369
Cdd:cd18545 115 SNGLINLIPDLLTlvgiVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 370 FVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVF 449
Cdd:cd18545 195 FAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIR 274
|
250
....*....|....*..
gi 1370557 450 GLSTFYSEiMQGAGAAS 466
Cdd:cd18545 275 NLSNFYNQ-LQSAMASA 290
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
492-722 |
7.73e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.84 E-value: 7.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHI 571
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEP--VLMSGTIRDNITYGL-----TYTPTKEEIRSVAKQCFCHNFITKFPntydtvigphgTLLSGGQKQRIAIA 644
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGLenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 645 RALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVM-KNGQVESTSTPRELFS 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
494-705 |
1.16e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 117.25 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 494 EFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTI--ALL-LLRyynPTTGTITIDNQDISKLnckslRRH 570
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLlkAILgLLK---PTSGSIRVFGKPLEKE-----RKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQ-------------EPVLMSGTIRdnitYGLTYTPTKEEIRSV------------AKQCFchnfitkfpntydtv 625
Cdd:cd03235 70 IGYVPQrrsidrdfpisvrDVVLMGLYGH----KGLFRRLSKADKAKVdealervglselADRQI--------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 626 igphgTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLmKSKSMTIVSIAHRLSTIRRSENVIVL 705
Cdd:cd03235 131 -----GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLL 204
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
493-733 |
2.35e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 117.04 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDIS---KLNCK 565
Cdd:COG4161 3 IQLKNINCFYG---SHQALFDINLECPSGETLVLLGPSGAGKSS----LLRVLNlletPDSGQLNIAGHQFDfsqKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 566 ---SLRRHIGIVQQE----PVLmsgTIRDNitygLTYTP------TKEEIRSVAKQCFCH----NFITKFPNtydtvigp 628
Cdd:COG4161 76 airLLRQKVGMVFQQynlwPHL---TVMEN----LIEAPckvlglSKEQAREKAMKLLARlrltDKADRFPL-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 629 hgtLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLmKSKSMTIVSIAHRLSTIRRSENVIVLGHD 708
Cdd:COG4161 141 ---HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEK 216
|
250 260
....*....|....*....|....*.
gi 1370557 709 GSVVEMGKfKELYANP-TSALSQLLN 733
Cdd:COG4161 217 GRIIEQGD-ASHFTQPqTEAFAHYLS 241
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
241-441 |
2.71e-29 |
|
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: 118.71 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 241 ILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDayvvSRSMTQKVSDGVKAL-ICGVVGVG---MMCSLSPQ 316
Cdd:cd18549 68 VMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITND----LFDISELAHHGPEDLfISIITIIGsfiILLTINVP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 317 LSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDiFQVGKTAAF 396
Cdd:cd18549 144 LTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR-FLESKKKAY 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1370557 397 TN-AKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYT 441
Cdd:cd18549 223 KAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYV 268
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
493-732 |
3.37e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.39 E-value: 3.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPsvqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNckSLRRHIG 572
Cdd:COG3840 2 LRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP--PAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQE----PVLmsgTIRDNITYGLT----YTPT-KEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAI 643
Cdd:COG3840 75 MLFQEnnlfPHL---TVAQNIGLGLRpglkLTAEqRAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 644 ARALIKKPTILILDEATSALD----------VEsegainytfgQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVE 713
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrqemldlVD----------ELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
250 260
....*....|....*....|
gi 1370557 714 MGKFKELYA-NPTSALSQLL 732
Cdd:COG3840 211 DGPTAALLDgEPPPALAAYL 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
515-752 |
3.72e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 119.04 E-value: 3.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 515 NFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL---RRHIGIVQQEPvLMS----GTIRD 587
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP-LASlnprMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 588 NITYGL-TYTP--TKEEIRS-----VAKQCFCHNFITKFPNTYdtvigphgtllSGGQKQRIAIARALIKKPTILILDEA 659
Cdd:PRK15079 120 IIAEPLrTYHPklSRQEVKDrvkamMLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 660 TSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIV--LGHdgsVVEMGKFKELYANPTSALSQLLnEKA 736
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVmyLGH---AVELGTYDEVYHNPLHPYTKAL-MSA 264
|
250
....*....|....*.
gi 1370557 737 APGPsDQQLQIEKVIE 752
Cdd:PRK15079 265 VPIP-DPDLERNKTIQ 279
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
493-710 |
9.74e-29 |
|
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: 113.02 E-value: 9.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPT-RPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTiallLLR-------YYnptTGTITidnqdisklnc 564
Cdd:cd03223 1 IELENLSLATPDgRVLL---KDLSFEIKPGDRLLITGPSGTGKSS----LFRalaglwpWG---SGRIG----------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 565 KSLRRHIGIVQQEPVLMSGTIRDNITYgltytptkeeirsvakqcfchnfitkfpntydtvigPHGTLLSGGQKQRIAIA 644
Cdd:cd03223 60 MPEGEDLLFLPQRPYLPLGTLREQLIY------------------------------------PWDDVLSGGEQQRLAFA 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 645 RALIKKPTILILDEATSALDVESEGAInYtfgQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGS 710
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEDRL-Y---QLLKELGITVISVGHRPSLWKFHDRVLDLDGEGG 165
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
493-726 |
1.92e-28 |
|
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: 114.26 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLncKSLRRHIG 572
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSG-TIRDNITYGLTYTPT-KEEIRSVAKQCF----CHNFITKFPNTydtvigphgtlLSGGQKQRIAIARA 646
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGLRLKKLpKAEIKERVAEALdlvqLEGYANRKPSQ-----------LSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANPTS 726
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
490-730 |
2.06e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.62 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 490 RGVIEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLR----YYNP-TTGTITIDNQDISKLNC 564
Cdd:PRK14247 1 MNKIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEArVSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 565 KSLRRHIGIVQQEP-VLMSGTIRDNITYGLTYT---PTKEEIRSVAKQCFCHNFItkFPNTYDTVIGPHGTLlSGGQKQR 640
Cdd:PRK14247 78 IELRRRVQMVFQIPnPIPNLSIFENVALGLKLNrlvKSKKELQERVRWALEKAQL--WDEVKDRLDAPAGKL-SGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 641 IAIARALIKKPTILILDEATSALDVESEGAINYTFGQLmkSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKEL 720
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
250
....*....|
gi 1370557 721 YANPTSALSQ 730
Cdd:PRK14247 233 FTNPRHELTE 242
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
493-725 |
2.27e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.89 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSY-PTRPSVQI-FKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDIS----KL 562
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERRaLYDVNVSIPSGSYVAIIGHTGSGKST----LLQHLNgllqPTSGTVTIGERVITagkkNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 563 NCKSLRRHIGIVQQ--EPVLMSGTIRDNITYG-LTYTPTKEEIRSVAKQC-----FCHNFITKFPntYDtvigphgtlLS 634
Cdd:PRK13634 79 KLKPLRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEEDAKQKAREMielvgLPEELLARSP--FE---------LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 635 GGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVE 713
Cdd:PRK13634 148 GGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVM-HKGTVFL 226
|
250
....*....|..
gi 1370557 714 MGKFKELYANPT 725
Cdd:PRK13634 227 QGTPREIFADPD 238
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
492-724 |
4.56e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 116.97 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKslRRHI 571
Cdd:PRK09452 14 LVELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVL---MsgTIRDNITYGLTY--TPtKEEIRSVAKQCF----CHNFITKFPntydtvigphgTLLSGGQKQRIA 642
Cdd:PRK09452 89 NTVFQSYALfphM--TVFENVAFGLRMqkTP-AAEITPRVMEALrmvqLEEFAQRKP-----------HQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 643 IARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAH-RLSTIRRSENVIVLgHDGSVVEMGKFKELY 721
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVM-RDGRIEQDGTPREIY 233
|
...
gi 1370557 722 ANP 724
Cdd:PRK09452 234 EEP 236
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
217-468 |
9.45e-28 |
|
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: 113.72 E-value: 9.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 217 FLSFFTVALLIGCAANFGRFI---LLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKV 293
Cdd:cd18589 35 FTAAITVMSLLTIASAVSEFVcdlIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 294 SDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAE 373
Cdd:cd18589 115 SLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 374 GNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLST 453
Cdd:cd18589 195 EGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLS 274
|
250
....*....|....*
gi 1370557 454 FYSEIMQGAGAASRL 468
Cdd:cd18589 275 YYPSVMKAVGSSEKI 289
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
479-741 |
1.62e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 120.27 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 479 SPTVGHKYKPDRGVIEFKDVSFSYptRPSVQ-IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQ 557
Cdd:PTZ00243 1295 SPTSAAPHPVQAGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGR 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 558 DISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPtkEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQ 637
Cdd:PTZ00243 1373 EIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQ 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 638 KQRIAIARALIKKPTILIL-DEATSALDVESEGAINYTfgqLMKSKS-MTIVSIAHRLSTIRRSENVIVLGHdGSVVEMG 715
Cdd:PTZ00243 1451 RQLMCMARALLKKGSGFILmDEATANIDPALDRQIQAT---VMSAFSaYTVITIAHRLHTVAQYDKIIVMDH-GAVAEMG 1526
|
250 260
....*....|....*....|....*.
gi 1370557 716 KFKELYANPTSALSQLLNekaAPGPS 741
Cdd:PTZ00243 1527 SPRELVMNRQSIFHSMVE---ALGRS 1549
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
510-730 |
1.78e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.06 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQ------DISKLNCKSLRRHIGIVQQEPVLMSG 583
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 584 -TIRDNITYGLTYTPTKE--EIRSVAKQCFchNFITKFPNTYDTVIGPhGTLLSGGQKQRIAIARALIKKPTILILDEAT 660
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEkrEIKKIVEECL--RKVGLWKEVYDRLNSP-ASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 661 SALDVESEGAINYTFGQLmkSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANPTSALSQ 730
Cdd:PRK14246 182 SMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
516-728 |
2.07e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.91 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 516 FKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDI---SKLNCKSLRRHIGIVQQEP---------VlmsG 583
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPygslnprkkV---G 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 584 TIRDN---ITYGLTYTPTKEEIRSVAKQcfchnfITKFPNTYDTVigPHgtLLSGGQKQRIAIARALIKKPTILILDEAT 660
Cdd:PRK11308 113 QILEEpllINTSLSAAERREKALAMMAK------VGLRPEHYDRY--PH--MFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 661 SALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKFKELYANP----TSAL 728
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVM-YLGRCVEKGTKEQIFNNPrhpyTQAL 254
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
213-468 |
2.34e-27 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 112.97 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 213 PLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQK 292
Cdd:cd18546 37 VLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 293 VSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVA 372
Cdd:cd18546 117 LVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 373 EGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTeytgNAVFG-- 450
Cdd:cd18546 197 ERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYL----RRFFApi 272
|
250 260
....*....|....*....|
gi 1370557 451 --LSTFYSEIMQGAGAASRL 468
Cdd:cd18546 273 qqLSQVFDSYQQARAALEKI 292
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
510-732 |
2.54e-27 |
|
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: 119.63 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTItidnqdisklnckslrRHIGIVQ---QEPVLMSGTIR 586
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------------KHSGRISfspQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 587 DNITYGLTYTPTKeeIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVE 666
Cdd:TIGR01271 505 DNIIFGLSYDEYR--YTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 667 SEGAI-NYTFGQLMKSKSMTIVSiaHRLSTIRRSENVIVLgHDGSVVEMGKFKELYANPTSALSQLL 732
Cdd:TIGR01271 583 TEKEIfESCLCKLMSNKTRILVT--SKLEHLKKADKILLL-HEGVCYFYGTFSELQAKRPDFSSLLL 646
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
493-727 |
2.88e-27 |
|
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: 110.89 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVQifkNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKslRRHIG 572
Cdd:cd03296 3 IEVRNVSKRFGDFVALD---DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSG-TIRDNITYGL-----TYTPTKEEIRSVAKQCFCHNFITKFPNTYdtvigPHGtlLSGGQKQRIAIARA 646
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLrvkprSERPPEAEIRAKVHELLKLVQLDWLADRY-----PAQ--LSGGQRQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANPTS 726
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
.
gi 1370557 727 A 727
Cdd:cd03296 231 P 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
492-724 |
3.02e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.09 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDIsKLNCKSL---R 568
Cdd:PRK13639 1 ILETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIVQQEP--VLMSGTIRDNITYG-LTYTPTKEEIRSVAKQCFCHNFITKFPNTydtviGPHGtlLSGGQKQRIAIAR 645
Cdd:PRK13639 78 KTVGIVFQNPddQLFAPTVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFENK-----PPHH--LSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 646 ALIKKPTILILDEATSALDVESEGAINYTFGQLMKsKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANP 724
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
492-726 |
3.21e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.95 E-value: 3.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTrpsVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYNP----TTGTITIDNQDI--SKLNCK 565
Cdd:PRK09493 1 MIEFKNVSKHFGP---TQVLHNIDLNIDQGEVVVIIGPSGSGKST----LLRCINKleeiTSGDLIVDGLKVndPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 566 SLRRHIGIV-QQEPVLMSGTIRDNITYGLTYT--PTKEEIRSVAKQCFCHNFITKFPNTYDTVigphgtlLSGGQKQRIA 642
Cdd:PRK09493 74 LIRQEAGMVfQQFYLFPHLTALENVMFGPLRVrgASKEEAEKQARELLAKVGLAERAHHYPSE-------LSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 643 IARALIKKPTILILDEATSALDVEsegaINYTFGQLMKS---KSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKE 719
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPE----LRHEVLKVMQDlaeEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
....*..
gi 1370557 720 LYANPTS 726
Cdd:PRK09493 223 LIKNPPS 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
493-727 |
4.53e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.32 E-value: 4.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKST----IALLLlryyNPTTGTITIDNQDIsKLNCKSLR 568
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTllriIAGLE----TPDSGRIVLNGRDL-FTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIVQQEPVL---MsgTIRDNITYGLTY-TPTKEEIRSVAK------QcfchnfITKFPNTYdtvigPHGtlLSGGQK 638
Cdd:COG1118 75 RRVGFVFQHYALfphM--TVAENIAFGLRVrPPSKAEIRARVEellelvQ------LEGLADRY-----PSQ--LSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 639 QRIAIARALIKKPTILILDEATSALDVesegainYTFGQLMKS-----KSMTIVSI--------AHRLstirrSENVIVL 705
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDA-------KVRKELRRWlrrlhDELGGTTVfvthdqeeALEL-----ADRVVVM 207
|
250 260
....*....|....*....|..
gi 1370557 706 gHDGSVVEMGKFKELYANPTSA 727
Cdd:COG1118 208 -NQGRIEQVGTPDEVYDRPATP 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
214-747 |
6.55e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 118.15 E-value: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 214 LYEFLSFFTVALLIGCAANFGRFILlrilseRVVARLR----ANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVsrsm 289
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESQYFQNVG------RVGFRLRstlvAAIFHKSLRLTHEARKNFASGKVTNMITTDANAL---- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 290 tQKVSDGVKALICGVVGVGM-MCSLSPQLSI------LLLFFTPPvlFSASVFGKQIRNTSKDLQEaTGQLTRVAEEQLS 362
Cdd:PLN03232 412 -QQIAEQLHGLWSAPFRIIVsMVLLYQQLGVaslfgsLILFLLIP--LQTLIVRKMRKLTKEGLQW-TDKRVGIINEILA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 363 GIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAkfFTTTSLLGDLSFLTVLAYGSYLVLQsqlsiGDLTAFMLYTE 442
Cdd:PLN03232 488 SMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSA--FNSFILNSIPVVVTLVSFGVFVLLG-----GDLTPARAFTS 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 443 YTGNAV--FGLSTFYSEIMQGAGA---ASRLFEL---TDRKPSISPTVghkyKPDRGVIEFKDVSFSYPTRPSVQIFKNL 514
Cdd:PLN03232 561 LSLFAVlrSPLNMLPNLLSQVVNAnvsLQRIEELllsEERILAQNPPL----QPGAPAISIKNGYFSWDSKTSKPTLSDI 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 515 NFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTitidnqdisklnCKSLRRHIGIVQQEPVLMSGTIRDNITYGLT 594
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS------------SVVIRGSVAYVPQVSWIFNATVRENILFGSD 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 595 YTPTK--EEIRSVAKQcfcHNfITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVEsegAIN 672
Cdd:PLN03232 705 FESERywRAIDVTALQ---HD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH---VAH 777
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 673 YTFGQLMKS--KSMTIVSIAHRLSTIRRSENVIVLGhDGSVVEMGKFKELYANptSALSQLLNEKAapGPSDQQLQI 747
Cdd:PLN03232 778 QVFDSCMKDelKGKTRVLVTNQLHFLPLMDRIILVS-EGMIKEEGTFAELSKS--GSLFKKLMENA--GKMDATQEV 849
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
492-722 |
7.21e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.95 E-value: 7.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHI 571
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEP--VLMSGTIRDNITYGLTYT--PTKEEIRSVAKQCFCHN---FITKFPntydtvigphgTLLSGGQKQRIAIA 644
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQgiPREEMIKRVDEALLAVNmldFKTREP-----------ARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 645 RALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVM-KAGEIIKEAAPSELFA 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
498-720 |
7.75e-27 |
|
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: 111.10 E-value: 7.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 498 VSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTItidnqdisklnckslrRHIGIVQ-- 575
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------------KHSGRISfs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 576 -QEPVLMSGTIRDNITYGLTYTPTKeeIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTIL 654
Cdd:cd03291 104 sQFSWIMPGTIKENIIFGVSYDEYR--YKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 655 ILDEATSALDVESEGAI-NYTFGQLMKSKSMTIVSiaHRLSTIRRSENVIVLgHDGSVVEMGKFKEL 720
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVT--SKMEHLKKADKILIL-HEGSSYFYGTFSEL 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
492-720 |
8.22e-27 |
|
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: 110.17 E-value: 8.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTG-TITIDNQDISKLNCKSLRRH 570
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQEpvlMSGTIRDNIT------------YGLTYTPTKEEIR------------SVAKQCFCHnfitkfpntydtvi 626
Cdd:COG1119 80 IGLVSPA---LQLRFPRDETvldvvlsgffdsIGLYREPTDEQRErarellellglaHLADRPFGT-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 627 gphgtlLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLG 706
Cdd:COG1119 143 ------LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL 216
|
250
....*....|....
gi 1370557 707 HDGSVVEMGKFKEL 720
Cdd:COG1119 217 KDGRVVAAGPKEEV 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
513-726 |
8.84e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 112.51 E-value: 8.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 513 NLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlncKSLR-RHIGIVQQEPVL---MSgtIRDN 588
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQqRDICMVFQSYALfphMS--LGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 589 ITYGLTYTP-TKEEIRSVAKQCFCHNFITKFPNTYDTVIgphgtllSGGQKQRIAIARALIKKPTILILDEATSALDVES 667
Cdd:PRK11432 99 VGYGLKMLGvPKEERKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 668 EGAINYTFGQLMKSKSMTIVSIAHRLS-TIRRSENVIVLgHDGSVVEMGKFKELYANPTS 726
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVTHDQSeAFAVSDTVIVM-NKGKIMQIGSPQELYRQPAS 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
509-735 |
9.43e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.84 E-value: 9.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 509 QIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDI--------SKLNCKSLRRHIGIVQQ 576
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTT----LLRCINlleqPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 577 EPVLMSG-TIRDNITYG--LTYTPTKEEIRSVAKQCFCHNFITKFPNTYdtvigPHgtLLSGGQKQRIAIARALIKKPTI 653
Cdd:PRK11264 93 NFNLFPHrTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSY-----PR--RLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 654 LILDEATSALDVESEGAINYTFGQLMKSKSmTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANPTSALSQLLN 733
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
..
gi 1370557 734 EK 735
Cdd:PRK11264 245 EK 246
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
512-723 |
5.34e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.60 E-value: 5.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 512 KNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDIS--KLNCKSLRRHIGIVQQEP--VLMSG 583
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKST----LIQHLNgllkPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 584 TIRDNITYGLT-YTPTKEEIrsvakqcfcHNFITKFPNT----YDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDE 658
Cdd:PRK13637 100 TIEKDIAFGPInLGLSEEEI---------ENRVKRAMNIvgldYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 659 ATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYAN 723
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
493-732 |
1.55e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 106.85 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTR------PSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS 566
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEPvlmSGTIRDNITYG------------LTYTPTKEEIRSVAKQcfchnfITKFPNTYDtvIGPHgtLLS 634
Cdd:COG4167 85 RCKHIRMIFQDP---NTSLNPRLNIGqileeplrlntdLTAEEREERIFATLRL------VGLLPEHAN--FYPH--MLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 635 GGQKQRIAIARALIKKPTILILDEATSALD--VESEgAINYTFgQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSV 711
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDmsVRSQ-IINLML-ELQEKLGISYIYVSQHLGIVKHiSDKVLVM-HQGEV 228
|
250 260
....*....|....*....|.
gi 1370557 712 VEMGKFKELYANPTSALSQLL 732
Cdd:COG4167 229 VEYGKTAEVFANPQHEVTKRL 249
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
493-733 |
2.21e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 105.48 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQ--DISK-LNCK 565
Cdd:PRK11124 3 IQLNGINCFYG---AHQALFDITLDCPQGETLVLLGPSGAGKSS----LLRVLNllemPRSGTLNIAGNhfDFSKtPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 566 ---SLRRHIGIVQQE----PVLmsgTIRDNIT------YGLTYTPTKEEIRSVAKQCFCHNFITKFPntydtvigPHgtl 632
Cdd:PRK11124 76 airELRRNVGMVFQQynlwPHL---TVQQNLIeapcrvLGLSKDQALARAEKLLERLRLKPYADRFP--------LH--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKsMTIVSIAHRLSTIRRSENVIVLGHDGSVV 712
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
250 260
....*....|....*....|..
gi 1370557 713 EMGKfKELYANP-TSALSQLLN 733
Cdd:PRK11124 221 EQGD-ASCFTQPqTEAFKNYLS 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
492-732 |
3.30e-25 |
|
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: 110.54 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPT-RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRY--YNP--TTGTITIDNQDISKLNCKS 566
Cdd:COG4172 6 LLSVEDLSVAFGQgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpDPAahPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRR----HIGIVQQEPvlMSG-----TIRDNITYGLT--YTPTKEEIRSVAKQCFCHnfiTKFP------NTYdtvigPH 629
Cdd:COG4172 86 LRRirgnRIAMIFQEP--MTSlnplhTIGKQIAEVLRlhRGLSGAAARARALELLER---VGIPdperrlDAY-----PH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 630 gtLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHD 708
Cdd:COG4172 156 --QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVM-RQ 232
|
250 260
....*....|....*....|....
gi 1370557 709 GSVVEMGKFKELYANPTSALSQLL 732
Cdd:COG4172 233 GEIVEQGPTAELFAAPQHPYTRKL 256
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
487-705 |
5.58e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.03 E-value: 5.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 487 KPDRGVIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS 566
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTKEEIRSVAKqcfchnFITKFpNTYDTVIGPHGTLLSGGQKQRIAIARA 646
Cdd:PRK10247 79 YRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLD------DLERF-ALPDTILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVL 705
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
492-732 |
6.03e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.79 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPSV--------QIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNpTTGTITIDNQDISKLN 563
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 564 CKSL---RRHIGIVQQEPVlMSGTIRDN----ITYGL-----TYTPTKEEIRSVAKQCFC-------HNFITKFpntydt 624
Cdd:PRK15134 354 RRQLlpvRHRIQVVFQDPN-SSLNPRLNvlqiIEEGLrvhqpTLSAAQREQQVIAVMEEVgldpetrHRYPAEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 625 vigphgtllSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVI 703
Cdd:PRK15134 427 ---------SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRAlCHQVI 497
|
250 260
....*....|....*....|....*....
gi 1370557 704 VLGHdGSVVEMGKFKELYANPTSALSQLL 732
Cdd:PRK15134 498 VLRQ-GEVVEQGDCERVFAAPQQEYTRQL 525
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
504-664 |
7.85e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.95 E-value: 7.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 504 TRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNP---TTGTITIDNQDISKLNckSLRRHIGIVQQEPVL 580
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP--AEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 581 ---MSgtIRDNITYGLTYTPTKEEIRSVAKQCF----CHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKKPTI 653
Cdd:COG4136 88 fphLS--VGENLAFALPPTIGRAQRRARVEQALeeagLAGFADRDPAT-----------LSGGQRARVALLRALLAEPRA 154
|
170
....*....|.
gi 1370557 654 LILDEATSALD 664
Cdd:COG4136 155 LLLDEPFSKLD 165
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
492-724 |
8.44e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.47 E-value: 8.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRY--YNP---TTGTITIDNQDI--SKLNC 564
Cdd:PRK14239 5 ILQVSDLSVYYNKKKAL---NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 565 KSLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTK------EEIRSVAKQCFCHNFITKfpNTYDTVIGphgtlLSGGQK 638
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKdkqvldEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 639 QRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSiaHRLSTIRRSENVIVLGHDGSVVEMGKFK 718
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT--RSMQQASRISDRTGFFLDGDLIEYNDTK 232
|
....*.
gi 1370557 719 ELYANP 724
Cdd:PRK14239 233 QMFMNP 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
492-723 |
1.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.78 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPSVQ---IFKNLNFKIAPGSSVCIVGPSGRGKSTIA-----LLLlryynPTTGTITIDNQDISKL- 562
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAkhmnaLLI-----PSEGKVYVDGLDTSDEe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 563 NCKSLRRHIGIVQQEP--VLMSGTIRDNITYG---LTYTPtkEEIRSVAKQCFchnfitKFPNTYD-TVIGPHgtLLSGG 636
Cdd:PRK13633 79 NLWDIRNKAGMVFQNPdnQIVATIVEEDVAFGpenLGIPP--EEIRERVDESL------KKVGMYEyRRHAPH--LLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 637 QKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGK 716
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVM-DSGKVVMEGT 227
|
....*..
gi 1370557 717 FKELYAN 723
Cdd:PRK13633 228 PKEIFKE 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
413-759 |
1.74e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 110.60 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 413 FLTVLAYGSYLVLQsqlsiGDLTAFMLYTEYTGNAV--FGLSTFYSEIMQGAGAA---SRLFEL---TDRKPSISPTVgh 484
Cdd:PLN03130 536 LVTVVSFGVFTLLG-----GDLTPARAFTSLSLFAVlrFPLFMLPNLITQAVNANvslKRLEELllaEERVLLPNPPL-- 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 485 kyKPDRGVIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIdnqdisklnc 564
Cdd:PLN03130 609 --EPGLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------- 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 565 ksLRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTKEE--IRSVAKQcfcHNfITKFPNTYDTVIGPHGTLLSGGQKQRIA 642
Cdd:PLN03130 677 --IRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYEraIDVTALQ---HD-LDLLPGGDLTEIGERGVNISGGQKQRVS 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 643 IARALIKKPTILILDEATSALD--VESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRsenvIVLGHDGSVVEMGKFKEL 720
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDahVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDR----IILVHEGMIKEEGTYEEL 826
|
330 340 350
....*....|....*....|....*....|....*....
gi 1370557 721 YANptSALSQLLNEKAapGPSDQQLQIEKVIEKEDLNES 759
Cdd:PLN03130 827 SNN--GPLFQKLMENA--GKMEEYVEENGEEEDDQTSSK 861
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
507-715 |
1.75e-24 |
|
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: 102.37 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 507 SVQIFKNL---NFKIA---PGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQ---DISK-LNCKSLRRHIGIVQQ 576
Cdd:cd03297 3 CVDIEKRLpdfTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 577 EPVLMSG-TIRDNITYGLTYTPTKEEIRSVAKQCFCHNfITKFPNTYdtvigPHGtlLSGGQKQRIAIARALIKKPTILI 655
Cdd:cd03297 83 QYALFPHlNVRENLAFGLKRKRNREDRISVDELLDLLG-LDHLLNRY-----PAQ--LSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 656 LDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMG 715
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
496-712 |
2.15e-24 |
|
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: 101.56 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 496 KDVSFSYptRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlncKSLRRHIGIVQ 575
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 576 QEP--VLMSGTIRDNITYGLTYTPTKEEIRSVAKQCFChnfitkfPNTYDTVigpHGTLLSGGQKQRIAIARALIKKPTI 653
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLD-------LYALKER---HPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 654 LILDEATSALDVESEGAINYTFGQLMKSKSmTIVSIAHRLSTIRRSENVIVLGHDGSVV 712
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
492-667 |
3.49e-24 |
|
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: 101.02 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLR----YYNPTTGTITIDNQDISKlNCKSL 567
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPIRD-AREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEPVLMSG-TIRDNIT-----YGLTytPTKEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRI 641
Cdd:COG4133 74 RRRLAYLGHADGLKPElTVRENLRfwaalYGLR--ADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRV 140
|
170 180
....*....|....*....|....*.
gi 1370557 642 AIARALIKKPTILILDEATSALDVES 667
Cdd:COG4133 141 ALARLLLSPAPLWLLDEPFTALDAAG 166
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
493-724 |
4.33e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.42 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYyNPTTGTITID------NQDI--SKLNC 564
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEgrveffNQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 565 KSLRRHIGIVQQEPVLMSGTIRDNITYGLT---YTPtKEEIRSVAKQCFchnfitKFPNTYDTV---IGPHGTLLSGGQK 638
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgWRP-KLEIDDIVESAL------KDADLWDEIkhkIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 639 QRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHD-----GSVVE 713
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVE 236
|
250
....*....|.
gi 1370557 714 MGKFKELYANP 724
Cdd:PRK14258 237 FGLTKKIFNSP 247
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
492-713 |
4.45e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 101.74 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKST-IALL--LLRyynPTTGTITIDNQDISKLN---- 563
Cdd:COG4181 8 IIELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTlLGLLagLDR---PTSGTVRLAGQDLFALDedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 564 CKSLRRHIGIVQQEPVLMSG-TIRDNITYGLtytptkeEIRSvAKQCFC----------------HnfitkFPNTydtvi 626
Cdd:COG4181 85 ARLRARHVGFVFQSFQLLPTlTALENVMLPL-------ELAG-RRDARArarallervglghrldH-----YPAQ----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 627 gphgtlLSGGQKQRIAIARALIKKPTILILDEATSALDvESEGA--INYTFgQLMKSKSMTIVSIAHRLSTIRRSENVIV 704
Cdd:COG4181 147 ------LSGGEQQRVALARAFATEPAILFADEPTGNLD-AATGEqiIDLLF-ELNRERGTTLVLVTHDPALAARCDRVLR 218
|
....*....
gi 1370557 705 LgHDGSVVE 713
Cdd:COG4181 219 L-RAGRLVE 226
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
226-440 |
4.74e-24 |
|
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: 103.25 E-value: 4.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 226 LIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVV 305
Cdd:cd18548 50 LLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 306 GVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIR 385
Cdd:cd18548 130 AIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKAND 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 386 DIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLY 440
Cdd:cd18548 210 DLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINY 264
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
214-468 |
5.10e-24 |
|
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: 102.91 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 214 LYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLgSDA----YVVSRSM 289
Cdd:cd18570 41 LNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDAnkirEAISSTT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 290 TQKVSDGVKALICGVVgvgmMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQS 369
Cdd:cd18570 120 ISLFLDLLMVIISGII----LFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 370 FVAEGNEL----SRYNVAIRDIFQVGKTAAFTNakffTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTG 445
Cdd:cd18570 196 LNAEEQFLkkieKKFSKLLKKSFKLGKLSNLQS----SIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFL 271
|
250 260
....*....|....*....|...
gi 1370557 446 NAVFGLSTFYSEIMQGAGAASRL 468
Cdd:cd18570 272 GPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
493-664 |
7.33e-24 |
|
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: 100.41 E-value: 7.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKslRRHIG 572
Cdd:cd03301 1 VELENVTKRFGNVTAL---DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVL---MsgTIRDNITYGLTYTPT-KEEI----RSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIA 644
Cdd:cd03301 76 MVFQNYALyphM--TVYDNIAFGLKLRKVpKDEIdervREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALG 142
|
170 180
....*....|....*....|
gi 1370557 645 RALIKKPTILILDEATSALD 664
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLD 162
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
492-724 |
1.01e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.80 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYptRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDISKLNCKSL 567
Cdd:PRK13652 3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKST----LFRHFNgilkPTSGSVLIRGEPITKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEP--VLMSGTIRDNITYGLTYTPTKEE-----IRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQR 640
Cdd:PRK13652 77 RKFVGLVFQNPddQIFSPTVEQDIAFGPINLGLDEEtvahrVSSALHMLGLEELRDRVPHH-----------LSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 641 IAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKEL 720
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
....
gi 1370557 721 YANP 724
Cdd:PRK13652 226 FLQP 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
493-712 |
1.24e-23 |
|
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: 98.27 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLN-CKSLRRHI 571
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQepvlmsgtirdnitygltytptkeeirsvakqcfchnfitkfpntydtvigphgtlLSGGQKQRIAIARALIKKP 651
Cdd:cd03216 78 AMVYQ--------------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 652 TILILDEATSALDV-ESEgainyTFGQLM---KSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVV 712
Cdd:cd03216 102 RLLILDEPTAALTPaEVE-----RLFKVIrrlRAQGVAVIFISHRLDEVFEiADRVTVL-RDGRVV 161
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
491-743 |
1.45e-23 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 101.47 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 491 GVIEFKDVSFSYpTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNpTTGTITIDNQDISKLNCKSLRRH 570
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQEPVLMSGTIRDNIT-YGltyTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIK 649
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 650 KPTILILDEATSALDVESEGAINYTFGQLMksKSMTIVSIAHRLSTIRRSENVIvlghdgsVVEMGKFKELyanptSALS 729
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAF--ADCTVILSEHRIEAMLECQRFL-------VIEENKVRQY-----DSIQ 221
|
250
....*....|....*...
gi 1370557 730 QLLNEKA----APGPSDQ 743
Cdd:cd03289 222 KLLNEKShfkqAISPSDR 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
493-737 |
4.82e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSY-PTRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDI----SKL 562
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKST----LMQHFNallkPSSGTITIAGYHItpetGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 563 NCKSLRRHIGIVQQ--EPVLMSGTIRDNITYG-LTYTPTKEEIRSVAKQcfchnFITKFpNTYDTVIGPHGTLLSGGQKQ 639
Cdd:PRK13641 79 NLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSEDEAKEKALK-----WLKKV-GLSEDLISKSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 640 RIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSkSMTIVSIAHRLSTIRR-SENVIVLGHdGSVVEMGKFK 718
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEyADDVLVLEH-GKLIKHASPK 230
|
250
....*....|....*....
gi 1370557 719 ELYANPTSALSQLLNEKAA 737
Cdd:PRK13641 231 EIFSDKEWLKKHYLDEPAT 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
492-720 |
7.58e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.17 E-value: 7.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLR----YYNPTTGTITIDNQDISKLNCK-S 566
Cdd:COG1129 4 LLEMRGISKSFG---GVKALDGVSLELRPGEVHALLGENGAGKST----LMKilsgVYQPDSGEILLDGEPVRFRSPRdA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEPVLMSG-TIRDNITygLTYTPTK------EEIRSVAKQCFchnfitkfpNTYDTVIGPHgTL---LSGG 636
Cdd:COG1129 77 QAAGIAIIHQELNLVPNlSVAENIF--LGREPRRgglidwRAMRRRARELL---------ARLGLDIDPD-TPvgdLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 637 QKQRIAIARALIKKPTILILDEATSALDvESEgaINYTFGQL--MKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVE 713
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLT-ERE--VERLFRIIrrLKAQGVAIIYISHRLDEVFEiADRVTVL-RDGRLVG 220
|
....*..
gi 1370557 714 MGKFKEL 720
Cdd:COG1129 221 TGPVAEL 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
493-715 |
7.96e-23 |
|
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: 97.18 E-value: 7.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSvqifkNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLncKSLRRHIG 572
Cdd:cd03298 1 VRLDKIRFSYGEQPM-----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA--PPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSG-TIRDNITYG----LTYTPT-KEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARA 646
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGlspgLKLTAEdRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMG 715
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFL-DNGRIAAQG 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
488-760 |
8.08e-23 |
|
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: 104.99 E-value: 8.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 488 PDRGVIEFKDVSFSYpTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNpTTGTITIDNQDISKLNCKSL 567
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEPVLMSGTIRDNITYGLTYTptKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARAL 647
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFSGTFRKNLDPYEQWS--DEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSI 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 648 IKKPTILILDEATSALDVESEGAINYTFGQLMksKSMTIVSIAHRLSTIRRSENVIvlghdgsVVEMGKFKELyanptSA 727
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF--SNCTVILSEHRVEALLECQQFL-------VIEGSSVKQY-----DS 1434
|
250 260 270
....*....|....*....|....*....|....*..
gi 1370557 728 LSQLLNE----KAAPGPSDQQlqieKVIEKEDLNESK 760
Cdd:TIGR01271 1435 IQKLLNEtslfKQAMSAADRL----KLFPLHRRNSSK 1467
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
493-715 |
8.91e-23 |
|
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: 97.26 E-value: 8.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVcIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlNCKSLRRHIG 572
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSG-TIRDNITY-----GLTYTPTKEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARA 646
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVKARVDEVLELVNLGDRAKKKIGS-----------LSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSmTIVSiAHRLSTIRRSENVIVLGHDGSVVEMG 715
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRI-VILS-THIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
492-725 |
1.71e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.14 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTIT---IDNQDISKLncKSLR 568
Cdd:PRK13644 1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKL--QGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIVQQEP--VLMSGTIRDNITYG---LTYTPTkeEIRSVAKQCFCHNFITKF----PNTydtvigphgtlLSGGQKQ 639
Cdd:PRK13644 77 KLVGIVFQNPetQFVGRTVEEDLAFGpenLCLPPI--EIRKRVDRALAEIGLEKYrhrsPKT-----------LSGGQGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 640 RIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKsKSMTIVSIAHRLSTIRRSENVIVLGHdGSVVEMGKFKE 719
Cdd:PRK13644 144 CVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDR-GKIVLEGEPEN 221
|
....*.
gi 1370557 720 LYANPT 725
Cdd:PRK13644 222 VLSDVS 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
509-733 |
1.94e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.73 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 509 QIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDIS-------------KLNCKSLRRHI 571
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKST----FLRCINflekPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVLMSG-TIRDNI------TYGLTYTPTKEE-IRSVAKQCFCHNFITKFPntydtvigphgTLLSGGQKQRIAI 643
Cdd:PRK10619 95 TMVFQHFNLWSHmTVLENVmeapiqVLGLSKQEARERaVKYLAKVGIDERAQGKYP-----------VHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 644 ARALIKKPTILILDEATSALDVESEGAINYTFGQLMKsKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYAN 723
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
250
....*....|.
gi 1370557 724 PTSA-LSQLLN 733
Cdd:PRK10619 243 PQSPrLQQFLK 253
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
515-664 |
4.13e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.80 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 515 NFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISklNCKSLRRHIGIVQQEPVLMSG-TIRDNITYG- 592
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 593 ---LTYTPT-KEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKKPTILILDEATSALD 664
Cdd:PRK10771 97 npgLKLNAAqREKLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
506-710 |
5.80e-22 |
|
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: 95.09 E-value: 5.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 506 PSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL----RRHIGIVQQEPVLM 581
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 582 SGTIRDNITYGLTYTptKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATS 661
Cdd:cd03290 92 NATVEENITFGSPFN--KQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1370557 662 ALDVE-SEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLgHDGS 710
Cdd:cd03290 170 ALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAM-KDGS 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
492-695 |
1.21e-21 |
|
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: 93.38 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPS---VQIFKNLNFKIAPGSSVCIVGPSGRGKSTI--ALLLLRYYNPTTGTITIDNQDISKlncKS 566
Cdd:cd03213 3 TLSFRNLTVTVKSSPSksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEPVLMSG-TIRDNITYGLtytptkeEIRSvakqcfchnfitkfpntydtvigphgtlLSGGQKQRIAIAR 645
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMFAA-------KLRG----------------------------LSGGERKRVSIAL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1370557 646 ALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIaHRLST 695
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSI-HQPSS 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
512-726 |
1.43e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.80 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 512 KNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLR----RHIGIVQQEPVLMSG-TIR 586
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHmTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 587 DNITYGLTYT-----PTKEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKKPTILILDEATS 661
Cdd:PRK10070 125 DNTAFGMELAginaeERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 662 ALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANPTS 726
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
243-437 |
1.55e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 95.63 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 243 SERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSD----AYVVSRSMTQKVSDGVKAlicgVVGVGMMCSLSPQLS 318
Cdd:cd18550 67 GQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDvggaQSVVTGTLTSVVSNVVTL----VATLVAMLALDWRLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 319 ILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLS--GIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAF 396
Cdd:cd18550 143 LLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGVRQAL 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1370557 397 TNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAF 437
Cdd:cd18550 223 AGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAF 263
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
179-468 |
1.66e-21 |
|
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: 95.70 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 179 IGMSIPKVIGIVLDTLKTSSGSDFFDLKIPIFSLplyefLSFFTVALligcaaNFGRFILLRILSERVVARLRANVIKKT 258
Cdd:cd18568 17 LGLALPLFTQIILDRVLVHKNISLLNLILIGLLI-----VGIFQILL------SAVRQYLLDYFANRIDLSLLSDFYKHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 259 LHQDAEFFDNHKVGDLISRLGSDAYV---VSRSMTQKVSDGVKALICGvvgvGMMCSLSPQLSILLLFFTPPVLFSASVF 335
Cdd:cd18568 86 LSLPLSFFASRKVGDIITRFQENQKIrrfLTRSALTTILDLLMVFIYL----GLMFYYNLQLTLIVLAFIPLYVLLTLLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 336 GKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSR----YNVAIRDIFQVGKTAAFTNakffTTTSLLGDL 411
Cdd:cd18568 162 SPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRwenkFAKALNTRFRGQKLSIVLQ----LISSLINHL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 412 SFLTVLAYGSYLVLQSQLSIGDLTAF-MLYTEYTgNAVFGLSTFYSEIMQGAGAASRL 468
Cdd:cd18568 238 GTIAVLWYGAYLVISGQLTIGQLVAFnMLFGSVI-NPLLALVGLWDELQETRISVERL 294
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
471-729 |
1.70e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.21 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 471 LTDRKPSISPTVGHKYKPdrgVIEFKDVSFSYPTRPSVQifkNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTG 550
Cdd:PRK11607 1 MNDAIPRPQAKTRKALTP---LLEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 551 TITIDNQDISKLncKSLRRHIGIVQQEPVLMSG-TIRDNITYGLTYTP-TKEEIRSVAKQCFCHNFITKFPNTydtviGP 628
Cdd:PRK11607 75 QIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQNIAFGLKQDKlPKAEIASRVNEMLGLVHMQEFAKR-----KP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 629 HGtlLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHD 708
Cdd:PRK11607 148 HQ--LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
|
250 260
....*....|....*....|.
gi 1370557 709 GSVVEMGKFKELYANPTSALS 729
Cdd:PRK11607 226 GKFVQIGEPEEIYEHPTTRYS 246
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
492-724 |
1.77e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.19 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYptRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHI 571
Cdd:PRK13647 4 IIEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEP--VLMSGTIRDNITYG-----LTYTPTKEEIRSVAKQCFCHNFITKFPNtydtvigpHgtlLSGGQKQRIAIA 644
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPY--------H---LSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 645 RALIKKPTILILDEATSALDVESEGAINYTFGQLMKsKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKfKELYANP 724
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KSLLTDE 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
493-713 |
2.01e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.44 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVQifkNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlNCKSLRRHIG 572
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVN---GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVL-MSGTIRDN-ITYGLTYTPTKEEIRSVAKQCFchNFiTKFPNTYDTVIgphgTLLSGGQKQRIAIARALIKK 650
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRYFGMSTREIEAVIPSLL--EF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370557 651 PTILILDEATSALDVESEGAINYTFGQLMkSKSMTIVSIAHRLSTIRR-SENVIVLGHDGSVVE 713
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAE 253
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
509-726 |
3.45e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.92 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 509 QIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSlrRHIGIVQQEPVL---MsgTI 585
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALfrhM--TV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 586 RDNITYGLTYTPTKE-----EIRSVAKQCFCHNFITKFPNTYdtvigPhgTLLSGGQKQRIAIARALIKKPTILILDEAT 660
Cdd:PRK10851 92 FDNIAFGLTVLPRRErpnaaAIKAKVTQLLEMVQLAHLADRY-----P--AQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 661 SALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANPTS 726
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
493-667 |
3.71e-21 |
|
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: 92.57 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVQIfKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlNCKSLRRHIG 572
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSG-TIRDNITY-----GLTYTPTKEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARA 646
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLRVLGLTDKANKRART-----------LSGGMKRKLSLAIA 147
|
170 180
....*....|....*....|.
gi 1370557 647 LIKKPTILILDEATSALDVES 667
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPAS 168
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
508-723 |
3.74e-21 |
|
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: 92.88 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 508 VQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNC-KSLRRHIGIVQQEPVLMSG-TI 585
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 586 RDNITYGLtYTPTKEEIRSVAKQCFchnfiTKFPNTYDTVIGPHGTLlSGGQKQRIAIARALIKKPTILILDEATSAL-- 663
Cdd:cd03224 93 EENLLLGA-YARRRAKRKARLERVY-----ELFPRLKERRKQLAGTL-SGGEQQMLAIARALMSRPKLLLLDEPSEGLap 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 664 ----DVESegAInytfgQLMKSKSMTIVSIAHRLSTIRR-SENVIVLGHdGSVVEMGKFKELYAN 723
Cdd:cd03224 166 kiveEIFE--AI-----RELRDEGVTILLVEQNARFALEiADRAYVLER-GRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
492-722 |
3.91e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 3.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQ--DISKLNCKSLRR 569
Cdd:PRK13636 5 ILKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 570 HIGIVQQEP--VLMSGTIRDNITYG-LTYTPTKEEIRSVAKQCFCHNFITKFPNTydtviGPHGtlLSGGQKQRIAIARA 646
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGaVNLKLPEDEVRKRVDNALKRTGIEHLKDK-----PTHC--LSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIR-RSENVIVLgHDGSVVEMGKFKELYA 722
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVM-KEGRVILQGNPKEVFA 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
492-740 |
9.67e-21 |
|
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: 92.95 E-value: 9.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPT------RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLN-- 563
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 564 -CKSLRRHIGIVQQE---PVLMSGTIRDNITYGLTYTPTKEEIRSVAKQcfchNFITKFPNTYDTVIGPHGTLLSGGQKQ 639
Cdd:TIGR02769 82 qRRAFRRDVQLVFQDspsAVNPRMTVRQIIGEPLRHLTSLDESEQKARI----AELLDMVGLRSEDADKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 640 RIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKE 719
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQ 237
|
250 260
....*....|....*....|.
gi 1370557 720 LYANPTSALSQLLNEKAAPGP 740
Cdd:TIGR02769 238 LLSFKHPAGRNLQSAVLPEHP 258
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
496-713 |
1.21e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 496 KDVSFSYPT------RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLN---CKS 566
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEP---VLMSGTIRDNITYGLTYTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPhgtlLSGGQKQRIAI 643
Cdd:PRK10419 87 FRRDIQMVFQDSisaVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ----LSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370557 644 ARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVE 713
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVM-DNGQIVE 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
509-714 |
1.41e-20 |
|
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: 91.43 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 509 QIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLN-CKSLRRHIGIVQQE----PVLmsg 583
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIAYVPQGreifPRL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 584 TIRDNITYGLTYTPTKEeiRSVAKQCFchnfiTKFPNTYDtVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATsal 663
Cdd:TIGR03410 91 TVEENLLTGLAALPRRS--RKIPDEIY-----ELFPVLKE-MLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT--- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 664 dvesEGA-------INYTFGQLMKSKSMTIV----------SIAHRLSTIRRSENVivlgHDGSVVEM 714
Cdd:TIGR03410 160 ----EGIqpsiikdIGRVIRRLRAEGGMAILlveqyldfarELADRYYVMERGRVV----ASGAGDEL 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
493-721 |
1.55e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.50 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYP--TRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDI---SK-LNCKS 566
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQ--EPVLMSGTIRDNITYG-LTYTPTKEEIRSVAKQCF-----CHNFITKFPNTydtvigphgtlLSGGQK 638
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpQNFGVSQEEAEALAREKLalvgiSESLFEKNPFE-----------LSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 639 QRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSkSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFK 718
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
...
gi 1370557 719 ELY 721
Cdd:PRK13649 231 DIF 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
495-667 |
1.78e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 495 FKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDnqdisklncKSLRrhIGIV 574
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 575 QQEPVLMSG-TIRDNITYGLTytptkeEIRSVAKQcfcHNFITKFPNTYDTVIGPHGTL--------------------- 632
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDA------ELRALEAE---LEELEAKLAEPDEDLERLAELqeefealggweaearaeeils 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1370557 633 ---------------LSGGQKQRIAIARALIKKPTILILDEATSALDVES 667
Cdd:COG0488 138 glgfpeedldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
503-715 |
2.25e-20 |
|
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: 90.50 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 503 PTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlNCKSLRRHIGIVQ-QEPVLM 581
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSdSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 582 SGTIRDNITY-----GLTYTPTKEEIRSVAKQCFCHNFITKfpntydtvigpHGTLLSGGQKQRIAIARALIKKPTILIL 656
Cdd:cd03266 92 RLTARENLEYfaglyGLKGDELTARLEELADRLGMEELLDR-----------RVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 657 DEATSALDVESEGAInYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMG 715
Cdd:cd03266 161 DEPTTGLDVMATRAL-REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
519-737 |
3.33e-20 |
|
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: 93.24 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 519 APGSSVC-IVGPSGRGKSTiaLL-----LLRyynPTTGTITIDN---QDISK-LNCKSLRRHIGIVQQEPVL---MSgtI 585
Cdd:COG4148 22 LPGRGVTaLFGPSGSGKTT--LLraiagLER---PDSGRIRLGGevlQDSARgIFLPPHRRRIGYVFQEARLfphLS--V 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 586 RDNITYGLTYTPTKEeiRSVAkqcfchnfitkfpntYDTVI-----------GPHGtlLSGGQKQRIAIARALIKKPTIL 654
Cdd:COG4148 95 RGNLLYGRKRAPRAE--RRIS---------------FDEVVellgighlldrRPAT--LSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 655 ILDEATSALDVESEGAI-NYtFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKFKELYANPtsALSQLL 732
Cdd:COG4148 156 LMDEPLAALDLARKAEIlPY-LERLRDELDIPILYVSHSLDEVARlADHVVLL-EQGRVVASGPLAEVLSRP--DLLPLA 231
|
....*
gi 1370557 733 NEKAA 737
Cdd:COG4148 232 GGEEA 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
514-724 |
3.50e-20 |
|
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: 92.87 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 514 LNFKIaPGSSVC-IVGPSGRGKSTIALLLLRYYNPTTGTITIDN---QDISKLNCKSL-RRHIGIVQQEPVLMSG-TIRD 587
Cdd:TIGR02142 16 ADFTL-PGQGVTaIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIFLPPeKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 588 NITYGLTYTPTKEEIRSVAKqcfchnfITKFPNTYDTVIGPHGTLlSGGQKQRIAIARALIKKPTILILDEATSALDVES 667
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFER-------VIELLGIGHLLGRLPGRL-SGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 668 EGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANP 724
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
492-724 |
5.40e-20 |
|
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: 89.66 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL-RRH 570
Cdd:COG0410 3 MLEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQE----PVLmsgTIRDNITYGLTYTPTKEEIRSVAKQCFchnfiTKFPNTYDtVIGPHGTLLSGGQKQRIAIARA 646
Cdd:COG0410 80 IGYVPEGrrifPSL---TVEENLLLGAYARRDRAEVRADLERVY-----ELFPRLKE-RRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 647 LIKKPTILILDEATSAL------DVESegAInytfgQLMKSKSMTIV----------SIAHRlstirrsenVIVLGHdGS 710
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLapliveEIFE--II-----RRLNREGVTILlveqnarfalEIADR---------AYVLER-GR 213
|
250
....*....|....
gi 1370557 711 VVEMGKFKELYANP 724
Cdd:COG0410 214 IVLEGTAAELLADP 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
493-722 |
8.40e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYP--TRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDI-SKLNCK 565
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKST----LIQNINallkPTTGTVTVDDITItHKTKDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 566 SL---RRHIGIVQQEPvlMSGTIRDNITYGLTYTPTK-----EEIRSVAKQC-----FCHNFITKFPNTydtvigphgtl 632
Cdd:PRK13646 79 YIrpvRKRIGMVFQFP--ESQLFEDTVEREIIFGPKNfkmnlDEVKNYAHRLlmdlgFSRDVMSQSPFQ----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSV 711
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVM-KEGSI 224
|
250
....*....|.
gi 1370557 712 VEMGKFKELYA 722
Cdd:PRK13646 225 VSQTSPKELFK 235
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
493-664 |
1.22e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.37 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVS--FSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLR----YYNPTTGTITIDNQDISKLncKS 566
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKST----LLNaiagSLPPDSGSILIDGKDVTKL--PE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRR--HIGIVQQEPvlMSGT-----IRDNI--------TYGLTYTPTKEEIRSVAKQcfchnfITKF----PNTYDTVIG 627
Cdd:COG1101 76 YKRakYIGRVFQDP--MMGTapsmtIEENLalayrrgkRRGLRRGLTKKRRELFREL------LATLglglENRLDTKVG 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1370557 628 phgtLLSGGQKQRIAIARALIKKPTILILDEATSALD 664
Cdd:COG1101 148 ----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
493-667 |
1.23e-19 |
|
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: 85.96 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNqdisklnckslRRHIG 572
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQepvlmsgtirdnitygltytptkeeirsvakqcfchnfitkfpntydtvigphgtlLSGGQKQRIAIARALIKKPT 652
Cdd:cd03221 67 YFEQ--------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170
....*....|....*
gi 1370557 653 ILILDEATSALDVES 667
Cdd:cd03221 91 LLLLDEPTNHLDLES 105
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
488-724 |
1.33e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.77 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 488 PDRGVIEFKDVSFSYPTRP--------SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDI 559
Cdd:PRK10261 309 DGEPILQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 560 SKLN---CKSLRRHIGIVQQEPvLMSGTIRDNITYGLT-------YTPTKEEIRSVAKQCFCHNFITKFPNTYdtvigPH 629
Cdd:PRK10261 389 DTLSpgkLQALRRDIQFIFQDP-YASLDPRQTVGDSIMeplrvhgLLPGKAAAARVAWLLERVGLLPEHAWRY-----PH 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 630 GtlLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDG 709
Cdd:PRK10261 463 E--FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLG 540
|
250
....*....|....*
gi 1370557 710 SVVEMGKFKELYANP 724
Cdd:PRK10261 541 QIVEIGPRRAVFENP 555
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
492-667 |
1.48e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 88.26 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVS--FSYPTRPSVQI--FKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQ----DISKLN 563
Cdd:COG4778 4 LLEVENLSktFTLHLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 564 CK---SLRRH-IGIVQQ---------------EPVLMSGTirdnitygltytpTKEEIRSVAKQCFCHNFITK-----FP 619
Cdd:COG4778 84 PReilALRRRtIGYVSQflrviprvsaldvvaEPLLERGV-------------DREEARARARELLARLNLPErlwdlPP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1370557 620 NTYdtvigphgtllSGGQKQRIAIARALIKKPTILILDEATSALDVES 667
Cdd:COG4778 151 ATF-----------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN 187
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
493-720 |
1.54e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 88.20 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlNCKSLRRHIG 572
Cdd:cd03265 1 IEVENLVKKYGDFEAV---RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSG-TIRDNIT-----YGLTYTPTKEEIRSVAKQCFCHNFITKFPNTYdtvigphgtllSGGQKQRIAIARA 646
Cdd:cd03265 77 IVFQDLSVDDElTGWENLYiharlYGVPGAERRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKEL 720
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
214-468 |
1.72e-19 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 89.57 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 214 LYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGsDAYVVSRSMTQKV 293
Cdd:cd18782 41 LYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 294 SDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAE 373
Cdd:cd18782 120 LTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 374 ----GNELSRYNVAIRDIFQVGKTAAFTNAkfftTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVF 449
Cdd:cd18782 200 lkarWRWQNRYARSLGEGFKLTVLGTTSGS----LSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPIL 275
|
250
....*....|....*....
gi 1370557 450 GLSTFYSEIMQGAGAASRL 468
Cdd:cd18782 276 RLSTLWQQFQELRVSLERL 294
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
512-724 |
2.21e-19 |
|
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: 87.88 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 512 KNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNcKSLRRHIGIV---QQEPVLMSGTIRDN 588
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGrtfQIPRLFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 589 I-----------TYGLTYTPTKEEIRSVAKQC--FCHnfITKFpntYDTVIGphgtLLSGGQKQRIAIARALIKKPTILI 655
Cdd:cd03219 96 VmvaaqartgsgLLLARARREEREARERAEELleRVG--LADL---ADRPAG----ELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370557 656 LDEATSAL-DVESEGAINYTfgQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKFKELYANP 724
Cdd:cd03219 167 LDEPAAGLnPEETEELAELI--RELRERGITVLLVEHDMDVVMSlADRVTVL-DQGRVIAEGTPDEVRNNP 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
493-664 |
2.43e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYP-TRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlncKSLRRhi 571
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG---PGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVLMSG-TIRDNITYGLTYTPT-KEEIRSVAKQCF----CHNFITKFPntYDtvigphgtlLSGGQKQRIAIAR 645
Cdd:COG4525 79 GVVFQKDALLPWlNVLDNVAFGLRLRGVpKAERRARAEELLalvgLADFARRRI--WQ---------LSGGMRQRVGIAR 147
|
170
....*....|....*....
gi 1370557 646 ALIKKPTILILDEATSALD 664
Cdd:COG4525 148 ALAADPRFLLMDEPFGALD 166
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
493-725 |
3.04e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.06 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSyptRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITIDNQDISKLNCKSLR 568
Cdd:PRK09536 4 IDVSDLSVE---FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTT----LLRAINgtltPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIVQQEPVL-MSGTIRDNITYGLT-----YTPTKEEIRSVAKQCFCHNFITKFPntyDTVIgphgTLLSGGQKQRIA 642
Cdd:PRK09536 77 RRVASVPQDTSLsFEFDVRQVVEMGRTphrsrFDTWTETDRAAVERAMERTGVAQFA---DRPV----TSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 643 IARALIKKPTILILDEATSALDvesegaINYTFGQLMKSKSM-----TIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKF 717
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLD------INHQVRTLELVRRLvddgkTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
....*...
gi 1370557 718 KELYANPT 725
Cdd:PRK09536 224 ADVLTADT 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
491-723 |
3.24e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 491 GVIEFKDVSFSYPTRPSVQiFKNLN---FKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTG-TITIDNQ---DISKLN 563
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFE-FKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAipaNLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 564 -CKSLRRHIGIVQQEP--VLMSGTIRDNITYG-LTYTPTKEEIRSvakqcfchnfitKFPNTYDTVIGPHGTL------L 633
Cdd:PRK13645 84 eVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpVNLGENKQEAYK------------KVPELLKLVQLPEDYVkrspfeL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 634 SGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVE 713
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
250
....*....|
gi 1370557 714 MGKFKELYAN 723
Cdd:PRK13645 232 IGSPFEIFSN 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
492-709 |
3.44e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.24 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYptRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS---LR 568
Cdd:PRK10908 1 MIRFEHVSKAY--LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIG-IVQQEPVLMSGTIRDNITYGLTYT-PTKEEI-RSVAKQCFCHNFITKFPNtydtvigpHGTLLSGGQKQRIAIAR 645
Cdd:PRK10908 79 RQIGmIFQDHHLLMDRTVYDNVAIPLIIAgASGDDIrRRVSAALDKVGLLDKAKN--------FPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370557 646 ALIKKPTILILDEATSALDVESEGAINYTFGQLMKSkSMTIVSIAHRLSTI-RRSENVIVL-------GHDG 709
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLIsRRSYRMLTLsdghlhgGVGG 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
221-574 |
3.47e-19 |
|
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: 92.17 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 221 FTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDayvvsrsmTQKVSDGVKAL 300
Cdd:COG4615 54 FAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTED--------VRTISQAFVRL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 301 ICGVVGVGM-------MCSLSPQLSILLLfftppVLFSASVFGKQIRntskdLQEATGQLTRVAEEQ----------LSG 363
Cdd:COG4615 126 PELLQSVALvlgclayLAWLSPPLFLLTL-----VLLGLGVAGYRLL-----VRRARRHLRRAREAEdrlfkhfralLEG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 364 IKTV-------QSFVAEgnELSRYNVAIRDIfqvgKTAAFTnakFFTTTSLLGDLSFLTVLAYGSYLVLQ-SQLSIGDLT 435
Cdd:COG4615 196 FKELklnrrrrRAFFDE--DLQPTAERYRDL----RIRADT---IFALANNWGNLLFFALIGLILFLLPAlGWADPAVLS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 436 AF---MLYTEYtgnAVFGLSTFYSEIMQGAGAASRL----FELTDRKPSISPTVGHKYKPDRGVIEFKDVSFSYPTRPSV 508
Cdd:COG4615 267 GFvlvLLFLRG---PLSQLVGALPTLSRANVALRKIeeleLALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGD 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 509 QIFK--NLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIV 574
Cdd:COG4615 344 EGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAV 411
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
492-667 |
4.67e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDnqdisklncKSLRrhI 571
Cdd:COG0488 315 VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------ETVK--I 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVLMSG--TIRDNITYGLTYTpTKEEIRSVAkQCFchNFitkfpnTYDTV---IGPhgtlLSGGQKQRIAIARA 646
Cdd:COG0488 381 GYFDQHQEELDPdkTVLDELRDGAPGG-TEQEVRGYL-GRF--LF------SGDDAfkpVGV----LSGGEKARLALAKL 446
|
170 180
....*....|....*....|.
gi 1370557 647 LIKKPTILILDEATSALDVES 667
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIET 467
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
493-715 |
5.34e-19 |
|
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: 86.12 E-value: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVQifkNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLncKSLRRHIG 572
Cdd:cd03268 1 LKTNDLTKTYGKKRVLD---DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVL---MSGtiRDNITYGLTYTPTKEEIrsvAKQCFchnfitkfpntydTVIGPHGT------LLSGGQKQRIAI 643
Cdd:cd03268 76 ALIEAPGFypnLTA--RENLRLLARLLGIRKKR---IDEVL-------------DVVGLKDSakkkvkGFSLGMKQRLGI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370557 644 ARALIKKPTILILDEATSALDVESEGAINYTFgQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMG 715
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELI-LSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
510-715 |
6.68e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSG-TIRDN 588
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 589 ITYG----LTY----TPTKEEIRSVAKQcfchnfITKFPNTYDTVIgphgTLLSGGQKQRIAIARALIKKPTILILDEAT 660
Cdd:PRK11231 97 VAYGrspwLSLwgrlSAEDNARVNQAME------QTRINHLADRRL----TDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 661 SALDVESEGAINYTFGQlMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMG 715
Cdd:PRK11231 167 TYLDINHQVELMRLMRE-LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-730 |
6.83e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.20 E-value: 6.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 509 QIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN---------PTTGTITIDNQDI--SKLNCKSLRRHIGIVQQE 577
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKST----LLRTFNrllelneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 578 PVLMSG-TIRDNITYGLTYT---PTKEEIRSVAKqcfchnFITKFPNTYDTV---IGPHGTLLSGGQKQRIAIARALIKK 650
Cdd:PRK14267 94 PNPFPHlTIYDNVAIGVKLNglvKSKKELDERVE------WALKKAALWDEVkdrLNDYPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 651 PTILILDEATSALDVESEGAINYTFGQLmkSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANPTSALSQ 730
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
214-465 |
1.22e-18 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 87.15 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 214 LYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKV 293
Cdd:cd18540 41 LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 294 SDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAE 373
Cdd:cd18540 121 VDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVRE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 374 GNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLST 453
Cdd:cd18540 201 EKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLAR 280
|
250
....*....|..
gi 1370557 454 FYSEiMQGAGAA 465
Cdd:cd18540 281 VLAE-LQSAQAS 291
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
499-732 |
1.90e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.00 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 499 SFSYPT----RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIV 574
Cdd:PRK15112 13 TFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 575 QQEPV-----------LMSGTIRDNItyGLTYTPTKEEIRSVAKQCfchNFITKFPNTYdtvigPHgtLLSGGQKQRIAI 643
Cdd:PRK15112 93 FQDPStslnprqrisqILDFPLRLNT--DLEPEQREKQIIETLRQV---GLLPDHASYY-----PH--MLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 644 ARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKFKELYA 722
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVM-HQGEVVERGSTADVLA 239
|
250
....*....|
gi 1370557 723 NPTSALSQLL 732
Cdd:PRK15112 240 SPLHELTKRL 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
493-756 |
2.05e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.68 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRPSVQI--FKNLNFKIAPGSSVCIVGPSGRGKSTI-----ALLLlryynPTTGTITIDNQDISKL--- 562
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFiehlnALLL-----PDTGTIEWIFKDEKNKkkt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 563 ---------------------NCKSLRRHIGIVQQ--EPVLMSGTIRDNITYG-LTYTPTKEEIRSVAKQcfchnfitkf 618
Cdd:PRK13651 78 kekekvleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpVSMGVSKEEAKKRAAK---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 619 pntYDTVIG-PHGTL------LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSkSMTIVSIAH 691
Cdd:PRK13651 148 ---YIELVGlDESYLqrspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTH 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 692 RL-STIRRSENVIVLgHDGSVVEMG---------KF-KELYANPTSALSqLLNEKAAPGpsdqqLQIEKVIEKEDL 756
Cdd:PRK13651 224 DLdNVLEWTKRTIFF-KDGKIIKDGdtydilsdnKFlIENNMEPPKLLN-FVNKLEKKG-----IDVPKVTSIEEL 292
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
492-715 |
2.05e-18 |
|
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: 85.02 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYP-TRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKST----IALLLLRYYNpTTGTITIDNQDISKlncKS 566
Cdd:cd03234 3 VLPWWDVGLKAKnWNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPRKP---DQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEPVLMSG-TIRDNITYG----LTYTPTKEEIRSVA-----KQCfchnfitkfpntYDTVIGphGTL---L 633
Cdd:cd03234 79 FQKCVAYVRQDDILLPGlTVRETLTYTailrLPRKSSDAIRKKRVedvllRDL------------ALTRIG--GNLvkgI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 634 SGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVE 713
Cdd:cd03234 145 SGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVY 224
|
..
gi 1370557 714 MG 715
Cdd:cd03234 225 SG 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
510-720 |
3.04e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.42 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSG-TIRDN 588
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 589 ITYG-LTYTPT-----KEEIRSVAKQCFCHNFITKFPNTYDTvigphgtlLSGGQKQRIAIARALIKKPTILILDEATSA 662
Cdd:PRK10253 102 VARGrYPHQPLftrwrKEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 663 LDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKEL 720
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
473-748 |
4.91e-18 |
|
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: 89.62 E-value: 4.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 473 DRKPsISPTVGHKykpdrgvIEFKDVSFSYpTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTI 552
Cdd:TIGR00957 625 ERRT-IKPGEGNS-------ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 553 TIdnqdisklnckslRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTKeeIRSVAKQCFCHNFITKFPNTYDTVIGPHGTL 632
Cdd:TIGR00957 696 HM-------------KGSVAYVPQQAWIQNDSLRENILFGKALNEKY--YQQVLEACALLPDLEILPSGDRTEIGEKGVN 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAI-NYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGhDGSV 711
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMS-GGKI 839
|
250 260 270
....*....|....*....|....*....|....*..
gi 1370557 712 VEMGKFKELYANpTSALSQLLNEKAapgPSDQQLQIE 748
Cdd:TIGR00957 840 SEMGSYQELLQR-DGAFAEFLRTYA---PDEQQGHLE 872
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
493-738 |
8.26e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.86 E-value: 8.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPT-RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL---- 567
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEPVLMSG-TIRDNITYGLTYTPTKEEIRsvakQCFCHNFITKFpnTYDTVIGPHGTLLSGGQKQRIAIARA 646
Cdd:PRK10535 85 REHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQR----LLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLmKSKSMTIVSIAHRLSTIRRSENVIVLgHDGsvvemgkfkELYANPTS 726
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEI-RDG---------EIVRNPPA 227
|
250
....*....|..
gi 1370557 727 ALSQLLNEKAAP 738
Cdd:PRK10535 228 QEKVNVAGGTEP 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
493-720 |
1.25e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCK-SLRRHI 571
Cdd:PRK09700 6 ISMAGIGKSFG---PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQE-PVLMSGTIRDNITYGltYTPTKE----------EIRSVAKQCFchnFITKFPNTYDTVIGPhgtlLSGGQKQR 640
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIG--RHLTKKvcgvniidwrEMRVRAAMML---LRVGLKVDLDEKVAN----LSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 641 IAIARALIKKPTILILDEATSALdveSEGAINYTFGQL--MKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFK 718
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMnqLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
..
gi 1370557 719 EL 720
Cdd:PRK09700 231 DV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
501-724 |
1.37e-17 |
|
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: 82.59 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 501 SYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNC-KSLRRHIGIVQQEPV 579
Cdd:cd03218 9 RYGKRKVV---NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 580 LMSG-TIRDNITYGLTYTP-TKEEIRSVAKQcFCHNF-ITKFPNTYdtvigphGTLLSGGQKQRIAIARALIKKPTILIL 656
Cdd:cd03218 86 IFRKlTVEENILAVLEIRGlSKKEREEKLEE-LLEEFhITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370557 657 DEATSALDVESEGAINYTFGQLmKSKSMTIVSIAHR----LSTIRRSenVIVlgHDGSVVEMGKFKELYANP 724
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNvretLSITDRA--YII--YEGKVLAEGTPEEIAANE 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
505-732 |
1.69e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 505 RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITID-------NQDISKLNCKS---LRR----H 570
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRQVIELSEQSaaqMRHvrgaD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQEPvlMSG-----TIRDNI--TYGLTYTPTKEEIRSVAKQCFCHnfiTKFPNTyDTVIGPHGTLLSGGQKQRIAI 643
Cdd:PRK10261 106 MAMIFQEP--MTSlnpvfTVGEQIaeSIRLHQGASREEAMVEAKRMLDQ---VRIPEA-QTILSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 644 ARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYAN 723
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
....*....
gi 1370557 724 PTSALSQLL 732
Cdd:PRK10261 260 PQHPYTRAL 268
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
509-744 |
3.56e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 509 QIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYnPT------TGTITIDNQDISKLNCKSLRR----HIGIVQQEP 578
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 579 VLMSG---TIRDNIT------YGLTYTPTKEEIRSVAKQCFCHNFITKFpNTYdtvigPHGtlLSGGQKQRIAIARALIK 649
Cdd:PRK15134 102 MVSLNplhTLEKQLYevlslhRGMRREAARGEILNCLDRVGIRQAAKRL-TDY-----PHQ--LSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 650 KPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLGHdGSVVEMGKFKELYANPTSAL 728
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQN-GRCVEQNRAATLFSAPTHPY 252
|
250
....*....|....*....
gi 1370557 729 SQ-LLNEKAA--PGPSDQQ 744
Cdd:PRK15134 253 TQkLLNSEPSgdPVPLPEP 271
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
498-664 |
4.03e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.05 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 498 VSFSYPTRPSVQifkNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlncKSLRRhiGIV-QQ 576
Cdd:PRK11248 7 LYADYGGKPALE---DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG---PGAER--GVVfQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 577 EPVLMSGTIRDNITYGLTYTPT-KEEIRSVAKQC--------FCHNFITKfpntydtvigphgtlLSGGQKQRIAIARAL 647
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVeKMQRLEIAHQMlkkvglegAEKRYIWQ---------------LSGGQRQRVGIARAL 143
|
170
....*....|....*..
gi 1370557 648 IKKPTILILDEATSALD 664
Cdd:PRK11248 144 AANPQLLLLDEPFGALD 160
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
492-725 |
4.42e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.14 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIalllLRYYNPTT---------GTITIDNQDI--S 560
Cdd:PRK14243 10 VLRTENLNVYYGSFLAV---KNVWLDIPKNQITAFIGPSGCGKSTI----LRCFNRLNdlipgfrveGKVTFHGKNLyaP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 561 KLNCKSLRRHIGIVQQEPVLMSGTIRDNITYG---LTYTPTKEEI--RSVAKQCFchnfitkfpntYDTV---IGPHGTL 632
Cdd:PRK14243 83 DVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDELveRSLRQAAL-----------WDEVkdkLKQSGLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINytfgQLMKS--KSMTIVSIAHRLSTIRRSENVIVL----- 705
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIE----ELMHElkEQYTIIIVTHNMQQAARVSDMTAFfnvel 227
|
250 260
....*....|....*....|....
gi 1370557 706 ----GHDGSVVEMGKFKELYANPT 725
Cdd:PRK14243 228 teggGRYGYLVEFDRTEKIFNSPQ 251
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
492-708 |
4.45e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.74 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLR----YYNPTTGTITIDNQDISKLNCKSL 567
Cdd:PRK13548 2 MLEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKST----LLRalsgELSPDSGEVRLNGRPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEPVL-MSGTIRDNITYGLT-----YTPTKEEIRSVAKQCFCHNFITKFpntYDTvigphgtlLSGGQKQRI 641
Cdd:PRK13548 75 ARRRAVLPQHSSLsFPFTVEEVVAMGRAphglsRAEDDALVAAALAQVDLAHLAGRD---YPQ--------LSGGEQQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 642 AIARALI------KKPTILILDEATSALDVesegainytFGQLmksksmTIVSIAHRLsTIRRSENVIVLGHD 708
Cdd:PRK13548 144 QLARVLAqlwepdGPPRWLLLDEPTSALDL---------AHQH------HVLRLARQL-AHERGLAVIVVLHD 200
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
509-723 |
5.05e-17 |
|
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: 80.26 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 509 QIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLL--RYYNPTTGTITIDNQDISKLNC-KSLRRHIGIVQQEPVLMSGti 585
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPPeERARLGIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 586 rdnITygltytpTKEEIRSVAKQcfchnfitkfpntydtvigphgtlLSGGQKQRIAIARALIKKPTILILDEATSALDV 665
Cdd:cd03217 92 ---VK-------NADFLRYVNEG------------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 666 ES----EGAINYtfgqlMKSKSMTIVSIAH--RLSTIRRSENVIVLgHDGSVVEMGKF---KELYAN 723
Cdd:cd03217 138 DAlrlvAEVINK-----LREEGKSVLIITHyqRLLDYIKPDRVHVL-YDGRIVKSGDKelaLEIEKK 198
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
243-468 |
8.56e-17 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. 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: 349998 [Multi-domain] Cd Length: 299 Bit Score: 81.70 E-value: 8.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 243 SERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALICGVVGVGMMCSLSPQLSILLL 322
Cdd:cd18554 74 ANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 323 FFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFF 402
Cdd:cd18554 154 VIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTF 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 403 TTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQGAGAASRL 468
Cdd:cd18554 234 SAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
243-437 |
8.61e-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: 82.32 E-value: 8.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 243 SERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQKVSDGVKALicGVVGVGMMCSLSP--QLSIL 320
Cdd:cd18558 87 AGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNI--ATFGTGFIIGFIRgwKLTLV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 321 LLFFTPPVLFSASVFGKQIRN-TSKDLQEATGQlTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNA 399
Cdd:cd18558 165 ILAISPVLGLSAVVWAKILSGfTDKEKKAYAKA-GAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFN 243
|
170 180 190
....*....|....*....|....*....|....*....
gi 1370557 400 KFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGD-LTAF 437
Cdd:cd18558 244 ISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEvLTVF 282
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
493-715 |
8.87e-17 |
|
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: 80.27 E-value: 8.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPT-------------------RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTIT 553
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 554 IDNQDISKLNckslrrhigivqqepvLMSG-----TIRDNIT-YGLTYTPTKEEIRSVAkqcfchNFITKFpntydTVIG 627
Cdd:cd03220 81 VRGRVSSLLG----------------LGGGfnpelTGRENIYlNGRLLGLSRKEIDEKI------DEIIEF-----SELG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 628 PHGTL----LSGGQKQRIAIARALIKKPTILILDEATSALDVE-SEGAINYTFGQLMKSKSMTIVSiaHRLSTIRRSENV 702
Cdd:cd03220 134 DFIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVS--HDPSSIKRLCDR 211
|
250
....*....|...
gi 1370557 703 IVLGHDGSVVEMG 715
Cdd:cd03220 212 ALVLEKGKIRFDG 224
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
487-688 |
2.89e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 83.37 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 487 KPDRGVIEFKDVSFSYPTRPSvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITidnqdisklncKS 566
Cdd:PLN03073 503 RPGPPIISFSDASFGYPGGPL--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RS 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRHIGIVQQEPVLMSGTIRDNITYGLTYTPTKEEIRSVAKqcfchnfITKFPNTYDTVIGPHGTlLSGGQKQRIAIARA 646
Cdd:PLN03073 570 AKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAH-------LGSFGVTGNLALQPMYT-LSGGQKSRVAFAKI 641
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1370557 647 LIKKPTILILDEATSALDVES-----EGAINYTFGQLMKSKSMTIVS 688
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAvealiQGLVLFQGGVLMVSHDEHLIS 688
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
512-691 |
3.11e-16 |
|
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: 78.66 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 512 KNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlncKSLRRHIgIVQQEPVLMSGTIRDNITY 591
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE---PGPDRMV-VFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 592 GLT---YTPTKEEIRSVAKQcfcHNFITKFPNTYDTVIGPhgtlLSGGQKQRIAIARALIKKPTILILDEATSALDVESE 668
Cdd:TIGR01184 78 AVDrvlPDLSKSERRAIVEE---HIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|...
gi 1370557 669 GAINYTFGQLMKSKSMTIVSIAH 691
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTH 173
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
221-458 |
5.14e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 79.43 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 221 FTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSdAYVVSRSMTQKVsdgVKAL 300
Cdd:cd18567 48 FGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGF---VEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 301 ICGVVGVG---MMCSLSPQLSIL-LLFFTPPVLFSASVFGKQIRNTSKdlqeatgQLTRVAEEQ------LSGIKTVQSF 370
Cdd:cd18567 124 LDGLMAILtlvMMFLYSPKLALIvLAAVALYALLRLALYPPLRRATEE-------QIVASAKEQshfletIRGIQTIKLF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 371 VAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFG 450
Cdd:cd18567 197 GREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASS 276
|
....*...
gi 1370557 451 LSTFYSEI 458
Cdd:cd18567 277 LIDKLFEL 284
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
495-724 |
7.14e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 495 FKDVSFSYPTrpsVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKslRRHIGIV 574
Cdd:PRK11000 6 LRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 575 QQE----PVLmsgTIRDNITYGLTYTPT-KEEIRSVAKQC-----FCHnFITKFPNTydtvigphgtlLSGGQKQRIAIA 644
Cdd:PRK11000 81 FQSyalyPHL---SVAENMSFGLKLAGAkKEEINQRVNQVaevlqLAH-LLDRKPKA-----------LSGGQRQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 645 RALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAH-RLSTIRRSENVIVLGHdGSVVEMGKFKELYAN 723
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDA-GRVAQVGKPLELYHY 224
|
.
gi 1370557 724 P 724
Cdd:PRK11000 225 P 225
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
514-710 |
7.15e-16 |
|
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: 81.72 E-value: 7.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 514 LNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQdisklnCKslrrhIGIVQQEPVLMSGTIRDNITYGL 593
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK------GK-----LFYVPQRPYMTLGTLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 594 TYTPTKE------EIRSVAKQCFCHNFITKfpNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVES 667
Cdd:TIGR00954 540 SSEDMKRrglsdkDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1370557 668 EGAINytfgQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGS 710
Cdd:TIGR00954 618 EGYMY----RLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGG 656
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
493-664 |
7.35e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.89 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTRpsVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYY----NPTTGTITIDNQDISKLNCKSlr 568
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVagleRITSGEIWIGGRVVNELEPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIVQQEPVL---MSgtIRDNITYGLTY--TPtKEEIRS----VAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQ 639
Cdd:PRK11650 76 RDIAMVFQNYALyphMS--VRENMAYGLKIrgMP-KAEIEErvaeAARILELEPLLDRKPRE-----------LSGGQRQ 141
|
170 180
....*....|....*....|....*
gi 1370557 640 RIAIARALIKKPTILILDEATSALD 664
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
513-724 |
7.36e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.92 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 513 NLNFKIA---PGSSVC-IVGPSGRGKSTIALLLLRYYNPTTGTITIDNQ---DI-SKLNCKSLRRHIGIVQQEPVLMSG- 583
Cdd:PRK11144 12 DLCLTVNltlPAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFPHy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 584 TIRDNITYGLTYTpTKEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKKPTILILDEATSAL 663
Cdd:PRK11144 92 KVRGNLRYGMAKS-MVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370557 664 DV--ESEgAINYtFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKFKELYANP 724
Cdd:PRK11144 160 DLprKRE-LLPY-LERLAREINIPILYVSHSLDEILRlADRVVVL-EQGKVKAFGPLEEVWASS 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
492-719 |
9.01e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPS-------------------VQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRY----YNPT 548
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKST----LLKLiagiLEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 549 TGTITIdNQDISKLnckslrrhIGI---VQQEpvlMSGtiRDNI-----TYGLtytpTKEEIRSVAKQC--FC--HNFIt 616
Cdd:COG1134 80 SGRVEV-NGRVSAL--------LELgagFHPE---LTG--RENIylngrLLGL----SRKEIDEKFDEIveFAelGDFI- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 617 kfpntyDTvigPHGTlLSGGQKQRIAIARALIKKPTILILDEATSALDVE----SEGAINytfgQLMKS-KSMTIVSiaH 691
Cdd:COG1134 141 ------DQ---PVKT-YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR----ELRESgRTVIFVS--H 204
|
250 260
....*....|....*....|....*....
gi 1370557 692 RLSTIRR-SENVIVLgHDGSVVEMGKFKE 719
Cdd:COG1134 205 SMGAVRRlCDRAIWL-EKGRLVMDGDPEE 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
510-713 |
9.83e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.92 E-value: 9.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYY--NPTTGTITIDNQDISklnckslrrhigivQQEPVLmsgtirD 587
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG--------------REASLI------D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 588 NItYGLTYTPTKEEIRSVAKQCFCHNFITKFPNtydtvigphgtlLSGGQKQRIAIARALIKKPTILILDEATSALDVES 667
Cdd:COG2401 105 AI-GRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1370557 668 EGAINYTFGQLMKSKSMTIVSIAHRLSTIR--RSENVIVLGHDGSVVE 713
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVATHHYDVIDdlQPDLLIFVGYGGVPEE 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
500-725 |
1.30e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.74 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 500 FSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN----PTTGTITID----NQDISKL--------- 562
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKST----LVTHFNglikSKYGTIQVGdiyiGDKKNNHelitnpysk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 563 ---NCKSLRRHIGIVQQEP--VLMSGTIRDNITYG-LTYTPTKEEIRSVAKQcfchnFITKFPNTYDTV-IGPHGtlLSG 635
Cdd:PRK13631 107 kikNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGpVALGVKKSEAKKLAKF-----YLNKMGLDDSYLeRSPFG--LSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 636 GQKQRIAIARALIKKPTILILDEATSALDVESEGAINytfgQLM---KSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVV 712
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM----QLIldaKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|...
gi 1370557 713 EMGKFKELYANPT 725
Cdd:PRK13631 256 KTGTPYEIFTDQH 268
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
492-720 |
1.43e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNcKSLRRHI 571
Cdd:PRK15439 11 LLCARSISKQYS---GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GI--VQQEPVLMSG-TIRDNITYGLTYTP-TKEEIRSVAKQCFCHnfitkfpntydtvIGPH---GTLLSGGQkQRIAIA 644
Cdd:PRK15439 87 GIylVPQEPLLFPNlSVKENILFGLPKRQaSMQKMKQLLAALGCQ-------------LDLDssaGSLEVADR-QIVEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 645 RALIKKPTILILDEATSALdveSEGAINYTFGQL--MKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKEL 720
Cdd:PRK15439 153 RGLMRDSRILILDEPTASL---TPAETERLFSRIreLLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
510-679 |
1.60e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKST----IALLLLryynPTTGTITIDNQDISKLNCKSLRRHIGivQQEPVLMSGTI 585
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTllrlIAGLLP----PAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 586 RDNITYGLTYTPTKEEIRSVAKQCFCHNFITKFPNTYdtvigphgtlLSGGQKQRIAIARALIKKPTILILDEATSALDV 665
Cdd:PRK13539 91 AENLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170
....*....|....
gi 1370557 666 ESEGAinytFGQLM 679
Cdd:PRK13539 161 AAVAL----FAELI 170
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
492-721 |
1.82e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.85 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSY-PTRP-SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLN----CK 565
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 566 SLRRHIGIVQQEP--VLMSGTIRDNITYG-LTYTPTKEEIRSVAKQ-----CFCHNFITKFPNTydtvigphgtlLSGGQ 637
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGpQNFGIPKEKAEKIAAEklemvGLADEFWEKSPFE-----------LSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 638 KQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSkSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKF 717
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
....
gi 1370557 718 KELY 721
Cdd:PRK13643 229 SDVF 232
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
507-698 |
3.02e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 507 SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS---LR-RHIG-IVQQEPVLM 581
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGfIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 582 SGTIRDNITYGLTYTPTK-EEIRSVAKQCFCHNFITKFPNTydtvigpHGTLLSGGQKQRIAIARALIKKPTILILDEAT 660
Cdd:PRK11629 101 DFTALENVAMPLLIGKKKpAEINSRALEMLAAVGLEHRANH-------RPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1370557 661 SALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR 698
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR 211
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
214-439 |
4.91e-15 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 76.40 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 214 LYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLgSDAYVVSRSMTQKV 293
Cdd:cd18783 41 LYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 294 SDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAE 373
Cdd:cd18783 120 FGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 374 GNELSRYNV----AIRDIFQVGKTAAFTNakffTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFML 439
Cdd:cd18783 200 PRQRREWDErvarAIRARFAVGRLSNWPQ----TLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNM 265
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
501-705 |
6.82e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.81 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 501 SYPTRPSVQifkNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITidnqdisklncKSLRRHIGIVQQ---E 577
Cdd:NF040873 1 GYGGRPVLH---GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-----------RAGGARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 578 PVLMSGTIRDNITYGL-----TYTPTKEEIRSVAKQCFCHNFITKFPNTydtvigPHGTLlSGGQKQRIAIARALIKKPT 652
Cdd:NF040873 67 PDSLPLTVRDLVAMGRwarrgLWRRLTRDDRAAVDDALERVGLADLAGR------QLGEL-SGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 653 ILILDEATSALDVESEGAINytfgQLMK---SKSMTIVSIAHRLSTIRRSENVIVL 705
Cdd:NF040873 140 LLLLDEPTTGLDAESRERII----ALLAeehARGATVVVVTHDLELVRRADPCVLL 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
513-724 |
7.42e-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: 75.08 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 513 NLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLncKSLRR-HIGIVQ--QEPVLMSG-TIRDN 588
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL--PPHRIaRLGIARtfQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 589 I------------TYGLTYTP----TKEEIRSVAKQC--FCHnfITKFPNTYdtvigphGTLLSGGQKQRIAIARALIKK 650
Cdd:COG0411 100 VlvaaharlgrglLAALLRLPrarrEEREARERAEELleRVG--LADRADEP-------AGNLSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 651 PTILILDEATSAL-DVESEGAINyTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLgHDGSVVEMGKFKELYANP 724
Cdd:COG0411 171 PKLLLLDEPAAGLnPEETEELAE-LIRRLRDERGITILLIEHDMDLVMGlADRIVVL-DFGRVIAEGTPAEVRADP 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
492-705 |
8.35e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQdisKLNCKS----L 567
Cdd:COG3845 5 ALELRGITKRFG---GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSprdaI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEPVLMSG-TIRDNITYGLTYTPT--------KEEIRSVAKQcfchnfitkfpntY------DTVIGPhgtl 632
Cdd:COG3845 79 ALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGgrldrkaaRARIRELSER-------------YgldvdpDAKVED---- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSAL-DVESEGainyTFGQL--MKSKSMTIVSIAHRLSTIRR-SENVIVL 705
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADE----LFEILrrLAAEGKSIIFITHKLREVMAiADRVTVL 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
493-715 |
9.43e-15 |
|
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: 73.85 E-value: 9.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPTrpsVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNckslRRHIG 572
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQEPVLMSG-TIRDNITY-----GLTYTPTKEEIRSvakqcfchnFITKFPntydtvIGPHGTL----LSGGQKQRIA 642
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVYlaqlkGLKKEEARRRIDE---------WLERLE------LSEYANKrveeLSKGNQQKVQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 643 IARALIKKPTILILDEATSALDVESEGAINYTFGQLmKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMG 715
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
467-695 |
1.15e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.00 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 467 RLFELTDRKPSISPTVGHKYKPDRGVIEFKDVSfsyptrpsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTI--ALLLLRY 544
Cdd:PLN03211 50 KFENMKNKGSNIKRILGHKPKISDETRQIQERT----------ILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 545 YNPTTGTITIDNQDISKlncKSLRRhIGIVQQEPVLMSG-TIRDNITY----GLTYTPTKEEIRSVAKQCFCHNFITKFP 619
Cdd:PLN03211 120 GNNFTGTILANNRKPTK---QILKR-TGFVTQDDILYPHlTVRETLVFcsllRLPKSLTKQEKILVAESVISELGLTKCE 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370557 620 NTydtVIGPHGTL-LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKsKSMTIVSIAHRLST 695
Cdd:PLN03211 196 NT---IIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSS 268
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
492-664 |
1.39e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 75.23 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPSVQifkNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlNCKSLRRHI 571
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVD---GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQ----EPVLmsgTIRDNIT-----YGLTYTPTKEEIRSVAKqcfchnfITKFPNTYDTVIGPhgtlLSGGQKQRIA 642
Cdd:PRK13537 83 GVVPQfdnlDPDF---TVRENLLvfgryFGLSAAAARALVPPLLE-------FAKLENKADAKVGE----LSGGMKRRLT 148
|
170 180
....*....|....*....|..
gi 1370557 643 IARALIKKPTILILDEATSALD 664
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
496-725 |
1.53e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 496 KDVSFSYPTRPSVQIFkNLNFkiaPGSSVC-IVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIV 574
Cdd:PRK10575 15 RNVSFRVPGRTLLHPL-SLTF---PAGKVTgLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 575 -QQEPVLMSGTIRDNITYGlTY--------------TPTKEEIRSVAKQCFCHNFITKfpntydtvigphgtlLSGGQKQ 639
Cdd:PRK10575 91 pQQLPAAEGMTVRELVAIG-RYpwhgalgrfgaadrEKVEEAISLVGLKPLAHRLVDS---------------LSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 640 RIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKE 719
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
....*.
gi 1370557 720 LYANPT 725
Cdd:PRK10575 235 LMRGET 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
513-737 |
1.82e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.16 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 513 NLNFKIAPGSSVCIVGPSGRGKS--TIALLLLRYY--NPTTGTITIDNQDISKLNCKSLRRHIG----IVQQEPvlMSGT 584
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvsSLAIMGLIDYpgRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDP--MTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 585 irdNITYGLTYtptkeEIRSVAKQCFCHNFITKFPNTYD--TVIG-----------PHGtlLSGGQKQRIAIARALIKKP 651
Cdd:PRK11022 103 ---NPCYTVGF-----QIMEAIKVHQGGNKKTRRQRAIDllNQVGipdpasrldvyPHQ--LSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 652 TILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANP----TSA 727
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPrhpyTQA 252
|
250
....*....|
gi 1370557 728 LSQLLNEKAA 737
Cdd:PRK11022 253 LLRALPEFAQ 262
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
509-720 |
4.17e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 509 QIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLL--RYYNPTTGTITIDNQDISKLN-CKSLRRHIGIVQQEPVLMSG-T 584
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSpDERARAGIFLAFQYPVEIPGvS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 585 IRD------NITYGLTYTPTK--EEIRSVAKQC-FCHNFITKFPNTydtvigphGtlLSGGQKQRIAIARALIKKPTILI 655
Cdd:COG0396 94 VSNflrtalNARRGEELSAREflKLLKEKMKELgLDEDFLDRYVNE--------G--FSGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370557 656 LDEATSALDVE-----SEGaINytfgqLMKSKSMTIVSIAH--RLSTIRRSENVIVLgHDGSVVEMGKfKEL 720
Cdd:COG0396 164 LDETDSGLDIDalrivAEG-VN-----KLRSPDRGILIITHyqRILDYIKPDFVHVL-VDGRIVKSGG-KEL 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
493-733 |
4.79e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.99 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKD--VSFSYPTrPSVQIFKNLNFKIAPGSSVCIVGPSGRGKS--TIALL-LLRYYNPTTGTITIDNQDISKLNCKSL 567
Cdd:PRK09473 13 LDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqtAFALMgLLAANGRIGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRhigiVQQEPVLMsgTIRDNITYGLTYTPTKEEIRSVAKQcfcHNFITK---FPNT---YDTV----------IGPHGt 631
Cdd:PRK09473 92 NK----LRAEQISM--IFQDPMTSLNPYMRVGEQLMEVLML---HKGMSKaeaFEESvrmLDAVkmpearkrmkMYPHE- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 632 lLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRS-ENVIVLgHDGS 710
Cdd:PRK09473 162 -FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGIcDKVLVM-YAGR 239
|
250 260
....*....|....*....|....
gi 1370557 711 VVEMGKFKELYANPTSALSQ-LLN 733
Cdd:PRK09473 240 TMEYGNARDVFYQPSHPYSIgLLN 263
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
492-725 |
7.08e-14 |
|
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: 75.22 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPT--RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTIT-------IDNQDISKL 562
Cdd:TIGR03269 279 IIKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 563 NCKSLRRHIGIVQQEPVLMS-GTIRDNITYGLTYTPTKEEIRSVA---------KQCFCHNFITKFPNTydtvigphgtl 632
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPhRTVLDNLTEAIGLELPDELARMKAvitlkmvgfDEEKAEEILDKYPDE----------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVV 712
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
250
....*....|...
gi 1370557 713 EMGKFKELYANPT 725
Cdd:TIGR03269 508 KIGDPEEIVEELT 520
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
526-727 |
7.21e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.82 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 526 IVGPSGRGKSTIALLLLRYYNPTTG-----TITIDNQDI-SKLNCKSLRRHIGIVQQEPVLMSGTIRDNITYGL---TYT 596
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVrahKLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 597 PTKEeIRSVAKQCFCHnfitkfPNTYDTV---IGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINY 673
Cdd:PRK14271 132 PRKE-FRGVAQARLTE------VGLWDAVkdrLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1370557 674 TFGQLmkSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYANPTSA 727
Cdd:PRK14271 205 FIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
496-664 |
9.65e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.02 E-value: 9.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 496 KDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLnckslRRHIGIVQ 575
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 576 QEPVLMS-GTIRDNITYGLtytptKEEIRSVAKQCF----CHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKK 650
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGL-----KGQWRDAALQALaavgLADRANEWPAA-----------LSGGQKQRVALARALIHR 151
|
170
....*....|....
gi 1370557 651 PTILILDEATSALD 664
Cdd:PRK11247 152 PGLLLLDEPLGALD 165
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
493-756 |
1.86e-13 |
|
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: 73.68 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 493 IEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLL--LRYYNPTTGTI------------------ 552
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 553 ----------TIDNQDISKLNC-----KSLRRHIGIVQQEPVLMSG--TIRDNITYGLtytptkEEIRSVAKQCfchnfI 615
Cdd:TIGR03269 78 vgepcpvcggTLEPEEVDFWNLsdklrRRIRKRIAIMLQRTFALYGddTVLDNVLEAL------EEIGYEGKEA-----V 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 616 TKFPNTYDTVIGPHGTL-----LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIA 690
Cdd:TIGR03269 147 GRAVDLIEMVQLSHRIThiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTS 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 691 HRLSTIRRSENVIVLGHDGSVVEMGkfkelyaNPTSALSQLLNEKAAPGPSDQQLQIEKVIEKEDL 756
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKEEG-------TPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNV 285
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
511-673 |
2.36e-13 |
|
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: 69.00 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 511 FKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRH-IGIV----QQEPVLMSGTI 585
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 586 RDNITygltytptkeeIRSvakqcfchnfitkfpntydtvigphgtLLSGGQKQRIAIARALIKKPTILILDEATSALDV 665
Cdd:cd03215 96 AENIA-----------LSS---------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
....*...
gi 1370557 666 eseGAINY 673
Cdd:cd03215 138 ---GAKAE 142
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
511-732 |
2.90e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.73 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 511 FKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL----RRHI-----GIVQQEP--- 578
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 579 VLMSGTIRDNIT----------YGltytptkeEIRSVAKQCFCH-----NFITKFPNTYdtvigphgtllSGGQKQRIAI 643
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYG--------DIRATAGDWLERveidaARIDDLPTTF-----------SGGMQQRLQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 644 ARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKELYAN 723
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDD 242
|
....*....
gi 1370557 724 PTSALSQLL 732
Cdd:PRK11701 243 PQHPYTQLL 251
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
492-686 |
4.68e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.52 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKL-NCKSLRRH 570
Cdd:PRK11614 5 MLSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 571 IGIVQQ-EPVLMSGTIRDNITYGLTYTPTKEEIRSVAKqcfchnFITKFPNTYDTVIGPHGTLlSGGQKQRIAIARALIK 649
Cdd:PRK11614 82 VAIVPEgRRVFSRMTVEENLAMGGFFAERDQFQERIKW------VYELFPRLHERRIQRAGTM-SGGEQQMLAIGRALMS 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1370557 650 KPTILILDEATSALDVESEGAINYTFGQLmKSKSMTI 686
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTI 190
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
505-752 |
5.79e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.39 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 505 RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIaLLLLRYYNPT----TGTITIDNQdisKLNCKSLRRHIGIVQQEPVL 580
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTL-MNALAFRSPKgvkgSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 581 M-SGTIRDNITYG----LTYTPTKEEIRSVAKQcfchnFITK--FPNTYDTVIGPHGTL--LSGGQKQRIAIARALIKKP 651
Cdd:TIGR00955 111 IpTLTVREHLMFQahlrMPRRVTKKEKRERVDE-----VLQAlgLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 652 TILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGK-------FKEL---- 720
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSpdqavpfFSDLghpc 265
|
250 260 270
....*....|....*....|....*....|....*..
gi 1370557 721 --YANPTSALSQLLnekaAPGPSDQQ---LQIEKVIE 752
Cdd:TIGR00955 266 peNYNPADFYVQVL----AVIPGSENesrERIEKICD 298
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
514-721 |
5.91e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.66 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 514 LNFKIAPGSSVCIVGPSGRGKSTiallLLRYYnptTGTITIDNQDISKL---------------NCKSLRRHIG-IVQQE 577
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKST----LLRHL---SGLITGDKSAGSHIellgrtvqregrlarDIRKSRANTGyIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 578 PVLMSGTIRDNITYG-LTYTP---------TKEEiRSVAKQCFCHNFITKFpnTYDTVigphgTLLSGGQKQRIAIARAL 647
Cdd:PRK09984 96 NLVNRLSVLENVLIGaLGSTPfwrtcfswfTREQ-KQRALQALTRVGMVHF--AHQRV-----STLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 648 IKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLS-TIRRSENVIVL--GH---DGSVVEMG--KFKE 719
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVALrqGHvfyDGSSQQFDneRFDH 247
|
..
gi 1370557 720 LY 721
Cdd:PRK09984 248 LY 249
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
502-724 |
1.30e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.12 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 502 YPTRPSVqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDnqdisklnckslrRHIGIVQQEPVLM 581
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 582 SGTIRDNItygLTYTPTKEE-IRSVAKQCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEAT 660
Cdd:PTZ00243 734 NATVRGNI---LFFDEEDAArLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 661 SALDVE-SEGAINYTFGQLMKSKsmTIVSIAHRLSTIRRSENVIVLGhDGSVVEMGKFKELYANP 724
Cdd:PTZ00243 811 SALDAHvGERVVEECFLGALAGK--TRVLATHQVHVVPRADYVVALG-DGRVEFSGSSADFMRTS 872
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
179-437 |
1.42e-12 |
|
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: 69.08 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 179 IGMSIPKVIGIVLDTLKTSSGSDFFDLKIpifslplyefLSFFTVALLIGCAaNFGRFILLRILSERVVARLRANVIKKT 258
Cdd:cd18555 17 LTLLIPILTQYVIDNVIVPGNLNLLNVLG----------IGILILFLLYGLF-SFLRGYIIIKLQTKLDKSLMSDFFEHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 259 LHQDAEFFDNHKVGDLISRLGSDAYVvsRSM-TQKVSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFGK 337
Cdd:cd18555 86 LKLPYSFFENRSSGDLLFRANSNVYI--RQIlSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 338 QIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVL 417
Cdd:cd18555 164 KIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLIL 243
|
250 260
....*....|....*....|
gi 1370557 418 AYGSYLVLQSQLSIGDLTAF 437
Cdd:cd18555 244 WIGAYLVINGELTLGELIAF 263
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
499-707 |
1.60e-12 |
|
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: 68.13 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 499 SFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlNCKSLRRHIGIV--QQ 576
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 577 E------PVLMSGTIRDNItYGLTYTPTKEEIRSVAKQCFCHNFItkfpntyDTVIgphgTLLSGGQKQRIAIARALIKK 650
Cdd:cd03267 104 TqlwwdlPVIDSFYLLAAI-YDLPPARFKKRLDELSELLDLEELL-------DTPV----RQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 651 PTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLGH 707
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDK 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
513-724 |
1.85e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.09 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 513 NLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHiGIV---QQEPVLMSGTIRDN- 588
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVrtfQHVRLFREMTVIENl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 589 -----------ITYGLTYTPT--KEEIRSVAKQCFCHNFI--TKFPNTydtvigPHGTlLSGGQKQRIAIARALIKKPTI 653
Cdd:PRK11300 102 lvaqhqqlktgLFSGLLKTPAfrRAESEALDRAATWLERVglLEHANR------QAGN-LAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370557 654 LILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLGHdGSVVEMGKFKELYANP 724
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQ-GTPLANGTPEEIRNNP 245
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
501-658 |
1.98e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 67.75 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 501 SYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKST---IALLLLRyynPTTGTITIDNQDISKLnckSL----RRHIGI 573
Cdd:COG1137 12 SYGKRTVV---KDVSLEVNQGEIVGLLGPNGAGKTTtfyMIVGLVK---PDSGRIFLDGEDITHL---PMhkraRLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 574 VQQEPVLMSG-TIRDNITYGL-TYTPTKEEIRSVAKQcFCHNF-ITKFPNTYdtvigphGTLLSGGQKQRIAIARALIKK 650
Cdd:COG1137 83 LPQEASIFRKlTVEDNILAVLeLRKLSKKEREERLEE-LLEEFgITHLRKSK-------AYSLSGGERRRVEIARALATN 154
|
....*...
gi 1370557 651 PTILILDE 658
Cdd:COG1137 155 PKFILLDE 162
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
506-709 |
2.20e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 506 PSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTT--GTITIDNQDISKLNCK-SLRRHIGIVQQEPVLMS 582
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRdTERAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 583 GTirdnitygltytptkeeirSVAKQCFCHNFITKFPNT-YDTV--------------IGPHGTL--LSGGQKQRIAIAR 645
Cdd:PRK13549 96 EL-------------------SVLENIFLGNEITPGGIMdYDAMylraqkllaqlkldINPATPVgnLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370557 646 ALIKKPTILILDEATSALdVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDG 709
Cdd:PRK13549 157 ALNKQARLLILDEPTASL-TESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
509-664 |
3.07e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 509 QIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS-LRRHIGIVQQEP-VLMSGTIR 586
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEAsIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 587 DNITYGLTYTP--TKEEIRSVAKQCFCHNFITKFPNTYdtvigphGTLLSGGQKQRIAIARALIKKPTILILDEATSALD 664
Cdd:PRK10895 97 DNLMAVLQIRDdlSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
492-720 |
3.78e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.83 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNckslRRHI 571
Cdd:COG4152 1 MLELKGLTKRFGDKTAV---DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVL---MsgTIRDNITY-----GLTytptKEEIRSVAKQcfchnFITKF---PNTYDTVigphGTLlSGGQKQR 640
Cdd:COG4152 74 GYLPEERGLypkM--KVGEQLVYlarlkGLS----KAEAKRRADE-----WLERLglgDRANKKV----EEL-SKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 641 IAIARALIKKPTILILDEATSALDvesegAINytfGQLMKS-------KSMTIVSIAHRLSTIRR-SENVIVLgHDGSVV 712
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLD-----PVN---VELLKDvirelaaKGTTVIFSSHQMELVEElCDRIVII-NKGRKV 208
|
....*...
gi 1370557 713 EMGKFKEL 720
Cdd:COG4152 209 LSGSVDEI 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
492-707 |
4.73e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQdisklncksLRrhI 571
Cdd:PRK09544 4 LVSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVLmsgtirdNITYGLTYTptkeeirsvakqcfchNFITKFPNTYDTVIGP------HGTL-------LSGGQK 638
Cdd:PRK09544 70 GYVPQKLYL-------DTTLPLTVN----------------RFLRLRPGTKKEDILPalkrvqAGHLidapmqkLSGGET 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 639 QRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIR-RSENVIVLGH 707
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMaKTDEVLCLNH 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
507-709 |
8.63e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.31 E-value: 8.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 507 SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTT--GTITIDNQDISKLNCKSL-RRHIGIVQQEPVLMSG 583
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 584 -TIRDNITYGLTYTPTKEEIRSVAKQCFCHNFITKFPNTYDTVIGPHGTLlSGGQKQRIAIARALIKKPTILILDEATSA 662
Cdd:TIGR02633 93 lSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDY-GGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1370557 663 LdVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDG 709
Cdd:TIGR02633 172 L-TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
470-670 |
8.86e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 470 ELTDRKPSISPTVGHKykpdrgVIEFKDVSfsyptRPSVqiFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTT 549
Cdd:COG1129 240 ELEDLFPKRAAAPGEV------VLEVEGLS-----VGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADS 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 550 GTITIDNQDISKLNCK-SLRRHIGIV----QQEPVLMSGTIRDNIT---------YGLTytPTKEEIRSVAKqcfchnFI 615
Cdd:COG1129 307 GEIRLDGKPVRIRSPRdAIRAGIAYVpedrKGEGLVLDLSIRENITlasldrlsrGGLL--DRRRERALAEE------YI 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 616 TKF---PNTYDTVIGphgtLLSGGQKQRIAIARALIKKPTILILDEATSALDVeseGA 670
Cdd:COG1129 379 KRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV---GA 429
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
487-680 |
9.70e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 487 KPDRGVIEFKDVSfsYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKS 566
Cdd:COG3845 252 EPGEVVLEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 567 LRRH-IGIVQQEP----VLMSGTIRDNITYGLTYTPT--------KEEIRSVAKQCfchnfITKF---PNTYDTVIGphg 630
Cdd:COG3845 330 RRRLgVAYIPEDRlgrgLVPDMSVAENLILGRYRRPPfsrggfldRKAIRAFAEEL-----IEEFdvrTPGPDTPAR--- 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1370557 631 tLLSGGQKQRIAIARALIKKPTILILDEATSALDVeseGAINYTFGQLMK 680
Cdd:COG3845 402 -SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV---GAIEFIHQRLLE 447
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
492-671 |
1.36e-11 |
|
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: 68.04 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQdisklnckslrRHI 571
Cdd:TIGR03719 322 VIEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-----------VKL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEpvlmsgtiRDNItygltyTPTK---EEI-----------RSVAKQCFCHNFITKFPNTYDTVigphgTLLSGGQ 637
Cdd:TIGR03719 388 AYVDQS--------RDAL------DPNKtvwEEIsggldiiklgkREIPSRAYVGRFNFKGSDQQKKV-----GQLSGGE 448
|
170 180 190
....*....|....*....|....*....|....
gi 1370557 638 KQRIAIARALIKKPTILILDEATSALDVESEGAI 671
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRAL 482
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
479-664 |
1.40e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 479 SPTVGHKYKPDRGVIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTiaLLLL-------RYYNPTT-- 549
Cdd:PRK10938 247 EPSARHALPANEPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKST--LLSLitgdhpqGYSNDLTlf 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 550 -------GTItidnQDIsklnckslRRHIGIVQQEPVL---MSGTIRDNITYGL-----TYTPTKEEIRSVAKQcfchnf 614
Cdd:PRK10938 322 grrrgsgETI----WDI--------KKHIGYVSSSLHLdyrVSTSVRNVILSGFfdsigIYQAVSDRQQKLAQQ------ 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 615 itkfpntYDTVIGPHGTL-------LSGGQkQRIA-IARALIKKPTILILDEATSALD 664
Cdd:PRK10938 384 -------WLDILGIDKRTadapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
492-740 |
2.16e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.17 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL---R 568
Cdd:PRK11831 7 LVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 569 RHIGIVQQEPVLMSG-TIRDNITYgltytPTKEEIRSVAkqcfchnfitkfPNTYDTV------IGPHGTL------LSG 635
Cdd:PRK11831 84 KRMSMLFQSGALFTDmNVFDNVAY-----PLREHTQLPA------------PLLHSTVmmkleaVGLRGAAklmpseLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 636 GQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMG 715
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
|
250 260
....*....|....*....|....*
gi 1370557 716 KFKELYANPTSALSQLLnEKAAPGP 740
Cdd:PRK11831 227 SAQALQANPDPRVRQFL-DGIADGP 250
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
520-706 |
4.83e-11 |
|
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: 61.62 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 520 PGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIvqqepvlmsgtirdnitygltytptk 599
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 600 eeirsvakqcfchnfitkfpntydtviGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAIN-----YT 674
Cdd:smart00382 55 ---------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRL 107
|
170 180 190
....*....|....*....|....*....|....*...
gi 1370557 675 FGQLMKSKSMTIVSIAHRLS------TIRRSENVIVLG 706
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLL 145
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
497-722 |
5.11e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 497 DVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQ--DISKLNCKSLRRHIGIV 574
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 575 QQEP--VLMSGTIRDNITYGLTYTPTKEE---------IRSVAKQCFCHNFITkfpntydtvigphgtLLSGGQKQRIAI 643
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSLRNLGVPEAeitrrvdeaLTLVDAQHFRHQPIQ---------------CLSHGQKKRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 644 ARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSiAHRLSTIRR-SENVIVLGHdGSVVEMGKFKELYA 722
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEiSDAVYVLRQ-GQILTHGAPGEVFA 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
511-709 |
6.23e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 511 FKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSlRRHIGIV------QQEPVLMSGT 584
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 585 IRDNiTYGLTYT-------PTKEeiRSVAKQcFCHNFITKFPNTYDTVIGphgtlLSGGQKQRIAIARALIKKPTILILD 657
Cdd:PRK15439 358 LAWN-VCALTHNrrgfwikPARE--NAVLER-YRRALNIKFNHAEQAART-----LSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 658 EATSALDVESEGAInYtfgQLMKS---KSMTIVSIAHRLSTIRR-SENVIVLgHDG 709
Cdd:PRK15439 429 EPTRGVDVSARNDI-Y---QLIRSiaaQNVAVLFISSDLEEIEQmADRVLVM-HQG 479
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
245-439 |
7.99e-11 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 63.67 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 245 RVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGS----DAYVVSRSMTqkvsdGVKALICGVVGVGMMCSLSPQLSIL 320
Cdd:cd18588 72 RIDAELGARLFRHLLRLPLSYFESRQVGDTVARVRElesiRQFLTGSALT-----LVLDLVFSVVFLAVMFYYSPTLTLI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 321 LLFFTPPVLFSASVFGKQIRNTSKDLQ----EATGQLTrvaeEQLSGIKTVQSFVAEG-------NELSRYnvaIRDIFQ 389
Cdd:cd18588 147 VLASLPLYALLSLLVTPILRRRLEEKFqrgaENQSFLV----ETVTGIETVKSLAVEPqfqrrweELLARY---VKASFK 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1370557 390 VGKTAAFTNakffTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAF-ML 439
Cdd:cd18588 220 TANLSNLAS----QIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFnML 266
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
510-667 |
1.07e-10 |
|
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: 61.61 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNcKSLRRHI-------GIvqqEPVLms 582
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENIlylghlpGL---KPEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 583 gTIRDNITYgltYTPTkeeirSVAKQCFCHNFITK-----FPNTydtvigPHGTLlSGGQKQRIAIARALIKKPTILILD 657
Cdd:TIGR01189 89 -SALENLHF---WAAI-----HGGAQRTIEDALAAvgltgFEDL------PAAQL-SAGQQRRLALARLWLSRRPLWILD 152
|
170
....*....|
gi 1370557 658 EATSALDVES 667
Cdd:TIGR01189 153 EPTTALDKAG 162
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
512-720 |
1.41e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.57 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 512 KNLNFKIAPGSSVCIVGPSGRGKST-IALL--LLRyynPTTGTITIDNQDISKlNCKSLRRHIGIV----QQ----EPVL 580
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTtIKMLtgILV---PTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrSQlwwdLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 581 MSGTIRDNItYGLTYTPTKEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKKPTILILDEAT 660
Cdd:COG4586 115 DSFRLLKAI-YRIPDAEYKKRLDELVELLDLGELLDTPVRQ-----------LSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370557 661 SALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLGHdGSVVEMGKFKEL 720
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDH-GRIIYDGSLEEL 242
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
496-667 |
1.63e-10 |
|
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: 64.57 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 496 KDVSFSYPtrPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRyynpttgtIT--IDnQDISKLNCKSLRRHIGI 573
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKST----LLR--------IMagVD-KDFNGEARPQPGIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 574 VQQEPVL-MSGTIRDNITYGLTYT----------------PTKEEIRSVAKQ---------CFCHNFITKFPNTYDTVIG 627
Cdd:TIGR03719 73 LPQEPQLdPTKTVRENVEEGVAEIkdaldrfneisakyaePDADFDKLAAEQaelqeiidaADAWDLDSQLEIAMDALRC 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1370557 628 PHG----TLLSGGQKQRIAIARALIKKPTILILDEATSALDVES 667
Cdd:TIGR03719 153 PPWdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
469-691 |
2.14e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 469 FELTDRKPSISPTvghKYKPDRGVIEFKDVSFSYPTRP-SVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNP 547
Cdd:PRK10522 302 LALAPYKAEFPRP---QAFPDWQTLELRNVTFAYQDNGfSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 548 TTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNityGLTYTPTK-----EEIRSVAKQCFCHNFITKfpnty 622
Cdd:PRK10522 376 QSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPE---GKPANPALvekwlERLKMAHKLELEDGRISN----- 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 623 dtvigphgTLLSGGQKQRIAIARALIKKPTILILDEATSALDVEsegaINYTFGQ----LMKSKSMTIVSIAH 691
Cdd:PRK10522 448 --------LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH----FRREFYQvllpLLQEMGKTIFAISH 508
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
491-672 |
3.61e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.95 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 491 GVIEFKDVSFSYPT-RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIA-LLLLRYYNPT-TGTITIDNQDISklncKSL 567
Cdd:cd03232 2 SVLTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLdVLAGRKTAGViTGEILINGRPLD----KNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 568 RRHIGIVQQEPVLMSG-TIRDNITYgltytptkeeirsvakqcfchnfitkfpntydtvigpHGTL--LSGGQKQRIAIA 644
Cdd:cd03232 78 QRSTGYVEQQDVHSPNlTVREALRF-------------------------------------SALLrgLSVEQRKRLTIG 120
|
170 180
....*....|....*....|....*...
gi 1370557 645 RALIKKPTILILDEATSALDveSEGAIN 672
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLD--SQAAYN 146
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
214-471 |
4.27e-10 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain] Cd Length: 294 Bit Score: 61.72 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 214 LYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSD---AYVVSRSMT 290
Cdd:cd18569 41 LRPLLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRVQSNdrvANLLSGQLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 291 QKVSDGVKALICGVVgvgmMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAeeqLSGIKTVQSF 370
Cdd:cd18569 121 TTVLNLVMAVFYALL----MLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTT---MSGLQMIETL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 371 VAEGNE----------LSRYNVAIRdifQVGKTAAFTNAkfftTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAF-ML 439
Cdd:cd18569 194 KASGAEsdffsrwagyQAKVLNAQQ---ELGRTNQLLGA----LPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFqSL 266
|
250 260 270
....*....|....*....|....*....|..
gi 1370557 440 yteytgnavfgLSTFYSEIMQGAGAASRLFEL 471
Cdd:cd18569 267 -----------MASFLAPVNSLVGLGGTLQEM 287
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
503-664 |
4.41e-10 |
|
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: 59.97 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 503 PTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKST----IALLLLRYYNPTtGTITIDNQDiSKLNCKSLRRHIGIVQQEP 578
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIP-YKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 579 VLMSgtirdnitygltyTPTKEEIRSVAKQCFCHNFITKFpntydtvigphgtllSGGQKQRIAIARALIKKPTILILDE 658
Cdd:cd03233 93 VHFP-------------TLTVRETLDFALRCKGNEFVRGI---------------SGGERKRVSIAEALVSRASVLCWDN 144
|
....*.
gi 1370557 659 ATSALD 664
Cdd:cd03233 145 STRGLD 150
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
497-664 |
4.78e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 497 DVSFSYPTRPSVQifkNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQ 576
Cdd:PRK13540 6 ELDFDYHDQPLLQ---QISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 577 EPVLMSGTIRDNITYGLTYTPTKEEIRSVAKqcfchnfITKFPNTYDTVIGphgtLLSGGQKQRIAIARALIKKPTILIL 656
Cdd:PRK13540 83 SGINPYLTLRENCLYDIHFSPGAVGITELCR-------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLL 151
|
....*...
gi 1370557 657 DEATSALD 664
Cdd:PRK13540 152 DEPLVALD 159
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
507-691 |
5.08e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 507 SVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRY--YNPTTGTITIDNQDISKLNcKSLRRHIGIVQ--QEPVLMS 582
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFLafQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 583 GTirDNITY-GLTYTptkeeirsvAKQCFcHNFITKFPNTYDTVIGPHGTLL---------------SGGQKQRIAIARA 646
Cdd:CHL00131 98 GV--SNADFlRLAYN---------SKRKF-QGLPELDPLEFLEIINEKLKLVgmdpsflsrnvnegfSGGEKKRNEILQM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1370557 647 LIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSmTIVSIAH 691
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITH 209
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
504-713 |
5.77e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 504 TRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYnPT---TGTITIDNQ-----DISKlnckSLRRHIGIVQ 575
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIRD----SEALGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 576 QE----PVLmsgTIRDNI-------TYGL-----TYTPTKEEIRSVAkqcfchnfITKFPNTYDTVIGPhgtllsgGQKQ 639
Cdd:NF040905 85 QElaliPYL---SIAENIflgneraKRGVidwneTNRRARELLAKVG--------LDESPDTLVTDIGV-------GKQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 640 RIAIARALIKKPTILILDEATSAL-DVESEGAINytfgqLM---KSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVE 713
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-----LLlelKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
496-720 |
8.37e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 496 KDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCK-SLRRHIGIV 574
Cdd:PRK10982 2 SNISKSFP---GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 575 QQE-PVLMSGTIRDNITYGlTYtPTKEEIRSVAKQcfcHNFITKFPNTYDTVIGPHGTL--LSGGQKQRIAIARALIKKP 651
Cdd:PRK10982 79 HQElNLVLQRSVMDNMWLG-RY-PTKGMFVDQDKM---YRDTKAIFDELDIDIDPRAKVatLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370557 652 TILILDEATSALdveSEGAINYTFG--QLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKEL 720
Cdd:PRK10982 154 KIVIMDEPTSSL---TEKEVNHLFTiiRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
502-732 |
9.92e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 502 YPTRPSVqifKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNP----TTGTITIDNQDISKlncKSLR-RHIGIVQQ 576
Cdd:PRK10418 13 QAAQPLV---HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAP---CALRgRKIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 577 EPVLMSGTIRDNITYGltytptKEEIRSVAKQCFCHNFI-----TKFPNTyDTVIGPHGTLLSGGQKQRIAIARALIKKP 651
Cdd:PRK10418 87 NPRSAFNPLHTMHTHA------RETCLALGKPADDATLTaaleaVGLENA-ARVLKLYPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 652 TILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRR-SENVIVLGHdGSVVEMGKFKELYANPTSALSQ 730
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSH-GRIVEQGDVETLFNAPKHAVTR 238
|
..
gi 1370557 731 LL 732
Cdd:PRK10418 239 SL 240
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
514-719 |
1.48e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 514 LNFKIAPGSSVCIVGPSGRGKST----IALLLlryynPTTGTITIDNQDISKLNCKSLRRHIG-IVQQE--PVLMsgtir 586
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTllarMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQtpPFAM----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 587 DNITYGLTYTPTKEEIRSVAKQCfchNFITKFPNTYDTVIGPHGTLlSGGQKQRIAIARALIK-KPTI------LILDEA 659
Cdd:PRK03695 85 PVFQYLTLHQPDKTRTEAVASAL---NEVAEALGLDDKLGRSVNQL-SGGEWQRVRLAAVVLQvWPDInpagqlLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370557 660 TSALDVESEGAInYTFGQLMKSKSMTIVSIAHRLS-TIRRSENVIVLgHDGSVVEMGKFKE 719
Cdd:PRK03695 161 MNSLDVAQQAAL-DRLLSELCQQGIAVVMSSHDLNhTLRHADRVWLL-KQGKLLASGRRDE 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
499-704 |
4.66e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 499 SFSYptrpsVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDnQD--ISKLnckslrrhigivQQ 576
Cdd:PRK11147 12 SFSD-----APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDliVARL------------QQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 577 EPVL-MSGTIRDNITYGL--------TY---------TPTKEEIRSVAK--QCFCHNFITKFPNTYDTVIG-----PHGT 631
Cdd:PRK11147 74 DPPRnVEGTVYDFVAEGIeeqaeylkRYhdishlvetDPSEKNLNELAKlqEQLDHHNLWQLENRINEVLAqlgldPDAA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 632 L--LSGGQKQRIAIARALIKKPTILILDEATSALDVEsegAINYtFGQLMKSKSMTIVSIAHRLSTIRRSENVIV 704
Cdd:PRK11147 154 LssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE---TIEW-LEGFLKTFQGSIIFISHDRSFIRNMATRIV 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
510-706 |
5.45e-09 |
|
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: 56.73 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNI 589
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 590 TYGLTYTPTKEEIRSVAKQCFchnfitkfpNTYDTVigPHGTLlSGGQKQRIAIARALIKKPTILILDEATSALDVESEG 669
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGL---------NGFEDR--PVAQL-SAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1370557 670 AINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLG 706
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
492-666 |
7.04e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDnqdiSKLNCKSLRRHI 571
Cdd:PRK11147 319 VFEMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVAYFDQHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVLMsgtirDNITYGltytptKEEI------RSVAKqcFCHNFItkFPntydtvigPHGTL-----LSGGQKQR 640
Cdd:PRK11147 392 AELDPEKTVM-----DNLAEG------KQEVmvngrpRHVLG--YLQDFL--FH--------PKRAMtpvkaLSGGERNR 448
|
170 180
....*....|....*....|....*.
gi 1370557 641 IAIARALIKKPTILILDEATSALDVE 666
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
492-670 |
1.17e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 492 VIEFKDVSFSYPTRpsvQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDnqDISKLnckslrrhi 571
Cdd:PRK11819 324 VIEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETVKL--------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEpvlmsgtiRDNItygltyTPTK---EEI-----------RSVAKQCFCHNFITKFPNTYDTVigphGTlLSGGQ 637
Cdd:PRK11819 390 AYVDQS--------RDAL------DPNKtvwEEIsggldiikvgnREIPSRAYVGRFNFKGGDQQKKV----GV-LSGGE 450
|
170 180 190
....*....|....*....|....*....|...
gi 1370557 638 KQRIAIARALIKKPTILILDEATSALDVESEGA 670
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRA 483
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
265-437 |
1.33e-08 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of 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: 350052 [Multi-domain] Cd Length: 294 Bit Score: 57.17 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 265 FFDNHKVGDLISRLGSDAYVvsRSM--TQKVS---DGvkALICGVVGVgmMCSLSPQL-SILLLFFTPPVLFSASVFGKQ 338
Cdd:cd18779 92 FFQQRSTGDLLMRLSSNATI--RELltSQTLSallDG--TLVLGYLAL--LFAQSPLLgLVVLGLAALQVALLLATRRRV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 339 IRNTSKDLQ---EATGQLTrvaeEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLT 415
Cdd:cd18779 166 RELMARELAaqaEAQSYLV----EALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLV 241
|
170 180
....*....|....*....|..
gi 1370557 416 VLAYGSYLVLQSQLSIGDLTAF 437
Cdd:cd18779 242 LLWVGAWQVLDGQLSLGTMLAL 263
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
494-713 |
1.53e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 494 EFKDVSFSYPtrpSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCK-SLRRHIG 572
Cdd:PRK11288 6 SFDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQE----PVLmsgTIRDNITYGltYTPTK------EEIRSVAKQCFCHnfitkfpntYDTVIGPHGTL--LSGGQKQR 640
Cdd:PRK11288 83 IIYQElhlvPEM---TVAENLYLG--QLPHKggivnrRLLNYEAREQLEH---------LGVDIDPDTPLkyLSIGQRQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 641 IAIARALIKKPTILILDEATSALDV-ESEgainytfgQLM------KSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVE 713
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLSArEIE--------QLFrvirelRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
508-691 |
2.48e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 508 VQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCK---SLR-RHIGIVQQ------- 576
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQsfmlipt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 577 ----EPVLMSGTIRdnityGLTYTPTKEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKKPT 652
Cdd:PRK10584 103 lnalENVELPALLR-----GESSRQSRNGAKALLEQLGLGKRLDHLPAQ-----------LSGGEQQRVALARAFNGRPD 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 1370557 653 ILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAH 691
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
470-720 |
2.92e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 470 ELTDRKPSISPTVGHKYKPDRGVIEFKDVSFSYPTRPSV-QIFKNLNFKIAPGSSVCIVGPSGRGKSTiaLLLLRYYNPT 548
Cdd:TIGR00956 737 DLTDESDDVNDEKDMEKESGEDIFHWRNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTT--LLNVLAERVT 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 549 TGTITIDNQDIS--KLNcKSLRRHIGIVQQEPV-LMSGTIRDNITYGL-----TYTPTKEEIRSVAKqcfchnfITKF-- 618
Cdd:TIGR00956 815 TGVITGGDRLVNgrPLD-SSFQRSIGYVQQQDLhLPTSTVRESLRFSAylrqpKSVSKSEKMEYVEE-------VIKLle 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 619 PNTY-DTVIGPHGTLLSGGQKQRIAIARALIKKPTILI-LDEATSALDVESEGAINytfgQLMKSKSMTIVSIahrLSTI 696
Cdd:TIGR00956 887 MESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSIC----KLMRKLADHGQAI---LCTI 959
|
250 260
....*....|....*....|....
gi 1370557 697 rrsenvivlgHDGSVVEMGKFKEL 720
Cdd:TIGR00956 960 ----------HQPSAILFEEFDRL 973
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
512-709 |
3.01e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 55.70 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 512 KNLNFKIAPGSSVCIVGPSGRGKSTIAllllryyNPTTGTITIDNQDISKLNCKSLRRHIGI--------VQQEPVlmsG 583
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLI-------NDTLYPALARRLHLKKEQPGNHDRIEGLehidkvivIDQSPI---G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 584 -TIRDNityGLTYTPTKEEIRSVakqcFC---------------------------------HNFITKFPNTYDTV---- 625
Cdd:cd03271 82 rTPRSN---PATYTGVFDEIREL----FCevckgkrynretlevrykgksiadvldmtveeaLEFFENIPKIARKLqtlc 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 626 --------IGPHGTLLSGGQKQRIAIARALIKK---PTILILDEATSALDVESEGAINYTFGQLMKsKSMTIVSIAHRLS 694
Cdd:cd03271 155 dvglgyikLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVD-KGNTVVVIEHNLD 233
|
250
....*....|....*
gi 1370557 695 TIRRSENVIVLGHDG 709
Cdd:cd03271 234 VIKCADWIIDLGPEG 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
506-696 |
4.24e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 506 PSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCK-SLRRHIGIVQQEPVLMSG- 583
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKsSQEAGIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 584 TIRDNITYGLTYTPT------KEEIRSVAKqcfchnFITKFPNTY--DTVIGPhgtlLSGGQKQRIAIARALIKKPTILI 655
Cdd:PRK10762 95 TIAENIFLGREFVNRfgridwKKMYAEADK------LLARLNLRFssDKLVGE----LSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1370557 656 LDEATSAL-DVESEG---AINYtfgqlMKSKSMTIVSIAHRLSTI 696
Cdd:PRK10762 165 MDEPTDALtDTETESlfrVIRE-----LKSQGRGIVYISHRLKEI 204
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
192-439 |
5.14e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 55.28 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 192 DTLKTSSGSDFFDLKIPIFSLPLYEFL----SFFTVALL-IGCAANFGRFILLRILSERVVA--------RLRANVIKKT 258
Cdd:cd18566 6 QVLLASLFINILALATPLFILQVYDRVipneSIPTLQVLvIGVVIAILLESLLRLLRSYILAwigarfdhRLSNAAFEHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 259 LHQDAEFFDNHKVGDLISRLGSdayvvsrsmTQKVSD---GVKALIC-----GVVGVGMMCSLSPQLSILLLFFTPPVLF 330
Cdd:cd18566 86 LSLPLSFFEREPSGAHLERLNS---------LEQIREfltGQALLALldlpfVLIFLGLIWYLGGKLVLVPLVLLGLFVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 331 SASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNV----AIRDIFQVGKTAAFTNakffTTTS 406
Cdd:cd18566 157 VAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERlqanAAYAGFKVAKINAVAQ----TLGQ 232
|
250 260 270
....*....|....*....|....*....|...
gi 1370557 407 LLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFML 439
Cdd:cd18566 233 LFSQVSMVAVVAFGALLVINGDLTVGALIACTM 265
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
470-706 |
8.99e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 470 ELTDRKPSISPTVGhkykpdRGVIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKS-TIALLLLRYYNPT 548
Cdd:PRK13549 243 ELTALYPREPHTIG------EVILEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRW 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 549 TGTITIDNQDISKLNC-KSLRRHI----------GIVqqePVLMSGtirDNITYG-LTYTPTKEEIRSVAKQCFCHNFIT 616
Cdd:PRK13549 317 EGEIFIDGKPVKIRNPqQAIAQGIamvpedrkrdGIV---PVMGVG---KNITLAaLDRFTGGSRIDDAAELKTILESIQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 617 KFpntydTVIGPHGTL----LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSkSMTIVSIAHR 692
Cdd:PRK13549 391 RL-----KVKTASPELaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSE 464
|
250
....*....|....*
gi 1370557 693 LSTIR-RSENVIVLG 706
Cdd:PRK13549 465 LPEVLgLSDRVLVMH 479
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
464-672 |
9.22e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 464 AASRL-----FELTDRKPS--ISPTVGHKY--KPDRGVIEFKDVSFSYPTRPsvqIFKNLNFKIAPGSSVCIVGPSGRGK 534
Cdd:PRK15064 282 ATSRAkqidkIKLEEVKPSsrQNPFIRFEQdkKLHRNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 535 STIALLLLRYYNPTTGTIT-IDN-------QDISK--LNCKSLRRHIGIVQQEpvlmsgtiRDNITygltytptkeEIRS 604
Cdd:PRK15064 359 TTLLRTLVGELEPDSGTVKwSENanigyyaQDHAYdfENDLTLFDWMSQWRQE--------GDDEQ----------AVRG 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 605 V-AKQCFCHNFITKFPNtydtvigphgtLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAIN 672
Cdd:PRK15064 421 TlGRLLFSQDDIKKSVK-----------VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLN 478
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
512-687 |
1.09e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 512 KNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSL-----------RRHIGIVQQEPVL 580
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangivyisedRKRDGLVLGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 581 --MSGTIRDNITYGLTYTPTKEEIRSVAKqcFCHNFITKFPNTyDTVIGphgtLLSGGQKQRIAIARALIKKPTILILDE 658
Cdd:PRK10762 349 enMSLTALRYFSRAGGSLKHADEQQAVSD--FIRLFNIKTPSM-EQAIG----LLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190
....*....|....*....|....*....|..
gi 1370557 659 ATSALDVESEGAInYtfgQLM---KSKSMTIV 687
Cdd:PRK10762 422 PTRGVDVGAKKEI-Y---QLInqfKAEGLSII 449
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
526-666 |
1.28e-07 |
|
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: 53.57 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 526 IVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKlncKSlrrhigivQQEPVLMSGTIRDNITygltytptkEEIRSV 605
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY---KP--------QYIKADYEGTVRDLLS---------SITKDF 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370557 606 AKQCFCHNFITKfPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVE 666
Cdd:cd03237 90 YTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
505-715 |
1.83e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 505 RPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYYN------------PTTGTITIDNQDISKLNCKSLRRHIG 572
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKST----LLKALAgdltgggaprgaRVTGDVTLNGEPLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQQ--EPVLmSGTIRDNITYG-----LTYTPTKEEIRSVAKQCFCHNfitkfpnTYDTVIGPHGTLLSGGQKQRIAIAR 645
Cdd:PRK13547 87 VLPQaaQPAF-AFSAREIVLLGryphaRRAGALTHRDGEIAWQALALA-------GATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370557 646 AL---------IKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMG 715
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
511-743 |
2.95e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.58 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 511 FKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLrrhIGIVQQ------------EP 578
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQseevdwsfpvlvED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 579 VLMSGTIRDnitYGLTYTPTKEEirsvakqcfcHNFITKFPNTYDTVIGPHGTL--LSGGQKQRIAIARALIKKPTILIL 656
Cdd:PRK15056 100 VVMMGRYGH---MGWLRRAKKRD----------RQIVTAALARVDMVEFRHRQIgeLSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 657 DEATSALDVESEGAINYTFGQLMKSKSMTIVSiAHRLSTIRRSENVIVLgHDGSVVEMGKFKELY--ANPTSALSQLLNE 734
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDEGKTMLVS-THNLGSVTEFCDYTVM-VKGTVLASGPTETTFtaENLELAFSGVLRH 244
|
....*....
gi 1370557 735 KAAPGPSDQ 743
Cdd:PRK15056 245 VALNGSEES 253
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
477-706 |
3.02e-07 |
|
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: 53.68 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 477 SISPTVGHKYKPDrgVIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKS-TIALLLLRYYNPTTGTITID 555
Cdd:TIGR02633 244 SLYPHEPHEIGDV--ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFIN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 556 NQDISKLNC-KSLRRHIGIVQQE-------PVLMSGtirDNITYG-LTYTPTKEEIRSVAKQCFCHNFITKFPNTYDTVI 626
Cdd:TIGR02633 322 GKPVDIRNPaQAIRAGIAMVPEDrkrhgivPILGVG---KNITLSvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPF 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 627 GPHGTlLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKsKSMTIVSIAHRLSTIRR-SENVIVL 705
Cdd:TIGR02633 399 LPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGlSDRVLVI 476
|
.
gi 1370557 706 G 706
Cdd:TIGR02633 477 G 477
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
512-707 |
3.62e-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: 50.78 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 512 KNLNFKIAPGSSVCIVGPSGRGKSTIAllllryynpttgtitidNQDISKLNCKSLRRHIGIVQQEPVLMSGTIRDNITY 591
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLV-----------------NEGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 592 GLTYTPTKEEIRSvakqcfchnfitkfpntydtvigphgtlLSGGQKQRIAIARALIK--KPTILILDEATSALDVEseg 669
Cdd:cd03238 75 GLGYLTLGQKLST----------------------------LSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQ--- 123
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1370557 670 aINYTFGQLMK---SKSMTIVSIAHRLSTIRRSENVIVLGH 707
Cdd:cd03238 124 -DINQLLEVIKgliDLGNTVILIEHNLDVLSSADWIIDFGP 163
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
626-709 |
6.03e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.09 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 626 IGPHGTLLSGGQKQRIAIARALIKK---PTILILDEATSALDVESEGAINYTFGQLmKSKSMTIVSIAHRLSTIRRSENV 702
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVIKTADYI 901
|
....*..
gi 1370557 703 IVLGHDG 709
Cdd:TIGR00630 902 IDLGPEG 908
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
509-744 |
6.45e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.33 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 509 QIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLL--RYYNPTTGTITIDNQDISKLNCKSlRRHIGIVQ--QEPVLMSGT 584
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFMafQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 585 irDNITYGLTYTPTKEEIRSVAK------QCFCHNFITKFPNTYDTVIGPHGTLLSGGQKQRIAIARALIKKPTILILDE 658
Cdd:PRK09580 94 --SNQFFLQTALNAVRSYRGQEPldrfdfQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 659 ATSALDVESEGAINYTFGQLMKSK-SMTIVSIAHRLSTIRRSENVIVLgHDGSVVEMGKFkelyanptsALSQLLNEKAA 737
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSLRDGKrSFIIVTHYQRILDYIKPDYVHVL-YQGRIVKSGDF---------TLVKQLEEQGY 241
|
....*..
gi 1370557 738 PGPSDQQ 744
Cdd:PRK09580 242 GWLTEQQ 248
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
633-732 |
7.24e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.11 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVV 712
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90 100
....*....|....*....|
gi 1370557 713 EMGKFKELYANPTSALSQLL 732
Cdd:PRK15093 239 ETAPSKELVTTPHHPYTQAL 258
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
496-667 |
7.64e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 496 KDVSFSYPtrPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTiallLLRYY----NPTTGTITIDnQDISklnckslrrhI 571
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMagvdKEFEGEARPA-PGIK----------V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 572 GIVQQEPVL-MSGTIRDNITYGLTYTPTK----EEIRS------------VAKQcfchnfiTKFPNTYDTVIG------- 627
Cdd:PRK11819 73 GYLPQEPQLdPEKTVRENVEEGVAEVKAAldrfNEIYAayaepdadfdalAAEQ-------GELQEIIDAADAwdldsql 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1370557 628 ---------PHG----TLLSGGQKQRIAIARALIKKPTILILDEATSALDVES 667
Cdd:PRK11819 146 eiamdalrcPPWdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
505-693 |
8.28e-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: 53.09 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 505 RPSVQifkNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDIsKLNCKSLRRHIGIVQQEPVLMSG- 583
Cdd:TIGR01257 943 RPAVD---RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHl 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 584 TIRDNITY-----GLTYTPTKEEIRSVAKQCFCHNfiTKFPNTYDtvigphgtlLSGGQKQRIAIARALIKKPTILILDE 658
Cdd:TIGR01257 1019 TVAEHILFyaqlkGRSWEEAQLEMEAMLEDTGLHH--KRNEEAQD---------LSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190
....*....|....*....|....*....|....*.
gi 1370557 659 ATSALDVESEGAInytFGQLMKSKS-MTIVSIAHRL 693
Cdd:TIGR01257 1088 PTSGVDPYSRRSI---WDLLLKYRSgRTIIMSTHHM 1120
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
514-719 |
9.01e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 50.99 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 514 LNFKIAPGSSVCIVGPSGRGKSTiaLL-----LLRYynptTGTITIDNQDISKLNCKSLRRHIGIV--QQEPVLMSGtir 586
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST--LLarmagLLPG----QGEILLNGRPLSDWSAAELARHRAYLsqQQSPPFAMP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 587 dnityGLTY--------TPTKEEIRSVAKQCFCHNFITKFPNtydtvigpHGTLLSGGQKQRIAIARALIK-KPTI---- 653
Cdd:COG4138 86 -----VFQYlalhqpagASSEAVEQLLAQLAEALGLEDKLSR--------PLTQLSGGEWQRVRLAAVLLQvWPTInpeg 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370557 654 --LILDEATSALDVESEGAInYTFGQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSVVEMGKFKE 719
Cdd:COG4138 153 qlLLLDEPMNSLDVAQQAAL-DRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
470-665 |
1.82e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 470 ELTDRKPSISPTVGHKykpdrgVIEFKDVSFSYPTRPSVQIFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLL-RYY-NP 547
Cdd:NF040905 241 DLEDRYPERTPKIGEV------VFEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYgRN 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 548 TTGTITIDNQDISKLNCKSL-----------RRHIGIVQQEpvlmsgTIRDNITY-GLTYTPTK------EEIRsVAKQc 609
Cdd:NF040905 315 ISGTVFKDGKEVDVSTVSDAidaglayvtedRKGYGLNLID------DIKRNITLaNLGKVSRRgvidenEEIK-VAEE- 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370557 610 FCHNFITKFPNTYDTVIGphgtlLSGGQKQRIAIARALIKKPTILILDEATSALDV 665
Cdd:NF040905 387 YRKKMNIKTPSVFQKVGN-----LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
510-667 |
4.55e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 48.26 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKSTiaLL-----LLRyynPTTGTITIDNQDISKLnCKSLRR-------HIGIvqqE 577
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTS--LLrilagLAR---PDAGEVLWQGEPIRRQ-RDEYHQdllylghQPGI---K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 578 PVLmsgTIRDNITY--GLTYTPTKEEIRSVAKQcfchnfitkfpntydtvIGPHGTL------LSGGQKQRIAIARALIK 649
Cdd:PRK13538 87 TEL---TALENLRFyqRLHGPGDDEALWEALAQ-----------------VGLAGFEdvpvrqLSAGQQRRVALARLWLT 146
|
170
....*....|....*...
gi 1370557 650 KPTILILDEATSALDVES 667
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQG 164
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
506-664 |
1.73e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 506 PSVQIFKNLNFKIAPGSSVCIVGPSGRGKST----IALLLLRYYNPTTGTIT---IDNQDISK------LNCKSLRRHIG 572
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITydgITPEEIKKhyrgdvVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 573 IVQ-QEPVLMSGTIR--DNITYGLTYTPTKEEIRSVAKQCF--CHNFITKFPNtyDTVIGphgtlLSGGQKQRIAIARAL 647
Cdd:TIGR00956 152 HLTvGETLDFAARCKtpQNRPDGVSREEYAKHIADVYMATYglSHTRNTKVGN--DFVRG-----VSGGERKRVSIAEAS 224
|
170
....*....|....*..
gi 1370557 648 IKKPTILILDEATSALD 664
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLD 241
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
633-714 |
1.78e-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: 46.98 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSALDVEsegainytfgqlmksKSMTIVSIAHRLSTIRRSenVIVLGHDGSVV 712
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDIK---------------QRLNAARLIRELAEDDNY--VLVVEHDLAVL 202
|
..
gi 1370557 713 EM 714
Cdd:cd03236 203 DY 204
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
183-460 |
1.91e-05 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 47.14 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 183 IPKVIGIVLDTLKTSSGsdffdlKIPIFSLPLYEFLSFFTVALLIGCAANFgrfILLRI--LSERvvaRLRANVIKKTLH 260
Cdd:cd18583 15 VPRQLGIIVDSLSGGSG------KSPWKEIGLYVLLRFLQSGGGLGLLRSW---LWIPVeqYSYR---ALSTAAFNHVMN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 261 QDAEFFDNHKVGDLISRL--GSDAYVVSRSMTQKVsdgVKALICGVVGVGMMCSL-SPQLSILLLFFTPPVLFSASVFGK 337
Cdd:cd18583 83 LSMDFHDSKKSGEVLKAIeqGSSINDLLEQILFQI---VPMIIDLVIAIVYLYYLfDPYMGLIVAVVMVLYVWSTIKLTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 338 QIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDI----FQVGKTAAFTNAkfftTTSLLGDLSF 413
Cdd:cd18583 160 WRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYqkaeRKYLFSLNLLNA----VQSLILTLGL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1370557 414 LTVLAYGSYLVLQSQLSIGDLTAFMLY-TEYTGNAVFgLSTFYSEIMQ 460
Cdd:cd18583 236 LAGCFLAAYQVSQGQATVGDFVTLLTYwAQLSGPLNF-FATLYRSIQS 282
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
518-666 |
5.62e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 518 IAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDnQDIS-KlnckslRRHIGIVQQEPV---LMSgtirdnITYGL 593
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISyK------PQYIKPDYDGTVedlLRS------ITDDL 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 594 TYTPTKEEIrsvAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKKPTILILDEATSALDVE 666
Cdd:PRK13409 429 GSSYYKSEI---IKPLQLERLLDKNVKD-----------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
213-347 |
8.18e-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: 45.19 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 213 PLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGSDAYVVSRSMTQK 292
Cdd:cd18580 37 SGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLA 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1370557 293 VSDGVKALICGVVGVGMMCSLSPQLSILLLFFTPPVLFSASVFgkqiRNTSKDLQ 347
Cdd:cd18580 117 LLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYY----LRTSRQLR 167
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
184-461 |
8.69e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 45.29 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 184 PKVIGIVLDTLKTSSgsdFFDLKIPIFSLPLYEFLSFFTVALligcaaNFGRFILLRILSERVVARLRANVIKKTLHQDA 263
Cdd:cd18560 16 PLFLGRAVNALTLAK---VKDLESAVTLILLYALLRFSSKLL------KELRSLLYRRVQQNAYRELSLKTFAHLHSLSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 264 EFFDNHKVGDLISRL--GSDAyvVSRSMTQKVSDGVKALI-CGVVGVGMMCSLSPQLSILLLFFtppvLFSASVFGKQIR 340
Cdd:cd18560 87 DWHLSKKTGEVVRIMdrGTES--ANTLLSYLVFYLVPTLLeLIVVSVVFAFHFGAWLALIVFLS----VLLYGVFTIKVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 341 NTSKDLQEAT----GQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQvgktaafTNAKFFTTTSLLG------- 409
Cdd:cd18560 161 EWRTKFRRAAnkkdNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQK-------SSVKVQASLSLLNvgqqlii 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1370557 410 DLSFLTVLAYGSYLVLQSQLSIGDLTAFMLYTEYTGNAVFGLSTFYSEIMQG 461
Cdd:cd18560 234 QLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQS 285
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
633-665 |
1.04e-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: 45.93 E-value: 1.04e-04
10 20 30
....*....|....*....|....*....|...
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSALDV 665
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
307-439 |
1.15e-04 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 44.74 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 307 VGMMCSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRD 386
Cdd:cd18587 132 LAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAA 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370557 387 IFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDLTAFML 439
Cdd:cd18587 212 LARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVI 264
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
520-665 |
1.38e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 520 PGSSVCIVGPSGRGKSTIALLL--------------------LRYYnptTGTITidnQD-ISKLNCKSLR--RHIGIVQQ 576
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevLKRF---RGTEL---QNyFKKLYNGEIKvvHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 577 EPVLMSGTIRDNitygLTYTPTKEEIRSVAKQCFCHNFITKFPNTydtvigphgtlLSGGQKQRIAIARALIKKPTILIL 656
Cdd:PRK13409 172 IPKVFKGKVREL----LKKVDERGKLDEVVERLGLENILDRDISE-----------LSGGELQRVAIAAALLRDADFYFF 236
|
....*....
gi 1370557 657 DEATSALDV 665
Cdd:PRK13409 237 DEPTSYLDI 245
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
515-731 |
1.59e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 515 NFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIDNQDISKLNCKSLrrhigivQQepvLMSGTIRDNITYGL- 593
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL-------QK---LVSDEWQRNNTDMLs 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 594 -----TYTPTKEEIR-SVAKQCFCHNFITKF--------PNTYdtvigphgtlLSGGQKQRIAIARALIKKPTILILDEA 659
Cdd:PRK10938 93 pgeddTGRTTAEIIQdEVKDPARCEQLAQQFgitalldrRFKY----------LSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 660 TSALDVESEGAINYTFGQLMKSKsMTIVSIAHRLSTIRR-SENVIVLGhDGSVVEMGKFKELYANptSALSQL 731
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQSG-ITLVLVLNRFDEIPDfVQFAGVLA-DCTLAETGEREEILQQ--ALVAQL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
633-666 |
1.70e-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: 45.16 E-value: 1.70e-04
10 20 30
....*....|....*....|....*....|....
gi 1370557 633 LSGGQKQRIAIARALIKKPTILILDEATSALDVE 666
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
625-696 |
1.99e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 1.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370557 625 VIGPHGTLLSGGQKQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVSIAHRLSTI 696
Cdd:cd03222 64 VYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVL 135
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
621-688 |
2.06e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 2.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370557 621 TYDTVIGPhgtlLSGGQKQRIAIARALIKKPTILILDEATSALDVeseGAiNYTFGQLM-----KSKSMTIVS 688
Cdd:PRK10982 384 GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV---GA-KFEIYQLIaelakKDKGIIIIS 448
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
633-709 |
3.02e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 633 LSGGQKQRIAIARALI---KKPTILILDEATSALDVESEGAINYTFgQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDG 709
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVL-QSLTHQGHTVVIIEHNMHVVKVADYVLELGPEG 888
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
210-386 |
9.59e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 42.13 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 210 FSLPLYEFLSFFTVALLIGCAANFGrFILLRILSeRVVARLRA------NVIKKTLHQDAEFFDNHKVGDLISRLGSDAY 283
Cdd:cd18605 33 FFNFINDSFNFFLTVYGFLAGLNSL-FTLLRAFL-FAYGGLRAarrlhnKLLSSILFAKMSFFDKTPVGRILNRFSSDVY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 284 VVSRS--------MTQKVSdgvkaLICGVVGvgmMCSLSPQLSILLLfftpPVLFSASVFGKQIRNTSKDL----QEATG 351
Cdd:cd18605 111 TIDDSlpfilnilLAQLFG-----LLGYLVV---ICYQLPWLLLLLL----PLAFIYYRIQRYYRATSRELkrlnSVNLS 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1370557 352 QLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRD 386
Cdd:cd18605 179 PLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLEN 213
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
634-667 |
1.02e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|....
gi 1370557 634 SGGQKQRIAIARALIKKPTILILDEATSALDVES 667
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA 379
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
510-711 |
1.33e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 510 IFKNLNFKIAPGSSVCIVGPSGRGKSTIALLLLRYYNPTTGTITIdnqdisklnCKSLRrhIGIVQQEPVLMSGTIRDNI 589
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIK--LGYFAQHQLEFLRADESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 590 TYGLTYTP--TKEEIRsvakqcfchNFITKFPNTYDTVIGPHGTLlSGGQKQRIAIARALIKKPTILILDEATSALDVES 667
Cdd:PRK10636 396 QHLARLAPqeLEQKLR---------DYLGGFGFQGDKVTEETRRF-SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1370557 668 EGAINytfgQLMKSKSMTIVSIAHRLSTIRRSENVIVLGHDGSV 711
Cdd:PRK10636 466 RQALT----EALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
631-709 |
1.37e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 631 TLLSGGQKQRIAIARALIKKPT---ILILDEATSAL---DVEsegainytfgQLMK------SKSMTIVSIAHRLSTIRR 698
Cdd:PRK00349 829 TTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDIR----------KLLEvlhrlvDKGNTVVVIEHNLDVIKT 898
|
90
....*....|.
gi 1370557 699 SENVIVLGHDG 709
Cdd:PRK00349 899 ADWIIDLGPEG 909
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
178-460 |
1.64e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 41.47 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 178 SIGMSIPKVIGIVLDTLKTSSGSDFFDLkipifslpLYEFLSFFTVALLIGCAANFGRFILLRILSERVVARLRANVIKK 257
Cdd:cd18556 15 SILISISPVILAKITDLLTSSSSDSYNY--------IVVLAALYVITISATKLLGFLSLYLQSSLRVELIISISSSYFRY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 258 TLHQDAEFFDNHKVGDLISRL---GSDAYVVSRSMTQKVSDGVKALICGVVgvgmMCSLSPQLSILLLFFTPPVLFSA-- 332
Cdd:cd18556 87 LYEQPKTFFVKENSGDITQRLnqaSNDLYTLVRNLSTNILPPLLQLIIAIV----VILSSGDYFVAALFLLYAVLFVInn 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 333 SVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFVAEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLS 412
Cdd:cd18556 163 TIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNDRNSQKRYWKLTFKMLILNSLLNVIL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1370557 413 FLTVLAYGSYLVLQSQLSIGDltaFMLYTEYT---GNAVFGLSTFYSEIMQ 460
Cdd:cd18556 243 FGLSFFYSLYGVVNGQVSIGH---FVLITSYIlllSTPIESLGNMLSELRQ 290
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
636-664 |
2.95e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 2.95e-03
10 20
....*....|....*....|....*....
gi 1370557 636 GQKQRIAIARALIKKPTILILDEATSALD 664
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
563-720 |
4.04e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 563 NCKSLRRHIGIvqQEPVLM----SGTIRDNI-TYGLTYTPTKEEIRSVAKQcfchnFITKFPNTydTVIGPHGTLLSGGQ 637
Cdd:NF000106 79 NRRALRRTIG*--HRPVR*grreSFSGRENLyMIGR*LDLSRKDARARADE-----LLERFSLT--EAAGRAAAKYSGGM 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 638 KQRIAIARALIKKPTILILDEATSALDVESEGAINYTFGQLMKSKSMTIVS---------IAHRLSTIRRsenvivlghd 708
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTtqymeeaeqLAHELTVIDR---------- 219
|
170
....*....|..
gi 1370557 709 GSVVEMGKFKEL 720
Cdd:NF000106 220 GRVIADGKVDEL 231
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
631-736 |
4.04e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 631 TLLSGGQKQRIAIARALIKK---PTILILDEATSAL---DVEsegainytfgQLMKS------KSMTIVSIAHRLSTIRR 698
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKRstgKTLYILDEPTTGLhfhDIR----------KLLEVlhrlvdKGNTVVVIEHNLDVIKT 894
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1370557 699 SENVIVLGHD-----GSVVEMGKFKELYANPTS----ALSQLLNEKA 736
Cdd:COG0178 895 ADWIIDLGPEggdggGEIVAEGTPEEVAKVKASytgrYLKEYLEAAR 941
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
620-664 |
4.73e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.60 E-value: 4.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1370557 620 NTYDTVIG-PHGTLLSGGQKQRIAIARALIKKPTILILDEATSALD 664
Cdd:PLN03140 1006 NLKDAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
225-465 |
6.80e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 39.19 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 225 LLIGCAANFGRFILLRILSE--------RVVARLRANVIKKTLHQDAEFFDNHKVGDLISRLGS-----DAYVvSRSMTQ 291
Cdd:cd18561 38 PLAGIAGVIVLRAALLWLRErvahraaqRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDgvealEAYY-GRYLPQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 292 KVsdgVKALICGVVGVGMMcSLSPQLSILLLFFTPPVLFSASVFGKQIRNTSKDLQEATGQLTRVAEEQLSGIKTVQSFV 371
Cdd:cd18561 117 LL---VALLGPLLILIYLF-FLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 372 AEGNELSRYNVAIRDIFQVGKTAAFTNAKFFTTTSLLGDLSFLTVLAYGSYLVLQSQLSIGDL-TAFMLYTEYTgNAVFG 450
Cdd:cd18561 193 ASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLlLILFLSREFF-RPLRD 271
|
250
....*....|....*
gi 1370557 451 LSTFYSEIMQGAGAA 465
Cdd:cd18561 272 LGAYWHAGYQGISAA 286
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
626-728 |
7.16e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370557 626 IGPHGTLLSGGQKQRIAIARALI---KKPTILILDEATSALDVESEGAINYTFGQLMkSKSMTIVSIAHRLSTIRRSENV 702
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLV-SLGHSVIYIDHDPALLKQADYL 1771
|
90 100 110
....*....|....*....|....*....|.
gi 1370557 703 IVLGH-----DGSVVEMGKFKELYANPTSAL 728
Cdd:PRK00635 1772 IEMGPgsgktGGKILFSGPPKDISASKDSLL 1802
|
|
| |
