|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-681 |
0e+00 |
|
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: 1037.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 1 MPVLSRPRPWRGNTLKRTAVLLALAAYGAHKVYPLVRQCLAPARGLQAPAGEPTQEASGV----AAAKAGMNRVFLQRLL 76
Cdd:TIGR00954 1 MAVLSKYRLLRSTSNNKTDKQDSPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKHStiegAKKKAHVNGVFLGKLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 77 WLLRLLFPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEG 156
Cdd:TIGR00954 81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 157 QLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSR 236
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 237 GAGTAWPSaiaglvVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQ 316
Cdd:TIGR00954 241 GPAGLFAY------LFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 317 INLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATgysesdaeavKKAALEKKEEELVSErteaFTIARNLLTAAA 396
Cdd:TIGR00954 315 LNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKT----------HPAFLEMSEEELMQE----FYNNGRLLLKAA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 397 DAIERIMSSYKEVTELAGYTARVHEMFQVFEDVQRCHFKRPRELEDAQAGSGtiGRSGVRVEGplkiRGQVVDVEQGIIC 476
Cdd:TIGR00954 381 DALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREG--GRNSNLVPG----RGIVEYQDNGIKF 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 477 ENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQ 556
Cdd:TIGR00954 455 ENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 557 VIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS 636
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
7VR1_B 637 IDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGWKF 681
Cdd:TIGR00954 615 VDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
83-352 |
3.08e-121 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 363.85 E-value: 3.08e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 83 FPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSF 162
Cdd:pfam06472 6 FPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQRLALRF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 163 RSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAgtaw 242
Cdd:pfam06472 86 RTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRGP---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 243 psAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILL 322
Cdd:pfam06472 162 --AILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILR 239
|
250 260 270
....*....|....*....|....*....|
7VR1_B 323 ERLWYVMLEQFLMKYVWSASGLLMVAVPII 352
Cdd:pfam06472 240 RRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
122-688 |
2.54e-86 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 283.62 E-value: 2.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 122 IVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDV 201
Cdd:COG4178 55 LQARDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 202 VAFAASVAHLYSNLtkplLDVAVT--SYT-----LLRAARSRGAGTAWpsAIAGLVVF------LTANVLrAFspKFG-- 266
Cdd:COG4178 135 RLFTETTLSLSLGL----LSSVVTliSFIgilwsLSGSLTFTLGGYSI--TIPGYMVWaaliyaIIGTLL-TH--LIGrp 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 267 --ELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILLerlWYVMLEQFLmkyvwSASGL 344
Cdd:COG4178 206 liRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRRLIR---RQRNLTFFT-----TGYGQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 345 LMVAVPI-ITATGYsesdaeavkkaalekkeeelvserteaftIARNL----LTAAADAIERIMSS-------YKEVTEL 412
Cdd:COG4178 278 LAVIFPIlVAAPRY-----------------------------FAGEItlggLMQAASAFGQVQGAlswfvdnYQSLAEW 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 413 AGYTARVHEMFQVFEDVQRchfkrpreledAQAGSGTIGRSGvrvegplkirgqvvdvEQGIICENIPIVTPSGEVVVAS 492
Cdd:COG4178 329 RATVDRLAGFEEALEAADA-----------LPEAASRIETSE----------------DGALALEDLTLRTPDGRPLLED 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSVEDmqrkgYS 572
Cdd:COG4178 382 LSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA-----FS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 573 EQDLEAILDVVHLHHILQR--EGGweamcDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDA 650
Cdd:COG4178 457 DAELREALEAVGLGHLAERldEEA-----DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
7VR1_B 651 --GIALLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAA 688
Cdd:COG4178 532 lpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
474-679 |
2.78e-83 |
|
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: 261.32 E-value: 2.78e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSL 553
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 554 RDQVIYPdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03223 81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
7VR1_B 634 AVSIDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGW 679
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
482-659 |
3.10e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.60 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 482 VTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYK-------PPP---QRMFYIPQRPYMSV 550
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGeIYLDgkplsamPPPewrRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 551 GSLRDQVIYPDSvedMQRKGYSEQDLEAILDVVHL-HHILQreggweamcdwKDV--LSGGEKQRIGMARMFYHRPKYAL 627
Cdd:COG4619 88 GTVRDNLPFPFQ---LRERKFDRERALELLERLGLpPDILD-----------KPVerLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190
....*....|....*....|....*....|....*.
7VR1_B 628 LDECTSAVSID----VEGKIFQAAKDAGIALLSITH 659
Cdd:COG4619 154 LDEPTSALDPEntrrVEELLREYLAEEGRAVLWVSH 189
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
474-663 |
9.22e-24 |
|
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: 106.00 E-value: 9.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVL---------YKPPP--QRMFYI 542
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 543 PQRPYMSVGSLRDQViypdsveDMQRKGYSEQDLEAILDVVHLHHILQR-EGGWEAMcdwkdV------LSGGEKQRIGM 615
Cdd:COG4988 417 PQNPYLFAGTIRENL-------RLGRPDASDEELEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRLAL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
7VR1_B 616 ARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPSL 663
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlaKGRTVILITHRLAL 534
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
484-663 |
2.85e-23 |
|
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: 97.07 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY-------KPPP----QRMFYIPQRPYmsvgs 552
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrDLDLeslrKNIAYVPQDPF----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 553 lrdqvIYPDSVEDmqrkgyseqdleaildvvhlhhilqreggweamcdwkDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:cd03228 87 -----LFSGTIRE-------------------------------------NILSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190
....*....|....*....|....*....|...
7VR1_B 633 SAVSIDVEGKIFQA--AKDAGIALLSITHRPSL 663
Cdd:cd03228 125 SALDPETEALILEAlrALAKGKTVIVIAHRLST 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
484-663 |
6.08e-22 |
|
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: 101.06 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGvlykpppqRMFY--IPQRpYMSVGSLRDQV---- 557
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG--------RILIdgIDLR-QIDPASLRRQIgvvl 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 ----IYPDSVED---MQRKGYSEQDLEAILDVVHLHH-ILQREGGWEAMcdwkdV------LSGGEKQRIGMARMFYHRP 623
Cdd:COG2274 556 qdvfLFSGTIREnitLGDPDATDEEIIEAARLAGLHDfIEALPMGYDTV-----VgeggsnLSGGQRQRLAIARALLRNP 630
|
170 180 190 200
....*....|....*....|....*....|....*....|..
7VR1_B 624 KYALLDECTSAVSIDVEGKIFQA--AKDAGIALLSITHRPSL 663
Cdd:COG2274 631 RILILDEATSALDAETEAIILENlrRLLKGRTVIIIAHRLST 672
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
92-662 |
2.13e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 98.70 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 92 GLLALHSAALVSRTFLSVYVARLDGRLARCIVR-KDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSF----RSRL 166
Cdd:COG1132 21 GLLILALLLLLLSALLELLLPLLLGRIIDALLAgGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVvadlRRDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 167 VAHAYRL---YFSQQTYYRVSNMdgrlrnpdqsLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRaarsrgagTAWP 243
Cdd:COG1132 101 FEHLLRLplsFFDRRRTGDLLSR----------LTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV--------IDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 244 SAIAGLVVF-LTANVLRAFSPKFGELVAEEARRKGELrymhSRVVANS----EEIAFYGGHEVELALLQRSYQDLASQin 318
Cdd:COG1132 163 LALIVLLVLpLLLLVLRLFGRRLRKLFRRVQEALAEL----NGRLQESlsgiRVVKAFGREERELERFREANEELRRA-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 319 lilleRLWYVMLEQFLMKYVWSASGLLMVAVPIITATGYSESDAEAvkkaalekkeEELVserteAFTiarNLLTAAADA 398
Cdd:COG1132 237 -----NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTV----------GDLV-----AFI---LYLLRLFGP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 399 IERIMSSYKEVTELAGYTARVHEMFQVFEDVQrchfkrprelEDAQAGSGTIGRSGVRVEGplkirgqvvdveqgiicen 478
Cdd:COG1132 294 LRQLANVLNQLQRALASAERIFELLDEPPEIP----------DPPGAVPLPPVRGEIEFEN------------------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 479 ipiVT---PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------TYGGV---------LYKpppqRMF 540
Cdd:COG1132 345 ---VSfsyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDptsgriLIDGVdirdltlesLRR----QIG 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 541 YIPQRPYMSVGSLRDQVIYPdsvedmqRKGYSEQDLEAILDVVHLHHILQR-EGGWEAMcdwkdV------LSGGEKQRI 613
Cdd:COG1132 418 VVPQDTFLFSGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGGQRQRI 485
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
7VR1_B 614 GMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 662
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAHRLS 536
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
474-663 |
5.68e-21 |
|
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: 90.74 E-value: 5.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGE-VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLykpppqrmfyIPQRPYMSVG 551
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLrPTSGRVR----------LDGADISQWD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 552 S--LRDQViypdsvedmqrkGYSEQDLE----AILDvvhlhhilqreggweamcdwkDVLSGGEKQRIGMARMFYHRPKY 625
Cdd:cd03246 71 PneLGDHV------------GYLPQDDElfsgSIAE---------------------NILSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
7VR1_B 626 ALLDECTSAVSIDVEGKIFQA---AKDAGIALLSITHRPSL 663
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPET 158
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
489-663 |
2.45e-20 |
|
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: 90.34 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY------KPPP----QRMFYIPQRPYMSVGSLRDQV 557
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPTSGSVLLdgtdirQLDPadlrRNIGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 IYpdsvedmqrkGYSEQDLEAILDVVHLHHILQ-------------REGGweamcdwkDVLSGGEKQRIGMARMFYHRPK 624
Cdd:cd03245 99 TL----------GAPLADDERILRAAELAGVTDfvnkhpngldlqiGERG--------RGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
7VR1_B 625 YALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPSL 663
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSL 201
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
485-671 |
8.01e-20 |
|
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: 88.30 E-value: 8.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 485 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYkppPQRMFYIPQRPYMSVGSLRDQVIYpDSV 563
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSGSVSV---PGSIAYVSQEPWIQNGTIRENILF-GKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 564 EDMQRkgyseqdLEAILDVVHLHHILQR-EGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG 641
Cdd:cd03250 92 FDEER-------YEKVIKACALEPDLEIlPDGDLTEIGEKGInLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190
....*....|....*....|....*....|....*
7VR1_B 642 KIFQ-----AAKDAGIALLsITHRPSLWKYHTHLL 671
Cdd:cd03250 165 HIFEncilgLLLNNKTRIL-VTHQLQLLPHADQIV 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
493-663 |
9.32e-20 |
|
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: 86.53 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFYIPQrpymsvgsLRDQVIYpdsvedmqrkgy 571
Cdd:cd00267 18 VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKDIAKLPLEE--------LRRRIGY------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 572 seqdleaildvvhlhhILQreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDA- 650
Cdd:cd00267 78 ----------------VPQ--------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELa 127
|
170
....*....|....*
7VR1_B 651 --GIALLSITHRPSL 663
Cdd:cd00267 128 eeGRTVIIVTHDPEL 142
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
493-633 |
1.94e-19 |
|
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: 85.39 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRIL-GGLWPTYGGVLY----------KPPPQRMFYIPQ----RPYMSVgslRDQV 557
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPTEGTILLdgqdltdderKSLRKEIGYVFQdpqlFPRLTV---RENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7VR1_B 558 IYPDSVEDMQRKGYSEQDLEAI--LDVVHLHHILQREGGweamcdwkDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALekLGLGDLADRPVGERP--------GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
493-667 |
3.42e-19 |
|
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: 86.75 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQRPymsvgslRDQVIYPd 561
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGKDltklslkelrRKVGLVFQNP-------DDQFFGP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 562 SVED-----MQRKGYSEQDLEAI----LDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:cd03225 92 TVEEevafgLENLGLPEEEIEERveeaLELVGLEGLRDRS---------PFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
7VR1_B 633 SavSIDVEG-----KIFQAAKDAGIALLSITHRPSLWKYH 667
Cdd:cd03225 163 A--GLDPAGrrellELLKKLKAEGKTIIIVTHDLDLLLEL 200
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
485-676 |
3.02e-18 |
|
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: 84.12 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 485 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKPPPQRMF-----YIPQRPYMSvgslRDqvi 558
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPTSGSIRVFGKPLEKErkrigYVPQRRSID----RD--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 559 YPDSVED---MQR-------KGYSEQDLEAI---LDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKY 625
Cdd:cd03235 83 FPISVRDvvlMGLyghkglfRRLSKADKAKVdeaLERVGLSELADRQIG---------ELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
7VR1_B 626 ALLDECTSAVsiDVEGK-----IFQAAKDAGIALLSITH-RPSLWKYHTHLLQFDGE 676
Cdd:cd03235 154 LLLDEPFAGV--DPKTQediyeLLRELRREGMTILVVTHdLGLVLEYFDRVLLLNRT 208
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
477-663 |
3.48e-18 |
|
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: 88.56 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 477 ENIPIVTPSGE-VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVL------YKPPPQRMF-----YIPQ 544
Cdd:TIGR01842 320 ENVTIVPPGGKkPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadLKQWDRETFgkhigYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 545 RPYMSVGSLRDqviypdSVEDMQRKGYSEQDLEA-ILDVVHlHHILQREGGWE-AMCDWKDVLSGGEKQRIGMARMFYHR 622
Cdd:TIGR01842 400 DVELFPGTVAE------NIARFGENADPEKIIEAaKLAGVH-ELILRLPDGYDtVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
7VR1_B 623 PKYALLDECTSavSIDVEGKI-----FQAAKDAGIALLSITHRPSL 663
Cdd:TIGR01842 473 PKLVVLDEPNS--NLDEEGEQalanaIKALKARGITVVVITHRPSL 516
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
474-666 |
3.81e-18 |
|
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: 83.69 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEVVVASL---NIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGV------LYKPPP------- 536
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVrvdgtdISKLSEkelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 537 -QRMFYIPQR----PYMSVgslRDQVIYPDSVEDMQRKGYsEQDLEAILDVVHLHHILQReggweaMCDWkdvLSGGEKQ 611
Cdd:cd03255 81 rRHIGFVFQSfnllPDLTA---LENVELPLLLAGVPKKER-RERAEELLERVGLGDRLNH------YPSE---LSGGQQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
7VR1_B 612 RIGMARMFYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSLWKY 666
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEY 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
486-659 |
4.21e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.00 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-------PPP---QRMFYIPQRPYMSVGSLR 554
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLLFEgedistlKPEiyrQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 555 DQVIYPdsvEDMQRKGYSEQDLEAILDVVHL-HHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:PRK10247 99 DNLIFP---WQIRNQQPDPAIFLDDLERFALpDTILTKN---------IAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190
....*....|....*....|....*....|
7VR1_B 634 AVS----IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK10247 167 ALDesnkHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
486-661 |
2.74e-17 |
|
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: 80.99 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYK---------PPPQRMFYIPQRPymsvgslrd 555
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGeVLWNgepirdareDYRRRLAYLGHAD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 556 qVIYPD-SVED-------MQRKGYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:COG4133 85 -GLKPElTVREnlrfwaaLYGLRADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*....
7VR1_B 628 LDECTSAvsIDVEGK-----IFQAAKDAGIALLSITHRP 661
Cdd:COG4133 155 LDEPFTA--LDAAGVallaeLIAAHLARGGAVLLTTHQP 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
484-662 |
3.68e-17 |
|
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: 85.59 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------TYGGVLYKPPP-----QRMFYIPQRPYMSVGS 552
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpqsgsiTLGGVDLRDLDeddlrRRIAVVPQRPHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 553 LRD--QVIYPDSvedmqrkgySEQDLEAILDVVHLHHILQR-EGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALL 628
Cdd:COG4987 425 LREnlRLARPDA---------TDEELWAALERVGLGDWLAAlPDGLDTWLGEGGRrLSGGERRRLALARALLRDAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*...
7VR1_B 629 DECTSAVSIDVEGKI----FQAAKDAgiALLSITHRPS 662
Cdd:COG4987 496 DEPTEGLDAATEQALladlLEALAGR--TVLLITHRLA 531
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
477-659 |
5.95e-17 |
|
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: 79.99 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 477 ENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY--KPPPQRMFYipQRPYMSVGSL 553
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLngKPIKAKERR--KSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 554 RDQvIYPDSVED-----MQRKGYSEQDLEAILDVVHLHhilqreggweamcDWKDV----LSGGEKQRIGMARMFYHRPK 624
Cdd:cd03226 81 DYQ-LFTDSVREelllgLKELDAGNEQAETVLKDLDLY-------------ALKERhplsLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
7VR1_B 625 YALLDECTSAV---SIDVEGKIFQAAKDAGIALLSITH 659
Cdd:cd03226 147 LLIFDEPTSGLdykNMERVGELIRELAAQGKAVIVITH 184
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
474-663 |
7.86e-17 |
|
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: 84.26 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV-------LYKPPP----QRMFYI 542
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavngvpLADADAdswrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 543 PQRPYMSVGSLRDQVIypdsvedMQRKGYSEQDLEAILDVVHLHHILQ-REGGWEAMCDWKDV-LSGGEKQRIGMARMFY 620
Cdd:TIGR02857 402 PQHPFLFAGTIAENIR-------LARPDASDAEIREALERAGLDEFVAaLPQGLDTPIGEGGAgLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
7VR1_B 621 HRPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHRPSL 663
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
486-663 |
1.00e-16 |
|
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: 78.63 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYkpppqrmfyipqrpymsvgsLRDQviypdSVED 565
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL--------------------LDGK-----DLAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 566 MQRK------GYSEQdleaILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAV---- 635
Cdd:cd03214 66 LSPKelarkiAYVPQ----ALELLGLAHLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLdiah 132
|
170 180
....*....|....*....|....*...
7VR1_B 636 SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNL 160
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
474-662 |
1.56e-16 |
|
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: 79.58 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYI 542
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQKGQILIDGIDirdisrkslrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 543 PQRPYMSVGSLRDQVIYPDSVEDmqrkgysEQDLEAILDVVHLHH-ILQREGGWEA-MCDWKDVLSGGEKQRIGMARMFY 620
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNAT-------DEEVIEAAKEAGAHDfIMKLPNGYDTvLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
7VR1_B 621 HRPKYALLDECTSavSIDVEG-KIFQAAKDA---GIALLSITHRPS 662
Cdd:cd03254 156 RDPKILILDEATS--NIDTETeKLIQEALEKlmkGRTSIIIAHRLS 199
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
486-663 |
2.20e-16 |
|
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: 79.70 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY---KP----PP----QRMFYIPQRPYMSVGSlr 554
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlaslSRrelaRRIAYVPQEPPAPFGL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 555 dqviypdSVED---MQRKGY-------SEQDLEAI---LDVVHLHHILQReggweamcDWkDVLSGGEKQRIGMARMFYH 621
Cdd:COG1120 91 -------TVRElvaLGRYPHlglfgrpSAEDREAVeeaLERTGLEHLADR--------PV-DELSGGERQRVLIARALAQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
7VR1_B 622 RPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG1120 155 EPPLLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLHDLNL 200
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
484-663 |
4.03e-16 |
|
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: 78.14 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK---PPPQRMFYIPQRpymsVGSL----RD 555
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSGEVLVDgkdITKKNLRELRRK----VGLVfqnpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 556 QVIYPdSVED-----MQRKGYSEQDLEA----ILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYA 626
Cdd:COG1122 87 QLFAP-TVEEdvafgPENLGLPREEIRErveeALELVGLEHLADRP---------PHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
7VR1_B 627 LLDECTSavSIDVEGK-----IFQAAKDAGIALLSITHRPSL 663
Cdd:COG1122 157 VLDEPTA--GLDPRGRrelleLLKRLNKEGKTVIIVTHDLDL 196
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
477-663 |
5.55e-16 |
|
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: 81.72 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 477 ENIPIVTP-SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV-------LYKPPPQR----MFYIPQ 544
Cdd:COG4618 334 ENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSvrldgadLSQWDREElgrhIGYLPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 545 rpymsvgslrDQVIYPDSVED----MQrkgysEQDLEAILD---VVHLHHILQR----------EGGweamcdwkDVLSG 607
Cdd:COG4618 414 ----------DVELFDGTIAEniarFG-----DADPEKVVAaakLAGVHEMILRlpdgydtrigEGG--------ARLSG 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
7VR1_B 608 GEKQRIGMARMFYHRPKYALLDECTSavSIDVEG-----KIFQAAKDAGIALLSITHRPSL 663
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNS--NLDDEGeaalaAAIRALKARGATVVVITHRPSL 529
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
486-659 |
6.04e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 78.21 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYG-----GVLYKPPPQRMFYIPQRPYMSVGslrdqviY 559
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLLPPTSGtvrlfGKPPRRARRRIGYVPQRAEVDWD-------F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 560 PDSVED---MQR-------KGYSEQDLEAI---LDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRP 623
Cdd:COG1121 91 PITVRDvvlMGRygrrglfRRPSRADREAVdeaLERVGLEDLADRpigE------------LSGGQQQRVLLARALAQDP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
7VR1_B 624 KYALLDECTSAVsiDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:COG1121 159 DLLLLDEPFAGV--DAATeealyELLRELRREGKTILVVTH 197
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
483-630 |
6.79e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.21 E-value: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 483 TPSGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-----KPPPQRMFYIPQR----PYMSVg 551
Cdd:COG1116 19 TGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEkPTSGEVLVdgkpvTGPGPDRGVVFQEpallPWLTV- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7VR1_B 552 slRDQVIYPDSVEDMQRKgYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG1116 98 --LDNVALGLELRGVPKA-ERRERARELLELVGLAGFEDA---------YPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
488-630 |
8.16e-16 |
|
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: 77.13 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY-----KPPPQRMFYIPQR----PYMSVgslRDQV 557
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLeRPTSGEVLVdgepvTGPGPDRGYVFQQdallPWLTV---LDNV 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7VR1_B 558 IYPDSVEDMQRKGySEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03293 95 ALGLELQGVPKAE-ARERAEELLELVGLSGFENA---------YPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
489-659 |
1.31e-15 |
|
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: 76.84 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW------PTYGGVLYKPPP------------QRMFYIPQRPYMSV 550
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgaPDEGEVLLDGKDiydldvdvlelrRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 551 GSLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLhhilqreggWEAMCDWKDV--LSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03260 95 GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAAL---------WDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190
....*....|....*....|....*....|....*
7VR1_B 629 DECTSAVSI----DVEGKIFQAAKDAGIALlsITH 659
Cdd:cd03260 166 DEPTSALDPistaKIEELIAELKKEYTIVI--VTH 198
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
486-659 |
3.47e-15 |
|
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: 75.45 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYK-------PPPQRMF-YIPQR----PYMSVgs 552
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFIKPDSGKILLNgkditnlPPEKRDIsYVPQNyalfPHMTV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 553 lRDQVIYPDSVEDMQRKGYSEQDLEaILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:cd03299 89 -YKNIAYGLKKRKVDKKEIERKVLE-IAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|.
7VR1_B 633 SAVSIDVEGKIFQAAKDA----GIALLSITH 659
Cdd:cd03299 158 SALDVRTKEKLREELKKIrkefGVTVLHVTH 188
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
484-663 |
3.69e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.47 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASL---NIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK-------PPPQR-MF------YIPQR 545
Cdd:COG1136 15 GTGEGEVTALrgvSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVLIDgqdisslSERELaRLrrrhigFVFQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 546 ----PYMSVgslRDQVIYPDSVEDMQRKGySEQDLEAILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARM 618
Cdd:COG1136 95 fnllPELTA---LENVALPLLLAGVSRKE-RRERARELLERVGLGDRLDHrpsQ------------LSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
7VR1_B 619 FYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG1136 159 LVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTHDPEL 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
486-659 |
1.43e-14 |
|
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: 73.81 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK-------PPPQRMF-YIPQR----PYMSVGs 552
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLDgkditnlPPHKRPVnTVFQNyalfPHLTVF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 553 lrDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03300 91 --ENIAFG-----LRLKKLPKAEIKErvaeALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
7VR1_B 629 DECTSAV------SIDVEGKIFQaaKDAGIALLSITH 659
Cdd:cd03300 155 DEPLGALdlklrkDMQLELKRLQ--KELGITFVFVTH 189
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
505-662 |
3.00e-14 |
|
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: 72.33 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 505 ITGPNGCGKSSLFRILGGLWPTYGGVLY--------------KPPPQRMF-YIPQR----PYMSVgslRDQVIYpdsveD 565
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinLPPQQRKIgLVFQQyalfPHLNV---RENLAF-----G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 566 MQRKGYSE--QDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI 643
Cdd:cd03297 100 LKRKRNREdrISVDELLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180
....*....|....*....|...
7VR1_B 644 F----QAAKDAGIALLSITHRPS 662
Cdd:cd03297 171 LpelkQIKKNLNIPVIFVTHDLS 193
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
484-662 |
4.86e-14 |
|
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: 72.13 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK--------PPPQR--MFYIPQRPYMSVGS 552
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYvPENGRVLVDghdlaladPAWLRrqVGVVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 553 LRDQVIYPDSVEDMQRKGYSeqdleAILDVVHlHHILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:cd03252 92 IRDNIALADPGMSMERVIEA-----AKLAGAH-DFISELPEGYDTIVGEQGAgLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190
....*....|....*....|....*....|...
7VR1_B 632 TSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 662
Cdd:cd03252 166 TSALDYESEHAIMRNMHDicAGRTVIIIAHRLS 198
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
484-659 |
5.43e-14 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 70.91 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRIL-GGLWPTYGGVLYKPPP------------QRMFYIPQRPymsv 550
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLnGLLRPQSGAVLIDGEPldysrkgllerrQRVGLVFQDP---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 551 gslRDQVIYPDSVEDM----QRKGYSEQDLEAI----LDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHR 622
Cdd:TIGR01166 78 ---DDQLFAADVDQDVafgpLNLGLSEAEVERRvreaLTAVGASGLRERP---------THCLSGGEKKRVAIAGAVAMR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
7VR1_B 623 PKYALLDECTSAVsiDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:TIGR01166 146 PDVLLLDEPTAGL--DPAGreqmlAILRRLRAEGMTVVISTH 185
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
486-662 |
5.55e-14 |
|
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: 71.40 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY------KPPPQR-----MFyipQR----PYMS 549
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLeRPDSGEILIdgrdvtGVPPERrnigmVF---QDyalfPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 550 VgslRDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKY 625
Cdd:cd03259 89 V---AENIAFG-----LKLRGVPKAEIRArvreLLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
7VR1_B 626 ALLDECTSAvsIDVE------GKIFQAAKDAGIALLSITHRPS 662
Cdd:cd03259 152 LLLDEPLSA--LDAKlreelrEELKELQRELGITTIYVTHDQE 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
493-662 |
8.34e-14 |
|
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: 71.80 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL--------YKPPPQR--MFYIPQRPYMSVGSLRDQVIYPD 561
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYdPTSGEILldgvdirdLNLRWLRsqIGLVSQEPVLFDGTIAENIRYGK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 562 svedmqRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVE 640
Cdd:cd03249 102 ------PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180
....*....|....*....|....*
7VR1_B 641 gKIFQAAKD---AGIALLSITHRPS 662
Cdd:cd03249 176 -KLVQEALDramKGRTTIVIAHRLS 199
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
486-661 |
9.05e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYKP-------PPQRMFYIPQR----PYMSVGsl 553
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGgdiddpdVAEACHYLGHRnamkPALTVA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 554 rdqviypDSVEDMQR-KGYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMAR-MFYHRPKYaLLDEC 631
Cdd:PRK13539 92 -------ENLEFWAAfLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARlLVSNRPIW-ILDEP 154
|
170 180 190
....*....|....*....|....*....|....*.
7VR1_B 632 TSAvsIDVEGK-----IFQA-AKDAGIALLSiTHRP 661
Cdd:PRK13539 155 TAA--LDAAAValfaeLIRAhLAQGGIVIAA-THIP 187
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
489-659 |
1.07e-13 |
|
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: 71.37 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------TYGGVLYKPPPQRMFY-----IPQRPYMSV---GSLR 554
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERpwsgevTFDGRPVTRRRRKAFRrrvqmVFQDPYASLhprHTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 555 DQVIYPDSVedmQRKGYSEQDLEAILDVVHLH-HILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG1124 100 RILAEPLRI---HGLPDREERIAELLEQVGLPpSFLDRyphQ------------LSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190
....*....|....*....|....*....|....*...
7VR1_B 631 CTSAVsiDVegkIFQAA---------KDAGIALLSITH 659
Cdd:COG1124 165 PTSAL--DV---SVQAEilnllkdlrEERGLTYLFVSH 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
494-630 |
1.29e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 494 NIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVG-SLRDQVI--YPDSVEDMQRK- 569
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLdgDAELRALEAELe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 570 ------GYSEQDLEAIldvVHLHHILQREGGWEA--------------MCDW-KDV--LSGGEKQRIGMARMFYHRPKYA 626
Cdd:COG0488 98 eleaklAEPDEDLERL---AELQEEFEALGGWEAearaeeilsglgfpEEDLdRPVseLSGGWRRRVALARALLSEPDLL 174
|
....
7VR1_B 627 LLDE 630
Cdd:COG0488 175 LLDE 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
488-659 |
1.37e-13 |
|
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: 69.35 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEG--MHLLitGPNGCGKSSLFRILGGLW-PTYGGVLY--KPPP-------QRMFYIPQRPYmsvgslrd 555
Cdd:cd03230 14 TALDDISLTVEKGeiYGLL--GPNGAGKTTLIKIILGLLkPDSGEIKVlgKDIKkepeevkRRIGYLPEEPS-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 556 qvIYPD-SVEDmqrkgyseqdleaildvvHLHhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:cd03230 84 --LYENlTVRE------------------NLK------------------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190
....*....|....*....|....*....|
7VR1_B 635 vsIDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:cd03230 126 --LDPESrrefwELLRELKKEGKTILLSSH 153
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
493-659 |
1.94e-13 |
|
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: 70.57 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK------PPPQRMFYIPQR---PYMSVgslRDQV-IYPD 561
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitePGPDRMVVFQNYsllPWLTV---RENIaLAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 562 SVEDMQRKGYSEQDLEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI---- 637
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALVGLTEAADKR---------PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrg 151
|
170 180
....*....|....*....|..
7VR1_B 638 DVEGKIFQAAKDAGIALLSITH 659
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTH 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
474-664 |
2.31e-13 |
|
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: 73.40 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV----------LYKPPPQ----R 538
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIsgevlldgrdLLELSEAlrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 539 MFYIPQRPYMSVGSLR--DQVIYPDSVEDMQRKGYSEQDLEAiLDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMA 616
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgDQIAEALENLGLSRAEARARVLEL-LEAVGLERRLDR---------YPHQLSGGQRQRVAIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
7VR1_B 617 RMFYHRPKYALLDECTSA----VSIDVEGKIFQAAKDAGIALLSITHRPSLW 664
Cdd:COG1123 155 MALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
488-659 |
3.00e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 70.09 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY--KPPP-------QRMFYIPQRPYMsvgslrdqv 557
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTSGEVRVlgEDVArdpaevrRRIGYVPQEPAL--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 iYPD-SVEDM---------QRKGYSEQDLEAILDVVHLHHILQREGGWeamcdwkdvLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:COG1131 85 -YPDlTVRENlrffarlygLPRKEARERIDELLELFGLTDAADRKVGT---------LSGGMKQRLGLALALLHDPELLI 154
|
170 180 190
....*....|....*....|....*....|....*...
7VR1_B 628 LDECTSAVsiDVEG-----KIFQAAKDAGIA-LLSiTH 659
Cdd:COG1131 155 LDEPTSGL--DPEArrelwELLRELAAEGKTvLLS-TH 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
474-662 |
3.62e-13 |
|
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: 69.57 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL--------YKPPPQR--MFYI 542
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYdVSSGSILidgqdireVTLDSLRraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 543 PQrpymsvgslrDQVIYPDSVEDMQRKG---YSEQDLEAILDVVHLHH-ILQREGGWEAMCDWKDV-LSGGEKQRIGMAR 617
Cdd:cd03253 81 PQ----------DTVLFNDTIGYNIRYGrpdATDEEVIEAAKAAQIHDkIMRFPDGYDTIVGERGLkLSGGEKQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
7VR1_B 618 MFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 662
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAHRLS 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
480-659 |
6.19e-13 |
|
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: 71.86 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 480 PIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-------------KPPPQRMFYIPQR 545
Cdd:COG1123 271 PVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrPTSGSILFdgkdltklsrrslRELRRRVQMVFQD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 546 PY------MSVGslrDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLH-HILQR---EggweamcdwkdvLSGGEKQRIGM 615
Cdd:COG1123 351 PYsslnprMTVG---DIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRyphE------------LSGGQRQRVAI 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
7VR1_B 616 ARMFYHRPKYALLDECTSA--VSIdvegkifQA---------AKDAGIALLSITH 659
Cdd:COG1123 416 ARALALEPKLLILDEPTSAldVSV-------QAqilnllrdlQRELGLTYLFISH 463
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
486-661 |
6.36e-13 |
|
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: 69.34 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY----KPPPQRMFYIpqRPYMSV--GSLRDQVI 558
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlfgeRRGGEDVWEL--RKRIGLvsPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 559 YPDSVEDMQRKG----------YSEQDLE---AILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKY 625
Cdd:COG1119 93 RDETVLDVVLSGffdsiglyrePTDEQRErarELLELLGLAHLADRPFG---------TLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
7VR1_B 626 ALLDECTSavSIDVEGK------IFQAAKDAGIALLSITHRP 661
Cdd:COG1119 164 LILDEPTA--GLDLGARelllalLDKLAAEGAPTLVLVTHHV 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
489-659 |
6.47e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSvgslrdqVIYPDSVED--M 566
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLD-------TTLPLTVNRflR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 567 QRKGYSEQDLEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVsiDVEGK---- 642
Cdd:PRK09544 92 LRPGTKKEDILPALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV--DVNGQvaly 160
|
170
....*....|....*....
7VR1_B 643 --IFQAAKDAGIALLSITH 659
Cdd:PRK09544 161 dlIDQLRRELDCAVLMVSH 179
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
461-678 |
6.86e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 461 LKIRGQVVDVEQGIICENIPIVTPSGEVVVaslnirveegmhllITGPNGCGKSSLFRILGGLwPTY----GGVLYK--- 533
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHA--------------IMGPNGSGKSTLAKVLMGH-PKYevtsGSILLDged 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 534 ----PPPQR----MFYIPQRP------------YMSVGSLRDQVIypdSVEDMQRKgyseqdLEAILDVVHL-HHILQR- 591
Cdd:COG0396 66 ilelSPDERaragIFLAFQYPveipgvsvsnflRTALNARRGEEL---SAREFLKL------LKEKMKELGLdEDFLDRy 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 592 --EGgweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID---VEGKIFQAAKDAGIALLSITHRPSLWKY 666
Cdd:COG0396 137 vnEG-----------FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDalrIVAEGVNKLRSPDRGILIITHYQRILDY 205
|
250 260
....*....|....*....|
7VR1_B 667 ----HTHLLqFDG----EGG 678
Cdd:COG0396 206 ikpdFVHVL-VDGrivkSGG 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
486-659 |
1.13e-12 |
|
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: 68.35 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY------KPPP---QRMFYIPQRPYMSVG-SLR 554
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDSGSILIdgedvrKEPRearRQIGVLPDERGLYDRlTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 555 DQV-----IYPDSVEDMQRKG--YSEQ-DLEAILDvvhlhhilQREGGweamcdwkdvLSGGEKQRIGMARMFYHRPKYA 626
Cdd:COG4555 93 ENIryfaeLYGLFDEELKKRIeeLIELlGLEEFLD--------RRVGE----------LSTGMKKKVALARALVHDPKVL 154
|
170 180 190
....*....|....*....|....*....|....*...
7VR1_B 627 LLDECTSAvsIDVEG-----KIFQAAKDAGIALLSITH 659
Cdd:COG4555 155 LLDEPTNG--LDVMArrllrEILRALKKEGKTVLFSSH 190
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
505-675 |
1.52e-12 |
|
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: 67.50 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 505 ITGPNGCGKSSLFRILGGLWPTYGGVLY---KPPPQ--------RMFYIPQRPYMSVGSLRDQVIYpdsveDMQRKgySE 573
Cdd:cd03248 45 LVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQyehkylhsKVSLVGQEPVLFARSLQDNIAY-----GLQSC--SF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 574 QDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD-- 649
Cdd:cd03248 118 ECVKEAAQKAHAHSFISElaSGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDwp 197
|
170 180
....*....|....*....|....*.
7VR1_B 650 AGIALLSITHRPSLWKYHTHLLQFDG 675
Cdd:cd03248 198 ERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
484-660 |
1.71e-12 |
|
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: 67.52 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSS----LFRILgglwPTYGGVLY-------KPPP----QRMFYIPQRPYM 548
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILidgvdisKIGLhdlrSRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 549 SVGSLRDQvIYPDSVedmqrkgYSEQDLEAILDVVHL-HHILQREGGWEAM-CDWKDVLSGGEKQRIGMARMFYHRPKYA 626
Cdd:cd03244 90 FSGTIRSN-LDPFGE-------YSDEELWQALERVGLkEFVESLPGGLDTVvEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190
....*....|....*....|....*....|....*.
7VR1_B 627 LLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHR 660
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREafKDCTVLTIAHR 197
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
486-666 |
1.89e-12 |
|
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: 66.78 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwPTY----GGVLYK-------PPPQR----MFYIPQRPYMSV 550
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYevteGEILFKgeditdlPPEERarlgIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 551 GSlrdqviypdSVEDMQRkgyseqdleailDVvhlhhilqREGgweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03217 91 GV---------KNADFLR------------YV--------NEG-----------FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|....*....
7VR1_B 631 CTSAVSID---VEGKIFQAAKDAGIALLSITHRPSLWKY 666
Cdd:cd03217 131 PDSGLDIDalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
488-660 |
2.88e-12 |
|
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: 66.54 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVL---YKP----PPQRMFYIPQR----PYMSVgslRDQ 556
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdGKPldiaARNRIGYLPEErglyPKMKV---IDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 557 VIYPDSVEDMQRKgYSEQDLEAILDVVHL-HHILQReggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSA- 634
Cdd:cd03269 91 LVYLAQLKGLKKE-EARRRIDEWLERLELsEYANKR----------VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGl 159
|
170 180
....*....|....*....|....*...
7VR1_B 635 --VSIDVEGKIFQAAKDAGIALLSITHR 660
Cdd:cd03269 160 dpVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
488-660 |
3.00e-12 |
|
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: 67.08 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEG-MHLLItGPNGCGKSSLFRILGG-LWPTYGGVLYK-------PPPQ-------RMFYIPqRPY--MS 549
Cdd:cd03219 14 VALDDVSFSVRPGeIHGLI-GPNGAGKTTLFNLISGfLRPTSGSVLFDgeditglPPHEiarlgigRTFQIP-RLFpeLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 550 V------GSLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRP 623
Cdd:cd03219 92 VlenvmvAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAG---------ELSYGQQRRLEIARALATDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
7VR1_B 624 KYALLDECTSAVS---IDVEGKIFQAAKDAGIALLSITHR 660
Cdd:cd03219 163 KLLLLDEPAAGLNpeeTEELAELIRELRERGITVLLVEHD 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
489-660 |
3.90e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.47 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQRPYMSVGSLRD-- 555
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWdPQQGEILLNGQPiadyseaalrQAISVVSQRVHLFSATLRDnl 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 556 QVIYPDSvedmqrkgySEQDLEAILDVVHLHHILQREGGWEA-MCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:PRK11160 435 LLAAPNA---------SDEALIEVLQQVGLEKLLEDDKGLNAwLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180
....*....|....*....|....*...
7VR1_B 635 VSIDVEGKIFQAAKD--AGIALLSITHR 660
Cdd:PRK11160 506 LDAETERQILELLAEhaQNKTVLMITHR 533
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
489-659 |
4.51e-12 |
|
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: 66.38 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-----PPPQRMF--------YIPQRPY------M 548
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDgkdllKLSRRLRkirrkeiqMVFQDPMsslnprM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 549 SVGslrDQVIYPDSVEDMQRKgYSEQDLEAILDVVHLH---HILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHR 622
Cdd:cd03257 100 TIG---EQIAEPLRIHGKLSK-KEARKEAVLLLLVGVGlpeEVLNRyphE------------LSGGQRQRVAIARALALN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
7VR1_B 623 PKYALLDECTSAVSIDVEGKIFQAAKDA----GIALLSITH 659
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLqeelGLTLLFITH 204
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
489-659 |
9.05e-12 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 64.93 E-value: 9.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-PPPQRMFYIPQRpymsVGSLRD-QVIYPD--SV 563
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFDgKSYQKNIEALRR----IGALIEaPGFYPNltAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 564 EDMQRK----GYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDV 639
Cdd:cd03268 91 ENLRLLarllGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNG--LDP 159
|
170 180
....*....|....*....|....*
7VR1_B 640 EG-----KIFQAAKDAGIALLSITH 659
Cdd:cd03268 160 DGikelrELILSLRDQGITVLISSH 184
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
474-663 |
9.22e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.07 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLY------KPPPQRMfyipqrP 546
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKlLYGEERPTSGQVLVngqdlsRLKRREI------P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 547 YM--SVGslrdqVIYPD-------SVED-----MQRKGYSEQDL----EAILDVVHLHHILqreggwEAMCDwkdVLSGG 608
Cdd:COG2884 76 YLrrRIG-----VVFQDfrllpdrTVYEnvalpLRVTGKSRKEIrrrvREVLDLVGLSDKA------KALPH---ELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
7VR1_B 609 EKQRIGMARMFYHRPKYALLDECT----SAVSIDVEgKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTgnldPETSWEIM-ELLEEINRRGTTVLIATHDLEL 199
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
489-663 |
1.24e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.21 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMF---YI-------PQRPYMSVGSLRDQV 557
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTGGQVLLDGVPLVQYdhhYLhrqvalvGQEPVLFSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 IYpdsvedmqrkGYSEQDLEAILDVVHLHH----ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:TIGR00958 576 AY----------GLTDTPDEEIMAAAKAANahdfIMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190
....*....|....*....|....*....|.
7VR1_B 633 SAVSIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:TIGR00958 646 SALDAECEQLLQESRSRASRTVLLIAHRLST 676
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
489-655 |
1.28e-11 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 64.76 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLY-------KPPPQR----MFYIPQrpymsvgslrDQ 556
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFdgrditgLPPHERaragIGYVPE----------GR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 557 VIYPD-SVED-------MQRKGYSEQDLEAILDVV-HLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:cd03224 85 RIFPElTVEEnlllgayARRRAKRKARLERVYELFpRLKERRKQLAG---------TLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190
....*....|....*....|....*....|.
7VR1_B 628 LDECTSAVSIDVEGKIFQAA---KDAGIALL 655
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIrelRDEGVTIL 186
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
486-634 |
1.50e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.89 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK-------PPPQR----------MFyipqrPY 547
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLDgqdithvPAENRhvntvfqsyaLF-----PH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 548 MSVgslRDQVIYPdsvEDMQRKGYSEQD---LEAiLDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPK 624
Cdd:PRK09452 101 MTV---FENVAFG---LRMQKTPAAEITprvMEA-LRMVQLEEFAQRK---------PHQLSGGQQQRVAIARAVVNKPK 164
|
170
....*....|
7VR1_B 625 YALLDECTSA 634
Cdd:PRK09452 165 VLLLDESLSA 174
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
486-630 |
1.70e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.78 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVL-------YKPPPQR----MFyipQR----PYMS 549
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMldgvdlsHVPPYQRpinmMF---QSyalfPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 550 VgslrDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:PRK11607 108 V----EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK---------PHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
.
7VR1_B 630 E 630
Cdd:PRK11607 175 E 175
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
484-661 |
1.91e-11 |
|
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: 67.00 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG--VLYKPPPQ---------RMFYIPQRPYMSVGS 552
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevTLDGVPVSsldqdevrrRVSVCAQDAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 553 LRDQVIypdsvedMQRKGYSEQDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:TIGR02868 425 VRENLR-------LARPDATDEELWAALERVGLADWLRAlpDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|...
7VR1_B 631 CTSAVSIDVEGKIFQ--AAKDAGIALLSITHRP 661
Cdd:TIGR02868 498 PTEHLDAETADELLEdlLAALSGRTVVLITHHL 530
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
486-630 |
2.03e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 66.25 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG--------VLYKPPPQRMF-YIPQR----PYMSVgs 552
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGeiliggrdVTDLPPKDRNIaMVFQSyalyPHMTV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 553 lRDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKY 625
Cdd:COG3839 93 -YENIAFP-----LKLRKVPKAEIDRrvreAAELLGLEDLLDRkpkQ------------LSGGQRQRVALGRALVREPKV 154
|
....*
7VR1_B 626 ALLDE 630
Cdd:COG3839 155 FLLDE 159
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
474-643 |
2.67e-11 |
|
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: 63.75 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGeVVVASLNIRVEEGMHLLItGPNGCGKSSLFRILGGLW-PTYGGVL---YKPPPQRMF------YIP 543
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTpPSSGTIRidgQDVLKQPQKlrrrigYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 544 QR----PYMSVgslRDQVIYPDSVEDMQRKGySEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMF 619
Cdd:cd03264 79 QEfgvyPNFTV---REFLDYIAWLKGIPSKE-VKARVDEVLELVNLGDRAKKKIG---------SLSGGMRRRVGIAQAL 145
|
170 180
....*....|....*....|....
7VR1_B 620 YHRPKYALLDECTsaVSIDVEGKI 643
Cdd:cd03264 146 VGDPSILIVDEPT--AGLDPEERI 167
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
486-659 |
3.48e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.27 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWP--TYGGVLY--------KPPPQR-MFYIPQR----PYMS 549
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPafSASGEVLlngrrltaLPAEQRrIGILFQDdllfPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 550 VG-----SLrdqviyPDSVEDMQRKgyseQDLEAILDVVHLHHILQReggweamcdwkDV--LSGGEKQRIGMARMFYHR 622
Cdd:COG4136 93 VGenlafAL------PPTIGRAQRR----ARVEQALEEAGLAGFADR-----------DPatLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
7VR1_B 623 PKYALLDECTS----AVSIDVEGKIFQAAKDAGIALLSITH 659
Cdd:COG4136 152 PRALLLDEPFSkldaALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
486-630 |
5.35e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 65.05 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVAS-LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKpPPQRMFYIP--QRpymSVGSL-RDQVIYP- 560
Cdd:PRK11000 14 GDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPpaER---GVGMVfQSYALYPh 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7VR1_B 561 -DSVEDMQ--------RKGYSEQDLEAILDVVHLHHILQREGgweamcdwKDvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK11000 90 lSVAENMSfglklagaKKEEINQRVNQVAEVLQLAHLLDRKP--------KA-LSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
487-663 |
6.22e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwptyggvLYKPPPQRMFYIPQRPYMSVGSLRDQVI----YPDS 562
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-------LKGTPVAGCVDVPDNQFGREASLIDAIGrkgdFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 563 VEDMQRKGYSEqdleAILdvvhlhhilqreggweamcdWK---DVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID- 638
Cdd:COG2401 116 VELLNAVGLSD----AVL--------------------WLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQt 171
|
170 180
....*....|....*....|....*...
7VR1_B 639 ---VEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:COG2401 172 akrVARNLQKLARRAGITLVVATHHYDV 199
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
486-660 |
6.48e-11 |
|
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: 61.29 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYkpppqrmfyipqrpymsvgsLRDQVIYPDSVED 565
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL--------------------VDGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 566 MQRKGYSeqdleaildVVHlhhilQreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVS---IDVEGK 642
Cdd:cd03216 72 ARRAGIA---------MVY-----Q--------------LSVGERQMVEIARALARNARLLILDEPTAALTpaeVERLFK 123
|
170
....*....|....*...
7VR1_B 643 IFQAAKDAGIALLSITHR 660
Cdd:cd03216 124 VIRRLRAQGVAVIFISHR 141
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
486-643 |
1.35e-10 |
|
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: 64.76 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQRPYMSVGSLR 554
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSlkdidrhtlrQFINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 555 DQVIypdsvedMQ-RKGYSEQDLEAILDVVHLH-HILQREGGWEA-MCDWKDVLSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:TIGR01193 566 ENLL-------LGaKENVSQDEIWAACEIAEIKdDIENMPLGYQTeLSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170
....*....|..
7VR1_B 632 TSAVSIDVEGKI 643
Cdd:TIGR01193 639 TSNLDTITEKKI 650
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
488-630 |
1.37e-10 |
|
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: 61.50 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY--------KPPPQR---MFYipQR----PYMSVgs 552
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDRdiaMVF--QNyalyPHMTV-- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7VR1_B 553 lRDQVIYPDSVEDMQRKGYSEQDLEAIlDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:cd03301 90 -YDNIAFGLKLRKVPKDEIDERVREVA-ELLQIEHLLDRK---------PKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
486-659 |
1.66e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 63.19 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG--------VLYKPPPQRMF-YIPQR----PYMSVgs 552
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGrilldgrdVTGLPPEKRNVgMVFQDyalfPHLTV-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 553 lRDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKY 625
Cdd:COG3842 95 -AENVAFG-----LRMRGVPKAEIRArvaeLLELVGLEGLADRyphQ------------LSGGQQQRVALARALAPEPRV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
7VR1_B 626 ALLDECTSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:COG3842 157 LLLDEPLSA--LDAKLReemreeLRRLQRELGITFIYVTH 194
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
488-659 |
1.80e-10 |
|
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: 61.68 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLY----------KPPPQRMFYipqrpymsvgsLRDQ 556
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNYLPDSGSILVrhdggwvdlaQASPREILA-----------LRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 557 VIypdsvedmqrkGYSEQDLEAI-----LDVVH--LhhilqREGGW---EAMCDWKDVL-----------------SGGE 609
Cdd:COG4778 94 TI-----------GYVSQFLRVIprvsaLDVVAepL-----LERGVdreEARARARELLarlnlperlwdlppatfSGGE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
7VR1_B 610 KQRIGMARMFYHRPKYALLDECTSavSIDVEGK-----IFQAAKDAGIALLSITH 659
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTA--SLDAANRavvveLIEEAKARGTAIIGIFH 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
489-659 |
2.27e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.62 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPP-------QRMFYIPQR--PYMSVgslrdqvi 558
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGELLAGTAPlaearedTRLMFQDARllPWKKV-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 559 yPDSVEDMQRKGYSEQDLEAiLDVVHLHhilQREGGWEAmcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS-- 636
Cdd:PRK11247 99 -IDNVGLGLKGQWRDAALQA-LAAVGLA---DRANEWPA------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDal 167
|
170 180
....*....|....*....|....*
7VR1_B 637 --IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK11247 168 trIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
482-646 |
2.78e-10 |
|
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: 64.16 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 482 VTPsgevVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYP 560
Cdd:TIGR01271 438 VTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEGKIKHS---GRISFSPQTSWIMPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 561 DSVEDMQRKGYSE--QDLEAILDVVHLHHILQREGGWeamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID 638
Cdd:TIGR01271 511 LSYDEYRYTSVIKacQLEEDIALFPEKDKTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
....*...
7VR1_B 639 VEGKIFQA 646
Cdd:TIGR01271 583 TEKEIFES 590
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
484-660 |
2.89e-10 |
|
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: 60.02 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP---------QRMFYIPQRPYMSVGSL 553
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQQGEITLDGVPvsdlekalsSLISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 554 RDQVIYPdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTs 633
Cdd:cd03247 92 RNNLGRR--------------------------------------------FSGGERQRLALARILLQDAPIVLLDEPT- 126
|
170 180 190
....*....|....*....|....*....|...
7VR1_B 634 aVSIDVEGK------IFQAAKDAgiALLSITHR 660
Cdd:cd03247 127 -VGLDPITErqllslIFEVLKDK--TLIWITHH 156
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
492-645 |
4.43e-10 |
|
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: 63.43 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 492 SLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSVEDmqrkG 570
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVHMK---GSVAYVPQQAWIQNDSLRENILFGKALNE----K 728
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7VR1_B 571 YSEQDLEAILDVVHLHHIlqrEGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQ 645
Cdd:TIGR00957 729 YYQQVLEACALLPDLEIL---PSGDRTEIGEKGVnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
483-662 |
5.40e-10 |
|
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: 60.32 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 483 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRmfyipqrpYMSVGSLRDQV---- 557
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYdVDSGRILIDGHDVR--------DYTLASLRRQIglvs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 ----IYPDSVEDMQRKGYSEQDLEAILDVVHLHH----ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03251 83 qdvfLFNDTVAENIAYGRPGATREEVEEAARAANahefIMELPEGYDTVIGERGVkLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190
....*....|....*....|....*....|....*..
7VR1_B 629 DECTSAVSIDVEgKIFQAAKD---AGIALLSITHRPS 662
Cdd:cd03251 163 DEATSALDTESE-RLVQAALErlmKNRTTFVIAHRLS 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
486-659 |
6.33e-10 |
|
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: 58.74 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY------------KPPPQRMFYIPQR----PYM 548
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLeEPDSGSILIdgedltdledelPPLRRRIGMVFQDfalfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 549 SVgslRDQVIYPdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03229 92 TV---LENIALG--------------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190
....*....|....*....|....*....|....*
7VR1_B 629 DECTSA----VSIDVEGKIFQAAKDAGIALLSITH 659
Cdd:cd03229 125 DEPTSAldpiTRREVRALLKSLQAQLGITVVLVTH 159
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
486-661 |
6.89e-10 |
|
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: 59.43 E-value: 6.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMfyipQRPymsvgSLRDQVIYPDSVE 564
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRVLLNGGPLDF----QRD-----SIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 565 DMQRKgyseqdLEAILDVVHLHHILQREGGWEAMCD-----WKDV----LSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:cd03231 83 GIKTT------LSVLENLRFWHADHSDEQVEEALARvglngFEDRpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190
....*....|....*....|....*....|
7VR1_B 636 SIDVEGKIFQA----AKDAGIALLSiTHRP 661
Cdd:cd03231 157 DKAGVARFAEAmaghCARGGMVVLT-THQD 185
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
486-671 |
7.01e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.17 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRpymsvGSLRDQviYPDSVED 565
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR-----SEVPDS--LPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 566 M------QRKG----YSEQD---LEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:NF040873 77 LvamgrwARRGlwrrLTRDDraaVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
7VR1_B 633 SAVSIDVEGKIFQ---AAKDAGIALLSITHRPSLWKYHTHLL 671
Cdd:NF040873 148 TGLDAESRERIIAllaEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
489-646 |
9.90e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.26 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSVEDMQ 567
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPSEGKIKHS---GRISFSSQFSWIMPGTIKENIIFGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 568 RKGYSE--QDLEAILDVVHLHHILQREGGWeamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQ 645
Cdd:cd03291 129 YKSVVKacQLEEDITKFPEKDNTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
.
7VR1_B 646 A 646
Cdd:cd03291 201 S 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
474-660 |
1.08e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.78 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYG-----GV-LYKPPP----QRMFYIP 543
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGslkinGIeLRELDPeswrKHLSWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 544 QRPYMSVGSLRDQVIypdsvedMQRKGYSEQDLEAILDVVHLHHILQR-EGGWE-AMCDWKDVLSGGEKQRIGMARMFYH 621
Cdd:PRK11174 430 QNPQLPHGTLRDNVL-------LGNPDASDEQLQQALENAWVSEFLPLlPQGLDtPIGDQAAGLSVGQAQRLALARALLQ 502
|
170 180 190 200
....*....|....*....|....*....|....*....|.
7VR1_B 622 RPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHR 660
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQ 543
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
484-660 |
1.11e-09 |
|
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: 58.96 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSL----FRILGglwPTYG-----GVLYKPPP-----QRMFYIPQRPYMS 549
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLilalFRFLE---AEEGkieidGIDISTIPledlrSSLTIIPQDPTLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 550 VGSLRDQViypdSVEDMqrkgYSEQDLEAILDVvhlhhilqREGGweamcdwkDVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:cd03369 95 SGTIRSNL----DPFDE----YSDEEIYGALRV--------SEGG--------LNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190
....*....|....*....|....*....|...
7VR1_B 630 ECTSAVSIDVEGKIFQAAKD--AGIALLSITHR 660
Cdd:cd03369 151 EATASIDYATDALIQKTIREefTNSTILTIAHR 183
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
489-659 |
1.21e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 59.74 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY--KP----PPQRMFYI----PQRPYMSvgslrdqv 557
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLngRPlaawSPWELARRravlPQHSSLA-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 iYPDSVED---MQRKGYS------EQDLEAILDVVHLHHILQReggweamcDWKDvLSGGEKQRIGMAR-------MFYH 621
Cdd:COG4559 88 -FPFTVEEvvaLGRAPHGssaaqdRQIVREALALVGLAHLAGR--------SYQT-LSGGEQQRVQLARvlaqlwePVDG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
7VR1_B 622 RPKYALLDECTSAVSIDVEGKIFQAAKD---AGIALLSITH 659
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQlarRGGGVVAVLH 198
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
486-659 |
1.21e-09 |
|
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: 58.70 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-------VLYKPPP------QRMFYIPQR----PYM 548
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglKLTDDKKninelrQKVGMVFQQfnlfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 549 SVgsLRDQVIYPdsvedMQRKGYSEQDLEAILdvvhlHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRPK 624
Cdd:cd03262 92 TV--LENITLAP-----IKVKGMSKAEAEERA-----LELLEKVG----LADKADAypaqLSGGQQQRVAIARALAMNPK 155
|
170 180 190
....*....|....*....|....*....|....*....
7VR1_B 625 YALLDECTSA----VSIDVEGKIFQAAKDaGIALLSITH 659
Cdd:cd03262 156 VMLFDEPTSAldpeLVGEVLDVMKDLAEE-GMTMVVVTH 193
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
489-660 |
1.40e-09 |
|
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: 59.09 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-------PPPQR----MFYIPQRPymSVgsLRDQ 556
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDgqditklPMHKRarlgIGYLPQEA--SI--FRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 557 viypdSVED-------MQRKGYSEQD--LEAILDVVHLHHILQREGgweamcdwkDVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:cd03218 91 -----TVEEnilavleIRGLSKKEREekLEELLEEFHITHLRKSKA---------SSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
7VR1_B 628 LDECTSAVS----IDVEgKIFQAAKDAGI----------ALLSITHR 660
Cdd:cd03218 157 LDEPFAGVDpiavQDIQ-KIIKILKDRGIgvlitdhnvrETLSITDR 202
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
485-669 |
1.90e-09 |
|
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: 58.50 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 485 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLF-RILGGLWPTYGGVLY--KPPPQRMF------------YIPQRPYMS 549
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWsnKNESEPSFeatrsrnrysvaYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 550 VGSLRDQVIYPDSVEDMQRKGYSEQ-DLEAILDVvhLHHILQREGGWEAMCdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAcSLQPDIDL--LPFGDQTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
7VR1_B 629 DECTSAVSIDVEGKIFQAA-----KDAGIALLSITHRpslWKYHTH 669
Cdd:cd03290 165 DDPFSALDIHLSDHLMQEGilkflQDDKRTLVLVTHK---LQYLPH 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
505-632 |
3.03e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.33 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 505 ITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPY------------MSVGSLRDQV--------IYPDSVE 564
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQldptktvrenveEGVAEIKDALdrfneisaKYAEPDA 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7VR1_B 565 DMQRKGYSEQDLEAILDVVHLHHILQR-EGGWEAM-C---DWK-DVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:TIGR03719 116 DFDKLAAEQAELQEIIDAADAWDLDSQlEIAMDALrCppwDADvTKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
486-661 |
4.67e-09 |
|
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: 56.98 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKP---------PPQRMFYIPQRPYMSvGSLrd 555
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLrPDSGEVRWNGtplaeqrdePHENILYLGHLPGLK-PEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 556 qviypdSVEDMQR-----KGYSEQDLEAILDVVHLHHILQREGGWeamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:TIGR01189 89 ------SALENLHfwaaiHGGAQRTIEDALAAVGLTGFEDLPAAQ---------LSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|....*..
7VR1_B 631 CTsaVSIDVEG-KIFQAAKDA-----GIALLSiTHRP 661
Cdd:TIGR01189 154 PT--TALDKAGvALLAGLLRAhlargGIVLLT-THQD 187
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
497-659 |
7.73e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.33 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 497 VEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLykpppqRMFYIPQRPyMSVGSLRDQV--IY--PD------SVED- 565
Cdd:PRK13635 30 VYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI------TVGGMVLSE-ETVWDVRRQVgmVFqnPDnqfvgaTVQDd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 566 ----MQRKGYSEQDL----EAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS- 636
Cdd:PRK13635 103 vafgLENIGVPREEMvervDQALRQVGMEDFLNRE---------PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDp 173
|
170 180
....*....|....*....|....*.
7VR1_B 637 ---IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK13635 174 rgrREVLETVRQLKEQKGITVLSITH 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
486-659 |
1.18e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV------------LYKPPPQRMFYIPQRP------- 546
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGYLPQEAsifrrls 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 547 ----YMSVGSLRDqviypdSVEDMQRKGYSEQDLEAIldvvHLHHILQREGgweamcdwkDVLSGGEKQRIGMARMFYHR 622
Cdd:PRK10895 95 vydnLMAVLQIRD------DLSAEQREDRANELMEEF----HIEHLRDSMG---------QSLSGGERRRVEIARALAAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
7VR1_B 623 PKYALLDECTSAVS----IDVEgKIFQAAKDAGIALLSITH 659
Cdd:PRK10895 156 PKFILLDEPFAGVDpisvIDIK-RIIEHLRDSGLGVLITDH 195
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
497-659 |
1.38e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.66 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 497 VEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY----KPPPQRMFYIPQRPYMSVGSLRDQVIYPdSVED-----MQ 567
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdLLTEENVWDIRHKIGMVFQNPDNQFVGA-TVEDdvafgLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 568 RKGYSEQDLeaildVVHLHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDVEGK- 642
Cdd:PRK13650 109 NKGIPHEEM-----KERVNEALELVG----MQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEATSM--LDPEGRl 177
|
170 180
....*....|....*....|..
7VR1_B 643 -----IFQAAKDAGIALLSITH 659
Cdd:PRK13650 178 eliktIKGIRDDYQMTVISITH 199
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
505-662 |
1.81e-08 |
|
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: 57.04 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 505 ITGPNGCGKSSLFRILGGLWPTYGGVLY--------------KPPPQRMF-YIPQR----PYMSVgslRDQVIYPDSVED 565
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsrkgifLPPEKRRIgYVFQEarlfPHLSV---RGNLRYGMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 566 MQRKGYSEqdlEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIF- 644
Cdd:TIGR02142 105 PSERRISF---ERVIELLGIGHLLGRLPG---------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILp 172
|
170 180
....*....|....*....|.
7VR1_B 645 ---QAAKDAGIALLSITHRPS 662
Cdd:TIGR02142 173 yleRLHAEFGIPILYVSHSLQ 193
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
474-659 |
1.92e-08 |
|
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: 53.61 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIvTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQrpymsvgsl 553
Cdd:cd03221 1 IELENLSK-TYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 554 rdqviypdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180
....*....|....*....|....*...
7VR1_B 634 avSIDVEGKIF--QAAKDAGIALLSITH 659
Cdd:cd03221 100 --HLDLESIEAleEALKEYPGTVILVSH 125
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
488-659 |
2.04e-08 |
|
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: 55.82 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEG-MHLLItGPNGCGKSSLFRILGGLW-PTYGGVLYK-------PPPQ-------RMFYIPQ-RPYMSV 550
Cdd:COG0411 18 VAVDDVSLEVERGeIVGLI-GPNGAGKTTLFNLITGFYrPTSGRILFDgrditglPPHRiarlgiaRTFQNPRlFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 551 -------GSLRDQVIYPDSVEDMQRKGYSEQDL----EAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMF 619
Cdd:COG0411 97 lenvlvaAHARLGRGLLAALLRLPRARREEREAreraEELLERVGLADRADEPAG---------NLSYGQQRRLEIARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
7VR1_B 620 YHRPKYALLDECTSAVSI----DVEGKIFQAAKDAGIALLSITH 659
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPeeteELAELIRRLRDERGITILLIEH 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
474-669 |
2.16e-08 |
|
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: 55.11 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKPPPQRMFYIPQRPYM--SV 550
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKlIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 551 GS-------LRDQVIYPDSVEDMQRKGYSEQDLE----AILDVV---HLHHILQREggweamcdwkdvLSGGEKQRIGMA 616
Cdd:cd03292 81 GVvfqdfrlLPDRNVYENVAFALEVTGVPPREIRkrvpAALELVglsHKHRALPAE------------LSGGEQQRVAIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
7VR1_B 617 RMFYHRPKYALLDECTSAVSIDVEGKI---FQAAKDAGIALLSITHRPSLWKYHTH 669
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEImnlLKKINKAGTTVVVATHAKELVDTTRH 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
474-663 |
2.22e-08 |
|
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: 55.65 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 474 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPqrmfyIPQRPYMSVGS 552
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVePTSGSVLIDGTD-----INKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 553 LRDQV---------IYPDSVedMQ----------------RKGYSEQDLE---AILDVVHL-HHILQReggweamcdwKD 603
Cdd:cd03256 76 LRRQIgmifqqfnlIERLSV--LEnvlsgrlgrrstwrslFGLFPKEEKQralAALERVGLlDKAYQR----------AD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
7VR1_B 604 VLSGGEKQRIGMARMFYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 663
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLHQVDL 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
488-642 |
2.29e-08 |
|
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: 55.20 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY---------KPPPQRMFYIPQrpymsvgslrDQV 557
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrPTSGTAYIngysirtdrKAARQSLGYCPQ----------FDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 IYPD-SVEDMQR-----KGYSEQdlEAILDVVHLHHILQREggweamcDWKDV----LSGGEKQRIGMARMFYHRPKYAL 627
Cdd:cd03263 86 LFDElTVREHLRfyarlKGLPKS--EIKEEVELLLRVLGLT-------DKANKrartLSGGMKRKLSLAIALIGGPSVLL 156
|
170
....*....|....*
7VR1_B 628 LDECTSavSIDVEGK 642
Cdd:cd03263 157 LDEPTS--GLDPASR 169
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
484-659 |
2.70e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.85 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYKPPP------------QRMFYIPQRPymsv 550
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGEPikydkksllevrKTVGIVFQNP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 551 gslRDQVIYPDSVEDMQ----RKGYSEQDLEAildvvHLHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHR 622
Cdd:PRK13639 88 ---DDQLFAPTVEEDVAfgplNLGLSKEEVEK-----RVKEALKAVG----MEGFENKpphhLSGGQKKRVAIAGILAMK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
7VR1_B 623 PKYALLDECTSAVSIDVEGKIFQAAKD---AGIALLSITH 659
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDlnkEGITIIISTH 195
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
488-676 |
4.34e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSV---E 564
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDItvqE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 565 DMQRKGYSEQDLEAIL---DVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAV----SI 637
Cdd:PRK10253 101 LVARGRYPHQPLFTRWrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLdishQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
7VR1_B 638 DVEGKIFQAAKDAGIALLSITHR-PSLWKYHTHLLQF-DGE 676
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALrEGK 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
488-659 |
4.77e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.50 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFYIPQR------------PYMSVGslr 554
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEkPTEGQIFIDGEDVTHRSIQQRdicmvfqsyalfPHMSLG--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 555 DQVIYPdsvEDMQRKGYSE--QDLEAILDVVHLhhilqreGGWEAMcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:PRK11432 97 ENVGYG---LKMLGVPKEErkQRVKEALELVDL-------AGFEDR--YVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190
....*....|....*....|....*....|.
7VR1_B 633 SAVSIDV----EGKIFQAAKDAGIALLSITH 659
Cdd:PRK11432 165 SNLDANLrrsmREKIRELQQQFNITSLYVTH 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
493-659 |
5.24e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.00 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYG-----GVLYKpppqrmfyipqrpYMSVGSLRDQV--IY--PD- 561
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGeikidGITIS-------------KENLKEIRKKIgiIFqnPDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 562 -----SVED-----MQRKGYSEQDLEAILD----VVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:PRK13632 95 qfigaTVEDdiafgLENKKVPPKKMKDIIDdlakKVGMEDYLDKE---------PQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190
....*....|....*....|....*....|....*...
7VR1_B 628 LDECTSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13632 166 FDESTSM--LDPKGKreikkiMVDLRKTRKKTLISITH 201
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
481-634 |
7.15e-08 |
|
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: 54.57 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 481 IVTPSGEVV-VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP--------------QRMFYIPQ 544
Cdd:cd03294 30 ILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePTSGKVLIDGQDiaamsrkelrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 545 R----PYMSVgslRDQVIYPDSVEDMQRKGYSEQDLEAiLDVVHLhhilqreGGWEAmcDWKDVLSGGEKQRIGMARMFY 620
Cdd:cd03294 110 SfallPHRTV---LENVAFGLEVQGVPRAEREERAAEA-LELVGL-------EGWEH--KYPDELSGGMQQRVGLARALA 176
|
170
....*....|....
7VR1_B 621 HRPKYALLDECTSA 634
Cdd:cd03294 177 VDPDILLMDEAFSA 190
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
487-661 |
7.72e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.28 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTY-------GGVLY-------------KPPPQRMFYIPQR- 545
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskikvdGKVLYfgkdifqidaiklRKEVGMVFQQPNPf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 546 PYMSVgslRDQVIYPDSVEDMQRKgyseQDLEAILDvvhlhHILQREGGWEAMCDWKDV----LSGGEKQRIGMARMFYH 621
Cdd:PRK14246 103 PHLSI---YDNIAYPLKSHGIKEK----REIKKIVE-----ECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
7VR1_B 622 RPKYALLDECTSAVSI----DVEGKIFQAAKDAGIALLSitHRP 661
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIvnsqAIEKLITELKNEIAIVIVS--HNP 212
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
489-735 |
8.42e-08 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 54.04 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFYIPQRPYMSvgslRD-QVIYPDS---- 562
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEkPAQGTVSFRGQDLYQLDRKQRRAFR----RDvQLVFQDSpsav 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 563 -------------VEDMQRKGYSEQD--LEAILDVVHLHHilqreggwEAMCDWKDVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:TIGR02769 102 nprmtvrqiigepLRHLTSLDESEQKarIAELLDMVGLRS--------EDADKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 628 LDECTSAVSIDVEGKIFQAAKD----AGIALLSITHRPSLWKYHthllqfdgeggwkfekldsAARLSLTEEKQRLEQQL 703
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKlqqaFGTAYLFITHDLRLVQSF-------------------CQRVAVMDKGQIVEECD 234
|
250 260 270
....*....|....*....|....*....|....*....
7VR1_B 704 AGipkmqrrlQELC------QILGEAVAPAH-VPAPSPQ 735
Cdd:TIGR02769 235 VA--------QLLSfkhpagRNLQSAVLPEHpVRRSITT 265
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
492-630 |
9.81e-08 |
|
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: 53.50 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 492 SLNIRVEEGMHLLitGPNGCGKSSLFRILGGL-WPTYGGVLY-------KPPPQRMF-YIPQR----PYMSVgslRDQVI 558
Cdd:cd03296 22 SLDIPSGELVALL--GPSGSGKTTLLRLIAGLeRPDSGTILFggedatdVPVQERNVgFVFQHyalfRHMTV---FDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 559 Y----------PDSVEdMQRKgyseqdLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:cd03296 97 FglrvkprserPPEAE-IRAK------VHELLKLVQLDWLADR---------YPAQLSGGQRQRVALARALAVEPKVLLL 160
|
..
7VR1_B 629 DE 630
Cdd:cd03296 161 DE 162
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
483-659 |
3.16e-07 |
|
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: 51.81 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 483 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY-------------KPPPQRMFYIPQR-PY 547
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVdgtdltllsgkelRKARRRIGMIFQHfNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 548 MSVGSLRDQVIYPDSVEDMQRKgYSEQDLEAILDVVHLHHilqREGGWEAMcdwkdvLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:cd03258 94 LSSRTVFENVALPLEIAGVPKA-EIEERVLELLELVGLED---KADAYPAQ------LSGGQKQRVGIARALANNPKVLL 163
|
170 180 190
....*....|....*....|....*....|....*.
7VR1_B 628 LDECTSAVSIDVEGKIFQAAKDA----GIALLSITH 659
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDInrelGLTIVLITH 199
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
493-661 |
3.59e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.34 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYKPPP---------QRMFYIPQRPymsvGslrdqvIYPD- 561
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGeVLWQGEPirrqrdeyhQDLLYLGHQP----G------IKTEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 562 -SVEDMQ-----RKGYSEQDLEAILDVVHLHhilqregGWEamcdwkDV----LSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:PRK13538 90 tALENLRfyqrlHGPGDDEALWEALAQVGLA-------GFE------DVpvrqLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|....*.
7VR1_B 632 TSAvsIDVEG-KIFQA-----AKDAGIALLSiTHRP 661
Cdd:PRK13538 157 FTA--IDKQGvARLEAllaqhAEQGGMVILT-THQD 189
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
493-659 |
3.90e-07 |
|
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: 52.05 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGV----LYKPPPQRMFYIPQRpymsVGslrdqVIY--PD---- 561
Cdd:TIGR04520 21 VSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPTSGKVtvdgLDTLDEENLWEIRKK----VG-----MVFqnPDnqfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 562 --SVED-----MQRKGYSEQDLEAI----LDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:TIGR04520 92 gaTVEDdvafgLENLGVPREEMRKRvdeaLKLVGMEDFRDRE---------PHLLSGGQKQRVAIAGVLAMRPDIIILDE 162
|
170 180 190
....*....|....*....|....*....|....*
7VR1_B 631 CTSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:TIGR04520 163 ATSM--LDPKGRkevletIRKLNKEEGITVISITH 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
488-659 |
4.00e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 51.63 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY------KPPPQRMFYIPQR-----------PYMSv 550
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvNDPKVDERLIRQEagmvfqqfylfPHLT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 551 gSLRDQVIYPDSVEDMQRKGYSEQDLEaildvvhlhhILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK09493 94 -ALENVMFGPLRVRGASKEEAEKQARE----------LLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190
....*....|....*....|....*....|....
7VR1_B 631 CTSAvsIDVE-----GKIFQAAKDAGIALLSITH 659
Cdd:PRK09493 163 PTSA--LDPElrhevLKVMQDLAEEGMTMVIVTH 194
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
493-662 |
4.20e-07 |
|
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: 53.29 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLykpppqrmfyIPQRPYMSV--GSLR--------DQVIYPD 561
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTSGRIL----------IDGQDIRDVtqASLRaaigivpqDTVLFND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 562 SVED---MQRKGYSEQDLEAILDVVHLHH-ILQREGGWEAMcdwkdV------LSGGEKQRIGMARMFYHRPKYALLDEC 631
Cdd:COG5265 447 TIAYniaYGRPDASEEEVEAAARAAQIHDfIESLPDGYDTR-----VgerglkLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
170 180 190
....*....|....*....|....*....|...
7VR1_B 632 TSAVSIDVEGKIFQAAKDA--GIALLSITHRPS 662
Cdd:COG5265 522 TSALDSRTERAIQAALREVarGRTTLVIAHRLS 554
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
461-671 |
4.71e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 51.49 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 461 LKIRGQVVDVEQGIICENIPIVTPSGEVVVaslnirveegmhllITGPNGCGKSSLFRILGGlWPTY----GGVLYK--- 533
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHA--------------IMGPNGSGKSTLSKTIAG-HPSYevtsGTILFKgqd 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 534 ----PPPQR----MFYIPQRPYMSVGSlrdqviypdSVEDMQRKGY---SEQDLEAILDVVHLHHILQRE----GGWEAM 598
Cdd:TIGR01978 66 llelEPDERaragLFLAFQYPEEIPGV---------SNLEFLRSALnarRSARGEEPLDLLDFEKLLKEKlallDMDEEF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 599 CDwKDV---LSGGEKQRIGMARMFYHRPKYALLDECTSAVSID-----VEGkiFQAAKDAGIALLSITHRPSLWKY---- 666
Cdd:TIGR01978 137 LN-RSVnegFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDalkivAEG--INRLREPDRSFLIITHYQRLLNYikpd 213
|
....*
7VR1_B 667 HTHLL 671
Cdd:TIGR01978 214 YVHVL 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
507-632 |
5.36e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 507 GPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPY------------MSVGSLRDQV--------IYPDSVEDM 566
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQldpektvrenveEGVAEVKAALdrfneiyaAYAEPDADF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 567 QrKGYSEQ-DLEAILDvvhlhhilqREGGWE-------AM----C---DWK-DVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK11819 120 D-ALAAEQgELQEIID---------AADAWDldsqleiAMdalrCppwDAKvTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
..
7VR1_B 631 CT 632
Cdd:PRK11819 190 PT 191
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
489-659 |
6.34e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.97 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPPqrmfyIPQRPYMSVGSLRDQ---VIY----- 559
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQP-----MSKLSSAAKAELRNQklgFIYqfhhl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 560 -PD--SVED---------MQRKGYSEQDLEaILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYAL 627
Cdd:PRK11629 99 lPDftALENvamplligkKKPAEINSRALE-MLAAVGLEHRANHR---------PSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*.
7VR1_B 628 LDECTSAVSIDVEGKIFQAAKD----AGIALLSITH 659
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGElnrlQGTAFLVVTH 204
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
460-646 |
1.04e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 460 PLKIRGQVVDVEQGIICENIPIVTPSgevvVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTY-GGVLYKpppQ 537
Cdd:PLN03232 607 PLQPGAPAISIKNGYFSWDSKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAEtSSVVIR---G 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 538 RMFYIPQRPYMSVGSLRDQVIYPDSVEdmqrkgySEQDLEAIlDVVHLHHILQREGGWeamcDWKDV------LSGGEKQ 611
Cdd:PLN03232 680 SVAYVPQVSWIFNATVRENILFGSDFE-------SERYWRAI-DVTALQHDLDLLPGR----DLTEIgergvnISGGQKQ 747
|
170 180 190
....*....|....*....|....*....|....*
7VR1_B 612 RIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQA 646
Cdd:PLN03232 748 RVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDS 782
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
240-662 |
1.10e-06 |
|
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: 52.03 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 240 TAWPSAIAGLVVF-LTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVElallQRSYqDLASQIN 318
Cdd:TIGR02203 152 YSWQLTLIVVVMLpVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYE----TRRF-DAVSNRN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 319 LillerlwyvmleQFLMKYVwSASGLLMVAVPIITATGYSesdaeAVKKAALEkkeeELVSERTEAFTIArNLLTAAAda 398
Cdd:TIGR02203 227 R------------RLAMKMT-SAGSISSPITQLIASLALA-----VVLFIALF----QAQAGSLTAGDFT-AFITAMI-- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 399 ieRIMSSYKEVTELAGytaRVHEMFQVFEDVqrchFKRPRELEDAQAGSGTIGRsgvrVEGPLKIRGqvVDVEQGiicen 478
Cdd:TIGR02203 282 --ALIRPLKSLTNVNA---PMQRGLAAAESL----FTLLDSPPEKDTGTRAIER----ARGDVEFRN--VTFRYP----- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 479 ipivtPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLykpppqrMFYIPQRPYmSVGSLRDQV 557
Cdd:TIGR02203 342 -----GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYePDSGQIL-------LDGHDLADY-TLASLRRQV 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 --------IYPDSVED----MQRKGYSEQDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRP 623
Cdd:TIGR02203 409 alvsqdvvLFNDTIANniayGRTEQADRAEIERALAAAYAQDFVDKlpLGLDTPIGENGVLLSGGQRQRLAIARALLKDA 488
|
410 420 430 440
....*....|....*....|....*....|....*....|..
7VR1_B 624 KYALLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPS 662
Cdd:TIGR02203 489 PILILDEATSALDNESERLV-QAALERlmqGRTTLVIAHRLS 529
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
485-659 |
1.17e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 485 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwptyggVLYKPPPQRMFYIPQRPYMS--VGSLRDQV--IY- 559
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL------LLPDDNPNSKITVDGITLTAktVWDIREKVgiVFq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 560 -PD------SVED-----MQRKGYSEQDLEAILdvvhlHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRP 623
Cdd:PRK13640 92 nPDnqfvgaTVGDdvafgLENRAVPRPEMIKIV-----RDVLADVG----MLDYIDSepanLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
7VR1_B 624 KYALLDECTSAvsIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13640 163 KIIILDESTSM--LDPAGKeqilklIRKLKKKNNLTVISITH 202
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
490-666 |
1.22e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.25 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 490 VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP-TYGGVLY----------------KPPPQRMFYIPQ---RPYMS 549
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEVAWlgkdllgmkddewravRSDIQMIFQDPLaslNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 550 VGS-----LRdqVIYPDsvedMQRKGYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPK 624
Cdd:PRK15079 117 IGEiiaepLR--TYHPK----LSRQEVKDRVKAMMLKVGLLPNLINR---------YPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
7VR1_B 625 YALLDECTSAVSIDVEGKIF----QAAKDAGIALLSITHRPSLWKY 666
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVnllqQLQREMGLSLIFIAHDLAVVKH 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
486-634 |
1.72e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 49.99 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVaslnirveegmhllITGPNGCGKSSLFRILGGLWP------TYGGVLYKPPPQRMFYIPQR-----------PYM 548
Cdd:COG1126 27 GEVVV--------------IIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKDINKLRRKvgmvfqqfnlfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 549 SVgslRDQVIYPDsvedMQRKGYSEQDLEAI----LDVVHLHhilqreggweamcDWKDV----LSGGEKQRIGMAR--- 617
Cdd:COG1126 93 TV---LENVTLAP----IKVKKMSKAEAEERamelLERVGLA-------------DKADAypaqLSGGQQQRVAIARala 152
|
170
....*....|....*..
7VR1_B 618 MfyhRPKYALLDECTSA 634
Cdd:COG1126 153 M---EPKVMLFDEPTSA 166
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
488-660 |
1.76e-06 |
|
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: 49.67 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL------YKPP---PQRMFYIPQR----PYMSVgsl 553
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATvdgfdvVKEPaeaRRRLGFVSDStglyDRLTA--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 554 RDQVIYPDSVEDMQRKGYsEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTS 633
Cdd:cd03266 96 RENLEYFAGLYGLKGDEL-TARLEELADRLGMEELLDRRVG---------GFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190
....*....|....*....|....*....|
7VR1_B 634 AVSIDVEGKIF---QAAKDAGIALLSITHR 660
Cdd:cd03266 166 GLDVMATRALRefiRQLRALGKCILFSTHI 195
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
482-643 |
2.82e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 50.23 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 482 VTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKPPP----------QRMFYIPQRPYMSV 550
Cdd:PRK09536 11 VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRaINGTLTPTAGTVLVAGDDvealsaraasRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 551 GSLRDQVIYPDSVEDMQRKGYSEQDLEAILDvvhlhHILQReGGWEAMCDWK-DVLSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:PRK09536 91 EFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-----RAMER-TGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
|
170
....*....|....
7VR1_B 630 ECTSavSIDVEGKI 643
Cdd:PRK09536 165 EPTA--SLDINHQV 176
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
484-674 |
2.84e-06 |
|
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: 51.10 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSS----LFRIL---------GGLwpTYGGVLYKPPPQRMFYIPQRPYMSV 550
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINesaegeiiiDGL--NIAKIGLHDLRFKITIIPQDPVLFS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 551 GSLRDQvIYPDSvedmqrkGYSEQDLEAILDVVHLHHILQRE-GGWEAMC-DWKDVLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:TIGR00957 1374 GSLRMN-LDPFS-------QYSDEEVWWALELAHLKTFVSALpDKLDHECaEGGENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
7VR1_B 629 DECTSAVSIDVEGKIFQAAKDA--GIALLSITHRPSLWKYHTHLLQFD 674
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLD 1493
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
500-659 |
3.05e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 500 GMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPpQRMFYIPQRPYMSVgsLRD-QVIYPD---SVEDMQRKGYSeqd 575
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG-QRIDTLSPGKLQAL--RRDiQFIFQDpyaSLDPRQTVGDS--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 576 leaILDVVHLHHILQREGG-----W---------EAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG 641
Cdd:PRK10261 424 ---IMEPLRVHGLLPGKAAaarvaWllervgllpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
170 180
....*....|....*....|..
7VR1_B 642 KI----FQAAKDAGIALLSITH 659
Cdd:PRK10261 501 QIinllLDLQRDFGIAYLFISH 522
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
483-659 |
3.51e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.72 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 483 TPSGEVV-VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV------------------LYKPPPQRMFYIP 543
Cdd:PRK09473 24 TPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsatfngreilnlpekeLNKLRAEQISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 544 Q------RPYMSVGSLRDQVIypdsvedMQRKGYSEQD--LEAI--LDVVHLHHILQReggweaMCDWKDVLSGGEKQRI 613
Cdd:PRK09473 104 QdpmtslNPYMRVGEQLMEVL-------MLHKGMSKAEafEESVrmLDAVKMPEARKR------MKMYPHEFSGGMRQRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
7VR1_B 614 GMARMFYHRPKYALLDECTSAVSIDVEGKIF----QAAKDAGIALLSITH 659
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMtllnELKREFNTAIIMITH 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
507-630 |
3.78e-06 |
|
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: 49.71 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 507 GPNGCGKSSLFRILGGLWPTYGG-------VLYK-------PPPQRMF-YIPQ--R--PYMSV-GSLRdqviYPdsvedM 566
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGrirlggeVLQDsargiflPPHRRRIgYVFQeaRlfPHLSVrGNLL----YG-----R 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7VR1_B 567 QR--KGYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG4148 103 KRapRAERRISFDEVVELLGIGHLLDR---------RPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
493-630 |
4.36e-06 |
|
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: 48.44 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYK-------PPPQR----MFYIPQRpymsvgslRDqvIYP 560
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRFDgeditglPPHRIarlgIGYVPEG--------RR--IFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 561 D-SVED------MQRKGYSE--QDLEAILDVV-HLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG0410 92 SlTVEEnlllgaYARRDRAEvrADLERVYELFpRLKERRRQRAG---------TLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
507-643 |
4.99e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 507 GPNGCGKSSLFRIL---GGLWP---TYGGVLYKpppQRMFYIPQRPYMSvgsLRDQV-------------IYPDSVEDMQ 567
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPevtITGSIVYN---GHNIYSPRTDTVD---LRKEIgmvfqqpnpfpmsIYENVVYGLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 568 RKGYSEQdleAILDVVhLHHILQREGGWEAMcdwKDVL-------SGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVE 640
Cdd:PRK14239 112 LKGIKDK---QVLDEA-VEKSLKGASIWDEV---KDRLhdsalglSGGQQQRVCIARVLATSPKIILLDEPTSALDPISA 184
|
...
7VR1_B 641 GKI 643
Cdd:PRK14239 185 GKI 187
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
493-662 |
5.30e-06 |
|
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: 47.87 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYK------PPPQRmfyipqRPYMSVgsLRDQVIYPD-SVE 564
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINgvdvtaAPPAD------RPVSML--FQENNLFAHlTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 565 DMQRKGYS------EQDLEAIldvvhlHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID 638
Cdd:cd03298 89 QNVGLGLSpglkltAEDRQAI------EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180
....*....|....*....|....*...
7VR1_B 639 VEGKIFQAAKDA----GIALLSITHRPS 662
Cdd:cd03298 163 LRAEMLDLVLDLhaetKMTVLMVTHQPE 190
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
486-634 |
5.36e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 48.61 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY--KP----PPQRMFYI----PQRPYMSvgslr 554
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLngRPladwSPAELARRravlPQHSSLS----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 555 dqviYPDSVED---MQRKGYSEQDLE---------AILDVVHLHHILQREggweamcdwkdvLSGGEKQRIGMARMF--- 619
Cdd:PRK13548 89 ----FPFTVEEvvaMGRAPHGLSRAEddalvaaalAQVDLAHLAGRDYPQ------------LSGGEQQRVQLARVLaql 152
|
170
....*....|....*...
7VR1_B 620 ---YHRPKYALLDECTSA 634
Cdd:PRK13548 153 wepDGPPRWLLLDEPTSA 170
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
505-635 |
5.65e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.85 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 505 ITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP------------QRMFYIPQRPymsvgslRDQVIYPDSVED----MQ 567
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPldyskrgllalrQQVATVFQDP-------EQQIFYTDIDSDiafsLR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7VR1_B 568 RKGYSEQDL----EAILDVVHLHHILQReggwEAMCdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:PRK13638 105 NLGVPEAEItrrvDEALTLVDAQHFRHQ----PIQC-----LSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
488-660 |
7.05e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 48.57 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEG--MHLLitGPNGCGKSSLFR-ILGGLWPTYGGVLYK-----PPPQRMF-YIPQ----RPYMSVGslr 554
Cdd:COG4152 15 TAVDDVSFTVPKGeiFGLL--GPNGAGKTTTIRiILGILAPDSGEVLWDgepldPEDRRRIgYLPEerglYPKMKVG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 555 DQVIYpdsvedM-QRKGYSEQDLEAILDvvhlhHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRPKYALLD 629
Cdd:COG4152 90 EQLVY------LaRLKGLSKAEAKRRAD-----EWLERLG----LGDRANKkveeLSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190
....*....|....*....|....*....|....*.
7VR1_B 630 ECTS---AVSIDV-EGKIF-QAAKDAGIaLLSiTHR 660
Cdd:COG4152 155 EPFSgldPVNVELlKDVIReLAAKGTTV-IFS-SHQ 188
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
486-661 |
9.45e-06 |
|
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: 49.03 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL---WPTYGGVLYK----------PPPQRM------------- 539
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyEPTSGRIIYHvalcekcgyvERPSKVgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 540 ----FYIPQRPYMSVGSLR-------------DQVIYPDSVEDMQRKGYSEQD-----LEaILDVVHLHHI---LQREgg 594
Cdd:TIGR03269 92 eevdFWNLSDKLRRRIRKRiaimlqrtfalygDDTVLDNVLEALEEIGYEGKEavgraVD-LIEMVQLSHRithIARD-- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7VR1_B 595 weamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSavSID------VEGKIFQAAKDAGIALLSITHRP 661
Cdd:TIGR03269 169 ----------LSGGEKQRVVLARQLAKEPFLFLADEPTG--TLDpqtaklVHNALEEAVKASGISMVLTSHWP 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
489-659 |
1.91e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKS----SLFRIL--------GGLWPTYGGVLYKPPPQ--------RMFYIPQRPYM 548
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGESLLHASEQtlrgvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 549 SVG---SLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQReggweaMCDWKDVLSGGEKQRIGMARMFYHRPKY 625
Cdd:PRK15134 104 SLNplhTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKR------LTDYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190
....*....|....*....|....*....|....*...
7VR1_B 626 ALLDECTSAVSIDVEGKIFQAAKD----AGIALLSITH 659
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRElqqeLNMGLLFITH 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
483-659 |
2.18e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.04 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 483 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY--------------KPPPQRMFYIPQRPY 547
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVgdivvsstskqkeiKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 548 msvGSLRDQVIYPDSVEDMQRKGYSEQDLEAI----LDVVHLHHILQREGGWEamcdwkdvLSGGEKQRIGMARMFYHRP 623
Cdd:PRK13643 95 ---SQLFEETVLKDVAFGPQNFGIPKEKAEKIaaekLEMVGLADEFWEKSPFE--------LSGGQMRRVAIAGILAMEP 163
|
170 180 190
....*....|....*....|....*....|....*....
7VR1_B 624 KYALLDECTSAVSIDVE---GKIFQAAKDAGIALLSITH 659
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
488-659 |
2.33e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.00 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 488 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK----PPPQRMFYIPQRPYMSVGSLRDQVIYPDS 562
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDgldtSDEENLWDIRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 563 VEDM----QRKGYSEQDLEAILDvvhlhHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS-- 636
Cdd:PRK13633 104 EEDVafgpENLGIPPEEIRERVD-----ESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDps 178
|
170 180
....*....|....*....|....*
7VR1_B 637 --IDVEGKIFQAAKDAGIALLSITH 659
Cdd:PRK13633 179 grREVVNTIKELNKKYGITIILITH 203
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
505-665 |
2.35e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 505 ITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFyipQRPYMS-VG---SLRDQVIYPDSVEDMQRKGYSEQDLEAI 579
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMqPSSGNIYYKNCNINNI---AKPYCTyIGhnlGLKLEMTVFENLKFWSEIYNSAETLYAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 580 LDVVHLHHILQREggweamCdwkDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID----VEGKIFQAAKDAGIALL 655
Cdd:PRK13541 108 IHYFKLHDLLDEK------C---YSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEnrdlLNNLIVMKANSGGIVLL 178
|
170
....*....|
7VR1_B 656 SiTHRPSLWK 665
Cdd:PRK13541 179 S-SHLESSIK 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
486-630 |
2.66e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.37 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRpymsvgslRDQVIYPDSVED 565
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQH--------QEELDPDKTVLD 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 566 -MQRkgYSEQDLEaildvVHLHHILQREG--GWEAmcdWK--DVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:COG0488 399 eLRD--GAPGGTE-----QEVRGYLGRFLfsGDDA---FKpvGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
483-659 |
3.09e-05 |
|
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: 46.58 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 483 TPSGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP----TYGGVLYK-------PPPQ-------RMFYIP 543
Cdd:COG0444 13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgiTSGEILFDgedllklSEKElrkirgrEIQMIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 544 QRPY------MSVGslrDQVIYPdsvedMQR-KGYSEQDLEA----ILDVVHLHHILQR------EggweamcdwkdvLS 606
Cdd:COG0444 93 QDPMtslnpvMTVG---DQIAEP-----LRIhGGLSKAEAREraieLLERVGLPDPERRldryphE------------LS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
7VR1_B 607 GGEKQRIGMARMFYHRPKYALLDECTSA--VSIdvegkifQA---------AKDAGIALLSITH 659
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTAldVTI-------QAqilnllkdlQRELGLAILFITH 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
486-633 |
3.30e-05 |
|
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: 45.96 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-------------KPPPQRMFYIPQRPY---- 547
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPDSGEVLIdgedisglseaelYRLRRRMGMLFQSGAlfds 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 548 MSVGslrDQVIYPDSvedmQRKGYSEQDLEAI----LDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRP 623
Cdd:cd03261 92 LTVF---ENVAFPLR----EHTRLSEEEIREIvlekLEAVGLRGAEDL---------YPAELSGGMKKRVALARALALDP 155
|
170
....*....|
7VR1_B 624 KYALLDECTS 633
Cdd:cd03261 156 ELLLYDEPTA 165
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
484-659 |
3.63e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 46.38 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 484 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYKPPP-----QRMFYIPQRPYMSVGSLRDQV 557
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKPidysrKGLMKLRESVGMVFQDPDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 IYPDSVEDMQrkgYSEQDLEAILDVVH--LHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAv 635
Cdd:PRK13636 96 FSASVYQDVS---FGAVNLKLPEDEVRkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG- 171
|
170 180 190
....*....|....*....|....*....|
7VR1_B 636 sIDVEGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13636 172 -LDPMGVseimklLVEMQKELGLTIIIATH 200
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
507-659 |
4.31e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.93 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 507 GPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQR-PYMSVGSLRDQVI---YP-------DSVE 564
Cdd:PRK10575 44 GHNGSGKSTLLKMLGRHQpPSEGEILLDAQPleswsskafaRKVAYLPQQlPAAEGMTVRELVAigrYPwhgalgrFGAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 565 DMQRkgyseqdLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI----DVE 640
Cdd:PRK10575 124 DREK-------VEEAISLVGLKPLAHR---------LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVL 187
|
170
....*....|....*....
7VR1_B 641 GKIFQAAKDAGIALLSITH 659
Cdd:PRK10575 188 ALVHRLSQERGLTVIAVLH 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
605-660 |
4.33e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 4.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSID----VEGKIFQAAKDAGIALLSITHR 660
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
471-659 |
7.02e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 45.26 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 471 EQGIICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG---VLYKPPPQRM-----FYI 542
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisILGQPTRQALqknlvAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 543 PQrpymsvgSLRDQVIYPDSVED---MQRKGY----------SEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGE 609
Cdd:PRK15056 84 PQ-------SEEVDWSFPVLVEDvvmMGRYGHmgwlrrakkrDRQIVTAALARVDMVEFRHRQIG---------ELSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
7VR1_B 610 KQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI---FQAAKDAGIALLSITH 659
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIislLRELRDEGKTMLVSTH 200
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
505-681 |
7.52e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.08 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 505 ITGPNGCGKSSLFRILGGLWPTYGGVLykpppqrmfyipqrpymSVGslrdqviypDSVedmqRKGYSEQDLEAI----- 579
Cdd:TIGR03719 353 VIGPNGAGKSTLFRMITGQEQPDSGTI-----------------EIG---------ETV----KLAYVDQSRDALdpnkt 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 580 --------LDVVHLhhilqreGGWE----AMCDW---------KDV--LSGGEKQRIGMARMFYHRPKYALLDECTSavS 636
Cdd:TIGR03719 403 vweeisggLDIIKL-------GKREipsrAYVGRfnfkgsdqqKKVgqLSGGERNRVHLAKTLKSGGNVLLLDEPTN--D 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
7VR1_B 637 IDVEgkIFQAAKDA-----GIALLsITH-RPSLWKYHTHLLQFDGEGGWKF 681
Cdd:TIGR03719 474 LDVE--TLRALEEAllnfaGCAVV-ISHdRWFLDRIATHILAFEGDSHVEW 521
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
502-663 |
7.58e-05 |
|
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: 43.52 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 502 HLLITGPNGCGKSSLFRILGGlwptyggvLYKPPPQRMFYIpqrpymsvgslrdqviypdsvedmqrkgyseqDLEAILD 581
Cdd:smart00382 4 VILIVGPPGSGKTTLARALAR--------ELGPPGGGVIYI--------------------------------DGEDILE 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 582 VVHLHHILQREGGWEAMcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDAGIALLSITHRP 661
Cdd:smart00382 44 EVLDQLLLIIVGGKKAS------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNL 117
|
..
7VR1_B 662 SL 663
Cdd:smart00382 118 TV 119
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
489-662 |
8.19e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.83 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------------TYGGVLYKPP--PQRM-------FYIPQR-P 546
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearvegevrLFGRNIYSPDvdPIEVrrevgmvFQYPNPfP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 547 YMSvgslrdqvIYPDSVEDMQRKGY--SEQDLEAILDVVhlhhiLQREGGWEA----MCDWKDVLSGGEKQRIGMARMFY 620
Cdd:PRK14267 99 HLT--------IYDNVAIGVKLNGLvkSKKELDERVEWA-----LKKAALWDEvkdrLNDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
7VR1_B 621 HRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALlsITHRPS 662
Cdd:PRK14267 166 MKPKILLMDEPTANIdpvgTAKIEELLFELKKEYTIVL--VTHSPA 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
491-669 |
9.07e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 45.06 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 491 ASLNIRVEEGMHLLitGPNGCGKSSLFRILGGL-WPTYGGVLYKPPP--------QRMFyipQR--------------PY 547
Cdd:PRK10419 31 VSLSLKSGETVALL--GRSGCGKSTLARLLVGLeSPSQGNVSWRGEPlaklnraqRKAF---RRdiqmvfqdsisavnPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 548 MSVG-SLRDQVIYPDSVEDMQRKGYSEQDLEAI-LDVVHLHHILQReggweamcdwkdvLSGGEKQRIGMARMFYHRPKY 625
Cdd:PRK10419 106 KTVReIIREPLRHLLSLDKAERLARASEMLRAVdLDDSVLDKRPPQ-------------LSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
7VR1_B 626 ALLDECTSAVSIDVEGKIFQAAKD----AGIALLSITHRPSLWKYHTH 669
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKlqqqFGTACLFITHDLRLVERFCQ 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
490-674 |
1.30e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 45.34 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 490 VASLNIRVEEGMHLLITGPNGCGKSSLFRILgglwptyggvlykpppQRmFYIPQRPY----------MSVGSLRDQ--V 557
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLL----------------QR-VFDPQSGRilidgtdirtVTRASLRRNiaV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 IYPD------SVEDMQRKGY---SEQDLEAILDVVHLHH-ILQREGGWEAMCDWK-DVLSGGEKQRIGMARMFYHRPKYA 626
Cdd:PRK13657 414 VFQDaglfnrSIEDNIRVGRpdaTDEEMRAAAERAQAHDfIERKPDGYDTVVGERgRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
7VR1_B 627 LLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPSLWKYHTHLLQFD 674
Cdd:PRK13657 494 ILDEATSALDVETEAKV-KAALDElmkGRTTFIIAHRLSTVRNADRILVFD 543
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
443-645 |
1.35e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 443 AQAGSGTI---GRSGVRVEGPLKIRG---------QVVDVEQGIICENIPIVTPSGEVVVaslnirveegmhllITGPNG 510
Cdd:PTZ00243 631 PSSASRHIvegGTGGGHEATPTSERSaktpkmktdDFFELEPKVLLRDVSVSVPRGKLTV--------------VLGATG 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 511 CGKSSLFRILGGLWPTYGGVLYKpppQRMF-YIPQRPYMSVGSLRDQVIYPDsvedmqrkgysEQDLEAILDVVHLHH-- 587
Cdd:PTZ00243 697 SGKSTLLQSLLSQFEISEGRVWA---ERSIaYVPQQAWIMNATVRGNILFFD-----------EEDAARLADAVRVSQle 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
7VR1_B 588 --ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQ 645
Cdd:PTZ00243 763 adLAQLGGGLETEIGEKGVnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVE 823
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
605-705 |
1.57e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.19 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG---KIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGgwKF 681
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG--KI 230
|
90 100
....*....|....*....|....
7VR1_B 682 EKLDSAARLSLTEEKQRLEQQLAG 705
Cdd:PRK10619 231 EEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
492-637 |
1.98e-04 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 44.34 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 492 SLNIRveEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-------------KPPPQRMFYIPQRPY------MSVG 551
Cdd:COG4608 38 SFDIR--RGETLGLVGESGCGKSTLGRLLLRLEePTSGEILFdgqditglsgrelRPLRRRMQMVFQDPYaslnprMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 552 slrDQVIYPDSVEDMQRKGYSEQDLEAILDVVHL--HHiLQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKYA 626
Cdd:COG4608 116 ---DIIAEPLRIHGLASKAERRERVAELLELVGLrpEH-ADRyphE------------FSGGQRQRIGIARALALNPKLI 179
|
170
....*....|...
7VR1_B 627 LLDECTSA--VSI 637
Cdd:COG4608 180 VCDEPVSAldVSI 192
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
486-663 |
2.20e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.32 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 486 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPPQRMFYIPQRPYmsvgsLRDQV--IYPDS 562
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGHDITRLKNREVPF-----LRRQIgmIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 563 VEDMQRKGYSEQDLEAILDVVHLHHI-------LQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECT--- 632
Cdd:PRK10908 89 HLLMDRTVYDNVAIPLIIAGASGDDIrrrvsaaLDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTgnl 168
|
170 180 190
....*....|....*....|....*....|..
7VR1_B 633 -SAVSIDVEgKIFQAAKDAGIALLSITHRPSL 663
Cdd:PRK10908 169 dDALSEGIL-RLFEEFNRVGVTVLMATHDIGL 199
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
485-662 |
2.48e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.32 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 485 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGlwptyggvlYKPPPQRMFYIPQRPY--MSVGSLR-------- 554
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG---------YYPLTEGEIRLDGRPLssLSHSVLRqgvamvqq 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 555 DQVIYPDSVEDMQRKG--YSEQDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK10790 423 DPVVLADTFLANVTLGrdISEEQVWQALETVQLAELARSlpDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190
....*....|....*....|....*....|....
7VR1_B 631 CTSAVSIDVEGKIFQA--AKDAGIALLSITHRPS 662
Cdd:PRK10790 503 ATANIDSGTEQAIQQAlaAVREHTTLVVIAHRLS 536
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
492-630 |
2.60e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 43.92 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 492 SLNIRVEEGMHLLitGPNGCGKSSLFRILGGLWPTYGGVL---------YKPPPQRMFYIPQR----PYMSVGslrDQVI 558
Cdd:PRK10851 22 SLDIPSGQMVALL--GPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrLHARDRKVGFVFQHyalfRHMTVF---DNIA 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7VR1_B 559 YPDSV---EDMQRKGYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 630
Cdd:PRK10851 97 FGLTVlprRERPNAAAIKAKVTQLLEMVQLAHLADR---------YPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
496-616 |
2.94e-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: 44.00 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 496 RVEEG-MH----LLITGPNGCGKSSLFRILGG-LWPTYGGVlykPPPQRMFYIPQrpYMSVGslrdqviYPDSVEDMQRK 569
Cdd:COG1245 357 EVEGGeIRegevLGIVGPNGIGKTTFAKILAGvLKPDEGEV---DEDLKISYKPQ--YISPD-------YDGTVEEFLRS 424
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
7VR1_B 570 GYSEqDLEA------ILDVVHLHHILQREggweaMCDwkdvLSGGEKQRIGMA 616
Cdd:COG1245 425 ANTD-DFGSsyykteIIKPLGLEKLLDKN-----VKD----LSGGELQRVAIA 467
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
605-634 |
3.67e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.25 E-value: 3.67e-04
10 20 30
....*....|....*....|....*....|
7VR1_B 605 LSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSA 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
493-635 |
4.25e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL-----------YKPPPQRMFYIPQRPYMSVGSLRDQVIYP 560
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIindshnlkdinLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 561 -DSVEDMQ-------RKGYSEQ---------------DLEAILDVVHLHHILQREGGWEAMCDWKDV------------- 604
Cdd:PTZ00265 484 lYSLKDLEalsnyynEDGNDSQenknkrnscrakcagDLNDMSNTTDSNELIEMRKNYQTIKDSEVVdvskkvlihdfvs 563
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
7VR1_B 605 ----------------LSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:PTZ00265 564 alpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
605-634 |
4.96e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.14 E-value: 4.96e-04
10 20 30
....*....|....*....|....*....|
7VR1_B 605 LSGGEKQRIGMARMFYHRPKYALLDECTSA 634
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
605-663 |
5.21e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.07 E-value: 5.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
7VR1_B 605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI----FQAAKDAGIALLSITHRPSL 663
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIadllFSLNREHGTTLILVTHDLQL 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
505-648 |
5.40e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 505 ITGPNGCGKSSLFRILGG-LWPTYGGVLYKPppqRMFYIPQrpYMSVGslrdqviYPDSVEDMQRKG---------YSEq 574
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGvLKPDEGEVDPEL---KISYKPQ--YIKPD-------YDGTVEDLLRSItddlgssyyKSE- 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7VR1_B 575 dleaILDVVHLHHILQREggweaMCDwkdvLSGGEKQRIGMARMFYHRPKYALLDEcTSAvSIDVEGKIfQAAK 648
Cdd:PRK13409 437 ----IIKPLQLERLLDKN-----VKD----LSGGELQRVAIAACLSRDADLYLLDE-PSA-HLDVEQRL-AVAK 494
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
493-644 |
7.45e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGG-VLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSvedmqrkg 570
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDAsVVIR---GTVAYVPQVSWIFNATVRDNILFGSP-------- 704
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7VR1_B 571 YSEQDLEAILDVVHLHHILQR-EGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIF 644
Cdd:PLN03130 705 FDPERYERAIDVTALQHDLDLlPGGDLTEIGERGVnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
489-645 |
7.88e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.78 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP-TYGGVLYK--PPPQ--------RMFYIPQRPYMsvgslrdqv 557
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHdiPLTKlqldswrsRLAVVSQTPFL--------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 558 iYPDSVED---MQRKGYSEQDLEAILDVVHLHH-ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECT 632
Cdd:PRK10789 401 -FSDTVANniaLGRPDATQQEIEHVARLASVHDdILRLPQGYDTEVGERGVmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170
....*....|...
7VR1_B 633 SAVSIDVEGKIFQ 645
Cdd:PRK10789 480 SAVDGRTEHQILH 492
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
489-659 |
9.80e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 41.54 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYKPPP----------QRMFYIPQRPYMSVG-SLRDQ 556
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARlLTPQSGTVFLGDKPismlssrqlaRRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 557 VIYPDS----------VEDMQRkgySEQDLEAildvVHLHHILQReggweAMCDwkdvLSGGEKQRIGMARMFYHRPKYA 626
Cdd:PRK11231 97 VAYGRSpwlslwgrlsAEDNAR---VNQAMEQ----TRINHLADR-----RLTD----LSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190
....*....|....*....|....*....|....*.
7VR1_B 627 LLDECTSAVSID--VE-GKIFQAAKDAGIALLSITH 659
Cdd:PRK11231 161 LLDEPTTYLDINhqVElMRLMRELNTQGKTVVTVLH 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
542-660 |
1.29e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.27 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 542 IPQRPYMSVGSLRDQViypDSVEDmqrkgYSEQDLEAILDVVHLHHILQREG-GWEA-MCDWKDVLSGGEKQRIGMARMF 619
Cdd:PLN03232 1315 IPQSPVLFSGTVRFNI---DPFSE-----HNDADLWEALERAHIKDVIDRNPfGLDAeVSEGGENFSVGQRQLLSLARAL 1386
|
90 100 110 120
....*....|....*....|....*....|....*....|...
7VR1_B 620 YHRPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHR 660
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEfkSCTMLVIAHR 1429
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
605-662 |
1.34e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.93 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
7VR1_B 605 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPS 662
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI-QAALDElqkNRTSLVIAHRLS 540
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
507-635 |
1.67e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.92 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 507 GPNGCGKSSLFRI---LGGLWPT---------YGGVLYKP---PPQ---RMFYIPQRPYMSVGSLRDQVIYPDSVEDMQr 568
Cdd:PRK14243 43 GPSGCGKSTILRCfnrLNDLIPGfrvegkvtfHGKNLYAPdvdPVEvrrRIGMVFQKPNPFPKSIYDNIAYGARINGYK- 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7VR1_B 569 kgyseQDLEAILDvvhlhHILQREGGWEAMcdwKD-------VLSGGEKQRIGMARMFYHRPKYALLDECTSAV 635
Cdd:PRK14243 122 -----GDMDELVE-----RSLRQAALWDEV---KDklkqsglSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
487-675 |
2.70e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.83 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 487 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQR-------MFYIPQRPYMsvgslrdqvi 558
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDGKTATrgdrsrfMAYLGHLPGL---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 559 ypdsvedmqrkgysEQDLEAI-----LDVVHLHHILQREGGWEA---MCDWKDV----LSGGEKQRIGMARMFYHRPKYA 626
Cdd:PRK13543 94 --------------KADLSTLenlhfLCGLHGRRAKQMPGSALAivgLAGYEDTlvrqLSAGQKKRLALARLWLSPAPLW 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
7VR1_B 627 LLDEctSAVSIDVEG-----KIFQAAKDAGIALLSITH--RPSLwKYHTHLLQFDG 675
Cdd:PRK13543 160 LLDE--PYANLDLEGitlvnRMISAHLRGGGAALVTTHgaYAAP-PVRTRMLTLEA 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
489-630 |
5.13e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.83 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 489 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY--------KPPPQR---M------FYipqrPYMSVg 551
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvvneLEPADRdiaMvfqnyaLY----PHMSV- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 552 slRDQVIYPDSVEDMQrKGYSEQDLEAILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALL 628
Cdd:PRK11650 94 --RENMAYGLKIRGMP-KAEIEERVAEAARILELEPLLDRkprE------------LSGGQRQRVAMGRAIVREPAVFLF 158
|
..
7VR1_B 629 DE 630
Cdd:PRK11650 159 DE 160
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
493-525 |
5.16e-03 |
|
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: 39.05 E-value: 5.16e-03
10 20 30
....*....|....*....|....*....|...
7VR1_B 493 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP 525
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP 73
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
483-530 |
5.31e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 39.29 E-value: 5.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
7VR1_B 483 TPSGEVVVAS-LNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGV 530
Cdd:COG1134 34 TRREEFWALKdVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPTSGRV 83
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|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
483-633 |
5.33e-03 |
|
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: 40.28 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 483 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYG-----GVLYKPPP----QRMF-YIPQRPYMSVGS 552
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiqidGVSWNSVTlqtwRKAFgVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 553 LRDQViypDSVEDmqrkgYSEQDLEAILDVVHLHHILQR----------EGGWeamcdwkdVLSGGEKQRIGMARMFYHR 622
Cdd:TIGR01271 1308 FRKNL---DPYEQ-----WSDEEIWKVAEEVGLKSVIEQfpdkldfvlvDGGY--------VLSNGHKQLMCLARSILSK 1371
|
170
....*....|.
7VR1_B 623 PKYALLDECTS 633
Cdd:TIGR01271 1372 AKILLLDEPSA 1382
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
505-659 |
6.50e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 39.35 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 505 ITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPP----------QRMFYIPQRPYMS-VGS---------LRDQVIypdSV 563
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIeKVKSGEIFYNNQAitddnfeklrKHIGIVFQNPDNQfVGSivkydvafgLENHAV---PY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7VR1_B 564 EDMQRKGYseqdlEAILDVvhlhhilqreggweAMCDWKD----VLSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDV 639
Cdd:PRK13648 117 DEMHRRVS-----EALKQV--------------DMLERADyepnALSGGQKQRVAIAGVLALNPSVIILDEATSM--LDP 175
|
170 180
....*....|....*....|....*.
7VR1_B 640 EGK------IFQAAKDAGIALLSITH 659
Cdd:PRK13648 176 DARqnlldlVRKVKSEHNITIISITH 201
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
504-573 |
8.24e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 8.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7VR1_B 504 LItGPNGCGKSSLFRILGG-LWPTYGGVLYKpPPQRMfyipqrpymsvGSLR-DQVIYPD-SVEDMQRKGYSE 573
Cdd:PRK15064 32 LI-GANGCGKSTFMKILGGdLEPSAGNVSLD-PNERL-----------GKLRqDQFAFEEfTVLDTVIMGHTE 91
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