|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-781 |
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: 1005.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 1 MPVLSRPRPWRGNTLKRTAVLLALAAYGAHKVYPLVRQCLAPARGLQAPAGEPTQEASGV----AAAKAGMNRVFLQRLL 76
Cdd:TIGR00954 1 MAVLSKYRLLRSTSNNKTDKQDSPAAVGMNKVIELKRERAADRRGDKSGKEELTIVGKHStiegAKKKAHVNGVFLGKLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 77 WLLRLLFPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEG 156
Cdd:TIGR00954 81 FLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 157 QLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSR 236
Cdd:TIGR00954 161 ELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTALGSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 237 GAGTAWPSaiaglvVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQ 316
Cdd:TIGR00954 241 GPAGLFAY------LFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 317 INLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATgysesdaeavKKAALEKKEEELVSErteaFTIARNLLTAAA 396
Cdd:TIGR00954 315 LNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKT----------HPAFLEMSEEELMQE----FYNNGRLLLKAA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 397 DAIERIMSSYKEVTELAGYTARVHEMFQVFEDVQRCHFKRPRELEDAQAGSGtiGRSGVRVEGplkirgtsmcfwpipvh 476
Cdd:TIGR00954 381 DALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREG--GRNSNLVPG----------------- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 477 pgregcragslrtsawsswapggfpaercwsarlpsqtvaaghrtdspfeglsldysfktrgmwsphpcrtaresssqca 556
Cdd:TIGR00954 --------------------------------------------------------------------------------
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 557 scwlpreAGQVVDVEQGIICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPP 636
Cdd:TIGR00954 442 -------RGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK 514
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 637 QRMFYIPQRPYMSVGSLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMA 716
Cdd:TIGR00954 515 GKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMA 594
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217391356 717 RMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGWKF 781
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
83-352 |
6.17e-122 |
|
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: 368.48 E-value: 6.17e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 83 FPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSF 162
Cdd:pfam06472 6 FPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQRLALRF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 163 RSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAgtaw 242
Cdd:pfam06472 86 RTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRGP---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 243 psAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILL 322
Cdd:pfam06472 162 --AILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILR 239
|
250 260 270
....*....|....*....|....*....|
gi 2217391356 323 ERLWYVMLEQFLMKYVWSASGLLMVAVPII 352
Cdd:pfam06472 240 RRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
574-779 |
1.32e-82 |
|
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: 261.70 E-value: 1.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSL 653
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 654 RDQVIYPdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 733
Cdd:cd03223 81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217391356 734 AVSIDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGW 779
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
122-788 |
1.22e-72 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 248.95 E-value: 1.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 122 IVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDV 201
Cdd:COG4178 55 LQARDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAEDI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 202 VAFAASVAHLYSNLtkplLDVAVT--SYT-----LLRAARSRGAGTAWpsAIAGLVVF------LTANVLrAFspKFG-- 266
Cdd:COG4178 135 RLFTETTLSLSLGL----LSSVVTliSFIgilwsLSGSLTFTLGGYSI--TIPGYMVWaaliyaIIGTLL-TH--LIGrp 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 267 --ELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILLerlWYVMLEQFLmkyvwSASGL 344
Cdd:COG4178 206 liRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIANWRRLIR---RQRNLTFFT-----TGYGQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 345 LMVAVPI-ITATGYsesdaeavkkaalekkeeelvserteaftIARNL----LTAAADAIERIMSS-------YKEVTEL 412
Cdd:COG4178 278 LAVIFPIlVAAPRY-----------------------------FAGEItlggLMQAASAFGQVQGAlswfvdnYQSLAEW 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 413 AGYTARVHEMFQVFEDVQRchfkrpreledAQAGSGTIGRSgvrvegplkirgtsmcfwpipvhpgregcRAGSLRtsaw 492
Cdd:COG4178 329 RATVDRLAGFEEALEAADA-----------LPEAASRIETS-----------------------------EDGALA---- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 493 sswapggfpaercwsarlpsqtvaaghrtdspFEGLSLDysfktrgmwsphpcrtaresssqcascwlpreagqvvdveq 572
Cdd:COG4178 365 --------------------------------LEDLTLR----------------------------------------- 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 573 giicenipivTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGS 652
Cdd:COG4178 372 ----------TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGT 441
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 LRDQVIYPDSVEDmqrkgYSEQDLEAILDVVHLHHILQR--EGGweamcDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:COG4178 442 LREALLYPATAEA-----FSDAELREALEAVGLGHLAERldEEA-----DWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 731 CTSAVSIDVEGKIFQAAKDA--GIALLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAA 788
Cdd:COG4178 512 ATSALDEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
582-759 |
1.74e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.76 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 582 VTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYK-------PPP---QRMFYIPQRPYMSV 650
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGeIYLDgkplsamPPPewrRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 GSLRDQVIYPDSvedMQRKGYSEQDLEAILDVVHL-HHILQreggweamcdwKDV--LSGGEKQRIGMARMFYHRPKYAL 727
Cdd:COG4619 88 GTVRDNLPFPFQ---LRERKFDRERALELLERLGLpPDILD-----------KPVerLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217391356 728 LDECTSAVSID----VEGKIFQAAKDAGIALLSITH 759
Cdd:COG4619 154 LDEPTSALDPEntrrVEELLREYLAEEGRAVLWVSH 189
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
574-763 |
3.44e-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: 107.92 E-value: 3.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVL---------YKPPP--QRMFYI 642
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 643 PQRPYMSVGSLRDQViypdsveDMQRKGYSEQDLEAILDVVHLHHILQR-EGGWEAMcdwkdV------LSGGEKQRIGM 715
Cdd:COG4988 417 PQNPYLFAGTIRENL-------RLGRPDASDEELEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRLAL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217391356 716 ARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPSL 763
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlaKGRTVILITHRLAL 534
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
584-763 |
9.06e-24 |
|
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: 98.61 E-value: 9.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY-------KPPP----QRMFYIPQRPYmsvgs 652
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrDLDLeslrKNIAYVPQDPF----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 lrdqvIYPDSVEDmqrkgyseqdleaildvvhlhhilqreggweamcdwkDVLSGGEKQRIGMARMFYHRPKYALLDECT 732
Cdd:cd03228 87 -----LFSGTIRE-------------------------------------NILSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190
....*....|....*....|....*....|...
gi 2217391356 733 SAVSIDVEGKIFQA--AKDAGIALLSITHRPSL 763
Cdd:cd03228 125 SALDPETEALILEAlrALAKGKTVIVIAHRLST 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
584-763 |
1.48e-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: 103.38 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGvlykpppqRMFY--IPQRpYMSVGSLRDQV---- 657
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG--------RILIdgIDLR-QIDPASLRRQIgvvl 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 658 ----IYPDSVED---MQRKGYSEQDLEAILDVVHLHH-ILQREGGWEAMcdwkdV------LSGGEKQRIGMARMFYHRP 723
Cdd:COG2274 556 qdvfLFSGTIREnitLGDPDATDEEIIEAARLAGLHDfIEALPMGYDTV-----VgeggsnLSGGQRQRLAIARALLRNP 630
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217391356 724 KYALLDECTSAVSIDVEGKIFQA--AKDAGIALLSITHRPSL 763
Cdd:COG2274 631 RILILDEATSALDAETEAIILENlrRLLKGRTVIIIAHRLST 672
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
574-763 |
1.91e-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: 92.28 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGE-VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLykpppqrmfyIPQRPYMSVG 651
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLrPTSGRVR----------LDGADISQWD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 652 S--LRDQViypdsvedmqrkGYSEQDLE----AILDvvhlhhilqreggweamcdwkDVLSGGEKQRIGMARMFYHRPKY 725
Cdd:cd03246 71 PneLGDHV------------GYLPQDDElfsgSIAE---------------------NILSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217391356 726 ALLDECTSAVSIDVEGKIFQA---AKDAGIALLSITHRPSL 763
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPET 158
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
589-763 |
6.89e-21 |
|
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: 91.88 E-value: 6.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY------KPPP----QRMFYIPQRPYMSVGSLRDQV 657
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkPTSGSVLLdgtdirQLDPadlrRNIGYVPQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 658 IYpdsvedmqrkGYSEQDLEAILDVVHLHHILQ-------------REGGweamcdwkDVLSGGEKQRIGMARMFYHRPK 724
Cdd:cd03245 99 TL----------GAPLADDERILRAAELAGVTDfvnkhpngldlqiGERG--------RGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217391356 725 YALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPSL 763
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSL 201
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
593-763 |
2.36e-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: 88.46 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFYIPQrpymsvgsLRDQVIYpdsvedmqrkgy 671
Cdd:cd00267 18 VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKDIAKLPLEE--------LRRRIGY------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 672 seqdleaildvvhlhhILQreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDA- 750
Cdd:cd00267 78 ----------------VPQ--------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELa 127
|
170
....*....|....*
gi 2217391356 751 --GIALLSITHRPSL 763
Cdd:cd00267 128 eeGRTVIIVTHDPEL 142
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
593-767 |
7.77e-20 |
|
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: 88.68 E-value: 7.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQRPymsvgslRDQVIYPd 661
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGKDltklslkelrRKVGLVFQNP-------DDQFFGP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 662 SVED-----MQRKGYSEQDLEAI----LDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECT 732
Cdd:cd03225 92 TVEEevafgLENLGLPEEEIEERveeaLELVGLEGLRDRS---------PFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217391356 733 SavSIDVEG-----KIFQAAKDAGIALLSITHRPSLWKYH 767
Cdd:cd03225 163 A--GLDPAGrrellELLKKLKAEGKTIIIVTHDLDLLLEL 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
593-733 |
7.78e-20 |
|
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: 86.93 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRIL-GGLWPTYGGVLY----------KPPPQRMFYIPQ----RPYMSVgslRDQV 657
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPTEGTILLdgqdltdderKSLRKEIGYVFQdpqlFPRLTV---RENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217391356 658 IYPDSVEDMQRKGYSEQDLEAI--LDVVHLHHILQREGGweamcdwkDVLSGGEKQRIGMARMFYHRPKYALLDECTS 733
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALekLGLGDLADRPVGERP--------GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
561-762 |
8.12e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.08 E-value: 8.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 561 PREAGQVVDVEQGIICENipiVT---PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------TYGGV- 630
Cdd:COG1132 327 PPGAVPLPPVRGEIEFEN---VSfsyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDptsgriLIDGVd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 631 --------LYKpppqRMFYIPQRPYMSVGSLRDQVIYPdsvedmqRKGYSEQDLEAILDVVHLHH-ILQREGGWEAMcdw 701
Cdd:COG1132 404 irdltlesLRR----QIGVVPQDTFLFSGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEfIEALPDGYDTV--- 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217391356 702 kdV------LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 762
Cdd:COG1132 470 --VgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERlmKGRTTIVIAHRLS 536
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
585-771 |
9.41e-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: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 585 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYkppPQRMFYIPQRPYMSVGSLRDQVIYpDSV 663
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSGSVSV---PGSIAYVSQEPWIQNGTIRENILF-GKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 664 EDMQRkgyseqdLEAILDVVHLHHILQR-EGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG 741
Cdd:cd03250 92 FDEER-------YEKVIKACALEPDLEIlPDGDLTEIGEKGInLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190
....*....|....*....|....*....|....*
gi 2217391356 742 KIFQ-----AAKDAGIALLsITHRPSLWKYHTHLL 771
Cdd:cd03250 165 HIFEncilgLLLNNKTRIL-VTHQLQLLPHADQIV 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
585-776 |
7.93e-19 |
|
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: 85.66 E-value: 7.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 585 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKPPPQRMF-----YIPQRPYMSvgslRDqvi 658
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPTSGSIRVFGKPLEKErkrigYVPQRRSID----RD--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 659 YPDSVED---MQR-------KGYSEQDLEAI---LDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKY 725
Cdd:cd03235 83 FPISVRDvvlMGLyghkglfRRLSKADKAKVdeaLERVGLSELADRQIG---------ELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217391356 726 ALLDECTSAVsiDVEGK-----IFQAAKDAGIALLSITH-RPSLWKYHTHLLQFDGE 776
Cdd:cd03235 154 LLLDEPFAGV--DPKTQediyeLLRELRREGMTILVVTHdLGLVLEYFDRVLLLNRT 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
574-766 |
1.90e-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: 84.85 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEVVVASL---NIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGV------LYKPPP------- 636
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVrvdgtdISKLSEkelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 637 -QRMFYIPQR----PYMSVgslRDQVIYPDSVEDMQRKGYsEQDLEAILDVVHLHHILQReggweaMCDWkdvLSGGEKQ 711
Cdd:cd03255 81 rRHIGFVFQSfnllPDLTA---LENVELPLLLAGVPKKER-RERAEELLERVGLGDRLNH------YPSE---LSGGQQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217391356 712 RIGMARMFYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSLWKY 766
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEY 206
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
577-763 |
2.00e-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: 89.71 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 577 ENIPIVTPSGE-VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVL------YKPPPQRMF-----YIPQ 644
Cdd:TIGR01842 320 ENVTIVPPGGKkPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadLKQWDRETFgkhigYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 645 RPYMSVGSLRDqviypdSVEDMQRKGYSEQDLEA-ILDVVHlHHILQREGGWE-AMCDWKDVLSGGEKQRIGMARMFYHR 722
Cdd:TIGR01842 400 DVELFPGTVAE------NIARFGENADPEKIIEAaKLAGVH-ELILRLPDGYDtVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217391356 723 PKYALLDECTSavSIDVEGKI-----FQAAKDAGIALLSITHRPSL 763
Cdd:TIGR01842 473 PKLVVLDEPNS--NLDEEGEQalanaIKALKARGITVVVITHRPSL 516
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
586-759 |
4.92e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.00 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-------PPP---QRMFYIPQRPYMSVGSLR 654
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsPTSGTLLFEgedistlKPEiyrQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 655 DQVIYPdsvEDMQRKGYSEQDLEAILDVVHL-HHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTS 733
Cdd:PRK10247 99 DNLIFP---WQIRNQQPDPAIFLDDLERFALpDTILTKN---------IAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190
....*....|....*....|....*....|
gi 2217391356 734 AVS----IDVEGKIFQAAKDAGIALLSITH 759
Cdd:PRK10247 167 ALDesnkHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
586-761 |
1.38e-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: 82.14 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYK---------PPPQRMFYIPQRPymsvgslrd 655
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGeVLWNgepirdareDYRRRLAYLGHAD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 656 qVIYPD-SVED-------MQRKGYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYAL 727
Cdd:COG4133 85 -GLKPElTVREnlrfwaaLYGLRADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217391356 728 LDECTSAvsIDVEGK-----IFQAAKDAGIALLSITHRP 761
Cdd:COG4133 155 LDEPFTA--LDAAGVallaeLIAAHLARGGAVLLTTHQP 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
584-762 |
1.66e-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: 86.74 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------TYGGVLYKPPP-----QRMFYIPQRPYMSVGS 652
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpqsgsiTLGGVDLRDLDeddlrRRIAVVPQRPHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 LRD--QVIYPDSvedmqrkgySEQDLEAILDVVHLHHILQR-EGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALL 728
Cdd:COG4987 425 LREnlRLARPDA---------TDEELWAALERVGLGDWLAAlPDGLDTWLGEGGRrLSGGERRRLALARALLRDAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217391356 729 DECTSAVSIDVEGKI----FQAAKDAgiALLSITHRPS 762
Cdd:COG4987 496 DEPTEGLDAATEQALladlLEALAGR--TVLLITHRLA 531
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
586-763 |
2.31e-17 |
|
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: 80.56 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYkpppqrmfyipqrpymsvgsLRDQviypdSVED 665
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL--------------------LDGK-----DLAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 666 MQRK------GYSEQDLEAiLDVVHLhhilqreggweAMCDWkDVLSGGEKQRIGMARMFYHRPKYALLDECTSAV---- 735
Cdd:cd03214 66 LSPKelarkiAYVPQALEL-LGLAHL-----------ADRPF-NELSGGERQRVLLARALAQEPPILLLDEPTSHLdiah 132
|
170 180
....*....|....*....|....*...
gi 2217391356 736 SIDVEGKIFQAAKDAGIALLSITHRPSL 763
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNL 160
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
574-763 |
3.67e-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: 85.42 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV-------LYKPPP----QRMFYI 642
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavngvpLADADAdswrDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 643 PQRPYMSVGSLRDQVIypdsvedMQRKGYSEQDLEAILDVVHLHHILQ-REGGWEAMCDWKDV-LSGGEKQRIGMARMFY 720
Cdd:TIGR02857 402 PQHPFLFAGTIAENIR-------LARPDASDAEIREALERAGLDEFVAaLPQGLDTPIGEGGAgLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217391356 721 HRPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHRPSL 763
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLAL 519
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
560-763 |
3.82e-17 |
|
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: 85.57 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 560 LPREAGQVVdveqgiiCENIPIVTP-SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV-------L 631
Cdd:COG4618 324 LPRPKGRLS-------VENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSvrldgadL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 632 YKPPPQR----MFYIPQrpymsvgslrDQVIYPDSVED----MQrkgysEQDLEAILD---VVHLHHILQR--------- 691
Cdd:COG4618 397 SQWDREElgrhIGYLPQ----------DVELFDGTIAEniarFG-----DADPEKVVAaakLAGVHEMILRlpdgydtri 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217391356 692 -EGGweamcdwkDVLSGGEKQRIGMARMFYHRPKYALLDECTSavSIDVEG-----KIFQAAKDAGIALLSITHRPSL 763
Cdd:COG4618 462 gEGG--------ARLSGGQRQRIGLARALYGDPRLVVLDEPNS--NLDDEGeaalaAAIRALKARGATVVVITHRPSL 529
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
577-759 |
4.17e-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: 80.76 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 577 ENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY--KPPPQRMFYipQRPYMSVGSL 653
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLngKPIKAKERR--KSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 654 RDQvIYPDSVED-----MQRKGYSEQDLEAILDVVHLHhilqreggweamcDWKDV----LSGGEKQRIGMARMFYHRPK 724
Cdd:cd03226 81 DYQ-LFTDSVREelllgLKELDAGNEQAETVLKDLDLY-------------ALKERhplsLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217391356 725 YALLDECTSAV---SIDVEGKIFQAAKDAGIALLSITH 759
Cdd:cd03226 147 LLIFDEPTSGLdykNMERVGELIRELAAQGKAVIVITH 184
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
586-763 |
7.97e-17 |
|
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: 80.86 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY---KP----PP----QRMFYIPQRPYMSVGSlr 654
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlaslSRrelaRRIAYVPQEPPAPFGL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 655 dqviypdSVED---MQRKGY-------SEQDLEAI---LDVVHLHHILQReggweamcDWkDVLSGGEKQRIGMARMFYH 721
Cdd:COG1120 91 -------TVRElvaLGRYPHlglfgrpSAEDREAVeeaLERTGLEHLADR--------PV-DELSGGERQRVLIARALAQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217391356 722 RPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 763
Cdd:COG1120 155 EPPLLLLDEPTSHLdlahQLEVLELLRRLARERGRTVVMVLHDLNL 200
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
584-763 |
1.15e-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: 80.07 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK---PPPQRMFYIPQRpymsVGSL----RD 655
Cdd:COG1122 11 PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLkPTSGEVLVDgkdITKKNLRELRRK----VGLVfqnpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 656 QVIYPdSVED-----MQRKGYSEQDLEA----ILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYA 726
Cdd:COG1122 87 QLFAP-TVEEdvafgPENLGLPREEIRErveeALELVGLEHLADRP---------PHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217391356 727 LLDECTSavSIDVEGK-----IFQAAKDAGIALLSITHRPSL 763
Cdd:COG1122 157 VLDEPTA--GLDPRGRrelleLLKRLNKEGKTVIIVTHDLDL 196
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
574-762 |
1.82e-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: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYI 642
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYdPQKGQILIDGIDirdisrkslrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 643 PQRPYMSVGSLRDQVIYPDSVEDmqrkgysEQDLEAILDVVHLHH-ILQREGGWEA-MCDWKDVLSGGEKQRIGMARMFY 720
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNAT-------DEEVIEAAKEAGAHDfIMKLPNGYDTvLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217391356 721 HRPKYALLDECTSavSIDVEG-KIFQAAKDA---GIALLSITHRPS 762
Cdd:cd03254 156 RDPKILILDEATS--NIDTETeKLIQEALEKlmkGRTSIIIAHRLS 199
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
586-759 |
2.35e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYG-----GVLYKPPPQRMFYIPQRPYMSVGslrdqviY 659
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLLPPTSGtvrlfGKPPRRARRRIGYVPQRAEVDWD-------F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 660 PDSVED---MQR-------KGYSEQDLEAI---LDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRP 723
Cdd:COG1121 91 PITVRDvvlMGRygrrglfRRPSRADREAVdeaLERVGLEDLADRpigE------------LSGGQQQRVLLARALAQDP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217391356 724 KYALLDECTSAVsiDVEG-----KIFQAAKDAGIALLSITH 759
Cdd:COG1121 159 DLLLLDEPFAGV--DAATeealyELLRELRREGKTILVVTH 197
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
583-730 |
4.34e-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: 78.98 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 583 TPSGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY------KPPPQRMfYIPQR----PYMSV 650
Cdd:COG1116 19 TGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEkPTSGEVLVdgkpvtGPGPDRG-VVFQEpallPWLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 gslRDQVIYPDSVEDMqRKGYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:COG1116 98 ---LDNVALGLELRGV-PKAERRERARELLELVGLAGFEDA---------YPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
588-730 |
4.54e-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: 77.90 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY-----KPPPQRMFYIPQR----PYMSVgslRDQV 657
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLeRPTSGEVLVdgepvTGPGPDRGYVFQQdallPWLTV---LDNV 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217391356 658 IYPDSVEDMQRKGySEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 730
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 ... |
589-759 |
5.80e-16 |
|
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: 77.99 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW------PTYGGVLYKPPP------------QRMFYIPQRPYMSV 650
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgaPDEGEVLLDGKDiydldvdvlelrRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 GSLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLhhilqreggWEAMCDWKDV--LSGGEKQRIGMARMFYHRPKYALL 728
Cdd:cd03260 95 GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAAL---------WDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190
....*....|....*....|....*....|....*
gi 2217391356 729 DECTSAVSI----DVEGKIFQAAKDAGIALlsITH 759
Cdd:cd03260 166 DEPTSALDPistaKIEELIAELKKEYTIVI--VTH 198
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
584-763 |
1.29e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 77.01 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASL---NIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK-------PPPQR-MF------YIPQR 645
Cdd:COG1136 15 GTGEGEVTALrgvSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPTSGEVLIDgqdisslSERELaRLrrrhigFVFQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 646 ----PYMSVgslRDQVIYPDSVEDMQRKGySEQDLEAILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARM 718
Cdd:COG1136 95 fnllPELTA---LENVALPLLLAGVSRKE-RRERARELLERVGLGDRLDHrpsQ------------LSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217391356 719 FYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 763
Cdd:COG1136 159 LVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTHDPEL 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
586-759 |
4.06e-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: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYK-------PPPQRMF-YIPQR----PYMSVgs 652
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFIKPDSGKILLNgkditnlPPEKRDIsYVPQNyalfPHMTV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 lRDQVIYPDSVEDMQRKGYSEQDLEaILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECT 732
Cdd:cd03299 89 -YKNIAYGLKKRKVDKKEIERKVLE-IAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|.
gi 2217391356 733 SAVSIDVEGKIFQAAKDA----GIALLSITH 759
Cdd:cd03299 158 SALDVRTKEKLREELKKIrkefGVTVLHVTH 188
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
586-759 |
4.24e-15 |
|
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: 75.35 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK-------PPPQRMF-YIPQR----PYMSVGs 652
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFeTPTSGEILLDgkditnlPPHKRPVnTVFQNyalfPHLTVF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 lrDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALL 728
Cdd:cd03300 91 --ENIAFG-----LRLKKLPKAEIKErvaeALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217391356 729 DECTSAV------SIDVEGKIFQaaKDAGIALLSITH 759
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 ... |
605-762 |
1.14e-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: 73.87 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 605 ITGPNGCGKSSLFRILGGLWPTYGGVLY--------------KPPPQRMF-YIPQR----PYMSVgslRDQVIYpdsveD 665
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinLPPQQRKIgLVFQQyalfPHLNV---RENLAF-----G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 666 MQRKGYSE--QDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI 743
Cdd:cd03297 100 LKRKRNREdrISVDELLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180
....*....|....*....|...
gi 2217391356 744 F----QAAKDAGIALLSITHRPS 762
Cdd:cd03297 171 LpelkQIKKNLNIPVIFVTHDLS 193
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
584-762 |
1.67e-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: 74.06 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK--------PPPQR--MFYIPQRPYMSVGS 652
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYvPENGRVLVDghdlaladPAWLRrqVGVVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 LRDQVIYPDSVEDMQRKGYSeqdleAILDVVHlHHILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDEC 731
Cdd:cd03252 92 IRDNIALADPGMSMERVIEA-----AKLAGAH-DFISELPEGYDTIVGEQGAgLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190
....*....|....*....|....*....|...
gi 2217391356 732 TSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 762
Cdd:cd03252 166 TSALDYESEHAIMRNMHDicAGRTVIIIAHRLS 198
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
586-762 |
1.99e-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: 72.94 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY------KPPPQR-----MFyipQR----PYMS 649
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLeRPDSGEILIdgrdvtGVPPERrnigmVF---QDyalfPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 650 VgslRDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKY 725
Cdd:cd03259 89 V---AENIAFG-----LKLRGVPKAEIRArvreLLELVGLEGLLNR---------YPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217391356 726 ALLDECTSAvsIDVE------GKIFQAAKDAGIALLSITHRPS 762
Cdd:cd03259 152 LLLDEPLSA--LDAKlreelrEELKELQRELGITTIYVTHDQE 192
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
584-759 |
2.85e-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: 72.07 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRIL-GGLWPTYGGVLYKPPP------------QRMFYIPQRPymsv 650
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLnGLLRPQSGAVLIDGEPldysrkgllerrQRVGLVFQDP---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 gslRDQVIYPDSVEDM----QRKGYSEQDLEAI----LDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHR 722
Cdd:TIGR01166 78 ---DDQLFAADVDQDVafgpLNLGLSEAEVERRvreaLTAVGASGLRERP---------THCLSGGEKKRVAIAGAVAMR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217391356 723 PKYALLDECTSAVsiDVEG-----KIFQAAKDAGIALLSITH 759
Cdd:TIGR01166 146 PDVLLLDEPTAGL--DPAGreqmlAILRRLRAEGMTVVISTH 185
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
593-762 |
4.02e-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: 72.57 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL--------YKPPPQR--MFYIPQRPYMSVGSLRDQVIYPD 661
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYdPTSGEILldgvdirdLNLRWLRsqIGLVSQEPVLFDGTIAENIRYGK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 662 svedmqRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVE 740
Cdd:cd03249 102 ------PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180
....*....|....*....|....*
gi 2217391356 741 gKIFQAAKD---AGIALLSITHRPS 762
Cdd:cd03249 176 -KLVQEALDramKGRTTIVIAHRLS 199
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
589-759 |
5.15e-14 |
|
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: 72.53 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------TYGGVLYKPPPQRMFY-----IPQRPYMSV---GSLR 654
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERpwsgevTFDGRPVTRRRRKAFRrrvqmVFQDPYASLhprHTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 655 DQVIYPDSVedmQRKGYSEQDLEAILDVVHLH-HILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:COG1124 100 RILAEPLRI---HGLPDREERIAELLEQVGLPpSFLDRyphQ------------LSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217391356 731 CTSAVsiDVegkIFQAA---------KDAGIALLSITH 759
Cdd:COG1124 165 PTSAL--DV---SVQAEilnllkdlrEERGLTYLFVSH 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
594-730 |
5.78e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.49 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 594 NIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVG-SLRDQVI--YPDSVEDMQRK- 669
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLdgDAELRALEAELe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 670 ------GYSEQDLEAIldvVHLHHILQREGGWEA--------------MCDW-KDV--LSGGEKQRIGMARMFYHRPKYA 726
Cdd:COG0488 98 eleaklAEPDEDLERL---AELQEEFEALGGWEAearaeeilsglgfpEEDLdRPVseLSGGWRRRVALARALLSEPDLL 174
|
....
gi 2217391356 727 LLDE 730
Cdd:COG0488 175 LLDE 178
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
586-761 |
6.30e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYKPPPQ-------RMFYIPQR----PYMSVGsl 653
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDIddpdvaeACHYLGHRnamkPALTVA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 654 rdqviypDSVEDMQR-KGYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMAR-MFYHRPKYaLLDEC 731
Cdd:PRK13539 92 -------ENLEFWAAfLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARlLVSNRPIW-ILDEP 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217391356 732 TSAvsIDVEGK-----IFQA-AKDAGIALLSiTHRP 761
Cdd:PRK13539 155 TAA--LDAAAValfaeLIRAhLAQGGIVIAA-THIP 187
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
588-759 |
8.69e-14 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 71.63 E-value: 8.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY--KPPP-------QRMFYIPQRPYMsvgslrdqv 657
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPTSGEVRVlgEDVArdpaevrRRIGYVPQEPAL--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 658 iYPD-SVEDM---------QRKGYSEQDLEAILDVVHLHHILQREGGWeamcdwkdvLSGGEKQRIGMARMFYHRPKYAL 727
Cdd:COG1131 85 -YPDlTVRENlrffarlygLPRKEARERIDELLELFGLTDAADRKVGT---------LSGGMKQRLGLALALLHDPELLI 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217391356 728 LDECTSAVsiDVEG-----KIFQAAKDAGIA-LLSiTH 759
Cdd:COG1131 155 LDEPTSGL--DPEArrelwELLRELAAEGKTvLLS-TH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
574-764 |
1.06e-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: 74.55 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV----------LYKPPPQ----R 638
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIsgevlldgrdLLELSEAlrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 639 MFYIPQRPYMSVGSLR--DQVIYPDSVEDMQRKGYSEQDLEAiLDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMA 716
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgDQIAEALENLGLSRAEARARVLEL-LEAVGLERRLDR---------YPHQLSGGQRQRVAIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217391356 717 RMFYHRPKYALLDECTSA----VSIDVEGKIFQAAKDAGIALLSITHRPSLW 764
Cdd:COG1123 155 MALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
593-759 |
1.08e-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: 71.34 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK------PPPQRMFYIPQR---PYMSVgslRDQV-IYPD 661
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitePGPDRMVVFQNYsllPWLTV---RENIaLAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 662 SVEDMQRKGYSEQDLEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI---- 737
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALVGLTEAADKR---------PGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrg 151
|
170 180
....*....|....*....|..
gi 2217391356 738 DVEGKIFQAAKDAGIALLSITH 759
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTH 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
588-759 |
1.58e-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: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEG--MHLLitGPNGCGKSSLFRILGGLW-PTYGGVLY--KPPP-------QRMFYIPQRPYmsvgslrd 655
Cdd:cd03230 14 TALDDISLTVEKGeiYGLL--GPNGAGKTTLIKIILGLLkPDSGEIKVlgKDIKkepeevkRRIGYLPEEPS-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 656 qvIYPD-SVEDmqrkgyseqdleaildvvHLHhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSA 734
Cdd:cd03230 84 --LYENlTVRE------------------NLK------------------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190
....*....|....*....|....*....|
gi 2217391356 735 vsIDVEG-----KIFQAAKDAGIALLSITH 759
Cdd:cd03230 126 --LDPESrrefwELLRELKKEGKTILLSSH 153
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
580-759 |
2.26e-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: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 580 PIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-------------KPPPQRMFYIPQR 645
Cdd:COG1123 271 PVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrPTSGSILFdgkdltklsrrslRELRRRVQMVFQD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 646 PY------MSVGslrDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLH-HILQR---EggweamcdwkdvLSGGEKQRIGM 715
Cdd:COG1123 351 PYsslnprMTVG---DIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRyphE------------LSGGQRQRVAI 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217391356 716 ARMFYHRPKYALLDECTSA--VSIdvegkifQA---------AKDAGIALLSITH 759
Cdd:COG1123 416 ARALALEPKLLILDEPTSAldVSV-------QAqilnllrdlQRELGLTYLFISH 463
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
586-761 |
3.56e-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: 70.11 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY----KPPPQRMFYIpqRPYMSV--GSLRDQVI 658
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlfgeRRGGEDVWEL--RKRIGLvsPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 659 YPDSVEDMQRKG----------YSEQDLE---AILDVVHLHHILQREggweamcdWKDvLSGGEKQRIGMARMFYHRPKY 725
Cdd:COG1119 93 RDETVLDVVLSGffdsiglyrePTDEQRErarELLELLGLAHLADRP--------FGT-LSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217391356 726 ALLDECTSavSIDVEGK------IFQAAKDAGIALLSITHRP 761
Cdd:COG1119 164 LILDEPTA--GLDLGARelllalLDKLAAEGAPTLVLVTHHV 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
589-759 |
3.83e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSvgslrdqVIYPDSVED--M 666
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLD-------TTLPLTVNRflR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 667 QRKGYSEQDLEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVsiDVEGK---- 742
Cdd:PRK09544 92 LRPGTKKEDILPALKRVQAGHLIDAP---------MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV--DVNGQvaly 160
|
170
....*....|....*....
gi 2217391356 743 --IFQAAKDAGIALLSITH 759
Cdd:PRK09544 161 dlIDQLRRELDCAVLMVSH 179
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
574-762 |
3.96e-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: 69.95 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL--------YKPPPQR--MFYI 642
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYdVSSGSILidgqdireVTLDSLRraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 643 PQrpymsvgslrDQVIYPDSVEDMQRKG---YSEQDLEAILDVVHLHH-ILQREGGWEAMCDWKDV-LSGGEKQRIGMAR 717
Cdd:cd03253 81 PQ----------DTVLFNDTIGYNIRYGrpdATDEEVIEAAKAAQIHDkIMRFPDGYDTIVGERGLkLSGGEKQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217391356 718 MFYHRPKYALLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHRPS 762
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDvsKGRTTIVIAHRLS 197
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
588-760 |
9.16e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 68.08 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVL---YKP----PPQRMFYIPQR----PYMSVgslRDQ 656
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdGKPldiaARNRIGYLPEErglyPKMKV---IDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 657 VIYPDSVEDMQRKgYSEQDLEAILDVVHLHhilqreggweamcDWKDV----LSGGEKQRIGMARMFYHRPKYALLDECT 732
Cdd:cd03269 91 LVYLAQLKGLKKE-EARRRIDEWLERLELS-------------EYANKrveeLSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190
....*....|....*....|....*....|.
gi 2217391356 733 SA---VSIDVEGKIFQAAKDAGIALLSITHR 760
Cdd:cd03269 157 SGldpVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
605-775 |
9.54e-13 |
|
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: 68.65 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 605 ITGPNGCGKSSLFRILGGLWPTYGGVLY---KPPPQ--------RMFYIPQRPYMSVGSLRDQVIYpdsveDMQRKgySE 673
Cdd:cd03248 45 LVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQyehkylhsKVSLVGQEPVLFARSLQDNIAY-----GLQSC--SF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 674 QDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKD-- 749
Cdd:cd03248 118 ECVKEAAQKAHAHSFISElaSGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDwp 197
|
170 180
....*....|....*....|....*.
gi 2217391356 750 AGIALLSITHRPSLWKYHTHLLQFDG 775
Cdd:cd03248 198 ERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
588-760 |
1.01e-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: 68.62 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEG-MHLLItGPNGCGKSSLFRILGG-LWPTYGGVLYK-------PPPQ-------RMFYIPqRPY--MS 649
Cdd:cd03219 14 VALDDVSFSVRPGeIHGLI-GPNGAGKTTLFNLISGfLRPTSGSVLFDgeditglPPHEiarlgigRTFQIP-RLFpeLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 650 V------GSLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRP 723
Cdd:cd03219 92 VlenvmvAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAG---------ELSYGQQRRLEIARALATDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217391356 724 KYALLDECTSAVS---IDVEGKIFQAAKDAGIALLSITHR 760
Cdd:cd03219 163 KLLLLDEPAAGLNpeeTEELAELIRELRERGITVLLVEHD 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
589-759 |
1.05e-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: 68.30 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-----PPPQRMF--------YIPQRPY------M 648
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDgkdllKLSRRLRkirrkeiqMVFQDPMsslnprM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 649 SVGslrDQVIYPDSVEDMQRKgYSEQDLEAILDVVHLH---HILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHR 722
Cdd:cd03257 100 TIG---EQIAEPLRIHGKLSK-KEARKEAVLLLLVGVGlpeEVLNRyphE------------LSGGQRQRVAIARALALN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217391356 723 PKYALLDECTSAVSIDVEGKI---FQAAKDA-GIALLSITH 759
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQIldlLKKLQEElGLTLLFITH 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
586-759 |
1.06e-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: 68.73 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY------KPPP---QRMFYIPQRPYMSVG-SLR 654
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGlLKPDSGSILIdgedvrKEPRearRQIGVLPDERGLYDRlTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 655 DQV-----IYPDSVEDMQRKG--YSEQ-DLEAILDvvhlhhilQREGGweamcdwkdvLSGGEKQRIGMARMFYHRPKYA 726
Cdd:COG4555 93 ENIryfaeLYGLFDEELKKRIeeLIELlGLEEFLD--------RRVGE----------LSTGMKKKVALARALVHDPKVL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217391356 727 LLDECTSAvsIDVEG-----KIFQAAKDAGIALLSITH 759
Cdd:COG4555 155 LLDEPTNG--LDVMArrllrEILRALKKEGKTVLFSSH 190
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
584-760 |
1.82e-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: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSS----LFRILgglwPTYGGVLY-------KPPP----QRMFYIPQRPYM 648
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILidgvdisKIGLhdlrSRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 649 SVGSLRDQvIYPDSVedmqrkgYSEQDLEAILDVVHL-HHILQREGGWEAM-CDWKDVLSGGEKQRIGMARMFYHRPKYA 726
Cdd:cd03244 90 FSGTIRSN-LDPFGE-------YSDEELWQALERVGLkEFVESLPGGLDTVvEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217391356 727 LLDECTSAVSIDVEGKIFQAAKD--AGIALLSITHR 760
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREafKDCTVLTIAHR 197
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
586-766 |
2.20e-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: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwPTY----GGVLYK-------PPPQR----MFYIPQRPYMSV 650
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYevteGEILFKgeditdlPPEERarlgIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 GSlrdqviypdSVEDMQRkgyseqdleailDVvhlhhilqREGgweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:cd03217 91 GV---------KNADFLR------------YV--------NEG-----------FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217391356 731 CTSAVSID---VEGKIFQAAKDAGIALLSITHRPSLWKY 766
Cdd:cd03217 131 PDSGLDIDalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
574-763 |
2.59e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 67.00 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLY------KPPPQRMfyipqrP 646
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKlLYGEERPTSGQVLVngqdlsRLKRREI------P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 647 YM--SVGslrdqVIYPD-------SVED-----MQRKGYSEQDL----EAILDVVHLHHILqreggwEAMCDwkdVLSGG 708
Cdd:COG2884 76 YLrrRIG-----VVFQDfrllpdrTVYEnvalpLRVTGKSRKEIrrrvREVLDLVGLSDKA------KALPH---ELSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217391356 709 EKQRIGMARMFYHRPKYALLDECT----SAVSIDVEgKIFQAAKDAGIALLSITHRPSL 763
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTgnldPETSWEIM-ELLEEINRRGTTVLIATHDLEL 199
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
589-760 |
2.63e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 70.24 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQRPYMSVGSLRD-- 655
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWdPQQGEILLNGQPiadyseaalrQAISVVSQRVHLFSATLRDnl 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 656 QVIYPDSvedmqrkgySEQDLEAILDVVHLHHILQREGGWEA-MCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSA 734
Cdd:PRK11160 435 LLAAPNA---------SDEALIEVLQQVGLEKLLEDDKGLNAwLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180
....*....|....*....|....*...
gi 2217391356 735 VSIDVEGKIFQAAKD--AGIALLSITHR 760
Cdd:PRK11160 506 LDAETERQILELLAEhaQNKTVLMITHR 533
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
589-755 |
4.55e-12 |
|
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: 66.30 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLY-------KPPPQR----MFYIPQrpymsvgslrDQ 656
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFdgrditgLPPHERaragIGYVPE----------GR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 657 VIYPD-SVED-------MQRKGYSEQDLEAILDVV-HLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYAL 727
Cdd:cd03224 85 RIFPElTVEEnlllgayARRRAKRKARLERVYELFpRLKERRKQLAG---------TLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190
....*....|....*....|....*....|.
gi 2217391356 728 LDECTSAVSIDVEGKIFQAA---KDAGIALL 755
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIrelRDEGVTIL 186
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
586-730 |
9.90e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.41 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG--------VLYKPPPQRMF-YIPQR----PYMSVgs 652
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGeiliggrdVTDLPPKDRNIaMVFQSyalyPHMTV-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 lRDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKY 725
Cdd:COG3839 93 -YENIAFP-----LKLRKVPKAEIDRrvreAAELLGLEDLLDRkpkQ------------LSGGQRQRVALGRALVREPKV 154
|
....*
gi 2217391356 726 ALLDE 730
Cdd:COG3839 155 FLLDE 159
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
589-763 |
1.01e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.60 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMF---YI-------PQRPYMSVGSLRDQV 657
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYqPTGGQVLLDGVPLVQYdhhYLhrqvalvGQEPVLFSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 658 IYpdsvedmqrkGYSEQDLEAILDVVHLHH----ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECT 732
Cdd:TIGR00958 576 AY----------GLTDTPDEEIMAAAKAANahdfIMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190
....*....|....*....|....*....|.
gi 2217391356 733 SAVSIDVEGKIFQAAKDAGIALLSITHRPSL 763
Cdd:TIGR00958 646 SALDAECEQLLQESRSRASRTVLLIAHRLST 676
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
589-759 |
1.05e-11 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 64.93 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK-PPPQRMFYIPQRpymsVGSLRD-QVIYPD--SV 663
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFDgKSYQKNIEALRR----IGALIEaPGFYPNltAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 664 EDMQRK----GYSEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDV 739
Cdd:cd03268 91 ENLRLLarllGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDEPTNG--LDP 159
|
170 180
....*....|....*....|....*
gi 2217391356 740 EG-----KIFQAAKDAGIALLSITH 759
Cdd:cd03268 160 DGikelrELILSLRDQGITVLISSH 184
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
586-734 |
1.10e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.28 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYK-------PPPQR----------MFyipqrPY 647
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFeTPDSGRIMLDgqdithvPAENRhvntvfqsyaLF-----PH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 648 MSVgslRDQVIYPdsvEDMQRKGYSEQD---LEAiLDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPK 724
Cdd:PRK09452 101 MTV---FENVAFG---LRMQKTPAAEITprvMEA-LRMVQLEEFAQRK---------PHQLSGGQQQRVAIARAVVNKPK 164
|
170
....*....|
gi 2217391356 725 YALLDECTSA 734
Cdd:PRK09452 165 VLLLDESLSA 174
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
574-759 |
1.13e-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: 64.91 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGeVVVASLNIRVEEGMHLLItGPNGCGKSSLFRILGGLW-PTYGGVL---YKPPPQRMF------YIP 643
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTpPSSGTIRidgQDVLKQPQKlrrrigYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 644 QR----PYMSVgslRDQVIYPDSVEDMQRKGySEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMF 719
Cdd:cd03264 79 QEfgvyPNFTV---REFLDYIAWLKGIPSKE-VKARVDEVLELVNLGDRAKKKIG---------SLSGGMRRRVGIAQAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217391356 720 YHRPKYALLDECTsaVSIDVEGKI-F-----QAAKDAgIALLSiTH 759
Cdd:cd03264 146 VGDPSILIVDEPT--AGLDPEERIrFrnllsELGEDR-IVILS-TH 187
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
584-761 |
1.22e-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: 68.16 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG--VLYKPPPQ---------RMFYIPQRPYMSVGS 652
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevTLDGVPVSsldqdevrrRVSVCAQDAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 LRDQVIypdsvedMQRKGYSEQDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:TIGR02868 425 VRENLR-------LARPDATDEELWAALERVGLADWLRAlpDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|...
gi 2217391356 731 CTSAVSIDVEGKIFQ--AAKDAGIALLSITHRP 761
Cdd:TIGR02868 498 PTEHLDAETADELLEdlLAALSGRTVVLITHHL 530
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
586-730 |
1.22e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.17 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVL-------YKPPPQR----MFyipQR----PYMS 649
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMldgvdlsHVPPYQRpinmMF---QSyalfPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 650 VgslrDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLD 729
Cdd:PRK11607 108 V----EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK---------PHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
.
gi 2217391356 730 E 730
Cdd:PRK11607 175 E 175
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
586-759 |
2.05e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.04 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWP--TYGGVLY--------KPPPQR-MFYIPQR----PYMS 649
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPafSASGEVLlngrrltaLPAEQRrIGILFQDdllfPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 650 VG-----SLrdqviyPDSVEDMQRKgyseQDLEAILDVVHLHHILQReggweamcdwkDV--LSGGEKQRIGMARMFYHR 722
Cdd:COG4136 93 VGenlafAL------PPTIGRAQRR----ARVEQALEEAGLAGFADR-----------DPatLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217391356 723 PKYALLDECTS----AVSIDVEGKIFQAAKDAGIALLSITH 759
Cdd:COG4136 152 PRALLLDEPFSkldaALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
586-760 |
2.23e-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: 62.83 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYkpppqrmfyipqrpymsvgsLRDQVIYPDSVED 665
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL--------------------VDGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 666 MQRKGYSeqdleaildVVHlhhilQreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI-DVE--GK 742
Cdd:cd03216 72 ARRAGIA---------MVY-----Q--------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVErlFK 123
|
170
....*....|....*...
gi 2217391356 743 IFQAAKDAGIALLSITHR 760
Cdd:cd03216 124 VIRRLRAQGVAVIFISHR 141
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
568-778 |
2.78e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.32 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 568 VDVEQGIICENIPIVTPSGEVVVaslnirveegmhllITGPNGCGKSSLFRILGGLwPTY----GGVLYK-------PPP 636
Cdd:COG0396 8 VSVEGKEILKGVNLTIKPGEVHA--------------IMGPNGSGKSTLAKVLMGH-PKYevtsGSILLDgedilelSPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 637 QR----MFYIPQRP------------YMSVGSLRDQVIypdSVEDMQRKgyseqdLEAILDVVHL-HHILQR---EGgwe 696
Cdd:COG0396 73 ERaragIFLAFQYPveipgvsvsnflRTALNARRGEEL---SAREFLKL------LKEKMKELGLdEDFLDRyvnEG--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 697 amcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID---VEGKIFQAAKDAGIALLSITHRPSLWKY----HTH 769
Cdd:COG0396 141 --------FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDalrIVAEGVNKLRSPDRGILIITHYQRILDYikpdFVH 212
|
250
....*....|...
gi 2217391356 770 LLqFDG----EGG 778
Cdd:COG0396 213 VL-VDGrivkSGG 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
586-730 |
2.93e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.21 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVAS-LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKpPPQRMFYIP--QRpymSVGSL-RDQVIYP- 660
Cdd:PRK11000 14 GDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPpaER---GVGMVfQSYALYPh 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217391356 661 -DSVEDMQ--------RKGYSEQDLEAILDVVHLHHILQREGgweamcdwKDvLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:PRK11000 90 lSVAENMSfglklagaKKEEINQRVNQVAEVLQLAHLLDRKP--------KA-LSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
587-763 |
2.97e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 587 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwptyggvLYKPPPQRMFYIPQRPYMSVGSLRDQVI----YPDS 662
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-------LKGTPVAGCVDVPDNQFGREASLIDAIGrkgdFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 663 VEDMQRKGYSEqdleAILdvvhlhhilqreggweamcdWK---DVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID- 738
Cdd:COG2401 116 VELLNAVGLSD----AVL--------------------WLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQt 171
|
170 180
....*....|....*....|....*...
gi 2217391356 739 ---VEGKIFQAAKDAGIALLSITHRPSL 763
Cdd:COG2401 172 akrVARNLQKLARRAGITLVVATHHYDV 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
588-730 |
4.75e-11 |
|
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: 63.04 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY--------KPPPQR---MFYipQR----PYMSVgs 652
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdLPPKDRdiaMVF--QNyalyPHMTV-- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217391356 653 lRDQVIYPDSVEDMQRKGYSEQDLEAIlDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:cd03301 90 -YDNIAFGLKLRKVPKDEIDERVREVA-ELLQIEHLLDRK---------PKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
586-759 |
8.44e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 64.35 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG--------VLYKPPPQRMF-YIPQR----PYMSVgs 652
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGrilldgrdVTGLPPEKRNVgMVFQDyalfPHLTV-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 lRDQVIYPdsvedMQRKGYSEQDLEA----ILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKY 725
Cdd:COG3842 95 -AENVAFG-----LRMRGVPKAEIRArvaeLLELVGLEGLADRyphQ------------LSGGQQQRVALARALAPEPRV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217391356 726 ALLDECTSAvsIDVEGK------IFQAAKDAGIALLSITH 759
Cdd:COG3842 157 LLLDEPLSA--LDAKLReemreeLRRLQRELGITFIYVTH 194
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
588-759 |
9.14e-11 |
|
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: 62.84 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLY----------KPPPQRMFYipqrpymsvgsLRDQ 656
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKcIYGNYLPDSGSILVrhdggwvdlaQASPREILA-----------LRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 657 VIypdsvedmqrkGYSEQDLEAI-----LDVVH--LhhilqREGGW---EAMCDWKDVL-----------------SGGE 709
Cdd:COG4778 94 TI-----------GYVSQFLRVIprvsaLDVVAepL-----LERGVdreEARARARELLarlnlperlwdlppatfSGGE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217391356 710 KQRIGMARMFYHRPKYALLDECTSavSIDVEGK-----IFQAAKDAGIALLSITH 759
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTA--SLDAANRavvveLIEEAKARGTAIIGIFH 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
586-743 |
1.63e-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: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQRPYMSVGSLR 654
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSlkdidrhtlrQFINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 655 DQVIypdsvedMQ-RKGYSEQDLEAILDVVHLH-HILQREGGWEA-MCDWKDVLSGGEKQRIGMARMFYHRPKYALLDEC 731
Cdd:TIGR01193 566 ENLL-------LGaKENVSQDEIWAACEIAEIKdDIENMPLGYQTeLSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170
....*....|..
gi 2217391356 732 TSAVSIDVEGKI 743
Cdd:TIGR01193 639 TSNLDTITEKKI 650
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
589-759 |
1.66e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPP-------QRMFYIPQR--PYMSVgslrdqvi 658
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGELLAGTAPlaearedTRLMFQDARllPWKKV-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 659 yPDSVEDMQRKGYSEQDLEAiLDVVHLHhilQREGGWEAmcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS-- 736
Cdd:PRK11247 99 -IDNVGLGLKGQWRDAALQA-LAAVGLA---DRANEWPA------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDal 167
|
170 180
....*....|....*....|....*
gi 2217391356 737 --IDVEGKIFQAAKDAGIALLSITH 759
Cdd:PRK11247 168 trIEMQDLIESLWQQHGFTVLLVTH 192
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
583-762 |
2.05e-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: 61.86 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 583 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRmfyipqrpYMSVGSLRDQV---- 657
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYdVDSGRILIDGHDVR--------DYTLASLRRQIglvs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 658 ----IYPDSVEDMQRKGYSEQDLEAILDVVHLHH----ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALL 728
Cdd:cd03251 83 qdvfLFNDTVAENIAYGRPGATREEVEEAARAANahefIMELPEGYDTVIGERGVkLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217391356 729 DECTSAVSIDVEgKIFQAAKD---AGIALLSITHRPS 762
Cdd:cd03251 163 DEATSALDTESE-RLVQAALErlmKNRTTFVIAHRLS 198
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
584-760 |
2.06e-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: 60.40 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP---------QRMFYIPQRPYMSVGSL 653
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQQGEITLDGVPvsdlekalsSLISVLNQRPYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 654 RDQVIYPdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTs 733
Cdd:cd03247 92 RNNLGRR--------------------------------------------FSGGERQRLALARILLQDAPIVLLDEPT- 126
|
170 180 190
....*....|....*....|....*....|...
gi 2217391356 734 aVSIDVEGK------IFQAAKDAgiALLSITHR 760
Cdd:cd03247 127 -VGLDPITErqllslIFEVLKDK--TLIWITHH 156
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
586-759 |
2.33e-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: 60.28 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY------------KPPPQRMFYIPQR----PYM 648
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLeEPDSGSILIdgedltdledelPPLRRRIGMVFQDfalfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 649 SVgslRDQVIYPdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALL 728
Cdd:cd03229 92 TV---LENIALG--------------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190
....*....|....*....|....*....|....*
gi 2217391356 729 DECTSA----VSIDVEGKIFQAAKDAGIALLSITH 759
Cdd:cd03229 125 DEPTSAldpiTRREVRALLKSLQAQLGITVVLVTH 159
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
582-746 |
3.06e-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: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 582 VTPsgevVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYP 660
Cdd:TIGR01271 438 VTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEGKIKHS---GRISFSPQTSWIMPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 661 DSVEDMQRKGYSE--QDLEAILDVVHLHHILQREGGWeamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID 738
Cdd:TIGR01271 511 LSYDEYRYTSVIKacQLEEDIALFPEKDKTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
....*...
gi 2217391356 739 VEGKIFQA 746
Cdd:TIGR01271 583 TEKEIFES 590
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
589-760 |
3.58e-10 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 61.02 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEG--MHLLitGPNGCGKSSLFRILGGLW-PTYGGVLYK-------PPPQR----MFYIPQRPymSVgsLR 654
Cdd:cd03218 15 VVNGVSLSVKQGeiVGLL--GPNGAGKTTTFYMIVGLVkPDSGKILLDgqditklPMHKRarlgIGYLPQEA--SI--FR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 655 DQviypdSVED-------MQRKGYSEQD--LEAILDVVHLHHILQREGgweamcdwkDVLSGGEKQRIGMARMFYHRPKY 725
Cdd:cd03218 89 KL-----TVEEnilavleIRGLSKKEREekLEELLEEFHITHLRKSKA---------SSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217391356 726 ALLDECTSAVS----IDVEgKIFQAAKDAGI----------ALLSITHR 760
Cdd:cd03218 155 LLLDEPFAGVDpiavQDIQ-KIIKILKDRGIgvlitdhnvrETLSITDR 202
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
586-759 |
3.97e-10 |
|
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: 60.62 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-------VLYKPPP------QRMFYIPQR----PYM 648
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglKLTDDKKninelrQKVGMVFQQfnlfPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 649 SVgsLRDQVIYPdsvedMQRKGYSEQDLEAILdvvhlHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRPK 724
Cdd:cd03262 92 TV--LENITLAP-----IKVKGMSKAEAEERA-----LELLEKVG----LADKADAypaqLSGGQQQRVAIARALAMNPK 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217391356 725 YALLDECTSA----VSIDVEGKIFQAAKDaGIALLSITH 759
Cdd:cd03262 156 VMLFDEPTSAldpeLVGEVLDVMKDLAEE-GMTMVVVTH 193
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
586-771 |
5.10e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.55 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRpymsvGSLRDQviYPDSVED 665
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR-----SEVPDS--LPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 666 M------QRKG----YSEQD---LEAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECT 732
Cdd:NF040873 77 LvamgrwARRGlwrrLTRDDraaVDDALERVGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217391356 733 SAVSIDVEGKIFQ---AAKDAGIALLSITHRPSLWKYHTHLL 771
Cdd:NF040873 148 TGLDAESRERIIAllaEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
592-745 |
5.34e-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: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 592 SLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSVEDmqrkG 670
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVHMK---GSVAYVPQQAWIQNDSLRENILFGKALNE----K 728
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217391356 671 YSEQDLEAILDVVHLHHIlqrEGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQ 745
Cdd:TIGR00957 729 YYQQVLEACALLPDLEIL---PSGDRTEIGEKGVnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
586-761 |
5.75e-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: 59.81 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMfyipQRPymsvgSLRDQVIYPDSVE 664
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSpPLAGRVLLNGGPLDF----QRD-----SIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 665 DMQRKgyseqdLEAILDVVHLHHILQREGGWEAMCD-----WKDV----LSGGEKQRIGMARMFYHRPKYALLDECTSAV 735
Cdd:cd03231 83 GIKTT------LSVLENLRFWHADHSDEQVEEALARvglngFEDRpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190
....*....|....*....|....*....|
gi 2217391356 736 SIDVEGKIFQA----AKDAGIALLSiTHRP 761
Cdd:cd03231 157 DKAGVARFAEAmaghCARGGMVVLT-THQD 185
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
574-760 |
6.80e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.55 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYG-----GV-LYKPPP----QRMFYIP 643
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGslkinGIeLRELDPeswrKHLSWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 644 QRPYMSVGSLRDQVIypdsvedMQRKGYSEQDLEAILDVVHLHHILQR-EGGWE-AMCDWKDVLSGGEKQRIGMARMFYH 721
Cdd:PRK11174 430 QNPQLPHGTLRDNVL-------LGNPDASDEQLQQALENAWVSEFLPLlPQGLDtPIGDQAAGLSVGQAQRLALARALLQ 502
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217391356 722 RPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHR 760
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQ 543
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
589-759 |
7.30e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 60.51 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLY--KP----PPQRMFYI----PQRPYMSvgslrdqv 657
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLngRPlaawSPWELARRravlPQHSSLA-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 658 iYPDSVED---MQRKGYS------EQDLEAILDVVHLHHILQReggweamcDWKDvLSGGEKQRIGMAR-------MFYH 721
Cdd:COG4559 88 -FPFTVEEvvaLGRAPHGssaaqdRQIVREALALVGLAHLAGR--------SYQT-LSGGEQQRVQLARvlaqlwePVDG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217391356 722 RPKYALLDECTSAVSIDVEGKIFQAAKD---AGIALLSITH 759
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQlarRGGGVVAVLH 198
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
589-746 |
1.16e-09 |
|
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: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSVEDMQ 667
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEPSEGKIKHS---GRISFSSQFSWIMPGTIKENIIFGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 668 RKGYSE--QDLEAILDVVHLHHILQREGGWeamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQ 745
Cdd:cd03291 129 YKSVVKacQLEEDITKFPEKDNTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
.
gi 2217391356 746 A 746
Cdd:cd03291 201 S 201
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
584-760 |
1.29e-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: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSL----FRILGglwPTYG-----GVLYKPPP-----QRMFYIPQRPYMS 649
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLilalFRFLE---AEEGkieidGIDISTIPledlrSSLTIIPQDPTLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 650 VGSLRDQViypdSVEDMqrkgYSEQDLEAILDVvhlhhilqREGGweamcdwkDVLSGGEKQRIGMARMFYHRPKYALLD 729
Cdd:cd03369 95 SGTIRSNL----DPFDE----YSDEEIYGALRV--------SEGG--------LNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190
....*....|....*....|....*....|...
gi 2217391356 730 ECTSAVSIDVEGKIFQAAKD--AGIALLSITHR 760
Cdd:cd03369 151 EATASIDYATDALIQKTIREefTNSTILTIAHR 183
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
585-769 |
2.21e-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: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 585 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLF-RILGGLWPTYGGVLY--KPPPQRMF------------YIPQRPYMS 649
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWsnKNESEPSFeatrsrnrysvaYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 650 VGSLRDQVIYPDSVEDMQRKGYSEQ-DLEAILDVvhLHHILQREGGWEAMCdwkdvLSGGEKQRIGMARMFYHRPKYALL 728
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAcSLQPDIDL--LPFGDQTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217391356 729 DECTSAVSIDVEGKIFQAA-----KDAGIALLSITHRpslWKYHTH 769
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 ... |
605-732 |
2.38e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.72 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 605 ITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPY------------MSVGSLRDQV--------IYPDSVE 664
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQldptktvrenveEGVAEIKDALdrfneisaKYAEPDA 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217391356 665 DMQRKGYSEQDLEAILDVVHLHHILQR-EGGWEAM-C---DWK-DVLSGGEKQRIGMARMFYHRPKYALLDECT 732
Cdd:TIGR03719 116 DFDKLAAEQAELQEIIDAADAWDLDSQlEIAMDALrCppwDADvTKLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
586-761 |
3.51e-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: 57.37 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKP---------PPQRMFYIPQRPYMSvGSLrd 655
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLrPDSGEVRWNGtplaeqrdePHENILYLGHLPGLK-PEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 656 qviypdSVEDMQR-----KGYSEQDLEAILDVVHLHHILQREGGWeamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:TIGR01189 89 ------SALENLHfwaaiHGGAQRTIEDALAAVGLTGFEDLPAAQ---------LSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217391356 731 CTsaVSIDVEG-KIFQAAKDA-----GIALLSiTHRP 761
Cdd:TIGR01189 154 PT--TALDKAGvALLAGLLRAhlargGIVLLT-THQD 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
586-759 |
4.30e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 57.98 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV------------LYKPPPQRMFYIPQRP------- 646
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGYLPQEAsifrrls 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 647 ----YMSVGSLRDqviypdSVEDMQRKGYSEQDLEAIldvvHLHHILQREGgweamcdwkDVLSGGEKQRIGMARMFYHR 722
Cdd:PRK10895 95 vydnLMAVLQIRD------DLSAEQREDRANELMEEF----HIEHLRDSMG---------QSLSGGERRRVEIARALAAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217391356 723 PKYALLDECTSAVS----IDVEgKIFQAAKDAGIALLSITH 759
Cdd:PRK10895 156 PKFILLDEPFAGVDpisvIDIK-RIIEHLRDSGLGVLITDH 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
597-759 |
6.48e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.10 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 597 VEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLykpppqRMFYIPQRPyMSVGSLRDQV--IY--PD------SVED- 665
Cdd:PRK13635 30 VYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI------TVGGMVLSE-ETVWDVRRQVgmVFqnPDnqfvgaTVQDd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 666 ----MQRKGYSEQDL----EAILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS- 736
Cdd:PRK13635 103 vafgLENIGVPREEMvervDQALRQVGMEDFLNRE---------PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDp 173
|
170 180
....*....|....*....|....*.
gi 2217391356 737 ---IDVEGKIFQAAKDAGIALLSITH 759
Cdd:PRK13635 174 rgrREVLETVRQLKEQKGITVLSITH 199
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
588-759 |
8.93e-09 |
|
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: 57.36 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEG-MHLLItGPNGCGKSSLFRILGGLW-PTYGGVLYK-------PPPQ-------RMFYIPQ-RPYMSV 650
Cdd:COG0411 18 VAVDDVSLEVERGeIVGLI-GPNGAGKTTLFNLITGFYrPTSGRILFDgrditglPPHRiarlgiaRTFQNPRlFPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 -------GSLRDQVIYPDSVEDMQRKGYSEQDL----EAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMF 719
Cdd:COG0411 97 lenvlvaAHARLGRGLLAALLRLPRARREEREAreraEELLERVGLADRADEPAG---------NLSYGQQRRLEIARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217391356 720 YHRPKYALLDECTSAVSI----DVEGKIFQAAKDAGIALLSITH 759
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPeeteELAELIRRLRDERGITILLIEH 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
574-763 |
9.37e-09 |
|
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: 56.81 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPqrmfyIPQRPYMSVGS 652
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVePTSGSVLIDGTD-----INKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 LRDQV---------IYPDSVedMQ----------------RKGYSEQDLE---AILDVVHL-HHILQReggweamcdwKD 703
Cdd:cd03256 76 LRRQIgmifqqfnlIERLSV--LEnvlsgrlgrrstwrslFGLFPKEEKQralAALERVGLlDKAYQR----------AD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217391356 704 VLSGGEKQRIGMARMFYHRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALLSITHRPSL 763
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLdpasSRQVMDLLKRINREEGITVIVSLHQVDL 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
574-769 |
9.50e-09 |
|
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: 56.26 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKPPPQRMFYIPQRPYM--SV 650
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKlIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 GS-------LRDQVIYPDSVEDMQRKGYSEQDLE----AILDVV---HLHHILQREggweamcdwkdvLSGGEKQRIGMA 716
Cdd:cd03292 81 GVvfqdfrlLPDRNVYENVAFALEVTGVPPREIRkrvpAALELVglsHKHRALPAE------------LSGGEQQRVAIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217391356 717 RMFYHRPKYALLDECTSAVSIDVEGKI---FQAAKDAGIALLSITHRPSLWKYHTH 769
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEImnlLKKINKAGTTVVVATHAKELVDTTRH 204
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
605-762 |
1.33e-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: 57.81 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 605 ITGPNGCGKSSLFRILGGLWPTYGGVLY--------------KPPPQRMF-YIPQR----PYMSVgslRDQVIYPDSVED 665
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsrkgifLPPEKRRIgYVFQEarlfPHLSV---RGNLRYGMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 666 MQRKGYSEqdlEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIF- 744
Cdd:TIGR02142 105 PSERRISF---ERVIELLGIGHLLGRLPG---------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILp 172
|
170 180
....*....|....*....|.
gi 2217391356 745 ---QAAKDAGIALLSITHRPS 762
Cdd:TIGR02142 173 yleRLHAEFGIPILYVSHSLQ 193
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
597-759 |
1.61e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.66 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 597 VEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY----KPPPQRMFYIPQRPYMSVGSLRDQVIYPdSVED-----MQ 667
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdLLTEENVWDIRHKIGMVFQNPDNQFVGA-TVEDdvafgLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 668 RKGYSEQDLeaildVVHLHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDVEGK- 742
Cdd:PRK13650 109 NKGIPHEEM-----KERVNEALELVG----MQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEATSM--LDPEGRl 177
|
170 180
....*....|....*....|..
gi 2217391356 743 -----IFQAAKDAGIALLSITH 759
Cdd:PRK13650 178 eliktIKGIRDDYQMTVISITH 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
574-759 |
2.21e-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: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 574 IICENIPIvTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQrpymsvgsl 653
Cdd:cd03221 1 IELENLSK-TYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 654 rdqviypdsvedmqrkgyseqdleaildvvhlhhilqreggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTS 733
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180
....*....|....*....|....*...
gi 2217391356 734 avSIDVEGKIF--QAAKDAGIALLSITH 759
Cdd:cd03221 100 --HLDLESIEAleEALKEYPGTVILVSH 125
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
588-742 |
2.67e-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: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY---------KPPPQRMFYIPQrpymsvgslrDQV 657
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrPTSGTAYIngysirtdrKAARQSLGYCPQ----------FDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 658 IYPD-SVEDMQR-----KGYSEQdlEAILDVVHLHHILQREggweamcDWKDV----LSGGEKQRIGMARMFYHRPKYAL 727
Cdd:cd03263 86 LFDElTVREHLRfyarlKGLPKS--EIKEEVELLLRVLGLT-------DKANKrartLSGGMKRKLSLAIALIGGPSVLL 156
|
170
....*....|....*
gi 2217391356 728 LDECTSavSIDVEGK 742
Cdd:cd03263 157 LDEPTS--GLDPASR 169
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
581-734 |
3.04e-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: 55.73 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 581 IVTPSGEVV-VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP--------------QRMFYIPQ 644
Cdd:cd03294 30 ILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIePTSGKVLIDGQDiaamsrkelrelrrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 645 R----PYMSVgslRDQVIYPDSVEDMQRKGYSEQDLEAiLDVVHLhhilqreGGWEAmcDWKDVLSGGEKQRIGMARMFY 720
Cdd:cd03294 110 SfallPHRTV---LENVAFGLEVQGVPRAEREERAAEA-LELVGL-------EGWEH--KYPDELSGGMQQRVGLARALA 176
|
170
....*....|....
gi 2217391356 721 HRPKYALLDECTSA 734
Cdd:cd03294 177 VDPDILLMDEAFSA 190
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
584-759 |
3.17e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.85 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYKPPP------------QRMFYIPQRPymsv 650
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKGEPikydkksllevrKTVGIVFQNP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 gslRDQVIYPDSVEDMQ----RKGYSEQDLEAildvvHLHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHR 722
Cdd:PRK13639 88 ---DDQLFAPTVEEDVAfgplNLGLSKEEVEK-----RVKEALKAVG----MEGFENKpphhLSGGQKKRVAIAGILAMK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217391356 723 PKYALLDECTSAVSIDVEGKIFQAAKD---AGIALLSITH 759
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDlnkEGITIIISTH 195
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
589-835 |
3.88e-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: 55.58 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFYIPQRPYMSvgslRD-QVIYPDS---- 662
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEkPAQGTVSFRGQDLYQLDRKQRRAFR----RDvQLVFQDSpsav 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 663 -------------VEDMQRKGYSEQD--LEAILDVVHLHHilqreggwEAMCDWKDVLSGGEKQRIGMARMFYHRPKYAL 727
Cdd:TIGR02769 102 nprmtvrqiigepLRHLTSLDESEQKarIAELLDMVGLRS--------EDADKLPRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 728 LDECTSAVSIDVEGKIFQAAKD----AGIALLSITHRPSLWKYHthllqfdgeggwkfekldsAARLSLTEEKQRLEQQL 803
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKlqqaFGTAYLFITHDLRLVQSF-------------------CQRVAVMDKGQIVEECD 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 2217391356 804 AGipkmqrrlQELC------QILGEAVAPAH-VPAPSPQ 835
Cdd:TIGR02769 235 VA--------QLLSfkhpagRNLQSAVLPEHpVRRSITT 265
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
588-776 |
3.96e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.38 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSV---E 664
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDItvqE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 665 DMQRKGYSEQDLEAIL---DVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAV----SI 737
Cdd:PRK10253 101 LVARGRYPHQPLFTRWrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLdishQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217391356 738 DVEGKIFQAAKDAGIALLSITHR-PSLWKYHTHLLQF-DGE 776
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALrEGK 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
592-730 |
4.94e-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: 54.65 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 592 SLNIRVEEGMHLLitGPNGCGKSSLFRILGGL-WPTYGGVLY-------KPPPQRMF-YIPQR----PYMSVgslRDQVI 658
Cdd:cd03296 22 SLDIPSGELVALL--GPSGSGKTTLLRLIAGLeRPDSGTILFggedatdVPVQERNVgFVFQHyalfRHMTV---FDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 659 Y----------PDSVEdMQRKgyseqdLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALL 728
Cdd:cd03296 97 FglrvkprserPPEAE-IRAK------VHELLKLVQLDWLADR---------YPAQLSGGQRQRVALARALAVEPKVLLL 160
|
..
gi 2217391356 729 DE 730
Cdd:cd03296 161 DE 162
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
588-759 |
5.63e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.50 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFYIPQR------------PYMSVGslr 654
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEkPTEGQIFIDGEDVTHRSIQQRdicmvfqsyalfPHMSLG--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 655 DQVIYPdsvEDMQRKGYSE--QDLEAILDVVHLhhilqreGGWEAMcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECT 732
Cdd:PRK11432 97 ENVGYG---LKMLGVPKEErkQRVKEALELVDL-------AGFEDR--YVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190
....*....|....*....|....*....|.
gi 2217391356 733 SAVSIDV----EGKIFQAAKDAGIALLSITH 759
Cdd:PRK11432 165 SNLDANLrrsmREKIRELQQQFNITSLYVTH 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
593-759 |
6.14e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.00 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYG-----GVLYKpppqrmfyipqrpYMSVGSLRDQV--IY--PD- 661
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGeikidGITIS-------------KENLKEIRKKIgiIFqnPDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 662 -----SVED-----MQRKGYSEQDLEAILD----VVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYAL 727
Cdd:PRK13632 95 qfigaTVEDdiafgLENKKVPPKKMKDIIDdlakKVGMEDYLDKE---------PQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217391356 728 LDECTSAvsIDVEGK------IFQAAKDAGIALLSITH 759
Cdd:PRK13632 166 FDESTSM--LDPKGKreikkiMVDLRKTRKKTLISITH 201
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
587-761 |
7.31e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.67 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 587 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTY-------GGVLY-------------KPPPQRMFYIPQR- 645
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskikvdGKVLYfgkdifqidaiklRKEVGMVFQQPNPf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 646 PYMSVgslRDQVIYPDSVEDMQRKgyseQDLEAILDvvhlhHILQREGGWEAMCDWKDV----LSGGEKQRIGMARMFYH 721
Cdd:PRK14246 103 PHLSI---YDNIAYPLKSHGIKEK----REIKKIVE-----ECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217391356 722 RPKYALLDECTSAVSI----DVEGKIFQAAKDAGIALLSitHRP 761
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIvnsqAIEKLITELKNEIAIVIVS--HNP 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
583-759 |
1.51e-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: 52.97 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 583 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLY-------------KPPPQRMFYIPQR-PY 647
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLeRPTSGSVLVdgtdltllsgkelRKARRRIGMIFQHfNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 648 MSVGSLRDQVIYPDSVEDMQRKgYSEQDLEAILDVVHLHHilqREGGWEAMcdwkdvLSGGEKQRIGMARMFYHRPKYAL 727
Cdd:cd03258 94 LSSRTVFENVALPLEIAGVPKA-EIEERVLELLELVGLED---KADAYPAQ------LSGGQKQRVGIARALANNPKVLL 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217391356 728 LDECTSAVSIDVEGKIFQAAKDA----GIALLSITH 759
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDInrelGLTIVLITH 199
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
593-762 |
2.00e-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: 54.83 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLykpppqrmfyIPQRPYMSV--GSLR--------DQVIYPD 661
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYdVTSGRIL----------IDGQDIRDVtqASLRaaigivpqDTVLFND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 662 SVED---MQRKGYSEQDLEAILDVVHLHH-ILQREGGWEAMcdwkdV------LSGGEKQRIGMARMFYHRPKYALLDEC 731
Cdd:COG5265 447 TIAYniaYGRPDASEEEVEAAARAAQIHDfIESLPDGYDTR-----VgerglkLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
170 180 190
....*....|....*....|....*....|...
gi 2217391356 732 TSAVSIDVEGKIFQAAKDA--GIALLSITHRPS 762
Cdd:COG5265 522 TSALDSRTERAIQAALREVarGRTTLVIAHRLS 554
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
593-761 |
2.58e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.11 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYKPPP---------QRMFYIPQRPymsvGslrdqvIYPD- 661
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGeVLWQGEPirrqrdeyhQDLLYLGHQP----G------IKTEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 662 -SVEDMQ-----RKGYSEQDLEAILDVVHLHhilqregGWEamcdwkDV----LSGGEKQRIGMARMFYHRPKYALLDEC 731
Cdd:PRK13538 90 tALENLRfyqrlHGPGDDEALWEALAQVGLA-------GFE------DVpvrqLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217391356 732 TSAvsIDVEG-KIFQA-----AKDAGIALLSiTHRP 761
Cdd:PRK13538 157 FTA--IDKQGvARLEAllaqhAEQGGMVILT-THQD 189
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
589-759 |
3.16e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.13 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPPqrmfyIPQRPYMSVGSLRDQ---VIY----- 659
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVIFNGQP-----MSKLSSAAKAELRNQklgFIYqfhhl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 660 -PD--SVED---------MQRKGYSEQDLEaILDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYAL 727
Cdd:PRK11629 99 lPDftALENvamplligkKKPAEINSRALE-MLAAVGLEHRANHR---------PSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217391356 728 LDECTSAVSIDVEGKIFQAAKD----AGIALLSITH 759
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGElnrlQGTAFLVVTH 204
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
588-759 |
3.74e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.02 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY------KPPPQRMFYIPQR-----------PYMSv 650
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvNDPKVDERLIRQEagmvfqqfylfPHLT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 gSLRDQVIYPDSVEDMQRKGYSEQDLEaildvvhlhhILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:PRK09493 94 -ALENVMFGPLRVRGASKEEAEKQARE----------LLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 2217391356 731 CTSAvsIDVE-----GKIFQAAKDAGIALLSITH 759
Cdd:PRK09493 163 PTSA--LDPElrhevLKVMQDLAEEGMTMVIVTH 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
607-732 |
3.86e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 607 GPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPY------------MSVGSLRDQV--------IYPDSVEDM 666
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQldpektvrenveEGVAEVKAALdrfneiyaAYAEPDADF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 667 QrKGYSEQ-DLEAILDvvhlhhilqREGGWE-------AM----C---DWK-DVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:PRK11819 120 D-ALAAEQgELQEIID---------AADAWDldsqleiAMdalrCppwDAKvTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
..
gi 2217391356 731 CT 732
Cdd:PRK11819 190 PT 191
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
593-759 |
4.56e-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: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGV----LYKPPPQRMFYIPQRpymsVGslrdqVIY--PD---- 661
Cdd:TIGR04520 21 VSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlPTSGKVtvdgLDTLDEENLWEIRKK----VG-----MVFqnPDnqfv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 662 --SVED-----MQRKGYSEQDLEAI----LDVVHLHHILQREggweamcdwKDVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:TIGR04520 92 gaTVEDdvafgLENLGVPREEMRKRvdeaLKLVGMEDFRDRE---------PHLLSGGQKQRVAIAGVLAMRPDIIILDE 162
|
170 180 190
....*....|....*....|....*....|....*
gi 2217391356 731 CTSAvsIDVEGK------IFQAAKDAGIALLSITH 759
Cdd:TIGR04520 163 ATSM--LDPKGRkevletIRKLNKEEGITVISITH 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
588-760 |
7.73e-07 |
|
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: 50.83 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL------YKPP---PQRMFYIPQR----PYMSVgsl 653
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFATvdgfdvVKEPaeaRRRLGFVSDStglyDRLTA--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 654 RDQVIYPDSVEDMQRKGYsEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDECTS 733
Cdd:cd03266 96 RENLEYFAGLYGLKGDEL-TARLEELADRLGMEELLDRRVG---------GFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190
....*....|....*....|....*....|
gi 2217391356 734 AVSIDVEGKIF---QAAKDAGIALLSITHR 760
Cdd:cd03266 166 GLDVMATRALRefiRQLRALGKCILFSTHI 195
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
586-734 |
7.98e-07 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 51.15 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVaslnirveegmhllITGPNGCGKSSLFRILGGLWP------TYGGVLYKPPPQRMFYIPQR-----------PYM 648
Cdd:COG1126 27 GEVVV--------------IIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKDINKLRRKvgmvfqqfnlfPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 649 SVgslRDQVIYPDsvedMQRKGYSEQDLEAI----LDVVHLHhilqreggweamcDWKDV----LSGGEKQRIGMAR--- 717
Cdd:COG1126 93 TV---LENVTLAP----IKVKKMSKAEAEERamelLERVGLA-------------DKADAypaqLSGGQQQRVAIARala 152
|
170
....*....|....*..
gi 2217391356 718 MfyhRPKYALLDECTSA 734
Cdd:COG1126 153 M---EPKVMLFDEPTSA 166
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
585-759 |
1.37e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 585 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLwptyggVLYKPPPQRMFYIPQRPYMS--VGSLRDQV--IY- 659
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL------LLPDDNPNSKITVDGITLTAktVWDIREKVgiVFq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 660 -PD------SVED-----MQRKGYSEQDLEAILdvvhlHHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRP 723
Cdd:PRK13640 92 nPDnqfvgaTVGDdvafgLENRAVPRPEMIKIV-----RDVLADVG----MLDYIDSepanLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217391356 724 KYALLDECTSAvsIDVEGK------IFQAAKDAGIALLSITH 759
Cdd:PRK13640 163 KIIILDESTSM--LDPAGKeqilklIRKLKKKNNLTVISITH 202
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
590-766 |
1.44e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.25 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 590 VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP-TYGGVLY----------------KPPPQRMFYIPQ---RPYMS 649
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEVAWlgkdllgmkddewravRSDIQMIFQDPLaslNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 650 VGS-----LRdqVIYPDsvedMQRKGYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPK 724
Cdd:PRK15079 117 IGEiiaepLR--TYHPK----LSRQEVKDRVKAMMLKVGLLPNLINR---------YPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217391356 725 YALLDECTSAVSIDVEGKIF----QAAKDAGIALLSITHRPSLWKY 766
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVVnllqQLQREMGLSLIFIAHDLAVVKH 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
593-730 |
1.83e-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: 49.98 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG-VLYK-------PPPQR----MFYIPQRpymsvgslRDqvIYP 660
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRFDgeditglPPHRIarlgIGYVPEG--------RR--IFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 661 D-SVED------MQRKGYSE--QDLEAILDVV-HLHHILQREGGweamcdwkdVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:COG0410 92 SlTVEEnlllgaYARRDRAEvrADLERVYELFpRLKERRRQRAG---------TLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
600-759 |
2.13e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 600 GMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPpQRMFYIPQRPYMSVgsLRD-QVIYPD---SVEDMQRKGYSeqd 675
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG-QRIDTLSPGKLQAL--RRDiQFIFQDpyaSLDPRQTVGDS--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 676 leaILDVVHLHHILQREGG-----W---------EAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG 741
Cdd:PRK10261 424 ---IMEPLRVHGLLPGKAAaarvaWllervgllpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
170 180
....*....|....*....|..
gi 2217391356 742 KI----FQAAKDAGIALLSITH 759
Cdd:PRK10261 501 QIinllLDLQRDFGIAYLFISH 522
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
607-730 |
2.34e-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: 50.48 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 607 GPNGCGKSSLFRILGGLWPTYGG-------VLYK-------PPPQRMF-YIPQ--R--PYMSV-GSLRdqviYPdsvedM 666
Cdd:COG4148 32 GPSGSGKTTLLRAIAGLERPDSGrirlggeVLQDsargiflPPHRRRIgYVFQeaRlfPHLSVrGNLL----YG-----R 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217391356 667 QR--KGYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:COG4148 103 KRapRAERRISFDEVVELLGIGHLLDR---------RPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
590-746 |
2.44e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 590 VASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTY-GGVLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSVEdmq 667
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAEtSSVVIR---GSVAYVPQVSWIFNATVRENILFGSDFE--- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 668 rkgySEQDLEAIlDVVHLHHILQREGGWeamcDWKDV------LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG 741
Cdd:PLN03232 707 ----SERYWRAI-DVTALQHDLDLLPGR----DLTEIgergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
....*
gi 2217391356 742 KIFQA 746
Cdd:PLN03232 778 QVFDS 782
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
593-762 |
2.57e-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: 49.03 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYK------PPPQRmfyipqRPYMSVgsLRDQVIYPD-SVE 664
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINgvdvtaAPPAD------RPVSML--FQENNLFAHlTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 665 DMQRKGYS------EQDLEAIldvvhlHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID 738
Cdd:cd03298 89 QNVGLGLSpglkltAEDRQAI------EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180
....*....|....*....|....*...
gi 2217391356 739 VEGKIFQAAKDA----GIALLSITHRPS 762
Cdd:cd03298 163 LRAEMLDLVLDLhaetKMTVLMVTHQPE 190
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
588-760 |
2.80e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 50.11 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEG--MHLLitGPNGCGKSSLFR-ILGGLWPTYGGVLYK-----PPPQRMF-YIPQ-R---PYMSVGslr 654
Cdd:COG4152 15 TAVDDVSFTVPKGeiFGLL--GPNGAGKTTTIRiILGILAPDSGEVLWDgepldPEDRRRIgYLPEeRglyPKMKVG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 655 DQVIYpdsvedM-QRKGYSEQDLEAILDvvhlhHILQREGgweaMCDWKDV----LSGGEKQRIGMARMFYHRPKYALLD 729
Cdd:COG4152 90 EQLVY------LaRLKGLSKAEAKRRAD-----EWLERLG----LGDRANKkveeLSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217391356 730 ECTS---AVSIDV-EGKIF-QAAKDAGIaLLSiTHR 760
Cdd:COG4152 155 EPFSgldPVNVELlKDVIReLAAKGTTV-IFS-SHQ 188
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
582-743 |
2.86e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 50.61 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 582 VTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGGVLYKPPP----------QRMFYIPQRPYMSV 650
Cdd:PRK09536 11 VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRaINGTLTPTAGTVLVAGDDvealsaraasRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 GSLRDQVIYPDSVEDMQRKGYSEQDLEAILDvvhlhHILQReGGWEAMCDWK-DVLSGGEKQRIGMARMFYHRPKYALLD 729
Cdd:PRK09536 91 EFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-----RAMER-TGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
|
170
....*....|....
gi 2217391356 730 ECTSavSIDVEGKI 743
Cdd:PRK09536 165 EPTA--SLDINHQV 176
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
584-774 |
3.36e-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: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSS----LFRIL---------GGLwpTYGGVLYKPPPQRMFYIPQRPYMSV 650
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINesaegeiiiDGL--NIAKIGLHDLRFKITIIPQDPVLFS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 GSLRDQvIYPDSvedmqrkGYSEQDLEAILDVVHLHHILQRE-GGWEAMC-DWKDVLSGGEKQRIGMARMFYHRPKYALL 728
Cdd:TIGR00957 1374 GSLRMN-LDPFS-------QYSDEEVWWALELAHLKTFVSALpDKLDHECaEGGENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217391356 729 DECTSAVSIDVEGKIFQAAKDA--GIALLSITHRPSLWKYHTHLLQFD 774
Cdd:TIGR00957 1446 DEATAAVDLETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLD 1493
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
575-734 |
3.73e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 49.38 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 575 ICENIPIVTPSGEVVVaslnirveegmhllITGPNGCGKSSLFRILGG-LWPTYGGVLY--KP----PPQRMFYI----P 643
Cdd:PRK13548 17 LLDDVSLTLRPGEVVA--------------ILGPNGAGKSTLLRALSGeLSPDSGEVRLngRPladwSPAELARRravlP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 644 QRPYMSvgslrdqviYPDSVEDMQRKG-----YSEQDLEAIL-------DVVHLHHILQREggweamcdwkdvLSGGEKQ 711
Cdd:PRK13548 83 QHSSLS---------FPFTVEEVVAMGraphgLSRAEDDALVaaalaqvDLAHLAGRDYPQ------------LSGGEQQ 141
|
170 180
....*....|....*....|....*....
gi 2217391356 712 RIGMARMF------YHRPKYALLDECTSA 734
Cdd:PRK13548 142 RVQLARVLaqlwepDGPPRWLLLDEPTSA 170
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
583-759 |
4.12e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.72 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 583 TPSGEVV-VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGV------------------LYKPPPQRMFYIP 643
Cdd:PRK09473 24 TPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsatfngreilnlpekeLNKLRAEQISMIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 644 Q------RPYMSVGSLRDQVIypdsvedMQRKGYSEQD--LEAI--LDVVHLHHILQReggweaMCDWKDVLSGGEKQRI 713
Cdd:PRK09473 104 QdpmtslNPYMRVGEQLMEVL-------MLHKGMSKAEafEESVrmLDAVKMPEARKR------MKMYPHEFSGGMRQRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217391356 714 GMARMFYHRPKYALLDECTSAVSIDVEGKIF----QAAKDAGIALLSITH 759
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMtllnELKREFNTAIIMITH 220
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
568-771 |
4.24e-06 |
|
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: 48.80 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 568 VDVEQGIICENIPIVTPSGEVVVaslnirveegmhllITGPNGCGKSSLFRILGGlWPTY----GGVLYK-------PPP 636
Cdd:TIGR01978 8 VSVEDKEILKGVNLTVKKGEIHA--------------IMGPNGSGKSTLSKTIAG-HPSYevtsGTILFKgqdllelEPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 637 QR----MFYIPQRPYMSVGSlrdqviypdSVEDMQRKGY---SEQDLEAILDVVHLHHILQRE----GGWEAMCDwKDV- 704
Cdd:TIGR01978 73 ERaragLFLAFQYPEEIPGV---------SNLEFLRSALnarRSARGEEPLDLLDFEKLLKEKlallDMDEEFLN-RSVn 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217391356 705 --LSGGEKQRIGMARMFYHRPKYALLDECTSAVSID-----VEGkiFQAAKDAGIALLSITHRPSLWKY----HTHLL 771
Cdd:TIGR01978 143 egFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDalkivAEG--INRLREPDRSFLIITHYQRLLNYikpdYVHVL 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
607-743 |
5.82e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 607 GPNGCGKSSLFRIL---GGLWP---TYGGVLYKpppQRMFYIPQRPYMSvgsLRDQV-------------IYPDSVEDMQ 667
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPevtITGSIVYN---GHNIYSPRTDTVD---LRKEIgmvfqqpnpfpmsIYENVVYGLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 668 RKGYSEQdleAILDVVhLHHILQREGGWEAMcdwKDVL-------SGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVE 740
Cdd:PRK14239 112 LKGIKDK---QVLDEA-VEKSLKGASIWDEV---KDRLhdsalglSGGQQQRVCIARVLATSPKIILLDEPTSALDPISA 184
|
...
gi 2217391356 741 GKI 743
Cdd:PRK14239 185 GKI 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
605-735 |
6.48e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.85 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 605 ITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPP------------QRMFYIPQRPymsvgslRDQVIYPDSVED----MQ 667
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPldyskrgllalrQQVATVFQDP-------EQQIFYTDIDSDiafsLR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217391356 668 RKGYSEQDL----EAILDVVHLHHILQReggwEAMCdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAV 735
Cdd:PRK13638 105 NLGVPEAEItrrvDEALTLVDAQHFRHQ----PIQC-----LSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
577-762 |
1.05e-05 |
|
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: 48.94 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 577 ENIPIVTPSGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLykpppqrMFYIPQRPYmSVGSLR 654
Cdd:TIGR02203 334 RNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYePDSGQIL-------LDGHDLADY-TLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 655 DQV--------IYPDSVED----MQRKGYSEQDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFY 720
Cdd:TIGR02203 406 RQValvsqdvvLFNDTIANniayGRTEQADRAEIERALAAAYAQDFVDKlpLGLDTPIGENGVLLSGGQRQRLAIARALL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217391356 721 HRPKYALLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPS 762
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLV-QAALERlmqGRTTLVIAHRLS 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
586-761 |
1.11e-05 |
|
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: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL---WPTYGGVLYK----------PPPQRM------------- 639
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyEPTSGRIIYHvalcekcgyvERPSKVgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 640 ----FYIPQRPYMSVGSLR-------------DQVIYPDSVEDMQRKGYSEQD-----LEaILDVVHLHHI---LQREgg 694
Cdd:TIGR03269 92 eevdFWNLSDKLRRRIRKRiaimlqrtfalygDDTVLDNVLEALEEIGYEGKEavgraVD-LIEMVQLSHRithIARD-- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217391356 695 weamcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSavSID------VEGKIFQAAKDAGIALLSITHRP 761
Cdd:TIGR03269 169 ----------LSGGEKQRVVLARQLAKEPFLFLADEPTG--TLDpqtaklVHNALEEAVKASGISMVLTSHWP 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
586-730 |
1.29e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.52 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRIL-GGLWPTYGgvlykpppqrmfyipqrpymsvgslrdQVIYPDSVe 664
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPDSG---------------------------TVKLGETV- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 665 dmqRKGYSEQDLEA------ILDVV----------HLHHILQREG--GWEAmcdWK--DVLSGGEKQRIGMARMFYHRPK 724
Cdd:COG0488 379 ---KIGYFDQHQEEldpdktVLDELrdgapggteqEVRGYLGRFLfsGDDA---FKpvGVLSGGEKARLALAKLLLSPPN 452
|
....*.
gi 2217391356 725 YALLDE 730
Cdd:COG0488 453 VLLLDE 458
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
589-759 |
1.48e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKS----SLFRIL--------GGLWPTYGGVLYKPPPQ--------RMFYIPQRPYM 648
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGESLLHASEQtlrgvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 649 SVG---SLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQReggweaMCDWKDVLSGGEKQRIGMARMFYHRPKY 725
Cdd:PRK15134 104 SLNplhTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKR------LTDYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217391356 726 ALLDECTSAVSIDVEGKIFQAAKD----AGIALLSITH 759
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRElqqeLNMGLLFITH 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
586-733 |
1.65e-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: 47.11 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-------------KPPPQRMFYIPQRPY---- 647
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPDSGEVLIdgedisglseaelYRLRRRMGMLFQSGAlfds 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 648 MSVGslrDQVIYPDSvedmQRKGYSEQDLEAI----LDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRP 723
Cdd:cd03261 92 LTVF---ENVAFPLR----EHTRLSEEEIREIvlekLEAVGLRGAEDL---------YPAELSGGMKKRVALARALALDP 155
|
170
....*....|
gi 2217391356 724 KYALLDECTS 733
Cdd:cd03261 156 ELLLYDEPTA 165
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
602-762 |
1.74e-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: 45.44 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 602 HLLITGPNGCGKSSLFRILGGlwptyggvLYKPPPQRMFYIpqrpymsvgslrdqviypdsvedmqrkgyseqDLEAILD 681
Cdd:smart00382 4 VILIVGPPGSGKTTLARALAR--------ELGPPGGGVIYI--------------------------------DGEDILE 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 682 VVHLHHILQREGGWEAMcdwkdvLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI---------FQAAKDAGI 752
Cdd:smart00382 44 EVLDQLLLIIVGGKKAS------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleelrllLLLKSEKNL 117
|
170
....*....|
gi 2217391356 753 ALLSITHRPS 762
Cdd:smart00382 118 TVILTTNDEK 127
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
583-759 |
2.15e-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: 47.36 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 583 TPSGEV-VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP----TYGGVLYK-------PPPQ-------RMFYIP 643
Cdd:COG0444 13 TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgiTSGEILFDgedllklSEKElrkirgrEIQMIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 644 QRPY------MSVGslrDQVIYPdsvedMQR-KGYSEQDLEA----ILDVVHLHHILQR------EggweamcdwkdvLS 706
Cdd:COG0444 93 QDPMtslnpvMTVG---DQIAEP-----LRIhGGLSKAEAREraieLLERVGLPDPERRldryphE------------LS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217391356 707 GGEKQRIGMARMFYHRPKYALLDECTSA--VSIdvegkifQA---------AKDAGIALLSITH 759
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTAldVTI-------QAqilnllkdlQRELGLAILFITH 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
583-759 |
2.50e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.04 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 583 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY--------------KPPPQRMFYIPQRPY 647
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVgdivvsstskqkeiKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 648 msvGSLRDQVIYPDSVEDMQRKGYSEQDLEAI----LDVVHLHHILQREGGWEamcdwkdvLSGGEKQRIGMARMFYHRP 723
Cdd:PRK13643 95 ---SQLFEETVLKDVAFGPQNFGIPKEKAEKIaaekLEMVGLADEFWEKSPFE--------LSGGQMRRVAIAGILAMEP 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217391356 724 KYALLDECTSAVSIDVE---GKIFQAAKDAGIALLSITH 759
Cdd:PRK13643 164 EVLVLDEPTAGLDPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
588-759 |
2.72e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.00 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYK----PPPQRMFYIPQRPYMSVGSLRDQVIYPDS 662
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDgldtSDEENLWDIRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 663 VEDM----QRKGYSEQDLEAILDvvhlhHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVS-- 736
Cdd:PRK13633 104 EEDVafgpENLGIPPEEIRERVD-----ESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDps 178
|
170 180
....*....|....*....|....*
gi 2217391356 737 --IDVEGKIFQAAKDAGIALLSITH 759
Cdd:PRK13633 179 grREVVNTIKELNKKYGITIILITH 203
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
605-765 |
2.72e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 605 ITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQRMFyipQRPYMS-VG---SLRDQVIYPDSVEDMQRKGYSEQDLEAI 679
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMqPSSGNIYYKNCNINNI---AKPYCTyIGhnlGLKLEMTVFENLKFWSEIYNSAETLYAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 680 LDVVHLHHILQREggweamCdwkDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSID----VEGKIFQAAKDAGIALL 755
Cdd:PRK13541 108 IHYFKLHDLLDEK------C---YSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEnrdlLNNLIVMKANSGGIVLL 178
|
170
....*....|
gi 2217391356 756 SiTHRPSLWK 765
Cdd:PRK13541 179 S-SHLESSIK 187
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
584-759 |
2.84e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 46.76 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 584 PSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYKPPP-----QRMFYIPQRPYMSVGSLRDQV 657
Cdd:PRK13636 16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKPidysrKGLMKLRESVGMVFQDPDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 658 IYPDSVEDMQrkgYSEQDLEAILDVVH--LHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAv 735
Cdd:PRK13636 96 FSASVYQDVS---FGAVNLKLPEDEVRkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG- 171
|
170 180 190
....*....|....*....|....*....|
gi 2217391356 736 sIDVEGK------IFQAAKDAGIALLSITH 759
Cdd:PRK13636 172 -LDPMGVseimklLVEMQKELGLTIIIATH 200
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
561-781 |
3.55e-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: 47.24 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 561 PREAGQVVDVEQgiicenipiVTPS--GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLykpppqr 638
Cdd:TIGR03719 316 PRLGDKVIEAEN---------LTKAfgDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 639 mfyipqrpymSVGslrdqviypDSVedmqRKGYSEQDLEAI-------------LDVVHLhhilqreGGWE----AMCDW 701
Cdd:TIGR03719 380 ----------EIG---------ETV----KLAYVDQSRDALdpnktvweeisggLDIIKL-------GKREipsrAYVGR 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 702 ---------KDV--LSGGEKQRIGMARMFYHRPKYALLDECTSavSIDVEgkIFQAAKDA-----GIALLsITH-RPSLW 764
Cdd:TIGR03719 430 fnfkgsdqqKKVgqLSGGERNRVHLAKTLKSGGNVLLLDEPTN--DLDVE--TLRALEEAllnfaGCAVV-ISHdRWFLD 504
|
250
....*....|....*..
gi 2217391356 765 KYHTHLLQFDGEGGWKF 781
Cdd:TIGR03719 505 RIATHILAFEGDSHVEW 521
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
607-759 |
4.43e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.93 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 607 GPNGCGKSSLFRILGGLW-PTYGGVLYKPPP----------QRMFYIPQR-PYMSVGSLRDQVI---YP-------DSVE 664
Cdd:PRK10575 44 GHNGSGKSTLLKMLGRHQpPSEGEILLDAQPleswsskafaRKVAYLPQQlPAAEGMTVRELVAigrYPwhgalgrFGAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 665 DMQRkgyseqdLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSI----DVE 740
Cdd:PRK10575 124 DREK-------VEEAISLVGLKPLAHR---------LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVL 187
|
170
....*....|....*....
gi 2217391356 741 GKIFQAAKDAGIALLSITH 759
Cdd:PRK10575 188 ALVHRLSQERGLTVIAVLH 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
589-762 |
4.54e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.99 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP------------TYGGVLYKPP--PQRM-------FYIPQR-P 646
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearvegevrLFGRNIYSPDvdPIEVrrevgmvFQYPNPfP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 647 YMSvgslrdqvIYPDSVEDMQRKGY--SEQDLEAILDVVhlhhiLQREGGWEA----MCDWKDVLSGGEKQRIGMARMFY 720
Cdd:PRK14267 99 HLT--------IYDNVAIGVKLNGLvkSKKELDERVEWA-----LKKAALWDEvkdrLNDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217391356 721 HRPKYALLDECTSAV----SIDVEGKIFQAAKDAGIALlsITHRPS 762
Cdd:PRK14267 166 MKPKILLMDEPTANIdpvgTAKIEELLFELKKEYTIVL--VTHSPA 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
571-759 |
5.00e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 571 EQGIICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGG---VLYKPPPQRM-----FYI 642
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisILGQPTRQALqknlvAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 643 PQRPYMSVGslrdqviYPDSVED---MQRKGY----------SEQDLEAILDVVHLHHILQREGGweamcdwkdVLSGGE 709
Cdd:PRK15056 84 PQSEEVDWS-------FPVLVEDvvmMGRYGHmgwlrrakkrDRQIVTAALARVDMVEFRHRQIG---------ELSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217391356 710 KQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI---FQAAKDAGIALLSITH 759
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIislLRELRDEGKTMLVSTH 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
705-760 |
5.09e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 5.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 705 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSID----VEGKIFQAAKDAGIALLSITHR 760
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADKTIITIAHR 1418
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
591-769 |
6.39e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 45.45 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 591 ASLNIRVEEGMHLLitGPNGCGKSSLFRILGGL-WPTYGGVLYKPPP--------QRMFyipQR--------------PY 647
Cdd:PRK10419 31 VSLSLKSGETVALL--GRSGCGKSTLARLLVGLeSPSQGNVSWRGEPlaklnraqRKAF---RRdiqmvfqdsisavnPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 648 MSVG-SLRDQVIYPDSVEDMQRKGYSEQDLEAI-LDVVHLHHILQReggweamcdwkdvLSGGEKQRIGMARMFYHRPKY 725
Cdd:PRK10419 106 KTVReIIREPLRHLLSLDKAERLARASEMLRAVdLDDSVLDKRPPQ-------------LSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217391356 726 ALLDECTSAVSIDVEGKIFQAAKD----AGIALLSITHRPSLWKYHTH 769
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKlqqqFGTACLFITHDLRLVERFCQ 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
590-774 |
8.70e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 46.11 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 590 VASLNIRVEEGMHLLITGPNGCGKSSLFRILgglwptyggvlykpppQRmFYIPQRPY----------MSVGSLRDQ--V 657
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLL----------------QR-VFDPQSGRilidgtdirtVTRASLRRNiaV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 658 IYPD------SVEDMQRKG---YSEQDLEAILDVVHLHH-ILQREGGWEAMCDWK-DVLSGGEKQRIGMARMFYHRPKYA 726
Cdd:PRK13657 414 VFQDaglfnrSIEDNIRVGrpdATDEEMRAAAERAQAHDfIERKPDGYDTVVGERgRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217391356 727 LLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPSLWKYHTHLLQFD 774
Cdd:PRK13657 494 ILDEATSALDVETEAKV-KAALDElmkGRTTFIIAHRLSTVRNADRILVFD 543
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
705-805 |
1.30e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.57 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 705 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG---KIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGgwKF 781
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG--KI 230
|
90 100
....*....|....*....|....
gi 2217391356 782 EKLDSAARLSLTEEKQRLEQQLAG 805
Cdd:PRK10619 231 EEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
586-763 |
1.38e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.10 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPPQRMFYIPQRPYmsvgsLRDQV--IYPDS 662
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGHDITRLKNREVPF-----LRRQIgmIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 663 VEDMQRKGYSEQDLEAILDVVHLHHI-------LQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECT--- 732
Cdd:PRK10908 89 HLLMDRTVYDNVAIPLIIAGASGDDIrrrvsaaLDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTgnl 168
|
170 180 190
....*....|....*....|....*....|..
gi 2217391356 733 -SAVSIDVEgKIFQAAKDAGIALLSITHRPSL 763
Cdd:PRK10908 169 dDALSEGIL-RLFEEFNRVGVTVLMATHDIGL 199
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
585-762 |
1.52e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.48 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 585 SGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGlwptyggvlYKPPPQRMFYIPQRPY--MSVGSLR-------- 654
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG---------YYPLTEGEIRLDGRPLssLSHSVLRqgvamvqq 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 655 DQVIYPDSVEDMQRKG--YSEQDLEAILDVVHLHHILQR--EGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:PRK10790 423 DPVVLADTFLANVTLGrdISEEQVWQALETVQLAELARSlpDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190
....*....|....*....|....*....|....
gi 2217391356 731 CTSAVSIDVEGKIFQA--AKDAGIALLSITHRPS 762
Cdd:PRK10790 503 ATANIDSGTEQAIQQAlaAVREHTTLVVIAHRLS 536
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
592-737 |
1.81e-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: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 592 SLNIRveEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLY-------------KPPPQRMFYIPQRPY------MSVG 651
Cdd:COG4608 38 SFDIR--RGETLGLVGESGCGKSTLGRLLLRLEePTSGEILFdgqditglsgrelRPLRRRMQMVFQDPYaslnprMTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 652 slrDQVIYPDSVEDMQRKGYSEQDLEAILDVVHL--HHiLQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKYA 726
Cdd:COG4608 116 ---DIIAEPLRIHGLASKAERRERVAELLELVGLrpEH-ADRyphE------------FSGGQRQRIGIARALALNPKLI 179
|
170
....*....|...
gi 2217391356 727 LLDECTSA--VSI 737
Cdd:COG4608 180 VCDEPVSAldVSI 192
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
592-730 |
2.33e-04 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 44.30 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 592 SLNIRVEEGMHLLitGPNGCGKSSLFRILGGLWPTYGGVL---------YKPPPQRMFYIPQR----PYMSVGslrDQVI 658
Cdd:PRK10851 22 SLDIPSGQMVALL--GPSGSGKTTLLRIIAGLEHQTSGHIrfhgtdvsrLHARDRKVGFVFQHyalfRHMTVF---DNIA 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217391356 659 YPDSV---EDMQRKGYSEQDLEAILDVVHLHHILQReggweamcdWKDVLSGGEKQRIGMARMFYHRPKYALLDE 730
Cdd:PRK10851 97 FGLTVlprRERPNAAAIKAKVTQLLEMVQLAHLADR---------YPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
596-716 |
2.42e-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: 44.78 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 596 RVEEG-MH----LLITGPNGCGKSSLFRILGG-LWPTYGGVlykPPPQRMFYIPQrpYMSVGslrdqviYPDSVEDMQRK 669
Cdd:COG1245 357 EVEGGeIRegevLGIVGPNGIGKTTFAKILAGvLKPDEGEV---DEDLKISYKPQ--YISPD-------YDGTVEEFLRS 424
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2217391356 670 GYSEqDLEA------ILDVVHLHHILQREggweaMCDwkdvLSGGEKQRIGMA 716
Cdd:COG1245 425 ANTD-DFGSsyykteIIKPLGLEKLLDKN-----VKD----LSGGELQRVAIA 467
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
588-745 |
2.72e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 588 VVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKpppQRMF-YIPQRPYMSVGSLRDQVIYPDsvedm 666
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA---ERSIaYVPQQAWIMNATVRGNILFFD----- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 667 qrkgysEQDLEAILDVVHLHH----ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEG 741
Cdd:PTZ00243 746 ------EEDAARLADAVRVSQleadLAQLGGGLETEIGEKGVnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
....
gi 2217391356 742 KIFQ 745
Cdd:PTZ00243 820 RVVE 823
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
705-734 |
3.04e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.02 E-value: 3.04e-04
10 20 30
....*....|....*....|....*....|
gi 2217391356 705 LSGGEKQRIGMARMFYHRPKYALLDECTSA 734
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSA 170
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
705-734 |
3.93e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.53 E-value: 3.93e-04
10 20 30
....*....|....*....|....*....|
gi 2217391356 705 LSGGEKQRIGMARMFYHRPKYALLDECTSA 734
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
705-763 |
4.20e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.84 E-value: 4.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217391356 705 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKI----FQAAKDAGIALLSITHRPSL 763
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIadllFSLNREHGTTLILVTHDLQL 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
605-748 |
4.97e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 605 ITGPNGCGKSSLFRILGG-LWPTYGGVLYKPppqRMFYIPQrpYMSVGslrdqviYPDSVEDMQRKG---------YSEq 674
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGvLKPDEGEVDPEL---KISYKPQ--YIKPD-------YDGTVEDLLRSItddlgssyyKSE- 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217391356 675 dleaILDVVHLHHILQREggweaMCDwkdvLSGGEKQRIGMARMFYHRPKYALLDEcTSAvSIDVEGKIfQAAK 748
Cdd:PRK13409 437 ----IIKPLQLERLLDKN-----VKD----LSGGELQRVAIAACLSRDADLYLLDE-PSA-HLDVEQRL-AVAK 494
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
593-735 |
4.98e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVL-----------YKPPPQRMFYIPQRPYMSVGSLRDQVIYP 660
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIindshnlkdinLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 661 -DSVEDMQ-------RKGYSEQ---------------DLEAILDVVHLHHILQREGGWEAMCDWKDV------------- 704
Cdd:PTZ00265 484 lYSLKDLEalsnyynEDGNDSQenknkrnscrakcagDLNDMSNTTDSNELIEMRKNYQTIKDSEVVdvskkvlihdfvs 563
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217391356 705 ----------------LSGGEKQRIGMARMFYHRPKYALLDECTSAV 735
Cdd:PTZ00265 564 alpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
589-745 |
5.80e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.55 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP-TYGGVLYK--PPPQ--------RMFYIPQRPYMsvgslrdqv 657
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHdiPLTKlqldswrsRLAVVSQTPFL--------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 658 iYPDSVED---MQRKGYSEQDLEAILDVVHLHH-ILQREGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECT 732
Cdd:PRK10789 401 -FSDTVANniaLGRPDATQQEIEHVARLASVHDdILRLPQGYDTEVGERGVmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170
....*....|...
gi 2217391356 733 SAVSIDVEGKIFQ 745
Cdd:PRK10789 480 SAVDGRTEHQILH 492
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
589-759 |
7.33e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 42.31 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGVLYKPPP----------QRMFYIPQRPYMSVG-SLRDQ 656
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARlLTPQSGTVFLGDKPismlssrqlaRRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 657 VIYPDS----------VEDMQRkgySEQDLEAildvVHLHHILQReggweAMCDwkdvLSGGEKQRIGMARMFYHRPKYA 726
Cdd:PRK11231 97 VAYGRSpwlslwgrlsAEDNAR---VNQAMEQ----TRINHLADR-----RLTD----LSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217391356 727 LLDECTSAVSID--VE-GKIFQAAKDAGIALLSITH 759
Cdd:PRK11231 161 LLDEPTTYLDINhqVElMRLMRELNTQGKTVVTVLH 196
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
593-744 |
7.50e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFR-ILGGLWPTYGG-VLYKpppQRMFYIPQRPYMSVGSLRDQVIYPDSvedmqrkg 670
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDAsVVIR---GTVAYVPQVSWIFNATVRDNILFGSP-------- 704
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217391356 671 YSEQDLEAILDVVHLHHILQR-EGGWEAMCDWKDV-LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIF 744
Cdd:PLN03130 705 FDPERYERAIDVTALQHDLDLlPGGDLTEIGERGVnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
642-760 |
1.51e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.27 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 642 IPQRPYMSVGSLRDQViypDSVEDmqrkgYSEQDLEAILDVVHLHHILQREG-GWEA-MCDWKDVLSGGEKQRIGMARMF 719
Cdd:PLN03232 1315 IPQSPVLFSGTVRFNI---DPFSE-----HNDADLWEALERAHIKDVIDRNPfGLDAeVSEGGENFSVGQRQLLSLARAL 1386
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2217391356 720 YHRPKYALLDECTSAVSIDVEGKIFQAAKDA--GIALLSITHR 760
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEfkSCTMLVIAHR 1429
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
705-762 |
1.57e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.93 E-value: 1.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217391356 705 LSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIfQAAKDA---GIALLSITHRPS 762
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI-QAALDElqkNRTSLVIAHRLS 540
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
607-735 |
1.94e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.92 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 607 GPNGCGKSSLFRI---LGGLWPT---------YGGVLYKP---PPQ---RMFYIPQRPYMSVGSLRDQVIYPDSVEDMQr 668
Cdd:PRK14243 43 GPSGCGKSTILRCfnrLNDLIPGfrvegkvtfHGKNLYAPdvdPVEvrrRIGMVFQKPNPFPKSIYDNIAYGARINGYK- 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217391356 669 kgyseQDLEAILDvvhlhHILQREGGWEAMcdwKD-------VLSGGEKQRIGMARMFYHRPKYALLDECTSAV 735
Cdd:PRK14243 122 -----GDMDELVE-----RSLRQAALWDEV---KDklkqsglSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
587-775 |
2.75e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.22 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 587 EVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLW-PTYGGVLYKPPPQR-------MFYIPQRPYMsvgslrdqvi 658
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESGQIQIDGKTATrgdrsrfMAYLGHLPGL---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 659 ypdsvedmqrkgysEQDLEAI-----LDVVHLHHILQREGGWEA---MCDWKDV----LSGGEKQRIGMARMFYHRPKYA 726
Cdd:PRK13543 94 --------------KADLSTLenlhfLCGLHGRRAKQMPGSALAivgLAGYEDTlvrqLSAGQKKRLALARLWLSPAPLW 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217391356 727 LLDEctSAVSIDVEG-----KIFQAAKDAGIALLSITH--RPSLwKYHTHLLQFDG 775
Cdd:PRK13543 160 LLDE--PYANLDLEGitlvnRMISAHLRGGGAALVTTHgaYAAP-PVRTRMLTLEA 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
589-730 |
3.28e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.60 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 589 VVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY--------KPPPQR---M------FYipqrPYMSVg 651
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvvneLEPADRdiaMvfqnyaLY----PHMSV- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 652 slRDQVIYPDSVEDMQrKGYSEQDLEAILDVVHLHHILQR---EggweamcdwkdvLSGGEKQRIGMARMFYHRPKYALL 728
Cdd:PRK11650 94 --RENMAYGLKIRGMP-KAEIEERVAEAARILELEPLLDRkprE------------LSGGQRQRVAMGRAIVREPAVFLF 158
|
..
gi 2217391356 729 DE 730
Cdd:PRK11650 159 DE 160
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
593-625 |
4.55e-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: 39.44 E-value: 4.55e-03
10 20 30
....*....|....*....|....*....|...
gi 2217391356 593 LNIRVEEGMHLLITGPNGCGKSSLFRILGGLWP 625
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP 73
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
583-630 |
5.10e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 39.68 E-value: 5.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2217391356 583 TPSGEVVVAS-LNIRVEEGMHLLITGPNGCGKSSLFRILGG-LWPTYGGV 630
Cdd:COG1134 34 TRREEFWALKdVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPTSGRV 83
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
583-733 |
6.06e-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: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 583 TPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYG-----GVLYKPPP----QRMF-YIPQRPYMSVGS 652
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiqidGVSWNSVTlqtwRKAFgVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 653 LRDQViypDSVEDmqrkgYSEQDLEAILDVVHLHHILQR----------EGGWeamcdwkdVLSGGEKQRIGMARMFYHR 722
Cdd:TIGR01271 1308 FRKNL---DPYEQ-----WSDEEIWKVAEEVGLKSVIEQfpdkldfvlvDGGY--------VLSNGHKQLMCLARSILSK 1371
|
170
....*....|.
gi 2217391356 723 PKYALLDECTS 733
Cdd:TIGR01271 1372 AKILLLDEPSA 1382
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
586-743 |
6.62e-03 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 39.35 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 586 GEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY---------KPPPQRMFYIPQrpymsvgsLRDQ 656
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtaRSLSQQKGLIRQ--------LRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 657 ViypdsvedmqrkGYSEQDLE------AILDVVHLHHILQREGGWEAMCDWKDVL----------------SGGEKQRIG 714
Cdd:PRK11264 87 V------------GFVFQNFNlfphrtVLENIIEGPVIVKGEPKEEATARARELLakvglagketsyprrlSGGQQQRVA 154
|
170 180
....*....|....*....|....*....
gi 2217391356 715 MARMFYHRPKYALLDECTSAVSIDVEGKI 743
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEV 183
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
605-759 |
7.54e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 39.35 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 605 ITGPNGCGKSSLFRILGGL-WPTYGGVLYKPPP----------QRMFYIPQRPYMS-VGS---------LRDQVIypdSV 663
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIeKVKSGEIFYNNQAitddnfeklrKHIGIVFQNPDNQfVGSivkydvafgLENHAV---PY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 664 EDMQRKGYseqdlEAILDVvhlhhilqreggweAMCDWKD----VLSGGEKQRIGMARMFYHRPKYALLDECTSAvsIDV 739
Cdd:PRK13648 117 DEMHRRVS-----EALKQV--------------DMLERADyepnALSGGQKQRVAIAGVLALNPSVIILDEATSM--LDP 175
|
170 180
....*....|....*....|....*.
gi 2217391356 740 EGK------IFQAAKDAGIALLSITH 759
Cdd:PRK13648 176 DARqnlldlVRKVKSEHNITIISITH 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
590-759 |
8.38e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 39.67 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 590 VASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLY-------------KPPPQRMFYIPQRPY------MSV 650
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFdgqdldglsrralRPLRRRMQVVFQDPFgslsprMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217391356 651 GslrdQVIypdsVEDM--QRKGYSEQDLEA----ILDVVHLHH-ILQR---EggweamcdwkdvLSGGEKQRIGMARMFY 720
Cdd:COG4172 382 G----QII----AEGLrvHGPGLSAAERRArvaeALEEVGLDPaARHRyphE------------FSGGQRQRIAIARALI 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217391356 721 HRPKYALLDECTSA--VSIdvegkifQA---------AKDAGIALLSITH 759
Cdd:COG4172 442 LEPKLLVLDEPTSAldVSV-------QAqildllrdlQREHGLAYLFISH 484
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
604-673 |
9.61e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 9.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217391356 604 LItGPNGCGKSSLFRILGG-LWPTYGGVLYKpPPQRMfyipqrpymsvGSLR-DQVIYPD-SVEDMQRKGYSE 673
Cdd:PRK15064 32 LI-GANGCGKSTFMKILGGdLEPSAGNVSLD-PNERL-----------GKLRqDQFAFEEfTVLDTVIMGHTE 91
|
|
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