|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
137-825 |
0e+00 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 540.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 137 LPQRPPVDIEFcDISYSVTDS---HRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTA--QLSGSVLIN 211
Cdd:TIGR00955 10 VFGRVAQDGSW-KQLVSRLRGcfcRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvKGSGSVLLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 212 SKERNLRRFRKLSCYIMQDDVLIANLTVREAMMVAANLKLGKNMISYAKVVVVEEILETIGLKESVNTLT------CNLS 285
Cdd:TIGR00955 89 GMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIgvpgrvKGLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 286 GGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYE 365
Cdd:TIGR00955 169 GGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 366 GRVKGLVPYLSSLGYECPSYHNPADYVLEVASGEYGDavpklvdavksgackkyahKDYVLTLAQKGCNNDIIkgSGSGA 445
Cdd:TIGR00955 249 GSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGS-------------------ENESRERIEKICDSFAV--SDIGR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 446 ENAMAILTLEDEKPPLEdrqlepsipvddpaelkppkletqqsqnsdcsvvnmptnavddscsfsssKGTQNavggsgsg 525
Cdd:TIGR00955 308 DMLVNTNLWSGKAGGLV--------------------------------------------------KDSEN-------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 526 gpsavvgcmtslldshesvvtlPNKTGFPTSGWTQFWILLKRSFRTILRDKMLTHMRLFSHVIVGAIIGMIYYDVGNEAS 605
Cdd:TIGR00955 330 ----------------------MEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQK 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 606 KIMSNAGCIFFVSLFTTFTAMMPTILTFPTEMSVFVREHLNYWYSLKAFYFAKTIADMPFQIVFSSVYVLVVYYLTSQPM 685
Cdd:TIGR00955 388 GVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRS 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 686 ELERVSMFVLICVLNSLVAQSLGLLIG-AGMNIETGVFLGPVTTIPTILFSGFFVNFDTIPGYLQWVTYVSYVRYGFEGA 764
Cdd:TIGR00955 468 GATHFLTFLFLVTLVANVATSFGYLIScAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGL 547
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076684 765 MVAIYGMDR--AKMQCN-QMYCHYRVPkKFLEEMSMDNALFWVDAVALIGIFFALRIIAYFVLR 825
Cdd:TIGR00955 548 LINQWSDVDniECTSANtTGPCPSSGE-VILETLSFRNADLYLDLIGLVILIFFFRLLAYFALR 610
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
142-366 |
6.80e-92 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 287.14 E-value: 6.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 142 PVDIEFCDISYSVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKT-AQLSGSVLINSKERNLRRF 220
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTgLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYIMQDDVLIANLTVREAMMVAANLKlgknmisyakvvvveeiletiglkesvntltcNLSGGQRKRLSIALELVN 300
Cdd:cd03213 81 RKIIGYVPQDDILHPTLTVRETLMFAAKLR--------------------------------GLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 301 NPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEG 366
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
163-825 |
6.95e-77 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 262.51 E-value: 6.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAQLSGSVLINSKERNLRRFRKLScYIMQDDVLIANLTVRE 241
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 242 AMMVAANLKLGKNMISYAKVVVVEEILETIGLKESVNTLTCN-----LSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 317 STCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEGRVKGLVPYLSSLGYECPSYHNPADYVLEVA 396
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 397 SGEygdavpklvdavksgackkyahkdyvltlaqkgCNNDIIKgsgsgaenamailtlEDEKPPLEDRQlepsipVDDPA 476
Cdd:PLN03211 320 NGV---------------------------------CQTDGVS---------------EREKPNVKQSL------VASYN 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 477 ELKPPKLETqqsqnsdcsVVNMPTNAVDDSCSFSSSKGTQNAvggsgsggpsavvGCMTSLLDShesvvtlpnktgfpts 556
Cdd:PLN03211 346 TLLAPKVKA---------AIEMSHFPQANARFVGSASTKEHR-------------SSDRISIST---------------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 557 gW-TQFWILLKRSFRTiLRDKMLTHMRLFSHVIVGAIIGMIYYDvgNEASKIMSNAGCIFFVSLFTTFTAMMPTILTFPT 635
Cdd:PLN03211 388 -WfNQFSILLQRSLKE-RKHESFNTLRVFQVIAAALLAGLMWWH--SDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 636 EMSVFVREHLNYWYSLKAFYFAKTIADMPFQIVFSSVYVLVVYYLTSQPMELERVSMFVLICVLNSLVAQSLGLLIGAG- 714
Cdd:PLN03211 464 ERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAi 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 715 MNIETGVFLGPVTTIPTILFSGFFVNfdTIPGYLQWVTYVSYVRYGFEGAMVAIYGMDR---AKMQCNQMYCHYRVPKKF 791
Cdd:PLN03211 544 MDAKKASTIVTVTMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYRLLINVQYGEGKrisSLLGCSLPHGSDRASCKF 621
|
650 660 670
....*....|....*....|....*....|....
gi 161076684 792 LEEMSMDNALFWVDAVALIGIFFALRIIAYFVLR 825
Cdd:PLN03211 622 VEEDVAGQISPATSVSVLIFMFVGYRLLAYLALR 655
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
165-829 |
2.44e-70 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 253.11 E-value: 2.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQL--SGSVLINSKERNlRRFRKLSCYIMQDDVLIANLTVREA 242
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSFQRSIGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 243 MMVAANLKLGKNMISYAKVVVVEEILETIGLKESVNTLT----CNLSGGQRKRLSIALELVNNPP-VMFFDEPTSGLDSS 317
Cdd:TIGR00956 857 LRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQ 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 318 TCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQG-QCVYEGRV----KGLVPYLSSLG-YECPSYHNPADY 391
Cdd:TIGR00956 937 TAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDLgensHTIINYFEKHGaPKCPEDANPAEW 1016
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 392 VLEVasgeygdavpklvdavkSGAckkyahkdyvltlaqkgcnndiikGSGSGAEnamailtledekppledrqlepsip 471
Cdd:TIGR00956 1017 MLEV-----------------IGA------------------------APGAHAN------------------------- 1030
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 472 vDDPAELKPPKLETQQSQNSDCSVVNMPTNAVDDSCSFSSSKgtqnavggsgsggpsavvgcmtslldshesvvtlpnkt 551
Cdd:TIGR00956 1031 -QDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDALSK-------------------------------------- 1071
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 552 gFPTSGWTQFWILLKRSFRTILRDKMLTHMRLFSHVIVGAIIGMIYYDVGNEASKIMSNAGCIF-FVSLFTTF-TAMMPT 629
Cdd:TIGR00956 1072 -YAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQMFAVFmATVLFNPLiQQYLPP 1150
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 630 ILTfpTEMSVFVREHLNYWYSLKAFYFAKTIADMPFQIVFSSVYVLVVYY-------LTSQPMELERVSMFVLICVLNSL 702
Cdd:TIGR00956 1151 FVA--QRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYpvgfywnASKTGQVHERGVLFWLLSTMFFL 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 703 VAQSLGLL-IGAGMNIETG-VFLGPVTTIpTILFSGFFVNFDTIPGYLQWVTYVSYVRYGFEGAMVAIYG--MDRAK--- 775
Cdd:TIGR00956 1229 YFSTLGQMvISFNPNADNAaVLASLLFTM-CLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLAdvPVTCKvke 1307
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 776 ---------MQCNQ----------------------MYCHYRVPKKFLEEMSMDNALFWVDavalIGIFFA---LRIIAY 821
Cdd:TIGR00956 1308 lltfnppsgQTCGEymkpylenaggyllnpnatdscSFCQYSYTNDFLEPISSKYSGRWRN----FGIFIAfifFNIIAT 1383
|
....*...
gi 161076684 822 FVLRWKLH 829
Cdd:TIGR00956 1384 VFFYWLAR 1391
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
154-366 |
3.24e-64 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 214.44 E-value: 3.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 154 VTDSHRRGFKT--ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG--YKTAQLSGSVLINSKERNLRRFRKLSCYIMQ 229
Cdd:cd03234 9 VGLKAKNWNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrvEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 230 DDVLIANLTVREAMMVAANLKLGKNMISYAKVVVVE-EILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFD 308
Cdd:cd03234 89 DDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 309 EPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEG 366
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
145-366 |
1.10e-63 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 211.72 E-value: 1.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDshRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQL-SGSVLINSKERNlRRFRKL 223
Cdd:cd03232 4 LTWKNLNYTVPV--KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGViTGEILINGRPLD-KNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 224 SCYIMQDDVLIANLTVREAMMVAANLKlgknmisyakvvvveeiletiglkesvntltcNLSGGQRKRLSIALELVNNPP 303
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRFSALLR--------------------------------GLSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076684 304 VMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQ-GQCVYEG 366
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
564-767 |
1.29e-54 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 187.48 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 564 LLKRSFRTILRDKMLTHMRLFSHVIVGAIIGMIYYDVGNEASkIMSNAGCIFFVSLFTTFTAMMPTILTFPTEMSVFVRE 643
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 644 HLNYWYSLKAFYFAKTIADMPFQIVFSSVYVLVVYYLTSQPMELERVSMFVLICVLNSLVAQSLGLLIGA-GMNIETGVF 722
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISAlAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 161076684 723 LGPVTTIPTILFSGFFVNFDTIPGYLQWVTYVSYVRYGFEGAMVA 767
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
163-780 |
6.94e-52 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 197.25 E-value: 6.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyKTAQL----SGSVLIN--SKERNLRRFRKLSCYIMQDDVLIAN 236
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS-NTDGFhigvEGVITYDgiTPEEIKKHYRGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAMMVAANLKLGKNMI------SYAKVVVvEEILETIGLKESVNTLTCN-----LSGGQRKRLSIALELVNNPPVM 305
Cdd:TIGR00956 153 LTVGETLDFAARCKTPQNRPdgvsreEYAKHIA-DVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 306 FFDEPTSGLDSSTCFQLISLLRSLAR-GGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEGRVKGLVPYLSSLGYECPS 384
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPD 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 385 YHNPADYVLEVAS-------GEYGDAVPKLVDAVksgacKKYAHKdyvltlaqkgcnndiikgSGSGAenamailtlede 457
Cdd:TIGR00956 312 RQTTADFLTSLTSpaerqikPGYEKKVPRTPQEF-----ETYWRN------------------SPEYA------------ 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 458 kppledrQLEpsipvddpAELKPPKLETQQSQNSDcsvvnmptnAVDDSCSFSSSKGTQNAvggsgsggpsavvgcmtsl 537
Cdd:TIGR00956 357 -------QLM--------KEIDEYLDRCSESDTKE---------AYRESHVAKQSKRTRPS------------------- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 538 ldSHESVvtlpnktgfptSGWTQFWILLKRSFRTILRDKMLTHMRLFSHVIVGAIIGMIYYDVGNEASKIMSNAGCIFFV 617
Cdd:TIGR00956 394 --SPYTV-----------SFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 618 SLFTTFTAMMPTILTFptEMSVFVREHLNY-WYSLKAFYFAKTIADMPFQIVFSSVYVLVVYYLTSQPMELERVSMFVLI 696
Cdd:TIGR00956 461 ILFNAFSSLLEIASMY--EARPIVEKHRKYaLYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLI 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 697 CVLNSLVAQSLGLLIGAGM-NIETGVFLGPVTTIPTILFSGFFVNFDTIPGYLQWVTYVSYVRYGFEGAMVAiyGMDRAK 775
Cdd:TIGR00956 539 LFICTLAMSHLFRSIGAVTkTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVN--EFHGRR 616
|
....*
gi 161076684 776 MQCNQ 780
Cdd:TIGR00956 617 FECSQ 621
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
86-770 |
8.08e-52 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 196.99 E-value: 8.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 86 TNDLKQNSHGSQNNLCNGGLGSNNHALAPKVANNSGGSPNGQKKGTIALSHLPQR------PPVDIEFCDISYSV---TD 156
Cdd:PLN03140 803 AEEMEGEEDSIPRSLSSADGNNTREVAIQRMSNPEGLSKNRDSSLEAANGVAPKRgmvlpfTPLAMSFDDVNYFVdmpAE 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFK----TILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTA-QLSGSVLINSKERNLRRFRKLSCYIMQDD 231
Cdd:PLN03140 883 MKEQGVTedrlQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgYIEGDIRISGFPKKQETFARISGYCEQND 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 232 VLIANLTVREAMMVAANLKLGKNMISYAKVVVVEEILETI---GLKESVNTL--TCNLSGGQRKRLSIALELVNNPPVMF 306
Cdd:PLN03140 963 IHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVeldNLKDAIVGLpgVTGLSTEQRKRLTIAVELVANPSIIF 1042
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 307 FDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQ-GQCVYEGRV----KGLVPYLSSLG-- 379
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLgrnsHKIIEYFEAIPgv 1122
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 380 YECPSYHNPADYVLEVASgeygdavpkLVDAVKSGAckKYAHKDYVLTLAQKgcNNDIIKgsgsgaenamailtledekp 459
Cdd:PLN03140 1123 PKIKEKYNPATWMLEVSS---------LAAEVKLGI--DFAEHYKSSSLYQR--NKALVK-------------------- 1169
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 460 pledrqlEPSIPvddPAELKPPKLETQQSQNSdcsvvnmptnavddscsfssskgtqnavggsgsggpsavvgcmtslld 539
Cdd:PLN03140 1170 -------ELSTP---PPGASDLYFATQYSQST------------------------------------------------ 1191
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 540 shesvvtlpnktgfptsgWTQFWILLKRSFRTILRDKMLTHMRLFSHVIVGAIIGMIYYDVG---NEASKIMSNAGCIFF 616
Cdd:PLN03140 1192 ------------------WGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGtkrSNANDLTMVIGAMYA 1253
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 617 VSLFTTFTAMMPTILTFPTEMSVFVREHLNYWYSLKAFYFAKTIADMPFQIVFSSVYVLVVYYLTSQPMELERVSMFVLI 696
Cdd:PLN03140 1254 AVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFI 1333
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 697 CVLNSLVAQSLGLLIgagmnietgVFLGPVTTIPTI----------LFSGFFVNFDTIPGYLQWVTYVSYVRYGFEGAMV 766
Cdd:PLN03140 1334 SFFSFLYFTYYGMMT---------VSLTPNQQVAAIfaaafyglfnLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIV 1404
|
....
gi 161076684 767 AIYG 770
Cdd:PLN03140 1405 SQYG 1408
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
157-371 |
1.89e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.70 E-value: 1.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK--ERNLRRFRKLSCYIMQDDVLI 234
Cdd:COG1131 7 TKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT-SGEVRVLGEdvARDPAEVRRRIGYVPQEPALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 235 ANLTVREAMMVAANLKlGKNMISYAKVVvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGL 314
Cdd:COG1131 86 PDLTVRENLRFFARLY-GLPRKEARERI--DELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 315 DSSTCFQLISLLRSLARGGRTIVCTIHQPS--ARLfekFDHLYLLAQGQCVYEGRVKGL 371
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTVLLSTHYLEeaERL---CDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
146-361 |
8.06e-43 |
|
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: 154.55 E-value: 8.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 146 EFCDISYSVTDshrrGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK---ERNLRRFRK 222
Cdd:cd03225 1 ELKNLSFSYPD----GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT-SGEVLVDGKdltKLSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 223 LSCYIMQD-DVLIANLTVREAMMVAA-NLKLGKNMIsyakVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVN 300
Cdd:cd03225 76 KVGLVFQNpDDQFFGPTVEEEVAFGLeNLGLPEEEI----EERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076684 301 NPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSaRLFEKFDHLYLLAQGQ 361
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
145-366 |
7.83e-42 |
|
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: 152.66 E-value: 7.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSvtdshrRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK------ERNLR 218
Cdd:cd03261 1 IELRGLTKS------FGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD-SGEVLIDGEdisglsEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRKLSCYIMQDDVLIANLTVRE--AMMVAANLKLGKNMISyakvVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIAL 296
Cdd:cd03261 74 RLRRRMGMLFQSGALFDSLTVFEnvAFPLREHTRLSEEEIR----EIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR--GGRTIVCTiHQPSaRLFEKFDHLYLLAQGQCVYEG 366
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVT-HDLD-TAFAIADRIAVLYDGKIVAEG 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
163-371 |
1.33e-41 |
|
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: 152.32 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN--SKERNLRRFRKLSCYIMQDDVLIANLTVR 240
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD-SGSILIDgeDVRKEPREARRQIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 EAMMVAANLKlgkNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCF 320
Cdd:COG4555 93 ENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 161076684 321 QLISLLRSLARGGRTIVCTIHQPS--ARLfekFDHLYLLAQGQCVYEGRVKGL 371
Cdd:COG4555 170 LLREILRALKKEGKTVLFSSHIMQevEAL---CDRVVILHKGKVVAQGSLDEL 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
145-367 |
1.92e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.35 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRRgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK------ERNLR 218
Cdd:COG1136 5 LELRNLTKSYGTGEGE--VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPT-SGEVLIDGQdisslsERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRKLSC-YIMQDDVLIANLTVREammvaaNLKLGknmISYAKVVV------VEEILETIGLKESVNTLTCNLSGGQRKR 291
Cdd:COG1136 82 RLRRRHIgFVFQFFNLLPELTALE------NVALP---LLLAGVSRkerrerARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 292 LSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR-GGRTIVCTIHqpSARLFEKFDHLYLLAQGQCVYEGR 367
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTH--DPELAARADRVIRLRDGRIVSDER 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
145-366 |
1.47e-40 |
|
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: 149.02 E-value: 1.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRrgfktILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK---ERNLRRFR 221
Cdd:COG1122 1 IELENLSFSYPGGTP-----ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT-SGEVLVDGKditKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 KLSCYIMQD-DVLIANLTVREAmmVA---ANLKLGKNMIsyakVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALE 297
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEED--VAfgpENLGLPREEI----RERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 298 LVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSArLFEKFDHLYLLAQGQCVYEG 366
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADG 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
145-361 |
7.52e-40 |
|
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: 146.48 E-value: 7.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRRgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK------ERNLR 218
Cdd:cd03255 1 IELKNLSKTYGGGGEK--VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT-SGEVRVDGTdisklsEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFR--KLScYIMQDDVLIANLTVREAMMVAANL--KLGKNMISYAkvvvvEEILETIGLKESVNTLTCNLSGGQRKRLSI 294
Cdd:cd03255 78 AFRrrHIG-FVFQSFNLLPDLTALENVELPLLLagVPKKERRERA-----EELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 295 ALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPsaRLFEKFDHLYLLAQGQ 361
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP--ELAEYADRIIELRDGK 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
153-366 |
9.24e-39 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 142.79 E-value: 9.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGY--KTAQLSGSVLINSKE--RNLRRFRKLSCYIM 228
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSVEGDIHYNGIPykEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 229 QDDVLIANLTVREAMMVAANLKlGKNMISyakvvvveeiletiglkesvntltcNLSGGQRKRLSIALELVNNPPVMFFD 308
Cdd:cd03233 90 EEDVHFPTLTVRETLDFALRCK-GNEFVR-------------------------GISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 309 EPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEG 366
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
158-341 |
2.36e-38 |
|
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: 142.26 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 158 HRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN--SKERNLRRFRKLSCYIMQDDVLIA 235
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT-SGTAYINgySIRTDRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAMMVAANLK-LGKNMISyakvVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGL 314
Cdd:cd03263 89 ELTVREHLRFYARLKgLPKSEIK----EEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180
....*....|....*....|....*..
gi 161076684 315 DSSTCFQLISLLRSLaRGGRTIVCTIH 341
Cdd:cd03263 165 DPASRRAIWDLILEV-RKGRSIILTTH 190
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
157-361 |
4.90e-38 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 139.84 E-value: 4.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE--RNLRRFRKLSCYIMQDDVLI 234
Cdd:cd03230 7 SKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-SGEIKVLGKDikKEPEEVKRRIGYLPEEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 235 ANLTVREammvaaNLKlgknmisyakvvvveeiletiglkesvntltcnLSGGQRKRLSIALELVNNPPVMFFDEPTSGL 314
Cdd:cd03230 86 ENLTVRE------NLK---------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 161076684 315 DSSTCFQLISLLRSLARGGRTIVCTIHQPSaRLFEKFDHLYLLAQGQ 361
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGR 172
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
158-366 |
5.04e-37 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 139.24 E-value: 5.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 158 HRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINS------KERNLRRFRKLSCYIMQDD 231
Cdd:cd03256 9 TYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-SGSVLIDGtdinklKGKALRQLRRQIGMIFQQF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 232 VLIANLTVREAMMVAA-----NLKLGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMF 306
Cdd:cd03256 88 NLIERLSVLENVLSGRlgrrsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076684 307 FDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPS-ARLFekFDHLYLLAQGQCVYEG 366
Cdd:cd03256 168 ADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIVFDG 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
145-366 |
2.02e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 137.87 E-value: 2.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYsvtdshRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINskERNLRRF---- 220
Cdd:COG1120 2 LEAENLSV------GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLD--GRDLASLsrre 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 --RKLScYIMQDDVLIANLTVREamMVAanlkLGKN-------MISYAKVVVVEEILETIGLKE----SVNTltcnLSGG 287
Cdd:COG1120 73 laRRIA-YVPQEPPAPFGLTVRE--LVA----LGRYphlglfgRPSAEDREAVEEALERTGLEHladrPVDE----LSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 288 QRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPS--ARLfekFDHLYLLAQGQCVY 364
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlaARY---ADRLVLLKDGRIVA 218
|
..
gi 161076684 365 EG 366
Cdd:COG1120 219 QG 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
137-372 |
3.82e-36 |
|
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: 144.52 E-value: 3.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 137 LPQRPPVDIEFCDISYSVTDShrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-R 215
Cdd:COG4988 329 LPAAGPPSIELEDVSFSYPGG-----RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-SGSILINGVDlS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 216 NLRR--FRKLSCYIMQDDVLIAnLTVREammvaaNLKLGKNMISYAKVvvvEEILETIGLKESVNTL-----T------C 282
Cdd:COG4988 403 DLDPasWRRQIAWVPQNPYLFA-GTIRE------NLRLGRPDASDEEL---EAALEAAGLDEFVAALpdgldTplgeggR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 283 NLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTiHQPSARlfEKFDHLYLLAQGQC 362
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLALL--AQADRILVLDDGRI 549
|
250
....*....|
gi 161076684 363 VYEGRVKGLV 372
Cdd:COG4988 550 VEQGTHEELL 559
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
157-361 |
3.69e-35 |
|
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: 130.83 E-value: 3.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN---SKERNLRRFRKLSCYIMQddvl 233
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-SGEILIDgkdIAKLPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 234 ianltvreammvaanlklgknmisyakvvvveeiletiglkesvntltcnLSGGQRKRLSIALELVNNPPVMFFDEPTSG 313
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 161076684 314 LDSSTCFQLISLLRSLARGGRTIVCTIHQPSarLFEKF-DHLYLLAQGQ 361
Cdd:cd00267 111 LDPASRERLLELLRELAEEGRTVIIVTHDPE--LAELAaDRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
166-312 |
4.66e-35 |
|
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: 130.46 E-value: 4.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE---RNLRRFRKLSCYIMQDDVLIANLTVREA 242
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-EGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076684 243 MMVAANLKLGKNMISYAKvvvVEEILETIGL----KESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTS 312
Cdd:pfam00005 80 LRLGLLLKGLSKREKDAR---AEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
144-367 |
1.18e-34 |
|
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: 141.51 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSVTDSHrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINS---KERNLRRF 220
Cdd:COG2274 473 DIELENVSFRYPGDS----PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT-SGRILIDGidlRQIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYIMQDDVLIANlTVREammvaaNLKLGKNMISYAKVVvveEILETIGLKESVNTL-----T------CNLSGGQR 289
Cdd:COG2274 548 RRQIGVVLQDVFLFSG-TIRE------NITLGDPDATDEEII---EAARLAGLHDFIEALpmgydTvvgeggSNLSGGQR 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 290 KRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIHQPSarLFEKFDHLYLLAQGQCVYEGR 367
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS--TIRLADRIIVLDKGRIVEDGT 692
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
163-364 |
1.32e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRfRKLScYIMQDDVLIAN--LTVR 240
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT-SGTVRLFGKPPRRAR-RRIG-YVPQRAEVDWDfpITVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 EamMVAANLKLGKNM---ISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:COG1121 96 D--VVLMGRYGRRGLfrrPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 161076684 318 TCFQLISLLRSLARGGRTIVCTIHQPSArLFEKFDHLYLLAQGQCVY 364
Cdd:COG1121 174 TEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGLVAH 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
157-366 |
1.53e-34 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 129.86 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKErnlrrfrklscyimqddvlIAN 236
Cdd:cd03214 6 SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGKD-------------------LAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVRE-AMMVAanlklgknmisyakvvVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:cd03214 66 LSPKElARKIA----------------YVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 161076684 316 SSTCFQLISLLRSLAR-GGRTIVCTIHQPS-ARLFekFDHLYLLAQGQCVYEG 366
Cdd:cd03214 130 IAHQIELLELLRRLAReRGKTVVMVLHDLNlAARY--ADRVILLKDGRIVAQG 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
157-361 |
2.22e-34 |
|
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: 129.61 E-value: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK-----ERNLRRFRKLSCYIMQDD 231
Cdd:cd03229 7 SKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-SGSILIDGEdltdlEDELPPLRRRIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 232 VLIANLTVREammvaaNLKLGknmisyakvvvveeiletiglkesvntltcnLSGGQRKRLSIALELVNNPPVMFFDEPT 311
Cdd:cd03229 86 ALFPHLTVLE------NIALG-------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 161076684 312 SGLDSSTCFQLISLLRSL-ARGGRTIVCTIHQpsarLFEKF---DHLYLLAQGQ 361
Cdd:cd03229 129 SALDPITRREVRALLKSLqAQLGITVVLVTHD----LDEAArlaDRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
149-341 |
3.36e-34 |
|
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: 130.07 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 149 DISYSvtdsHRRGfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLSCYIM 228
Cdd:cd03226 4 NISFS----YKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES-SGSILLNGKPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 229 QD-DVLIANLTVREammvaaNLKLGkNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFF 307
Cdd:cd03226 78 QDvDYQLFTDSVRE------ELLLG-LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190
....*....|....*....|....*....|....
gi 161076684 308 DEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIH 341
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
166-367 |
2.89e-33 |
|
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: 128.32 E-value: 2.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-----------RNLRR-FrklscyimQDDVL 233
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-SGSVLFDGEDitglppheiarLGIGRtF--------QIPRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 234 IANLTVREAMMVAANLKLGKNMISYAKVVV-------VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMF 306
Cdd:cd03219 87 FPELTVLENVMVAAQARTGSGLLLARARREerearerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076684 307 FDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSArLFEKFDHLYLLAQGQCVYEGR 367
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEGT 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
145-361 |
3.81e-33 |
|
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: 125.57 E-value: 3.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRrgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINS---KERNLRRFR 221
Cdd:cd03228 1 IEFKNVSFSYPGRPK----PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-SGEILIDGvdlRDLDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 KLSCYIMQDDVLIaNLTVREammvaaNLklgknmisyakvvvveeiletiglkesvntltcnLSGGQRKRLSIALELVNN 301
Cdd:cd03228 76 KNIAYVPQDPFLF-SGTIRE------NI----------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 302 PPVMFFDEPTSGLDSSTCFQLISLLRSLaRGGRTIVCTIHQPSarLFEKFDHLYLLAQGQ 361
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLS--TIRDADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
137-367 |
5.79e-33 |
|
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: 134.89 E-value: 5.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 137 LPQRPPVDIEFCDISYSVTDSHRrgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINskERN 216
Cdd:COG4987 326 APAPGGPSLELEDVSFRYPGAGR----PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-SGSITLG--GVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 217 LRRF-----RKLSCYIMQDDVLIANlTVREammvaaNLKLGKNMISYAKVVVVeeiLETIGLKESVNTLT---------- 281
Cdd:COG4987 399 LRDLdeddlRRRIAVVPQRPHLFDT-TLRE------NLRLARPDATDEELWAA---LERVGLGDWLAALPdgldtwlgeg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 282 -CNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIHQPSArlFEKFDHLYLLAQG 360
Cdd:COG4987 469 gRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAG--LERMDRILVLEDG 545
|
....*..
gi 161076684 361 QCVYEGR 367
Cdd:COG4987 546 RIVEQGT 552
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
145-371 |
6.70e-33 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 127.40 E-value: 6.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSvtdshrRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK------ERNLR 218
Cdd:COG1127 6 IEVRNLTKS------FGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD-SGEILVDGQditglsEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRKLSCYIMQDDVLIANLTVREAMMVA--ANLKLGKNMISYakvvVVEEILETIGLKESVNTLTCNLSGGQRKRLSIAL 296
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSLTVFENVAFPlrEHTDLSEAEIRE----LVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSL--ARGGRTIVCTiHQ-PSArlFEKFDHLYLLAQGQCVYEGRVKGL 371
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVT-HDlDSA--FAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
163-366 |
2.62e-32 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 125.87 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLI------NSKERNLRRFRKLSCYIMQDDVLIAN 236
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-SGSILLegtditKLRGKKLRKLRRRIGMIFQHYNLIER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAMMVAA-----NLKLGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPT 311
Cdd:TIGR02315 94 LTVLENVLHGRlgykpTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 312 SGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPSarLFEKF-DHLYLLAQGQCVYEG 366
Cdd:TIGR02315 174 ASLDPKTSKQVMDYLKRINKEdGITVIINLHQVD--LAKKYaDRIVGLKAGEIVFDG 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
163-360 |
2.65e-32 |
|
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: 124.57 E-value: 2.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKerNLRRFRKLSCYIMQDDVLIAN--LTVR 240
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT-SGSIRVFGK--PLEKERKRIGYVPQRRSIDRDfpISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 EamMVAANLKLGKNMISYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:cd03235 89 D--VVLMGLYGHKGLFRRLSKADkakVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 161076684 318 TCFQLISLLRSLARGGRTIVCTIHQPSArLFEKFDHLYLLAQG 360
Cdd:cd03235 167 TQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
159-343 |
8.94e-32 |
|
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: 122.97 E-value: 8.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN--SKERNLRRFRKLSCYIMQDDVLIAN 236
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS-AGEVLWNgePIRDAREDYRRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAM-MVAANLKLGKNMISyakvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:COG4133 90 LTVRENLrFWAALYGLRADREA------IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180
....*....|....*....|....*...
gi 161076684 316 SSTCFQLISLLRSLARGGRTIVCTIHQP 343
Cdd:COG4133 164 AAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
163-371 |
1.89e-31 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 123.24 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN------SKERNLRRFRKLSCYIMQDDVLIAN 236
Cdd:COG3638 16 TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT-SGEILVDgqdvtaLRGRALRRLRRRIGMIFQQFNLVPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAMMVAAnlkLGK--------NMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFD 308
Cdd:COG3638 95 LSVLTNVLAGR---LGRtstwrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076684 309 EPTSGLDSSTCFQLISLLRSLAR-GGRTIVCTIHQPS-ARLFekFDHLYLLAQGQCVYEGRVKGL 371
Cdd:COG3638 172 EPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDlARRY--ADRIIGLRDGRVVFDGPPAEL 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
157-361 |
1.94e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 122.23 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKER---NLRRFRKLSCYIMQDDVL 233
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-SGEIYLDGKPLsamPPPEWRRQVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 234 IANlTVREAMMVAANLKLGKnmISYAKvvvVEEILETIGLKESVNTLTC-NLSGGQRKRLSIALELVNNPPVMFFDEPTS 312
Cdd:COG4619 86 WGG-TVRDNLPFPFQLRERK--FDRER---ALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 161076684 313 GLDSSTCFQLISLLRSL-ARGGRTIVCTIHQP--SARLfekFDHLYLLAQGQ 361
Cdd:COG4619 160 ALDPENTRRVEELLREYlAEEGRAVLWVSHDPeqIERV---ADRVLTLEAGR 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
153-366 |
2.39e-31 |
|
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: 122.61 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKtAQLSGSVLIN-------SKERNLRRFRKLSc 225
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL-KPTSGSIIFDgkdllklSRRLRKIRRKEIQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 226 YIMQD--DVLIANLTVREAMMvAANLKLGKNMISYAKVVVVEEILETIGLKESVntLTC---NLSGGQRKRLSIALELVN 300
Cdd:cd03257 86 MVFQDpmSSLNPRMTIGEQIA-EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEV--LNRyphELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 301 NPPVMFFDEPTSGLDSSTCFQLISLLRSL-ARGGRTIVCTIHQPSarLFEKF-DHLYLLAQGQCVYEG 366
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLG--VVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
161-366 |
1.15e-30 |
|
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: 120.01 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE--RNLRRFRKLSCyIMQDDVLIANLT 238
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD-SGEITFDGKSyqKNIEALRRIGA-LIEAPGFYPNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREAMMVAANLKlgknMISYAKVvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSST 318
Cdd:cd03268 89 ARENLRLLARLL----GIRKKRI---DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 161076684 319 CFQLISLLRSLARGGRTIVCTIHQPSArlFEKF-DHLYLLAQGQCVYEG 366
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSHLLSE--IQKVaDRIGIINKGKLIEEG 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
145-369 |
1.29e-30 |
|
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: 120.38 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRRGfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK------ERNLR 218
Cdd:cd03258 2 IELKNVSKVFGDTGGKV--TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT-SGSVLVDGTdltllsGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRKLSCYIMQDDVLIANLTVREAmmVAANLKLGKnmisYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIA 295
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSRTVFEN--VALPLEIAG----VPKAEIeerVLELLELVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076684 296 LELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSL-ARGGRTIVCTIHQPSArLFEKFDHLYLLAQGQCVYEGRVK 369
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVE 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
144-366 |
1.43e-30 |
|
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: 120.00 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSVTDSHRRGfktiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLI---NSKERNLRRF 220
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPA----LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT-SGSVLLdgtDIRQLDPADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYIMQDDVLIANlTVREammvaaNLKLGKnmiSYAKVVVVEEILETIGLKESVNTLT-----------CNLSGGQR 289
Cdd:cd03245 77 RRNIGYVPQDVTLFYG-TLRD------NITLGA---PLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 290 KRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLArGGRTIVCTIHQPSarLFEKFDHLYLLAQGQCVYEG 366
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
157-366 |
9.55e-30 |
|
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: 117.29 E-value: 9.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGeITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE--RNLRRFRKLSCYIMQDDVLI 234
Cdd:cd03264 7 TKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGQDvlKQPQKLRRRIGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 235 ANLTVREAMMVAANLKlgknMISYAKV-VVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSG 313
Cdd:cd03264 85 PNFTVREFLDYIAWLK----GIPSKEVkARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 161076684 314 LDSSTCFQLISLLRSLARgGRTIVCTIHQPSaRLFEKFDHLYLLAQGQCVYEG 366
Cdd:cd03264 161 LDPEERIRFRNLLSELGE-DRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
153-361 |
2.57e-29 |
|
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: 116.09 E-value: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRR-GFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLI-----NSKERNLRRFRKLSCY 226
Cdd:cd03262 2 EIKNLHKSfGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD-SGTIIIdglklTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 227 IMQDDVLIANLTVREAMMVAanLKLGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMF 306
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLA--PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 307 FDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPS-ARlfEKFDHLYLLAQGQ 361
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGfAR--EVADRVIFMDDGR 212
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
164-824 |
3.38e-29 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 125.73 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 164 TILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGY--KTAQLSGSVLINSKERNLRRFRKLSCYIMQDDVLIANLTVRE 241
Cdd:PLN03140 179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKldPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 242 AMMVAANLK-LGK--NMIS-------------------YAKVVVVEEI---------LETIGLKESVNTLTCN-----LS 285
Cdd:PLN03140 259 TLDFSARCQgVGTryDLLSelarrekdagifpeaevdlFMKATAMEGVksslitdytLKILGLDICKDTIVGDemirgIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 286 GGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR-GGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVY 364
Cdd:PLN03140 339 GGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILLSEGQIVY 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 365 EGRVKGLVPYLSSLGYECPSYHNPADYVLEVASgeygdavpklvdavksgacKKYAHKDYVltlaqkgcnndiikgsgsg 444
Cdd:PLN03140 419 QGPRDHILEFFESCGFKCPERKGTADFLQEVTS-------------------KKDQEQYWA------------------- 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 445 aenamailtleDEKPPLEdrqlepSIPVDDPAElKPPKLETQQSQNSDCSVvnmptnavddscSFSSSKGTQNAVGGSGS 524
Cdd:PLN03140 461 -----------DRNKPYR------YISVSEFAE-RFKSFHVGMQLENELSV------------PFDKSQSHKAALVFSKY 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 525 GGPsavvgcmtslldshesvvtlpnKTGFPTSGWTQFWILLKRS-----FRTI-------------LRDKMLTHMRLFSH 586
Cdd:PLN03140 511 SVP----------------------KMELLKACWDKEWLLMKRNafvyvFKTVqiiivaaiastvfLRTEMHTRNEEDGA 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 587 VIVGAII-GMIyydvgneaskimsnagciffVSLFTTFTAMMPTILTFPtemsVFVRE-----HLNYWYSLKAFyfaktI 660
Cdd:PLN03140 569 LYIGALLfSMI--------------------INMFNGFAELALMIQRLP----VFYKQrdllfHPPWTFTLPTF-----L 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 661 ADMPFQIVFSSVYVLVVYYLTSQPMELERVSMFVLICVLNSLVAQSLGLLIGA---GMNI-ETGvflGPVTTIPTILFSG 736
Cdd:PLN03140 620 LGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASvcrTMIIaNTG---GALVLLLVFLLGG 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 737 FFVNFDTIPGYLQWVTYVSYVRYGFEGAMVaiygmdrakmqcNQMYChyrvpKKFLEEMSMDNAL--------------- 801
Cdd:PLN03140 697 FILPKGEIPNWWEWAYWVSPLSYGFNALAV------------NEMFA-----PRWMNKMASDNSTrlgtavlnifdvftd 759
|
730 740
....*....|....*....|....*.
gi 161076684 802 ---FWVDAVALIGIFFALRIIAYFVL 824
Cdd:PLN03140 760 knwYWIGVGALLGFTILFNVLFTLAL 785
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
158-337 |
3.75e-29 |
|
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: 116.03 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 158 HRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLscYIMQDDVLIANL 237
Cdd:cd03293 12 GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT-SGEVLVDGEPVTGPGPDRG--YVFQQDALLPWL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREAMMVAANLKLGKNMISYAKvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:cd03293 89 TVLDNVALGLELQGVPKAEARER---AEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180
....*....|....*....|.
gi 161076684 318 TCFQLIS-LLRSLARGGRTIV 337
Cdd:cd03293 166 TREQLQEeLLDIWRETGKTVL 186
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
164-366 |
5.52e-29 |
|
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: 116.68 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 164 TILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-----------RNLRR-FrklscyimQDD 231
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT-SGRILFDGRDitglpphriarLGIARtF--------QNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 232 VLIANLTVREAMMVAANLKLGKNMISYAK------------VVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELV 299
Cdd:COG0411 89 RLFPELTVLENVLVAAHARLGRGLLAALLrlprarreereaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 300 NNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVctihqpsarLFE---KF-----DHLYLLAQGQCVYEG 366
Cdd:COG0411 169 TEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITIL---------LIEhdmDLvmglaDRIVVLDFGRVIAEG 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
145-372 |
7.46e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 116.06 E-value: 7.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRRgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE---RNLRRFR 221
Cdd:COG1124 2 LEVRNLSVSYGQGGRR--VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW-SGEVTFDGRPvtrRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 KLSCYIMQDDVLIAN--LTVREAMM-VAANLKLGKNMISyakvvvVEEILETIGLKESVntLTCN---LSGGQRKRLSIA 295
Cdd:COG1124 79 RRVQMVFQDPYASLHprHTVDRILAePLRIHGLPDREER------IAELLEQVGLPPSF--LDRYphqLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 296 LELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSL-ARGGRTIVCTIHqpSARLFEKF-DHLYLLAQGQCVYEGRVKGLV 372
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSH--DLAVVAHLcDRVAVMQNGRIVEELTVADLL 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
165-371 |
1.70e-28 |
|
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: 114.07 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSKE-RNL---RRFRKLSCYIMQDDVLIANLTVR 240
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL-LPPRSGSIRFDGRDiTGLpphERARAGIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 EammvaaNLKLGKNMISYAKVV-VVEEILETI-GLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSST 318
Cdd:cd03224 94 E------NLLLGAYARRRAKRKaRLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 161076684 319 CFQLISLLRSLARGGRTIVcTIHQPSARLFEKFDHLYLLAQGQCVYEGRVKGL 371
Cdd:cd03224 168 VEEIFEAIRELRDEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
172-371 |
4.71e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.93 E-value: 4.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 172 KFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSkeRNLRRF----RKLScYIMQDDVLIANLTVRE--AMMV 245
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLPPD-SGRILWNG--QDLTALppaeRPVS-MLFQENNLFPHLTVAQniGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 246 AANLKLgknmiSYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISL 325
Cdd:COG3840 97 RPGLKL-----TAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 161076684 326 LRSLARG-GRTIVCTIHQPS--ARLfekFDHLYLLAQGQCVYEGRVKGL 371
Cdd:COG3840 172 VDELCRErGLTVLMVTHDPEdaARI---ADRVLLVADGRIAADGPTAAL 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
124-337 |
5.14e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 119.24 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 124 PNGQKKGTIALSHLPQRPPVdIEFCDISYSVTDSHRRGFKtILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQ 203
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEPL-LEVRNLSKRYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 204 lSGSVLINSKE------RNLRRFRKLSCYIMQD--DVLIANLTVREAmmVAANLKLGKNMISYAKVVVVEEILETIGLKE 275
Cdd:COG1123 319 -SGSILFDGKDltklsrRSLRELRRRVQMVFQDpySSLNPRMTVGDI--IAEPLRLHGLLSRAERRERVAELLERVGLPP 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076684 276 SV-NTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR-GGRTIV 337
Cdd:COG1123 396 DLaDRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYL 459
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
173-366 |
8.65e-28 |
|
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: 111.82 E-value: 8.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 173 FRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERN-LRRFRKLSCYIMQDDVLIANLTVREAMMVAANLKL 251
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQ-SGRVLINGVDVTaAPPADRPVSMLFQENNLFAHLTVEQNVGLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 252 GKNMISYAKvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR 331
Cdd:cd03298 100 KLTAEDRQA---IEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 161076684 332 -GGRTIVCTIHQP--SARLfekFDHLYLLAQGQCVYEG 366
Cdd:cd03298 177 eTKMTVLMVTHQPedAKRL---AQRVVFLDNGRIAAQG 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
149-382 |
9.91e-28 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 112.47 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 149 DISYSVTDshrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG---YK-TaqlSGSVLINSKerNL------R 218
Cdd:COG0396 5 NLHVSVEG------KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEvT---SGSILLDGE--DIlelspdE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRK---LScyiMQDDVLIANLTVREAMMVAANLKLGKNMISYAKVVVVEEILETIGLKES-----VNTltcNLSGGQRK 290
Cdd:COG0396 74 RARAgifLA---FQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDfldryVNE---GFSGGEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 291 RLSIALELVNNPPVMFFDEPTSGLDsstcfqlISLLRSLARG-------GRTIVCTIHQPsaRLFE--KFDHLYLLAQGQ 361
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLD-------IDALRIVAEGvnklrspDRGILIITHYQ--RILDyiKPDFVHVLVDGR 218
|
250 260
....*....|....*....|.
gi 161076684 362 CVYEGRvKGLVPYLSSLGYEC 382
Cdd:COG0396 219 IVKSGG-KELALELEEEGYDW 238
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
145-337 |
1.01e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 112.88 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDshRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNlRRFRKLS 224
Cdd:COG1116 8 LELRGVSKRFPT--GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT-SGEVLVDGKPVT-GPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 225 cYIMQDDVLIANLTVREammvaaNLKLGKNMISYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNN 301
Cdd:COG1116 84 -VVFQEPALLPWLTVLD------NVALGLELRGVPKAERrerARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 161076684 302 PPVMFFDEPTSGLDSSTCFQLISLLRSL-ARGGRTIV 337
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVL 193
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
145-370 |
1.59e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 111.30 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHrrgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-RNLRRF--- 220
Cdd:COG2884 2 IRFENVSKRYPGGR-----EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT-SGQVLVNGQDlSRLKRReip 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 ---RKLScYIMQDDVLIANLTVRE----AMMVAanlklGKNMISYAKVVvvEEILETIGLKESVNTLTCNLSGGQRKRLS 293
Cdd:COG2884 76 ylrRRIG-VVFQDFRLLPDRTVYEnvalPLRVT-----GKSRKEIRRRV--REVLDLVGLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 294 IALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSarLFEKFDH-LYLLAQGQcVYEGRVKG 370
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE--LVDRMPKrVLELEDGR-LVRDEARG 222
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
165-341 |
2.10e-27 |
|
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: 109.82 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-----RNLRRFRKLSCYIMQ--DDVLIANL 237
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQ-SGAVLIDGEPldysrKGLLERRQRVGLVFQdpDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREAMMVAANLKLgknmiSYAKV-VVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:TIGR01166 86 VDQDVAFGPLNLGL-----SEAEVeRRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*
gi 161076684 317 STCFQLISLLRSLARGGRTIVCTIH 341
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTH 185
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
163-366 |
3.01e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 110.85 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN-----SKERNLRRFRKLSCYIMQDDVLIANL 237
Cdd:COG1126 14 LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPD-SGTITVDgedltDSKKDINKLRRKVGMVFQQFNLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREAMMVAanLKLGKNMiSYAKVV-VVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:COG1126 93 TVLENVTLA--PIKVKKM-SKAEAEeRAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 161076684 317 stcfQLI----SLLRSLARGGRTIVCTIHQPS-ARlfEKFDHLYLLAQGQCVYEG 366
Cdd:COG1126 170 ----ELVgevlDVMRDLAKEGMTMVVVTHEMGfAR--EVADRVVFMDGGRIVEEG 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
157-344 |
3.08e-27 |
|
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: 110.30 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK--------ERNLrrfrklsCYIM 228
Cdd:cd03259 7 SKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-SGEILIDGRdvtgvppeRRNI-------GMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 229 QDDVLIANLTVREAmmVAANLKLGKnmISYAKVV-VVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFF 307
Cdd:cd03259 79 QDYALFPHLTVAEN--IAFGLKLRG--VPKAEIRaRVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 161076684 308 DEPTSGLDSSTCFQLISLLRSL-ARGGRTIVCTIHQPS 344
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQE 192
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
154-412 |
3.61e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 116.54 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 154 VTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGY--KTAQLSGSVLINSKE----RNLRRFRKLScYI 227
Cdd:COG1123 10 LSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGRDllelSEALRGRRIG-MV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 228 MQD-DVLIANLTVREAMM-VAANLKLGKNMISYAkvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVM 305
Cdd:COG1123 89 FQDpMTQLNPVTVGDQIAeALENLGLSRAEARAR----VLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 306 FFDEPTSGLDSSTCFQLISLLRSLAR-GGRTIVCTIHQPsARLFEKFDHLYLLAQGQCVYEGRVKGL---------VPYL 375
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEIlaapqalaaVPRL 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 161076684 376 SSLGYECPSYHNPADYVLEVA--SGEYGDAVPKLVDAVK 412
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLEVRnlSKRYPVRGKGGVRAVD 282
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
145-367 |
6.10e-27 |
|
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: 110.01 E-value: 6.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDShrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINS---KERNLRRFR 221
Cdd:cd03253 1 IEFENVTFAYDPG-----RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-SGSILIDGqdiREVTLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 KLSCYIMQDDVLIaNLTVREammvaaNLKLGK------NMISYAKVVVVEEIL-------ETI----GLKesvntltcnL 284
Cdd:cd03253 75 RAIGVVPQDTVLF-NDTIGY------NIRYGRpdatdeEVIEAAKAAQIHDKImrfpdgyDTIvgerGLK---------L 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 285 SGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIHqpsaRLFE--KFDHLYLLAQGQC 362
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAH----RLSTivNADKIIVLKDGRI 213
|
....*
gi 161076684 363 VYEGR 367
Cdd:cd03253 214 VERGT 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
166-353 |
1.12e-26 |
|
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: 108.65 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLSCY------IMQDDVLIANLTV 239
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPT-SGTIRVNGQDVSDLRGRAIPYLrrkigvVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 240 REAMMVAANlklgknmISYAKVVV----VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:cd03292 96 YENVAFALE-------VTGVPPREirkrVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 161076684 316 SSTCFQLISLLRSLARGGRTIVCTIHqpSARLFEKFDH 353
Cdd:cd03292 169 PDTTWEIMNLLKKINKAGTTVVVATH--AKELVDTTRH 204
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
145-368 |
1.42e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.43 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYsvtdshRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINskERNLRRF--RK 222
Cdd:COG4559 2 LEAENLSV------RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS-SGEVRLN--GRPLAAWspWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 223 LSCY--IM-QDDVLIANLTVRE--AMMVAANLKLGKnmisyAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIA-- 295
Cdd:COG4559 73 LARRraVLpQHSSLAFPFTVEEvvALGRAPHGSSAA-----QDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArv 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 296 ----LELVNNPP-VMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPS-ARLFEkfDHLYLLAQGQCVYEGRV 368
Cdd:COG4559 148 laqlWEPVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNlAAQYA--DRILLLHQGRLVAQGTP 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
157-371 |
2.39e-26 |
|
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: 108.04 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG----YKTAQLSGSVLINSKErnlrrfrklscyIMQDDV 232
Cdd:cd03260 7 NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlIPGAPDEGEVLLDGKD------------IYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 233 LIANLTVREAMM----------VAANLKLGKNM--ISYAKVV--VVEEILETIGLKESVN--TLTCNLSGGQRKRLSIAL 296
Cdd:cd03260 75 DVLELRRRVGMVfqkpnpfpgsIYDNVAYGLRLhgIKLKEELdeRVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIH--QPSARLfekFDHLYLLAQGQCVYEGRVKGL 371
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHnmQQAARV---ADRTAFLLNGRLVEFGPTEQI 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
145-368 |
3.51e-26 |
|
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: 108.25 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYsvtdshRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSG-SVLINSKER---NLRRF 220
Cdd:COG1119 4 LELRNVTV------RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD-LPPTYGnDVRLFGERRggeDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYI---MQDDVLiANLTVREamMVA----ANLKLGKNmISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLS 293
Cdd:COG1119 77 RKRIGLVspaLQLRFP-RDETVLD--VVLsgffDSIGLYRE-PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 294 IALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR-GGRTIVCTIHQPSArLFEKFDHLYLLAQGQCVYEGRV 368
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAGPK 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
144-367 |
5.63e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.34 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSVTDShrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINS---KERNLRRF 220
Cdd:COG1132 339 EIEFENVSFSYPGD-----RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-SGRILIDGvdiRDLTLESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYIMQDDVLIaNLTVREammvaaNLKLGKNMISYAKVvvvEEILETIGLKESVNTL-----T------CNLSGGQR 289
Cdd:COG1132 413 RRQIGVVPQDTFLF-SGTIRE------NIRYGRPDATDEEV---EEAAKAAQAHEFIEALpdgydTvvgergVNLSGGQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 290 KRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVcTI-HQPSArlFEKFDHLYLLAQGQCVYEGR 367
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTI-VIaHRLST--IRNADRILVLDDGRIVEQGT 557
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
166-341 |
1.62e-25 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 105.53 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN--SKERNLRRFRKLSCYIMQDDVLIANLTVREAM 243
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT-SGRATVAghDVVREPREVRRRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 244 MVAANLKLGKNMISYAKVvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLI 323
Cdd:cd03265 95 YIHARLYGVPGAERRERI---DELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170
....*....|....*....
gi 161076684 324 SLLRSL-ARGGRTIVCTIH 341
Cdd:cd03265 172 EYIEKLkEEFGMTILLTTH 190
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
144-360 |
2.00e-25 |
|
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: 105.39 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSVtdshrRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLI---NSKERNLRRF 220
Cdd:cd03254 2 EIEFENVNFSY-----DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-KGQILIdgiDIRDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYIMQDDVLIANlTVREammvaaNLKLGKNmisYAKVVVVEEILETIGLKESVNTLT-----------CNLSGGQR 289
Cdd:cd03254 76 RSMIGVVLQDTFLFSG-TIME------NIRLGRP---NATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 290 KRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLaRGGRTIVCTIHQPS-------------ARLFEKFDHLYL 356
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLStiknadkilvlddGKIIEEGTHDEL 224
|
....
gi 161076684 357 LAQG 360
Cdd:cd03254 225 LAKK 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
145-369 |
3.07e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDShrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAqlSGSVLINSKE-----RNLR 218
Cdd:PRK13639 2 LETRDLKYSYPDG-----TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPT--SGEVLIKGEPikydkKSLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRKLSCYIMQ--DDVLIANlTVREAmmVA---ANLKLGKNMISYAkvvvVEEILETIGLKESVNTLTCNLSGGQRKRLS 293
Cdd:PRK13639 75 EVRKTVGIVFQnpDDQLFAP-TVEED--VAfgpLNLGLSKEEVEKR----VKEALKAVGMEGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 294 IALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQpsARLFEKF-DHLYLLAQGQCVYEGRVK 369
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEGTPK 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
161-366 |
3.44e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.48 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLSCYIM---QDDVLIANL 237
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ-SGTVFLGDKPISMLSSRQLARRLAllpQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREamMVAAN----LKL-GKnmISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTS 312
Cdd:PRK11231 92 TVRE--LVAYGrspwLSLwGR--LSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 313 GLDSSTCFQLISLLRSLARGGRTIVCTIH---QPSarlfEKFDHLYLLAQGQCVYEG 366
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQG 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
144-366 |
1.06e-24 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 110.34 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSVTDSHRrgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERN------L 217
Cdd:TIGR03375 463 EIEFRNVSFAYPGQET----PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPT-EGSVLLDGVDIRqidpadL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 218 RRFRKlscYIMQDDVLIANlTVREammvaaNLKLGKNMISYAKVVvveEILETIGLKESVNTLT-----------CNLSG 286
Cdd:TIGR03375 538 RRNIG---YVPQDPRLFYG-TLRD------NIALGAPYADDEEIL---RAAELAGVTEFVRRHPdgldmqigergRSLSG 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 287 GQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLArGGRTIVCTIHQPSarLFEKFDHLYLLAQGQCVYEG 366
Cdd:TIGR03375 605 GQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTS--LLDLVDRIIVMDNGRIVADG 681
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
166-337 |
1.44e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.18 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRK-----LSCyIMQDDVLIANLTVR 240
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD-SGEILLDGEPVRFRSPRDaqaagIAI-IHQELNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 EAMMVaANLKLGKNMISYAKVVV-VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTC 319
Cdd:COG1129 98 ENIFL-GREPRRGGLIDWRAMRRrARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREV 176
|
170
....*....|....*...
gi 161076684 320 FQLISLLRSLARGGRTIV 337
Cdd:COG1129 177 ERLFRIIRRLKAQGVAII 194
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
145-344 |
1.55e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 102.90 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDShrRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK------ERNLR 218
Cdd:COG4181 9 IELRGLTKTVGTG--AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPT-SGTVRLAGQdlfaldEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRKLSC-YIMQDDVLIANLTVREAMMVAANLKLGKNMISYAkvvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALE 297
Cdd:COG4181 86 RLRARHVgFVFQSFQLLPTLTALENVMLPLELAGRRDARARA-----RALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 161076684 298 LVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPS 344
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPA 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
176-361 |
2.03e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 102.25 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYKTAqLSGSVLINSKER-NLRRFRKLSCYIMQDDVLIANLTVREAMMVAANLKLGKN 254
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEP-ASGSIKVNDQSHtGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHPGLKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 255 MISYAKVvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLA-RGG 333
Cdd:TIGR01277 103 AEQQEKV---VDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCsERQ 179
|
170 180
....*....|....*....|....*...
gi 161076684 334 RTIVCTIHQPSaRLFEKFDHLYLLAQGQ 361
Cdd:TIGR01277 180 RTLLMVTHHLS-DARAIASQIAVVSQGK 206
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
135-366 |
2.32e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 108.37 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 135 SHLPQRPPVDIEFCDISYSVTDSHRrgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINskE 214
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYPDQPQ----PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ-QGEILLN--G 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 215 RNLRRF-----RKLSCYIMQDdVLIANLTVREammvaaNLKLGKNMISYAKVVvveEILETIGLK---ESVNTLTC---- 282
Cdd:PRK11160 402 QPIADYseaalRQAISVVSQR-VHLFSATLRD------NLLLAAPNASDEALI---EVLQQVGLEkllEDDKGLNAwlge 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 283 ---NLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIHqpsaRLF--EKFDHLYLL 357
Cdd:PRK11160 472 ggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH----RLTglEQFDRICVM 546
|
....*....
gi 161076684 358 AQGQCVYEG 366
Cdd:PRK11160 547 DNGQIIEQG 555
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
159-343 |
2.38e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.49 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAqLSGSVLINSKERNLRRFRKLSCYIMQDDVLIANLT 238
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREAMMVAANLkLGKNMISyakvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSST 318
Cdd:PRK13539 90 VAENLEFWAAF-LGGEELD------IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....*.
gi 161076684 319 CFQLISLLRS-LARGGrTIVCTIHQP 343
Cdd:PRK13539 163 VALFAELIRAhLAQGG-IVIAATHIP 187
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
164-343 |
8.21e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.62 E-value: 8.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 164 TILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKtAQLSGSVLINSKERnlrrfrklSCYIMQ----DDVLiaNLTV 239
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL-RPTSGTVRRAGGAR--------VAYVPQrsevPDSL--PLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 240 REAMMVAANLKLGK-NMISYAKVVVVEEILETIGL----KESVNTLtcnlSGGQRKRLSIALELVNNPPVMFFDEPTSGL 314
Cdd:NF040873 75 RDLVAMGRWARRGLwRRLTRDDRAAVDDALERVGLadlaGRQLGEL----SGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*....
gi 161076684 315 DSSTCFQLISLLRSLARGGRTIVCTIHQP 343
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
145-366 |
8.54e-24 |
|
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: 98.92 E-value: 8.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKErnlrrfrkls 224
Cdd:cd03247 1 LSINNVSFSYPEQE----QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ-QGEITLDGVP---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 225 cyimqddVLIANLTVREAMMVaanlklgknmISYAKVVVVEEILETIGLKesvntltcnLSGGQRKRLSIALELVNNPPV 304
Cdd:cd03247 66 -------VSDLEKALSSLISV----------LNQRPYLFDTTLRNNLGRR---------FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076684 305 MFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIHQPSArlFEKFDHLYLLAQGQCVYEG 366
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
145-366 |
1.50e-23 |
|
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: 100.31 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDshRRGFKtILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAqLSGSVLINS---KERNLRRFR 221
Cdd:cd03249 1 IEFKNVSFRYPS--RPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-TSGEILLDGvdiRDLNLRWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 KLSCYIMQDDVLIANlTVREammvaaNLKLGKNmisYAKVVVVEE------ILETI-GLKESVNTL----TCNLSGGQRK 290
Cdd:cd03249 77 SQIGLVSQEPVLFDG-TIAE------NIRYGKP---DATDEEVEEaakkanIHDFImSLPDGYDTLvgerGSQLSGGQKQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 291 RLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLrSLARGGRTIVCTIHQPSArlFEKFDHLYLLAQGQCVYEG 366
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQG 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
166-344 |
1.63e-23 |
|
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: 105.45 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSkeRNLRRF-----RKLSCYIMQDDVLIANltvr 240
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNG--VPLADAdadswRDQIAWVPQHPFLFAG---- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 eamMVAANLKLGKNmisYAKVVVVEEILETIGLKESVNTLTCN-----------LSGGQRKRLSIALELVNNPPVMFFDE 309
Cdd:TIGR02857 411 ---TIAENIRLARP---DASDAEIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190
....*....|....*....|....*....|....*
gi 161076684 310 PTSGLDSSTCFQLISLLRSLARgGRTIVCTIHQPS 344
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
145-342 |
2.43e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 102.08 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISysVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK------ERNLR 218
Cdd:COG1135 2 IELENLS--KTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPT-SGSVLVDGVdltalsERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRKLSCYIMQDDVLIANLTVREAmmVAANLKLGKnmisYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIA 295
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAEN--VALPLEIAG----VPKAEIrkrVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 161076684 296 LELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSL-ARGGRTIVCTIHQ 342
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHE 200
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
166-341 |
3.43e-23 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 100.93 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE--RNLRRFRKLSCYIMQDDVLIANLTVREAM 243
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPT-SGTARVAGYDvvREPRKVRRSIGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 244 MVAANLKLGKNMISYAKVvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLI 323
Cdd:TIGR01188 88 EMMGRLYGLPKDEAEERA---EELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIW 164
|
170
....*....|....*...
gi 161076684 324 SLLRSLARGGRTIVCTIH 341
Cdd:TIGR01188 165 DYIRALKEEGVTILLTTH 182
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
175-368 |
7.57e-23 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 97.37 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 175 NGEITAIMGPSGAGKSTLMNILAGYKTA-----QLSGSVLINS-KERNLR-RFRKLScYIMQDDVLIANLTVREammvaa 247
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPdggtiVLNGTVLFDSrKKINLPpQQRKIG-LVFQQYALFPHLNVRE------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 248 NLKLG-KNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLL 326
Cdd:cd03297 95 NLAFGlKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 161076684 327 RSLAR--GGRTIVCTiHQPSarlfekfdHLYLLAQGQCVYE-GRV 368
Cdd:cd03297 175 KQIKKnlNIPVIFVT-HDLS--------EAEYLADRIVVMEdGRL 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
165-371 |
8.48e-23 |
|
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: 98.13 E-value: 8.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-RNLRRFRKLS---CYIMQDDVLIANLTVR 240
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR-SGSIRFDGEDiTGLPPHRIARlgiGYVPEGRRIFPSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 EammvaaNLKLGknMISYAKVVVVEEILETIG-----LKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:COG0410 97 E------NLLLG--AYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076684 316 SSTCFQLISLLRSLARGGRTIVctihqpsarLFEKF--------DHLYLLAQGQCVYEGRVKGL 371
Cdd:COG0410 169 PLIVEEIFEIIRRLNREGVTIL---------LVEQNarfaleiaDRAYVLERGRIVLEGTAAEL 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
159-343 |
2.21e-22 |
|
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: 95.50 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAqLSGSVLINSKERNLRR--FRKLSCYIMQDDVLIAN 236
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGTPLAEQRdePHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREammvaaNLKLGKNMISYAKVVVvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:TIGR01189 88 LSALE------NLHFWAAIHGGAQRTI-EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*...
gi 161076684 317 STCFQLISLLRS-LARGGRTIVCTiHQP 343
Cdd:TIGR01189 161 AGVALLAGLLRAhLARGGIVLLTT-HQD 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
166-369 |
2.26e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.78 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNlRRFRKLSC-----YIMQDDVLIANLTVR 240
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT-KGTITINNINYN-KLDHKLAAqlgigIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 EAMMVAANLK---LGKNMISYAKV-VVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:PRK09700 99 ENLYIGRHLTkkvCGVNIIDWREMrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 161076684 317 STCFQLISLLRSLARGGRTIVCTIHQpSARLFEKFDHLYLLAQGQCVYEGRVK 369
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
141-372 |
3.13e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 98.75 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 141 PPVDIEFCDISYSVTDshrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSG--SVLINSKERNLR 218
Cdd:PRK13536 38 STVAIDLAGVSKSYGD------KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGM-TSPDAGkiTVLGVPVPARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRKLSCYIMQDDVLIANLTVREAMMVaanlkLGK--NMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIAL 296
Cdd:PRK13536 111 LARARIGVVPQFDNLDLEFTVRENLLV-----FGRyfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIH--QPSARLfekFDHLYLLAQGQCVYEGRVKGLV 372
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
165-369 |
4.73e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.14 E-value: 4.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG----YKTAQLSGSVLINSKE---RNLRRFRKLSCYIMQDDVLIANL 237
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGQDifkMDVIELRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREAmmVAANLKLGKNMISYAKVVV-VEEILETIGL----KESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTS 312
Cdd:PRK14247 98 SIFEN--VALGLKLNRLVKSKKELQErVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 313 GLDSSTCFQLISLLRSLARgGRTIVCTIHQP--SARLfekFDHLYLLAQGQCVYEGRVK 369
Cdd:PRK14247 176 NLDPENTAKIESLFLELKK-DMTIVLVTHFPqqAARI---SDYVAFLYKGQIVEWGPTR 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
145-372 |
4.76e-22 |
|
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: 95.76 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRrgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSkeRNLRRFrKLS 224
Cdd:cd03251 1 VEFKNVTFRYPGDGP----PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-SGRILIDG--HDVRDY-TLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 225 CY-----IMQDDVLIANLTVREammvaaNLKLGKNMISYAKVvvvEEILETIGLKESVNTLT-----------CNLSGGQ 288
Cdd:cd03251 73 SLrrqigLVSQDVFLFNDTVAE------NIAYGRPGATREEV---EEAARAANAHEFIMELPegydtvigergVKLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 289 RKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIHQPSArlFEKFDHLYLLAQGQCVYEGRV 368
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLST--IENADRIVVLEDGKIVERGTH 220
|
....
gi 161076684 369 KGLV 372
Cdd:cd03251 221 EELL 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
157-341 |
4.78e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 96.31 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE----RNLRRFRKLScyIM-QDD 231
Cdd:COG4604 8 SKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD-SGEVLVDGLDvattPSRELAKRLA--ILrQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 232 VLIANLTVREamMVAanlkLG-----KNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMF 306
Cdd:COG4604 85 HINSRLTVRE--LVA----FGrfpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 161076684 307 FDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIH 341
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
157-372 |
4.97e-22 |
|
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: 95.69 E-value: 4.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN----SKERNLRRFRKLSCYIMQDDV 232
Cdd:cd03218 7 SKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-SGKILLDgqdiTKLPMHKRARLGIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 233 LIANLTVREAMMVAANLKLGKNMISYAKVvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTS 312
Cdd:cd03218 86 IFRKLTVEENILAVLEIRGLSKKEREEKL---EELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076684 313 GLDSSTCFQLISLLRSLARGGRTIVCTIHqpSAR-LFEKFDHLYLLAQGQCVYEGRVKGLV 372
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDRGIGVLITDH--NVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
159-366 |
5.25e-22 |
|
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: 95.04 E-value: 5.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSKERNLRRFRKLScYIMQDDVLIANLT 238
Cdd:cd03269 9 RFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI-ILPDSGEVLFDGKPLDIAARNRIG-YLPEERGLYPKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREAMMVAANLK-LGKnmiSYAKvVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:cd03269 87 VIDQLVYLAQLKgLKK---EEAR-RRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 161076684 318 TCFQLISLLRSLARGGRTIVCTIHQpsARLFEKF-DHLYLLAQGQCVYEG 366
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTHQ--MELVEELcDRVLLLNKGRAVLYG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
145-361 |
7.23e-22 |
|
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: 93.43 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRrgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERN---LRRFR 221
Cdd:cd03246 1 LEVENVSFRYPGAEP----PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADISqwdPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 KLSCYIMQDDVLIANltvreammvaanlklgknmisyakvvvveEILETIglkesvntltcnLSGGQRKRLSIALELVNN 301
Cdd:cd03246 76 DHVGYLPQDDELFSG-----------------------------SIAENI------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 302 PPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSarLFEKFDHLYLLAQGQ 361
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGR 172
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
157-315 |
1.35e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 97.09 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK--------ERNLrrfrklsCYIM 228
Cdd:COG3842 12 SKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD-SGRILLDGRdvtglppeKRNV-------GMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 229 QDDVLIANLTVREAmmVAANLKLGKnmisYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVM 305
Cdd:COG3842 84 QDYALFPHLTVAEN--VAFGLRMRG----VPKAEIrarVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170
....*....|
gi 161076684 306 FFDEPTSGLD 315
Cdd:COG3842 158 LLDEPLSALD 167
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
166-366 |
1.43e-21 |
|
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: 93.97 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE--RNLRRFRKLSCYIMQDDVLIANLTVREAM 243
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGFDvvKEPAEARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 244 MVAANLKLGKNMISYAKVvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLI 323
Cdd:cd03266 100 EYFAGLYGLKGDELTARL---EELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 161076684 324 SLLRSLARGGRTIVCTIH--QPSARLfekFDHLYLLAQGQCVYEG 366
Cdd:cd03266 177 EFIRQLRALGKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
176-315 |
1.59e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLR--RFRKLScYIMQDDVLIANLTVREammvaaNLKLGK 253
Cdd:PRK10771 25 GERVAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGQDHTTTppSRRPVS-MLFQENNLFSHLTVAQ------NIGLGL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076684 254 N---MISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:PRK10771 97 NpglKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
157-315 |
2.11e-21 |
|
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: 93.84 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-RNLRRFRKLSCYIMQDDVLIA 235
Cdd:cd03300 7 SKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-SGEILLDGKDiTNLPPHKRPVNTVFQNYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAmmVAANL---KLGKNMISYAkvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTS 312
Cdd:cd03300 86 HLTVFEN--IAFGLrlkKLPKAEIKER----VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
...
gi 161076684 313 GLD 315
Cdd:cd03300 160 ALD 162
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
166-341 |
2.14e-21 |
|
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: 93.94 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-RNLRRFRKLSCYIMQDDVLIANLTVREamm 244
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-SGKILLNGKDiTNLPPEKRDISYVPQNYALFPHMTVYK--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 245 vaaNLKLGKNMISYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQ 321
Cdd:cd03299 91 ---NIAYGLKKRKVDKKEIerkVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180
....*....|....*....|
gi 161076684 322 LISLLRSLARGGRTIVctIH 341
Cdd:cd03299 168 LREELKKIRKEFGVTV--LH 185
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
165-372 |
2.58e-21 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 99.43 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQLsGSVLINSKE------RNLRRfrKLSCyIMQDDVLIaNLT 238
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQH-GQVLVDGVDlaiadpAWLRR--QMGV-VLQENVLF-SRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREammvaaNLKLGKNMISYAKVVVVEEI---LETI-GLKESVNTLT----CNLSGGQRKRLSIALELVNNPPVMFFDEP 310
Cdd:TIGR01846 547 IRD------NIALCNPGAPFEHVIHAAKLagaHDFIsELPQGYNTEVgekgANLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076684 311 TSGLDSSTCFQLISLLRSLARgGRTIVCTIHQPSArlFEKFDHLYLLAQGQCVYEGRVKGLV 372
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR-GRTVIIIAHRLST--VRACDRIIVLEKGQIAESGRHEELL 679
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
145-342 |
4.89e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.85 E-value: 4.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISysvtdsHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLM---NILAGYKTAQL-SGSVLINSKERNLRRF 220
Cdd:PRK09493 2 IEFKNVS------KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEEITSGDLiVDGLKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYIMQDDVLIANLTVREammvaaNLKLG----KNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIAL 296
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALE------NVMFGplrvRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQ 342
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
163-371 |
5.18e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.28 E-value: 5.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTL---MNILAGYKTAQ-------LSGSVLINSKERNLRRFRKLSCYIMQDDV 232
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQPEAGTirvgditIDTARSLSQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 233 LIANLTVREammvaaNLKLG----KNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFD 308
Cdd:PRK11264 96 LFPHRTVLE------NIIEGpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076684 309 EPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPS-ARlfEKFDHLYLLAQGQCVYEGRVKGL 371
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSfAR--DVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
165-372 |
5.38e-21 |
|
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: 92.93 E-value: 5.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKER---NLRRFRKLSCYIMQDDVLIaNLTVRE 241
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDGHDLalaDPAWLRRQVGVVLQENVLF-NRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 242 ammvaaNLKLGKNMISYAKVVVV-------EEILEtigLKESVNTLT----CNLSGGQRKRLSIALELVNNPPVMFFDEP 310
Cdd:cd03252 95 ------NIALADPGMSMERVIEAaklagahDFISE---LPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076684 311 TSGLDSSTCFQLISLLRSLArGGRTIVCTIHQPSArlFEKFDHLYLLAQGQCVYEGRVKGLV 372
Cdd:cd03252 166 TSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLST--VKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
159-341 |
5.61e-21 |
|
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: 91.93 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINS--------KERNLrrfrklsCYIMQD 230
Cdd:cd03301 9 RFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-SGRIYIGGrdvtdlppKDRDI-------AMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 231 DVLIANLTVREAMmvAANLKLGKnmisYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFF 307
Cdd:cd03301 81 YALYPHMTVYDNI--AFGLKLRK----VPKDEIderVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190
....*....|....*....|....*....|....*
gi 161076684 308 DEPTSGLDSSTCFQLISLLRSL-ARGGRTIVCTIH 341
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTH 189
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
157-337 |
5.77e-21 |
|
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: 90.57 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKErnlrrfrklscyimqddvlIAN 236
Cdd:cd03216 7 TKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-SGEILVDGKE-------------------VSF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAmmvaanLKLGKNMISyakvvvveeiletiglkesvntltcNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:cd03216 67 ASPRDA------RRAGIAMVY-------------------------QLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180
....*....|....*....|.
gi 161076684 317 STCFQLISLLRSLARGGRTIV 337
Cdd:cd03216 116 AEVERLFKVIRRLRAQGVAVI 136
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
163-366 |
6.09e-21 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 93.67 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG--YKTaqlSGSVLIN------SKERNLRRFRKLSCYIMQ--DDV 232
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGllKPT---SGTVTIDgrditaKKKKKLKDLRKKVGLVFQfpEHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 233 LIANlTVREAMMVA-ANLKLGKNMISYAkvvvVEEILETIGLKESVNTLTC-NLSGGQRKRLSIALELVNNPPVMFFDEP 310
Cdd:TIGR04521 95 LFEE-TVYKDIAFGpKNLGLSEEEAEER----VKEALELVGLDEEYLERSPfELSGGQMRRVAIAGVLAMEPEVLILDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 311 TSGLDSSTCFQLISLLRSLAR-GGRTIVCTIHQPS--ARLfekFDHLYLLAQGQCVYEG 366
Cdd:TIGR04521 170 TAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSMEdvAEY---ADRVIVMHKGKIVLDG 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
145-366 |
8.39e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.91 E-value: 8.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYsvtdshRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINskERNLRRF--RK 222
Cdd:PRK13548 3 LEARNLSV------RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLN--GRPLADWspAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 223 LSCY--IM-QDDVLIANLTVRE--AMMVAANLKLGKnmisyAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALE 297
Cdd:PRK13548 74 LARRraVLpQHSSLSFPFTVEEvvAMGRAPHGLSRA-----EDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 298 LV------NNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR-GGRTIVCTIHQPS-ARLFEkfDHLYLLAQGQCVYEG 366
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHeRGLAVIVVLHDLNlAARYA--DRIVLLHQGRLVADG 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
177-395 |
1.43e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 94.02 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 177 EITAIMGPSGAGKSTLMNILAGYKTAQ-----LSGSVLINSKER-----NLRRFRklscYIMQDDVLIANLTVREammva 246
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGLTRPDegeivLNGRTLFDSRKGiflppEKRRIG----YVFQEARLFPHLSVRG----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 247 aNLKLG--KNMISYaKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLIS 324
Cdd:TIGR02142 95 -NLRYGmkRARPSE-RRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 325 LLRSLARGGRT-IVCTIHQPS--ARLfekFDHLYLLAQGQCVYEGRV-----KGLVPYLSslgyecpsyHNPADYVLEV 395
Cdd:TIGR02142 173 YLERLHAEFGIpILYVSHSLQevLRL---ADRVVVLEDGRVAAAGPIaevwaSPDLPWLA---------REDQGSLIEG 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
145-342 |
1.52e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 93.71 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDIS--YSVtdshRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTL---MNILagykTAQLSGSVLINS------K 213
Cdd:PRK11153 2 IELKNISkvFPQ----GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLircINLL----ERPTSGRVLVDGqdltalS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 214 ERNLRRFRKLSCYIMQDDVLIANLTVREAmmVAANLKLG---KNMISyAKVvvvEEILETIGLKESVNTLTCNLSGGQRK 290
Cdd:PRK11153 74 EKELRKARRQIGMIFQHFNLLSSRTVFDN--VALPLELAgtpKAEIK-ARV---TELLELVGLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 161076684 291 RLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQ 342
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHE 200
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
159-315 |
1.98e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.23 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTA--QLSGSVLINSKERN-----LRRFRklscYIMQDD 231
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafSASGEVLLNGRRLTalpaeQRRIG----ILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 232 VLIANLTVREAMMVAANLKLGKNmisyAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPT 311
Cdd:COG4136 86 LLFPHLSVGENLAFALPPTIGRA----QRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
....
gi 161076684 312 SGLD 315
Cdd:COG4136 162 SKLD 165
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
145-380 |
2.04e-20 |
|
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: 91.17 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDshrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQL-SGSVLInsKERNL------ 217
Cdd:TIGR01978 1 LKIKDLHVSVED------KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVtSGTILF--KGQDLlelepd 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 218 RRFRK---LScyiMQDDVLIANLTVREAMMVAANLKLGKN------MISYAKvvVVEEILETIGLKE-----SVNTltcN 283
Cdd:TIGR01978 73 ERARAglfLA---FQYPEEIPGVSNLEFLRSALNARRSARgeepldLLDFEK--LLKEKLALLDMDEeflnrSVNE---G 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 284 LSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSST---CFQLISLLRSLARGgrTIVCTIHQpsaRLFE--KFDHLYLLA 358
Cdd:TIGR01978 145 FSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDAlkiVAEGINRLREPDRS--FLIITHYQ---RLLNyiKPDYVHVLL 219
|
250 260
....*....|....*....|..
gi 161076684 359 QGQCVYEGRVKgLVPYLSSLGY 380
Cdd:TIGR01978 220 DGRIVKSGDVE-LAKELEAKGY 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
153-366 |
3.17e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.18 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRR-GFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILaGYKTAQLSGSVLINSKE----------------R 215
Cdd:PRK10619 7 NVIDLHKRyGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGQTinlvrdkdgqlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 216 NLRRFRKLSCYIMQDDVLIANLTVREAMMVAANLKLGKNMISYAKVVVveEILETIGLKESVN-TLTCNLSGGQRKRLSI 294
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAV--KYLAKVGIDERAQgKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076684 295 ALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPS-ARLFEkfDHLYLLAQGQCVYEG 366
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGfARHVS--SHVIFLHQGKIEEEG 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
166-337 |
3.29e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.09 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRK-LSCYI-M--QDDVLIANLTVRE 241
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPD-SGEILIDGKPVRIRSPRDaIALGIgMvhQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 242 ammvaaNLKLG-----KNMISYAKVV-VVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGL- 314
Cdd:COG3845 100 ------NIVLGleptkGGRLDRKAARaRIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLt 173
|
170 180
....*....|....*....|....*..
gi 161076684 315 ----DsstcfQLISLLRSLARGGRTIV 337
Cdd:COG3845 174 pqeaD-----ELFEILRRLAAEGKSII 195
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
164-371 |
3.91e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 90.28 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 164 TILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLIN----SKERNLRRFRKLSCYIMQDDVLIANLTV 239
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGL-LPVKSGSIRLDgediTKLPPHERARAGIAYVPQGREIFPRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 240 REammvaaNLKLGKNMISYAKVVVVEEILETIG-LKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSST 318
Cdd:TIGR03410 93 EE------NLLTGLAALPRRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076684 319 CFQL---ISLLRslARGGRTIVctihqpsarLFEKF--------DHLYLLAQGQCVYEGRVKGL 371
Cdd:TIGR03410 167 IKDIgrvIRRLR--AEGGMAIL---------LVEQYldfarelaDRYYVMERGRVVASGAGDEL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
165-331 |
3.99e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.26 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVL--------INSKERNLRRFRKLScYIMQDDVLIAN 236
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT-SGDVIfngqpmskLSSAAKAELRNQKLG-FIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAmmVAANLKLGKNMISYAKVVVVEeILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:PRK11629 102 FTALEN--VAMPLLIGKKKPAEINSRALE-MLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170
....*....|....*
gi 161076684 317 STCFQLISLLRSLAR 331
Cdd:PRK11629 179 RNADSIFQLLGELNR 193
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
145-369 |
4.00e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.40 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDShrrgfKTILKSVSgkF---RNGEItAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK---ERNLR 218
Cdd:PRK13652 4 IETRDLCYSYSGS-----KEALNNIN--FiapRNSRI-AVIGPNGAGKSTLFRHFNGILKPT-SGSVLIRGEpitKENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRKLSCYIMQ--DDVLIANLTVREAMMVAANLKLGKNMISYAkvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIAL 296
Cdd:PRK13652 75 EVRKFVGLVFQnpDDQIFSPTVEQDIAFGPINLGLDEETVAHR----VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLA-RGGRTIVCTIHQPSArLFEKFDHLYLLAQGQCVYEGRVK 369
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPeTYGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTVE 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
118-366 |
6.32e-20 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 95.02 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 118 NNSGGSPNGQKKGTIALSHlpqrppvdiefcdisysVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILA 197
Cdd:TIGR03797 438 VDEAKTDPGKLSGAIEVDR-----------------VTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLL 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 198 GYKTAQlSGSVLINSKE---RNLRRFRKLSCYIMQDDVLI-----------ANLTVREAMMVAanlklgkNMISYAkvvv 263
Cdd:TIGR03797 501 GFETPE-SGSVFYDGQDlagLDVQAVRRQLGVVLQNGRLMsgsifeniaggAPLTLDEAWEAA-------RMAGLA---- 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 264 vEEI------LETIgLKESVNtltcNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTcfQLIsLLRSLARGGRTIV 337
Cdd:TIGR03797 569 -EDIrampmgMHTV-ISEGGG----TLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT--QAI-VSESLERLKVTRI 639
|
250 260
....*....|....*....|....*....
gi 161076684 338 CTIHQPSArlFEKFDHLYLLAQGQCVYEG 366
Cdd:TIGR03797 640 VIAHRLST--IRNADRIYVLDAGRVVQQG 666
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
165-343 |
7.86e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.41 E-value: 7.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNIL-------AG-YKTAQLSGSVLINSKERNLRR--FRklscYIMQDDVLI 234
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGtYRVAGQDVATLDADALAQLRRehFG----FIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 235 ANLTVREAMMVAANLK-LGKNmisyAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSG 313
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAgLERK----QRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190
....*....|....*....|....*....|
gi 161076684 314 LDSSTCFQLISLLRSLARGGRTIVCTIHQP 343
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
143-343 |
8.86e-20 |
|
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: 93.96 E-value: 8.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 143 VDIEFCDISYSVTDSHRrgfktILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINS---KERNLRR 219
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPP-----VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL-LDPLQGEVTLDGvpvSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 220 FRKLSCYIMQDDVLIANlTVREAMMVAANLKLGKNMISYAKVVVVEEILETI--GLKESVNTLTCNLSGGQRKRLSIALE 297
Cdd:TIGR02868 407 VRRRVSVCAQDAHLFDT-TVRENLRLARPDATDEELWAALERVGLADWLRALpdGLDTVLGEGGARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 161076684 298 LVNNPPVMFFDEPTSGLDSSTCFQLISLLRSlARGGRTIVCTIHQP 343
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
159-372 |
1.00e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.63 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLI--NSKERNLRRFRKLSCYIMQDDVLIAN 236
Cdd:PRK13537 16 RYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL-THPDAGSISLcgEPVPSRARHARQRVGVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAMMVaanlkLGK--NMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGL 314
Cdd:PRK13537 95 FTVRENLLV-----FGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 315 DSSTCFQLISLLRSLARGGRTIVCTIH--QPSARLfekFDHLYLLAQGQCVYEGRVKGLV 372
Cdd:PRK13537 170 DPQARHLMWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
166-361 |
1.18e-19 |
|
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: 88.94 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLSC-YIMQDDVLIANLTVREAmm 244
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD-SGTILFGGEDATDVPVQERNVgFVFQHYALFRHMTVFDN-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 245 VAANLKLGKNMISYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQ 321
Cdd:cd03296 95 VAFGLRVKPRSERPPEAEIrakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 161076684 322 LISLLRSLA-RGGRTIVCTIHQPSARLfEKFDHLYLLAQGQ 361
Cdd:cd03296 175 LRRWLRRLHdELHVTTVFVTHDQEEAL-EVADRVVVMNKGR 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
145-367 |
1.29e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 89.66 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDShrrgFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE---RNLRRFR 221
Cdd:PRK13632 8 IKVENVSFSYPNS----ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ-SGEIKIDGITiskENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 KLSCYIMQ--DDVLIAnLTVR-------EAMMVAANlKLGKNMISYAKVVVVEEILEtiglKESVNtltcnLSGGQRKRL 292
Cdd:PRK13632 83 KKIGIIFQnpDNQFIG-ATVEddiafglENKKVPPK-KMKDIIDDLAKKVGMEDYLD----KEPQN-----LSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 293 SIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR-GGRTIVCTIHQPSARLfeKFDHLYLLAQGQCVYEGR 367
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtRKKTLISITHDMDEAI--LADKVIVFSEGKLIAQGK 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
160-343 |
1.86e-19 |
|
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: 87.16 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 160 RGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSKERNLRR--FRKLSCYIMQDDVLIANL 237
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGL-SPPLAGRVLLNGGPLDFQRdsIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREammvaaNLKLGKNMISYAKVvvvEEILETIGLKeSVNTLTCN-LSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:cd03231 89 SVLE------NLRFWHADHSDEQV---EEALARVGLN-GFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180
....*....|....*....|....*..
gi 161076684 317 STCFQLISLLRSLARGGRTIVCTIHQP 343
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
173-366 |
2.37e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 93.92 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 173 FRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSK--ERNLRRFRKLSCYIMQDDVLIANLTVREAMMVAANLK 250
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGL-LPPTSGTVLVGGKdiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 251 lGKnmiSYAKVVV-VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSL 329
Cdd:TIGR01257 1032 -GR---SWEEAQLeMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170 180 190
....*....|....*....|....*....|....*...
gi 161076684 330 aRGGRTIV-CTIHQPSARLFEkfDHLYLLAQGQCVYEG 366
Cdd:TIGR01257 1108 -RSGRTIImSTHHMDEADLLG--DRIAIISQGRLYCSG 1142
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
157-315 |
4.13e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 89.75 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyktaqL----SGSVLIN--------SKERNLRrfrkls 224
Cdd:COG3839 10 SKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG-----LedptSGEILIGgrdvtdlpPKDRNIA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 225 cyiM--QDDVLIANLTVREAMmvAANLKLGKnmisYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELV 299
Cdd:COG3839 79 ---MvfQSYALYPHMTVYENI--AFPLKLRK----VPKAEIdrrVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170
....*....|....*.
gi 161076684 300 NNPPVMFFDEPTSGLD 315
Cdd:COG3839 150 REPKVFLLDEPLSNLD 165
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
141-367 |
9.08e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.52 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 141 PPVDIEFCDISysvtdshrRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRF 220
Cdd:PRK09536 2 PMIDVSDLSVE--------FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYIM---QDDVLIANLTVREAMMVAANLKLGK-NMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIAL 296
Cdd:PRK09536 73 RAASRRVAsvpQDTSLSFEFDVRQVVEMGRTPHRSRfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIH--QPSARLfekFDHLYLLAQGQCVYEGR 367
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHdlDLAARY---CDELVLLADGRVRAAGP 222
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
144-374 |
1.36e-18 |
|
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: 90.57 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSVtdshrrGF-KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-RNLRR-- 219
Cdd:TIGR01193 473 DIVINDVSYSY------GYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGFSlKDIDRht 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 220 FRKLSCYIMQDDVLIANlTVREAMMVAANLKLGKNMISyaKVVVVEEILETI-----GLKESVNTLTCNLSGGQRKRLSI 294
Cdd:TIGR01193 546 LRQFINYLPQEPYIFSG-SILENLLLGAKENVSQDEIW--AACEIAEIKDDIenmplGYQTELSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 295 ALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARggRTIVCTIHQPSarLFEKFDHLYLLAQGQCVYEGRVKGLVPY 374
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
166-369 |
1.63e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.66 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlsGSVLINSKE------RNLRRFRklsCYIMQDDVLIANLTV 239
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ--GEILLNGRPlsdwsaAELARHR---AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 240 RE--AMMVAANLKlgknmiSYAKVVVVEEILETIGLKESVNTLTCNLSGG--QRKRLSIALELV---NNPP--VMFFDEP 310
Cdd:COG4138 87 FQylALHQPAGAS------SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGewQRVRLAAVLLQVwptINPEgqLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076684 311 TSGLDSSTCFQLISLLRSLARGGRTIVCTIH--QPSARlfeKFDHLYLLAQGQCVYEGRVK 369
Cdd:COG4138 161 MNSLDVAQQAALDRLLRELCQQGITVVMSSHdlNHTLR---HADRVWLLKQGKLVASGETA 218
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
153-366 |
1.81e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 86.01 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRR-GFKTILKSVSGKFRNGEITAIMGPSGAGKSTL---MNILagyKTAQlSGSVLINSKE-------------- 214
Cdd:COG4598 10 EVRDLHKSfGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFlrcINLL---ETPD-SGEIRVGGEEirlkpdrdgelvpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 215 --RNLRRFR-KLScYIMQDDVLIANLTVREAMMVAAN--LKLGKN-MISYAkvvvvEEILETIGLKESVNTLTCNLSGGQ 288
Cdd:COG4598 86 drRQLQRIRtRLG-MVFQSFNLWSHMTVLENVIEAPVhvLGRPKAeAIERA-----EALLAKVGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 289 RKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPS-ARlfEKFDHLYLLAQGQCVYEG 366
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGfAR--DVSSHVVFLHQGRIEEQG 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
153-366 |
2.89e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 84.69 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRRGFKTI--LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSV----LINSKERNlRRFRKLSCY 226
Cdd:cd03267 22 SLKSLFKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT-SGEVrvagLVPWKRRK-KFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 227 IMQDDVLIANLTVREAmmvaanLKLGKNM--ISYAKVVV-VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPP 303
Cdd:cd03267 100 FGQKTQLWWDLPVIDS------FYLLAAIydLPPARFKKrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 304 VMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIH--QPSARLFEKfdhLYLLAQGQCVYEG 366
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHymKDIEALARR---VLVIDKGRLLYDG 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
157-343 |
3.55e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAQLSGSVLINSKErnlrrfrklscyIMQDDVLIA 235
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGaLKGTPVAGCVDVPDNQ------------FGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAMMVAAnlklgknmisyakvvvveEILETIGLKESVNTLTC--NLSGGQRKRLSIALELVNNPPVMFFDEPTSG 313
Cdd:COG2401 105 AIGRKGDFKDAV------------------ELLNAVGLSDAVLWLRRfkELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|.
gi 161076684 314 LDSSTCFQLISLLRSLAR-GGRTIVCTIHQP 343
Cdd:COG2401 167 LDRQTAKRVARNLQKLARrAGITLVVATHHY 197
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
163-366 |
3.67e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.56 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSKERNL----RRFRKLSCYIMQDDVLIANLT 238
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGI-VPRDAGNIIIDDEDISLlplhARARRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREAMMvaANLKLGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSST 318
Cdd:PRK10895 95 VYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 161076684 319 CFQLISLLRSLARGGRTIVCTIHQPSARLfEKFDHLYLLAQGQCVYEG 366
Cdd:PRK10895 173 VIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHG 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
165-342 |
3.72e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLI---------NSKERNLRRFRKLSCYIMQDDVLIA 235
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPD-SGQLNIaghqfdfsqKPSEKAIRLLRQKVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAMmVAANLKLGKnMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:COG4161 96 HLTVMENL-IEAPCKVLG-LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180
....*....|....*....|....*..
gi 161076684 316 SSTCFQLISLLRSLARGGRTIVCTIHQ 342
Cdd:COG4161 174 PEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
166-369 |
4.36e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSK-----ERNLRRFRKLSCYIMQ--DDVLIANLT 238
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGI-LKPSSGRILFDGKpidysRKGLMKLRESVGMVFQdpDNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREAMMVAANLKLGKNMISYAkvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSST 318
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKR----VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 161076684 319 CFQLISLLRSLARG-GRTIVCTIHQ-PSARLFekFDHLYLLAQGQCVYEGRVK 369
Cdd:PRK13636 177 VSEIMKLLVEMQKElGLTIIIATHDiDIVPLY--CDNVFVMKEGRVILQGNPK 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
176-342 |
4.76e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.30 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLI---------NSKERNLRRFRKLSCYIMQDDVLIANLTVREAMMVA 246
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPR-SGTLNIagnhfdfskTPSDKAIRELRRNVGMVFQQYNLWPHLTVQQNLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 247 AN--LKLGKN-MISYAKvvvveEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLI 323
Cdd:PRK11124 107 PCrvLGLSKDqALARAE-----KLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIV 181
|
170
....*....|....*....
gi 161076684 324 SLLRSLARGGRTIVCTIHQ 342
Cdd:PRK11124 182 SIIRELAETGITQVIVTHE 200
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
166-341 |
4.80e-18 |
|
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: 85.00 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAqlSGSVLINSKE---------RNLRRfRKLScYIMQDDVLIA 235
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRlIEPT--SGKVLIDGQDiaamsrkelRELRR-KKIS-MVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAmmVAANLKLgKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:cd03294 116 HRTVLEN--VAFGLEV-QGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190
....*....|....*....|....*....|..
gi 161076684 316 SstcfqLI------SLLRSLARGGRTIVCTIH 341
Cdd:cd03294 193 P-----LIrremqdELLRLQAELQKTIVFITH 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
130-361 |
5.93e-18 |
|
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: 83.67 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 130 GTIALSHLPQRppvdIEFCDISYSVTdshRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVL 209
Cdd:cd03248 1 GSLAPDHLKGI----VKFQNVTFAYP---TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-GGQVL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 210 INSKERNLRRfrklSCYIMQDDVLIANLTVREAMMVAANLKLGKNMISYAKVVVVEE-------ILE-TIGLKESVNTLT 281
Cdd:cd03248 73 LDGKPISQYE----HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQkahahsfISElASGYDTEVGEKG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 282 CNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIHQPSarLFEKFDHLYLLAQGQ 361
Cdd:cd03248 149 SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLS--TVERADQILVLDGGR 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
157-315 |
6.70e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERnlrrfrkLScYIMQDDVLIAN 236
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD-SGEVSIPKGLR-------IG-YLPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAMM-------------VAANLKLG---KNMISYAKVVV-------------VEEILETIGLKESV-NTLTCNLSG 286
Cdd:COG0488 76 LTVLDTVLdgdaelraleaelEELEAKLAepdEDLERLAELQEefealggweaearAEEILSGLGFPEEDlDRPVSELSG 155
|
170 180
....*....|....*....|....*....
gi 161076684 287 GQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
166-366 |
7.75e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.29 E-value: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGY----KTAQLSGSVLINSKE------RNLRRFRKLSCYIMQDDVLIA 235
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQregrlaRDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAMMVAA--NLKLGKNMISYAKVVVVEEILET---IGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEP 310
Cdd:PRK09984 100 RLSVLENVLIGAlgSTPFWRTCFSWFTREQKQRALQAltrVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 311 TSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPSARLfEKFDHLYLLAQGQCVYEG 366
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
176-341 |
9.03e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 82.98 E-value: 9.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSKERnlRRFRKLSCYIMQDDVLIAN--LTVREAMMVAANLKLGK 253
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGL-IPPAKGTVKVAGASP--GKGWRHIGYVPQRHEFAWDfpISVAHTVMSGRTGHIGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 254 -NMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG 332
Cdd:TIGR03771 83 lRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELAGA 162
|
....*....
gi 161076684 333 GRTIVCTIH 341
Cdd:TIGR03771 163 GTAILMTTH 171
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
124-371 |
9.24e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 9.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 124 PNGQKKGTIALSHLPQRppvdIEFCDISYSVTdshRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQ 203
Cdd:TIGR00958 462 PNIPLTGTLAPLNLEGL----IEFQDVSFSYP---NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 204 lSGSVLINSK---ERNLRRFRKLSCYIMQDDVLIANlTVREAMMVAANLKLGKNMISYAKVVVVEE-ILE-TIGLKESVN 278
Cdd:TIGR00958 535 -GGQVLLDGVplvQYDHHYLHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDfIMEfPNGYDTEVG 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 279 TLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSStCFQLISLLRSlaRGGRTIVCTIHQPSarLFEKFDHLYLLA 358
Cdd:TIGR00958 613 EKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE-CEQLLQESRS--RASRTVLLIAHRLS--TVERADQILVLK 687
|
250
....*....|...
gi 161076684 359 QGQCVYEGRVKGL 371
Cdd:TIGR00958 688 KGSVVEMGTHKQL 700
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
145-361 |
1.05e-17 |
|
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: 82.13 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRRGFKTiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyKTAQLSGSVLINSKErnlrrfrkls 224
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFT-LKDINLEVPKGELVAIVGPVGSGKSSLLSALLG-ELEKLSGSVSVPGSI---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 225 CYIMQDDVLIaNLTVREammvaaNLKLGKNMIS--YAKVV----------VVEEILET-IGLKESvntltcNLSGGQRKR 291
Cdd:cd03250 69 AYVSQEPWIQ-NGTIRE------NILFGKPFDEerYEKVIkacalepdleILPDGDLTeIGEKGI------NLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076684 292 LSIALELVNNPPVMFFDEPTSGLDSSTCFQLI-SLLRSLARGGRTIVCTIHQPSarLFEKFDHLYLLAQGQ 361
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQ--LLPHADQIVVLDNGR 204
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
137-366 |
1.19e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.68 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 137 LPQRPPVDIEFCDISYSVTDshrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK--- 213
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPG------RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-EGEILLDAQple 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 214 ERNLRRFRKLSCYIMQDDVLIANLTVREAMMVAA---NLKLGKnmISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRK 290
Cdd:PRK10575 77 SWSSKAFARKVAYLPQQLPAAEGMTVRELVAIGRypwHGALGR--FGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 291 RLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIH--QPSARLfekFDHLYLLAQGQCVYEG 366
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHdiNMAARY---CDYLVALRGGEMIAQG 230
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
144-341 |
1.31e-17 |
|
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: 82.54 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDisysVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILagYKTAQLS-GSVLINSKERN---LRR 219
Cdd:cd03244 2 DIEFKN----VSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLAL--FRLVELSsGSILIDGVDISkigLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 220 FRKLSCYIMQDDVLIANlTVREammvaaNLK-LGKnmisYAKvvvvEEI---LETIGLKESVNTL-----------TCNL 284
Cdd:cd03244 76 LRSRISIIPQDPVLFSG-TIRS------NLDpFGE----YSD----EELwqaLERVGLKEFVESLpggldtvveegGENL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 285 SGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSlARGGRTIVCTIH 341
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAH 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
145-366 |
1.49e-17 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 82.73 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSvtdshRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLM---NILagykTAQLSGSVLINSK---ERNLR 218
Cdd:cd03295 1 IEFENVTKR-----YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMkmiNRL----IEPTSGEIFIDGEdirEQDPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RFRKLSCYIMQDDVLIANLTVREAM-MVAANLKLGKNMISYAkvvvVEEILETIGL--KESVNTLTCNLSGGQRKRLSIA 295
Cdd:cd03295 72 ELRRKIGYVIQQIGLFPHMTVEENIaLVPKLLKWPKEKIRER----ADELLALVGLdpAEFADRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076684 296 LELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQpsarLFEKF---DHLYLLAQGQCVYEG 366
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHD----IDEAFrlaDRIAIMKNGEIVQVG 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
159-331 |
1.82e-17 |
|
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: 84.33 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGY--KTAQLSGSVLINSK------ERNLRRFR--KLScYIM 228
Cdd:COG0444 14 RRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpPPGITSGEILFDGEdllklsEKELRKIRgrEIQ-MIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 229 QD--DVLiaN--LTVREAMM--VAANLKLGKNMIsYAKVVvveEILETIGLKESVNTLTC---NLSGGQRKRLSIALELV 299
Cdd:COG0444 93 QDpmTSL--NpvMTVGDQIAepLRIHGGLSKAEA-RERAI---ELLERVGLPDPERRLDRyphELSGGMRQRVMIARALA 166
|
170 180 190
....*....|....*....|....*....|..
gi 161076684 300 NNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR 331
Cdd:COG0444 167 LEPKLLIADEPTTALDVTIQAQILNLLKDLQR 198
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
164-337 |
1.87e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 84.81 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 164 TILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINskernlrrfrklscyimqDDVLIANLTVRE-- 241
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPD-SGRIVLN------------------GRDLFTNLPPRErr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 242 --------A----MMVAAN-------LKLGKNMISyAKvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNP 302
Cdd:COG1118 77 vgfvfqhyAlfphMTVAENiafglrvRPPSKAEIR-AR---VEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 161076684 303 PVMFFDEPTSGLDSSTCFQLISLLRSL-ARGGRTIV 337
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTV 188
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
164-343 |
1.97e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.13 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 164 TILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTA-----QLSGSVL--INSKERNLRRFRKLScYIMQDDVLIAN 236
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGssgevSLVGQPLhqMDEEARAKLRAKHVG-FVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAMMVAANLKLGKNMISYAKVVvveEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:PRK10584 103 LNALENVELPALLRGESSRQSRNGAK---ALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180
....*....|....*....|....*...
gi 161076684 317 STCFQLISLLRSLARG-GRTIVCTIHQP 343
Cdd:PRK10584 180 QTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
153-337 |
2.11e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.99 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSK-------ERNLrrfrklsc 225
Cdd:COG4525 10 SVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGF-LAPSSGEITLDGVpvtgpgaDRGV-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 226 yIMQDDVLIANLTVREAmmVAANLKLgKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVM 305
Cdd:COG4525 81 -VFQKDALLPWLNVLDN--VAFGLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190
....*....|....*....|....*....|..
gi 161076684 306 FFDEPTSGLDSSTCFQLISLLRSLARGGRTIV 337
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRTGKGV 188
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
136-366 |
2.30e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.44 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 136 HLPQRPPVDIEFCDIsysVTDSHRrGfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlsGSVLINSKER 215
Cdd:PRK11174 341 ELASNDPVTIEAEDL---EILSPD-G-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ--GSLKINGIEL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 216 ---NLRRFRKLSCYIMQDDVLIANlTVREammvaaNLKLGKNMISYAKvvvVEEILETIGLKESVNTLTCNL-------- 284
Cdd:PRK11174 414 relDPESWRKHLSWVGQNPQLPHG-TLRD------NVLLGNPDASDEQ---LQQALENAWVSEFLPLLPQGLdtpigdqa 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 285 ---SGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTiHQPSArlFEKFDHLYLLAQGQ 361
Cdd:PRK11174 484 aglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQLED--LAQWDQIWVMQDGQ 560
|
....*
gi 161076684 362 CVYEG 366
Cdd:PRK11174 561 IVQQG 565
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
145-341 |
3.19e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.86 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRrgfktILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE---RNLRRFR 221
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-----ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ-RGRVKVMGREvnaENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 KLSCYIMQD-DVLIANLTVREAmmVA---ANLKLGKNMISYAkvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALE 297
Cdd:PRK13647 79 SKVGLVFQDpDDQVFSSTVWDD--VAfgpVNMGLDKDEVERR----VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 161076684 298 LVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIH 341
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
145-371 |
3.64e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.51 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSvtdshrRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyktaQL---SGSVLIN-------SKE 214
Cdd:PRK11831 8 VDMRGVSFT------RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGG----QIapdHGEILFDgenipamSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 215 RnLRRFRKLSCYIMQDDVLIANLTVREAmmVAANLKLGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSI 294
Cdd:PRK11831 78 R-LYTVRKRMSMLFQSGALFTDMNVFDN--VAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 295 ALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSL--ARGGRTIVCTIHQPsaRLFEKFDHLYLLAQGQCVYEGRVKGL 371
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVP--EVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
149-380 |
6.11e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 79.88 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 149 DISYSVTDshrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG---YKTAqlSGSVLInskernlrrfrklsc 225
Cdd:cd03217 5 DLHVSVGG------KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkYEVT--EGEILF--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 226 yimqDDVLIANLTVREammvAANLKLGKNMISYAKV--VVVEEILetiglkESVNTltcNLSGGQRKRLSIALELVNNPP 303
Cdd:cd03217 62 ----KGEDITDLPPEE----RARLGIFLAFQYPPEIpgVKNADFL------RYVNE---GFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 304 VMFFDEPTSGLDSSTcFQLIS-LLRSLARGGRTIVCTIHQpsARLFE--KFDHLYLLAQGQCVYEGRVKgLVPYLSSLGY 380
Cdd:cd03217 125 LAILDEPDSGLDIDA-LRLVAeVINKLREEGKSVLIITHY--QRLLDyiKPDRVHVLYDGRIVKSGDKE-LALEIEKKGY 200
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
159-396 |
9.04e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.27 E-value: 9.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSV------LINSKERNLRRFRKLSCYIMQDDV 232
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS-QGNVswrgepLAKLNRAQRKAFRRDIQMVFQDSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 233 LIAN--LTVREamMVAANLKLGKNMISYAKVVVVEEILETIGLKESV-NTLTCNLSGGQRKRLSIALELVNNPPVMFFDE 309
Cdd:PRK10419 100 SAVNprKTVRE--IIREPLRHLLSLDKAERLARASEMLRAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 310 PTSGLDSSTCFQLISLLRSL-ARGGRTIVCTIHqpSARLFEKFDHLYLLAQGQCVYEGRVKGlvpylsslgyECPSYHNP 388
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLqQQFGTACLFITH--DLRLVERFCQRVMVMDNGQIVETQPVG----------DKLTFSSP 245
|
....*...
gi 161076684 389 ADYVLEVA 396
Cdd:PRK10419 246 AGRVLQNA 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
166-351 |
9.79e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 9.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKL----SCYIMQDDVLIANLTVRE 241
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD-AGSILIDGQEMRFASTTAAlaagVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 242 ammvaaNLKLGK-----NMISYAKVV-VVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:PRK11288 99 ------NLYLGQlphkgGIVNRRLLNyEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 161076684 316 SSTCFQLISLLRSLARGGRTIVCTIHqpsaRLFEKF 351
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGRVILYVSH----RMEEIF 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
144-337 |
1.02e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.24 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSVtDSHRRGfktiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLI---NSKERNLRRF 220
Cdd:PRK13657 334 AVEFDDVSFSY-DNSRQG----VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ-SGRILIdgtDIRTVTRASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYIMQDDVLIaNLTVREammvaaNLKLGKNMISYAKVVVVEEI---LETI-----GLKESVNTLTCNLSGGQRKRL 292
Cdd:PRK13657 408 RRNIAVVFQDAGLF-NRSIED------NIRVGRPDATDEEMRAAAERaqaHDFIerkpdGYDTVVGERGRQLSGGERQRL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 161076684 293 SIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIV 337
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI 525
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
163-341 |
1.63e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAgyKTAQLSGSVLINSK---------ER--NLRRFRKLSCYIMQDD 231
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRveffnqniyERrvNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 232 VLIAnltvreaMMVAANLKLGKNMISYAKVVVVEEILETI--------GLKESVNTLTCNLSGGQRKRLSIALELVNNPP 303
Cdd:PRK14258 98 NLFP-------MSVYDNVAYGVKIVGWRPKLEIDDIVESAlkdadlwdEIKHKIHKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 161076684 304 VMFFDEPTSGLDSSTCFQLISLLRSLA-RGGRTIVCTIH 341
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSH 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
163-382 |
2.03e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 79.69 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQ-LSGSVL-----INSKERNLRrfRKLSCYI-MQDDVLIA 235
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKiLEGDILfkgesILDLEPEER--AHLGIFLaFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAMMVAANLK---LGKNMISYAKVV-VVEEILETIGLKESVNTLTCN--LSGGQRKRLSIALELVNNPPVMFFDE 309
Cdd:CHL00131 98 GVSNADFLRLAYNSKrkfQGLPELDPLEFLeIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 310 PTSGLDsstcfqlISLLRSLARG-------GRTIVCTIHQPsaRLFE--KFDHLYLLAQGQCVYEGRVKgLVPYLSSLGY 380
Cdd:CHL00131 178 TDSGLD-------IDALKIIAEGinklmtsENSIILITHYQ--RLLDyiKPDYVHVMQNGKIIKTGDAE-LAKELEKKGY 247
|
..
gi 161076684 381 EC 382
Cdd:CHL00131 248 DW 249
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
139-315 |
2.70e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 139 QRPPVdIEFCDISYSVTDshrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE---- 214
Cdd:PRK09452 10 SLSPL-VELRGISKSFDG------KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-SGRIMLDGQDithv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 215 ----RNLRRfrklscyIMQDDVLIANLTVREAmmVAANLKLGKnmISYAKVVV-VEEILETIGLKESVNTLTCNLSGGQR 289
Cdd:PRK09452 82 paenRHVNT-------VFQSYALFPHMTVFEN--VAFGLRMQK--TPAAEITPrVMEALRMVQLEEFAQRKPHQLSGGQQ 150
|
170 180
....*....|....*....|....*.
gi 161076684 290 KRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
159-372 |
3.98e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.13 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTI--LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG--YKTaqlSGSVLIN----SKERnlRRFRKLSCYIM-Q 229
Cdd:COG4586 29 RREYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilVPT---SGEVRVLgyvpFKRR--KEFARRIGVVFgQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 230 DDVLIANLTVREammvaaNLKLGKNM--IS---YAKVVvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPV 304
Cdd:COG4586 104 RSQLWWDLPAID------SFRLLKAIyrIPdaeYKKRL--DELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076684 305 MFFDEPTSGLDSSTCFQLISLLRSL-ARGGRTIVCTIHQPS--ARLFEKfdhLYLLAQGQCVYEGRVKGLV 372
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDdiEALCDR---VIVIDHGRIIYDGSLEELK 243
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
163-369 |
4.30e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.77 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSKE---RNLRRF------RKLscYimqddvl 233
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI-LAPDSGEVLWDGEPldpEDRRRIgylpeeRGL--Y------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 234 iANLTVREAMMVAANLK-LGKnmiSYAKVVVvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTS 312
Cdd:COG4152 84 -PKMKVGEQLVYLARLKgLSK---AEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 313 GLDSSTCFQLISLLRSLARGGRTIVCTIHQ-PSArlfEKF-DHLYLLAQGQCVYEGRVK 369
Cdd:COG4152 159 GLDPVNVELLKDVIRELAAKGTTVIFSSHQmELV---EELcDRIVIINKGRKVLSGSVD 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
166-368 |
4.76e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 78.28 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKErnLRRFRKLSCYIMQDDVLIANLTVREAMMV 245
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPT-SGGVILEGKQ--ITEPGPDRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 246 AANLKLgKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLIS- 324
Cdd:TIGR01184 78 AVDRVL-PDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEe 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 161076684 325 LLRSLARGGRTIVCTIHQPSARLFEKfDHLYLLAQGQCVYEGRV 368
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDEALLLS-DRVVMLTNGPAANIGQI 199
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
163-368 |
7.05e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.20 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK-------ERNLrrfrklscyIMQDDVLIA 235
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKpvegpgaERGV---------VFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAmmVAANLKLGkNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:PRK11248 84 WRNVQDN--VAFGLQLA-GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 161076684 316 SSTCFQLISLLRSL-ARGGRTIVCTIHQPSARLFEKFDhLYLLAQGqcvyEGRV 368
Cdd:PRK11248 161 AFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATE-LVLLSPG----PGRV 209
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
166-367 |
9.20e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.67 E-value: 9.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAqlSGSVLINSKERNLRRFRKLS---CYIMQDDVLIANLTVREA 242
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLEAWSAAELArhrAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 243 MMvaanLKLGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGG--QRKRLSIALELV---NNP--PVMFFDEPTSGLD 315
Cdd:PRK03695 90 LT----LHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVwpdINPagQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 161076684 316 SSTCFQLISLLRSLARGGRTIVCTIHQPSaRLFEKFDHLYLLAQGQCVYEGR 367
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSHDLN-HTLRHADRVWLLKQGKLLASGR 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
163-315 |
9.39e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.77 E-value: 9.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTL------MNILagYKTAQLSGSVLINSKErnlrrfrklscyIMQDDVLIAN 236
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNDL--IPGARVEGEILLDGED------------IYDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTvREAMMV---------------AANLKLgkNMISYAKVV--VVEEILETIGL----KESVNTLTCNLSGGQRKRLSIA 295
Cdd:COG1117 90 LR-RRVGMVfqkpnpfpksiydnvAYGLRL--HGIKSKSELdeIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIA 166
|
170 180
....*....|....*....|
gi 161076684 296 LELVNNPPVMFFDEPTSGLD 315
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALD 186
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
176-366 |
1.15e-15 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 79.37 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYKTAQ-----LSGSVLINSKER-NL----RRFrklsCYIMQDDVLIANLTVREammv 245
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIAGLERPDsgrirLGGEVLQDSARGiFLpphrRRI----GYVFQEARLFPHLSVRG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 246 aaNLKLG-KNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLIS 324
Cdd:COG4148 97 --NLLYGrKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 161076684 325 LLRSLARGGRT-IVCTIHQPS--ARLfekFDHLYLLAQGQCVYEG 366
Cdd:COG4148 175 YLERLRDELDIpILYVSHSLDevARL---ADHVVLLEQGRVVASG 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
158-346 |
1.16e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 77.09 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 158 HRRGFKTI--LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLrrfrklscyimqdDvlIA 235
Cdd:COG4778 17 HLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPD-SGSILVRHDGGWV-------------D--LA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAmmvaanLKLGKNMISY------------AKVVVVE-----------------EILETIGLKE-----SVNTLt 281
Cdd:COG4778 81 QASPREI------LALRRRTIGYvsqflrviprvsALDVVAEpllergvdreearararELLARLNLPErlwdlPPATF- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076684 282 cnlSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSAR 346
Cdd:COG4778 154 ---SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
174-366 |
1.37e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 174 RNGEITAIMGPSGAGKSTLMNILAGY-----KTAQLSGSVLIN-SKERNLRRFRKLSCYIMQ--DDVLIANLTVREAMMV 245
Cdd:PRK13643 30 KKGSYTALIGHTGSGKSTLLQHLNGLlqpteGKVTVGDIVVSStSKQKEIKPVRKKVGVVFQfpESQLFEETVLKDVAFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 246 AANLKLGKnmiSYAKVVVVEEiLETIGL-KESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLIS 324
Cdd:PRK13643 110 PQNFGIPK---EKAEKIAAEK-LEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 161076684 325 LLRSLARGGRTIVCTIHQPSaRLFEKFDHLYLLAQGQCVYEG 366
Cdd:PRK13643 186 LFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHIISCG 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
161-372 |
1.81e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKErnLRRF------RKLScYIMQDDVLI 234
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA-HGHVWLDGEH--IQHYaskevaRRIG-LLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 235 ANLTVREamMVAANLKLGKNMISYAK---VVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPT 311
Cdd:PRK10253 94 GDITVQE--LVARGRYPHQPLFTRWRkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076684 312 SGLDSSTCFQLISLLRSLAR-GGRTIVCTIHQPSaRLFEKFDHLYLLAQGQCVYEGRVKGLV 372
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNReKGYTLAAVLHDLN-QACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
140-315 |
1.98e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 140 RPPVDIEfcDISYSVTDshrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyKTAQLSGSVLINSkerNLrr 219
Cdd:COG0488 313 KKVLELE--GLSKSYGD------KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTVKLGE---TV-- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 220 frKLScYIMQD-DVLIANLTVREAMMVAAnlklgknmiSYAKVVVVEEILETIGLK-ESVNTLTCNLSGGQRKRLSIALE 297
Cdd:COG0488 379 --KIG-YFDQHqEELDPDKTVLDELRDGA---------PGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKL 446
|
170
....*....|....*...
gi 161076684 298 LVNNPPVMFFDEPTSGLD 315
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLD 464
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
166-338 |
2.20e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.97 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAQLSGSVLINSKE---RNLRRF-RKLSCYIMQDDVLIANLTVR 240
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTYEGEIIFEGEElqaSNIRDTeRAGIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 EAMMVAANLKLGKnMISYAKVVV-VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTC 319
Cdd:PRK13549 101 ENIFLGNEITPGG-IMDYDAMYLrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESET 179
|
170
....*....|....*....
gi 161076684 320 FQLISLLRSLARGGrtIVC 338
Cdd:PRK13549 180 AVLLDIIRDLKAHG--IAC 196
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
153-361 |
3.35e-15 |
|
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: 79.31 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAqlSGSVLINS---KERNLRRFRKLSCYIM 228
Cdd:TIGR01842 321 NVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGiWPPT--SGSVRLDGadlKQWDRETFGKHIGYLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 229 QDDVLIANltvreamMVAANL-KLGKN-----MISYAKVVVVEEILETI--GLKESVNTLTCNLSGGQRKRLSIALELVN 300
Cdd:TIGR01842 399 QDVELFPG-------TVAENIaRFGENadpekIIEAAKLAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076684 301 NPPVMFFDEPTSGLDSSTCFQLISLLRSL-ARGGRTIVCTiHQPSarLFEKFDHLYLLAQGQ 361
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVIT-HRPS--LLGCVDKILVLQDGR 530
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
157-331 |
6.86e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLS------------ 224
Cdd:PRK11701 13 TKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD-AGEVHYRMRDGQLRDLYALSeaerrrllrtew 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 225 CYIMQD--DVLianltvReaMMVAANLKLGKNMIS-----YAKV-VVVEEILETIGLKES-VNTLTCNLSGGQRKRLSIA 295
Cdd:PRK11701 92 GFVHQHprDGL------R--MQVSAGGNIGERLMAvgarhYGDIrATAGDWLERVEIDAArIDDLPTTFSGGMQQRLQIA 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 161076684 296 LELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR 331
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVR 199
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
168-337 |
7.13e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 73.62 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 168 SVSGKFRN-------GEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLS----CYIMQD---DVL 233
Cdd:cd03215 11 SVKGAVRDvsfevraGEIVGIAGLVGNGQTELAEALFGLRPPA-SGEITLDGKPVTRRSPRDAIragiAYVPEDrkrEGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 234 IANLTVREammvaanlklgkNMIsyakvvvveeiletiglkesvntLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSG 313
Cdd:cd03215 90 VLDLSVAE------------NIA-----------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180
....*....|....*....|....
gi 161076684 314 LDSSTCFQLISLLRSLARGGRTIV 337
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAVL 158
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
163-403 |
7.37e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.90 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNIL-------AGYKtaqLSGSVLINSKE----RNLRRFRKLSCYIMQ-- 229
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYR---YSGDVLLGGRSifnyRDVLEFRRRVGMLFQrp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 230 --------DDVLIAnltVREAMMVAANLKLGknmisyakvvVVEEILETIGLKESVNTLTCN----LSGGQRKRLSIALE 297
Cdd:PRK14271 111 npfpmsimDNVLAG---VRAHKLVPRKEFRG----------VAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 298 LVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLArgGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEGRVKGLvpylss 377
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL------ 249
|
250 260
....*....|....*....|....*.
gi 161076684 378 lgYECPSYHNPADYVLEVaSGEYGDA 403
Cdd:PRK14271 250 --FSSPKHAETARYVAGL-SGDVKDA 272
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
163-361 |
1.13e-14 |
|
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: 77.87 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSkeRNLRRFRK--LSCYI---MQDDVLIANl 237
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV-WPPTAGSVRLDG--ADLSQWDReeLGRHIgylPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVRE--AMM--------VAAnlklgknmisyAKVVVVEE-ILetiGLKESVNTLT----CNLSGGQRKRLSIALELVNNP 302
Cdd:COG4618 421 TIAEniARFgdadpekvVAA-----------AKLAGVHEmIL---RLPDGYDTRIgeggARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 303 PVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSarLFEKFDHLYLLAQGQ 361
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDGR 543
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
154-341 |
1.83e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 154 VTDSHRRGfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGY-KTAQLSGSVLINSKERNLRRfrKLSCYIMQDDV 232
Cdd:PRK15056 12 VTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFvRLASGKISILGQPTRQALQK--NLVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 233 LIAN--LTVREAMMVAANLKLGKNMISYAK-VVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDE 309
Cdd:PRK15056 89 VDWSfpVLVEDVVMMGRYGHMGWLRRAKKRdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190
....*....|....*....|....*....|..
gi 161076684 310 PTSGLDSSTCFQLISLLRSLARGGRTIVCTIH 341
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
164-366 |
2.10e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.27 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 164 TILKSVSGKFRNGEITAIMGPSGAGKSTLMN-----------------ILAGYKTAQLSGSVLINSKE-RNLRRFRKLSC 225
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiqvgdIYIGDKKNNHELITNPYSKKiKNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 226 YIMQ-DDVLIANLTVREAMMVAAnLKLGKNMISYAKVVvvEEILETIGLKES-VNTLTCNLSGGQRKRLSIALELVNNPP 303
Cdd:PRK13631 120 MVFQfPEYQLFKDTIEKDIMFGP-VALGVKKSEAKKLA--KFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076684 304 VMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQpSARLFEKFDHLYLLAQGQCVYEG 366
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTG 258
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
163-318 |
2.31e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.97 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN----SKERNLRRFRKLScYIMQDDVL--IAN 236
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD-SGSILIDgkdvTKLPEYKRAKYIG-RVFQDPMMgtAPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAMMVAAN------LKLG--KNMISYAKvvvveEILETI--GLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMF 306
Cdd:COG1101 97 MTIEENLALAYRrgkrrgLRRGltKKRRELFR-----ELLATLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLL 171
|
170
....*....|..
gi 161076684 307 FDEPTSGLDSST 318
Cdd:COG1101 172 LDEHTAALDPKT 183
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
161-356 |
2.35e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.72 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMN----ILAGYKTAQLSGSVL-----INSKERNLRRFRKLSCYIMQDD 231
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARVEGEVRlfgrnIYSPDVDPIEVRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 232 VLIANLTVREAmmVAANLKLGKNMISYAKV-VVVEEILETIGL----KESVNTLTCNLSGGQRKRLSIALELVNNPPVMF 306
Cdd:PRK14267 95 NPFPHLTIYDN--VAIGVKLNGLVKSKKELdERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 161076684 307 FDEPTSGLDSSTCFQLISLLRSLaRGGRTIVCTIHQP--SARLFEKFDHLYL 356
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPaqAARVSDYVAFLYL 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
166-369 |
2.75e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN-------SKERNLRRFRKLSCYIMQ--DDVLIAN 236
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPT-QGSVRVDdtlitstSKNKDIKQIRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAMMVAANLKLGKNmisyAKVVVVEEILETIGLKESV-NTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQE----EAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 316 SSTCFQLISLLRSLARGGRTIVCTIHqpsarLFEKF----DHLYLLAQGQCVYEGRVK 369
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTH-----LMDDVanyaDFVYVLEKGKLVLSGKPK 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
161-341 |
2.76e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQ-----LSGSVLINSKERNLRRFRKLSCYIMQDDVLIA 235
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSagkiwFSGHDITRLKNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVRE-----AMMVAANLKLGKNMISYAkvvvveeiLETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEP 310
Cdd:PRK10908 93 DRTVYDnvaipLIIAGASGDDIRRRVSAA--------LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 161076684 311 TSGLDSSTCFQLISLLRSLARGGRTIVCTIH 341
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
163-315 |
2.80e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.14 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-RNL---RRFRK-LScYIMQDDVLIANL 237
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-SGRIFLDGEDiTHLpmhKRARLgIG-YLPQEASIFRKL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 238 TVRE-AMMVAANLKLGKNMIsYAKVvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:COG1137 94 TVEDnILAVLELRKLSKKER-EERL---EELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
165-366 |
2.89e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVL-----INSKERNLRRFRKLSCYIMQD-DVLIANLT 238
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ-KGAVLwqgkpLDYSKRGLLALRQQVATVFQDpEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREAMMVA-ANLKLGKNMISYAkvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:PRK13638 95 IDSDIAFSlRNLGVPEAEITRR----VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 161076684 318 TCFQLISLLRSLARGGRTIVCTIHQPSArLFEKFDHLYLLAQGQCVYEG 366
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHG 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
145-337 |
3.00e-14 |
|
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: 76.40 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVtDSHRrgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINS------KERNLR 218
Cdd:COG5265 358 VRFENVSFGY-DPER----PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVT-SGRILIDGqdirdvTQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 219 RfrklscYI---MQDDVLIaNLTVREammvaaNLKLGKNMISYAKVVVVEE---ILETI--------------GLKesvn 278
Cdd:COG5265 432 A------AIgivPQDTVLF-NDTIAY------NIAYGRPDASEEEVEAAARaaqIHDFIeslpdgydtrvgerGLK---- 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 279 tltcnLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIV 337
Cdd:COG5265 495 -----LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV 548
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
174-341 |
3.24e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 77.36 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 174 RNGEITAIMGPSGAGKSTLMNILAGyKTAQLSGSVLINSKE--RNLRRFRKLSCYIMQDDVLIANLTVREAMMVAANLKl 251
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGKSilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLR- 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 252 gknmisyakVVVVEEI-------LETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLIS 324
Cdd:TIGR01257 2041 ---------GVPAEEIekvanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170
....*....|....*..
gi 161076684 325 LLRSLARGGRTIVCTIH 341
Cdd:TIGR01257 2112 TIVSIIREGRAVVLTSH 2128
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
163-355 |
3.40e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGY-----KTAQLSGSVLINSKE---RNLRRFRKLSCYIMQDDVLI 234
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydSKIKVDGKVLYFGKDifqIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 235 ANLTVREAMMVAANLKLGKNMISYAKvvVVEEILETIGLKESV----NTLTCNLSGGQRKRLSIALELVNNPPVMFFDEP 310
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKK--IVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 161076684 311 TSGLDSSTCfQLISLLRSLARGGRTIVCTIHQP--SARLFEKFDHLY 355
Cdd:PRK14246 181 TSMIDIVNS-QAIEKLITELKNEIAIVIVSHNPqqVARVADYVAFLY 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
166-365 |
4.16e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.25 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK---ERNLRRFRKLSCYIMQDDvliANLTVREA 242
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-SGEIFYNNQaitDDNFEKLRKHIGIVFQNP---DNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 243 MMVAANLKLGKNMISYAKVV-VVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQ 321
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHrRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 161076684 322 LISLLRSL-ARGGRTIVCTIHQPSARLfeKFDHLYLLAQGQcVYE 365
Cdd:PRK13648 181 LLDLVRKVkSEHNITIISITHDLSEAM--EADHVIVMNKGT-VYK 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
145-341 |
5.05e-14 |
|
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: 69.78 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDshrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyKTAQLSGSVLINSKERnlrrfrklS 224
Cdd:cd03221 1 IELENLSKTYGG------KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK--------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 225 CYIMQddvlianltvreammvaanlklgknmisyakvvvveeiletiglkesvntltcnLSGGQRKRLSIALELVNNPPV 304
Cdd:cd03221 66 GYFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*..
gi 161076684 305 MFFDEPTSGLDSSTCFQLISLLRSLArggRTIVCTIH 341
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP---GTVILVSH 125
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
161-329 |
6.33e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKFRNGEITAIMGPSGAGKST----LMNILAGYKTAQLSGSVLINSKERNLRRFRKLSCYIMQD--DVLI 234
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDpnSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 235 ANLTVREamMVAANLKLGKNMISYAKVVV-VEEILETIGLK-ESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTS 312
Cdd:PRK15134 377 PRLNVLQ--IIEEGLRVHQPTLSAAQREQqVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170
....*....|....*..
gi 161076684 313 GLDSSTCFQLISLLRSL 329
Cdd:PRK15134 455 SLDKTVQAQILALLKSL 471
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
168-367 |
1.30e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.56 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 168 SVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAqlSGSVLINSKE------------------RNLRRFRklscyim 228
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfYKPT--GGTILLRGQHieglpghqiarmgvvrtfQHVRLFR------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 229 qddvliaNLTVREAMMVAANLKLGKNMIS------------YAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIAL 296
Cdd:PRK11300 94 -------EMTVIENLLVAQHQQLKTGLFSgllktpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEGR 367
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
181-341 |
1.80e-13 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 72.53 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 181 IMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLSCYIM-QDDVLIANLTVREAmmVAANLKLGKNMISYA 259
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD-SGSIMLDGEDVTNVPPHLRHINMVfQSYALFPHMTVEEN--VAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 260 KVVVvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVC 338
Cdd:TIGR01187 78 KPRV-LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFVF 156
|
...
gi 161076684 339 TIH 341
Cdd:TIGR01187 157 VTH 159
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
653-828 |
1.92e-13 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 69.84 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 653 AFYFAKTIADMPFQIVFSSVYVLVVYYLTSQPMELERVSMFVLICVLNSLVAQSLGLLIGAGM-NIETGVFLGPVTTIPT 731
Cdd:COG0842 47 EILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLArSQEQASAISNLVILPL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 732 ILFSGFFVNFDTIPGYLQWVTYVSYVRYGFEGAMVAIYGmdrakmqcnqmychyrvpkkfleemSMDNALFWVDAVALIG 811
Cdd:COG0842 127 TFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLG-------------------------GAGLADVWPSLLVLLA 181
|
170
....*....|....*..
gi 161076684 812 IFFALRIIAYFVLRWKL 828
Cdd:COG0842 182 FAVVLLALALRLFRRRL 198
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
165-341 |
1.93e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.75 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLSC-YIMQDDVLIANLTVREAM 243
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDIT-SGDLFIGEKRMNDVPPAERGVgMVFQSYALYPHLSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 244 mvAANLKL---GKNMIsYAKVVVVEEILEtigLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCF 320
Cdd:PRK11000 97 --SFGLKLagaKKEEI-NQRVNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180
....*....|....*....|..
gi 161076684 321 QL-ISLLRSLARGGRTIVCTIH 341
Cdd:PRK11000 171 QMrIEISRLHKRLGRTMIYVTH 192
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
145-341 |
2.71e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVtdSHRRGFKTI-LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLI-------NSKERN 216
Cdd:PRK13641 3 IKFENVDYIY--SPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS-SGTITIagyhitpETGNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 217 LRRFRKLSCYIMQ--DDVLIANLTVREAMMVAANLKLGKNMisyAKVVVVEeILETIGLKESV-NTLTCNLSGGQRKRLS 293
Cdd:PRK13641 80 LKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE---AKEKALK-WLKKVGLSEDLiSKSPFELSGGQMRRVA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 161076684 294 IALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIH 341
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
134-342 |
3.66e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 134 LSHLPQRPPVDIEFCDISYSVTDShrrgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSK 213
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGV------EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI-VPPDSGTLEIGGN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 214 ER-NLR--RFRKLSCYIM-QDDVLIANLTVREAMMvaanLKLGKNMISYAKvvvVEEILETIGLKESVNTLTCNLSGGQR 289
Cdd:PRK15439 74 PCaRLTpaKAHQLGIYLVpQEPLLFPNLSVKENIL----FGLPKRQASMQK---MKQLLAALGCQLDLDSSAGSLEVADR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 161076684 290 KRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQ 342
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHK 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
152-337 |
3.84e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 152 YSVTDSHRRGFKTIlKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKtAQLSGSVLINSKERNLRR----FRKLSCYI 227
Cdd:PRK09700 266 FEVRNVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVD-KRAGGEIRLNGKDISPRSpldaVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 228 MQ---DDVLIANLTVREAMMVAANLKLGK--------NMISYAKVVvvEEILETIGLK-ESVNTLTCNLSGGQRKRLSIA 295
Cdd:PRK09700 344 TEsrrDNGFFPNFSIAQNMAISRSLKDGGykgamglfHEVDEQRTA--ENQRELLALKcHSVNQNITELSGGNQQKVLIS 421
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 161076684 296 LELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIV 337
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
144-366 |
4.41e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.83 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSVtdshrRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSkernlrrfRKL 223
Cdd:PRK10790 340 RIDIDNVSFAY-----RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT-EGEIRLDG--------RPL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 224 SCY-----------IMQDDVLIANltvreamMVAANLKLGKNmISYAKVVvveEILETIGLKESVNTLT----------- 281
Cdd:PRK10790 406 SSLshsvlrqgvamVQQDPVVLAD-------TFLANVTLGRD-ISEEQVW---QALETVQLAELARSLPdglytplgeqg 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 282 CNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTcFQLISLLRSLARGGRTIVCTIHQPSArLFEKfDHLYLLAQGQ 361
Cdd:PRK10790 475 NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT-EQAIQQALAAVREHTTLVVIAHRLST-IVEA-DTILVLHRGQ 551
|
....*
gi 161076684 362 CVYEG 366
Cdd:PRK10790 552 AVEQG 556
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
145-384 |
5.57e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.02 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDShrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE----RNLRRF 220
Cdd:PRK13644 2 IRLENVSYSYPDG-----TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ-KGKVLVSGIDtgdfSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYIMQD-DVLIANLTVREammvaaNLKLGKNMISYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIAL 296
Cdd:PRK13644 76 RKLVGIVFQNpETQFVGRTVEE------DLAFGPENLCLPPIEIrkrVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHqpSARLFEKFDHLYLLAQGQCVYEGRVKGLV--PY 374
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLsdVS 227
|
250
....*....|
gi 161076684 375 LSSLGYECPS 384
Cdd:PRK13644 228 LQTLGLTPPS 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
169-315 |
5.86e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.40 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 169 VSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQLSGSVLINSKERNLRRFRKLSCYIMQDDVLIANLTVREAmmVAAN 248
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVEQN--IAFG 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 249 LK---LGKNMISYAkvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:PRK11607 116 LKqdkLPKAEIASR----VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
144-367 |
6.80e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSV---TDSHRRGfktiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLI-------NSK 213
Cdd:PRK13634 2 DITFQKVEHRYqykTPFERRA----LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL-LQPTSGTVTIgervitaGKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 214 ERNLRRFRKLSCYIMQ--------DDVL--IA----NLTVREAmmvAANLKlgknmisyAKvvvveEILETIGLKESVNT 279
Cdd:PRK13634 77 NKKLKPLRKKVGIVFQfpehqlfeETVEkdICfgpmNFGVSEE---DAKQK--------AR-----EMIELVGLPEELLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 280 LT-CNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR-GGRTIVCTIHQ--PSARLfekFDHLY 355
Cdd:PRK13634 141 RSpFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSmeDAARY---ADQIV 217
|
250
....*....|..
gi 161076684 356 LLAQGQCVYEGR 367
Cdd:PRK13634 218 VMHKGTVFLQGT 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
145-341 |
7.94e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 69.83 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHrrgfKTILKSVSGKFRNGEITAIMGPSGAGKST---LMN-ILAGYKTAQLSGSVL-INSKERNLRR 219
Cdd:PRK13640 6 VEFKHVSFTYPDSK----KPALNDISFSIPRGSWTALIGHNGSGKSTiskLINgLLLPDDNPNSKITVDgITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 220 FRKLSCYIMQD-DVLIANLTVREAmmVAANLKlgKNMISYAKVV-VVEEILETIGLKESVNTLTCNLSGGQRKRLSIALE 297
Cdd:PRK13640 82 IREKVGIVFQNpDNQFVGATVGDD--VAFGLE--NRAVPRPEMIkIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 161076684 298 LVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR-GGRTIVCTIH 341
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITH 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
163-366 |
8.02e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.76 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQ-LSGSVLINSK--------ERNLRRFRKLS-C------- 225
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEpTSGRIIYHVAlcekcgyvERPSKVGEPCPvCggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 226 ---YIMQDDVLIANLTVREAMM------------VAANLKLGKNMISYAKVVVVE---EILETIGLKESVNTLTCNLSGG 287
Cdd:TIGR03269 93 evdFWNLSDKLRRRIRKRIAIMlqrtfalygddtVLDNVLEALEEIGYEGKEAVGravDLIEMVQLSHRITHIARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 288 QRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPSArLFEKFDHLYLLAQGQCVYEG 366
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEV-IEDLSDKAIWLENGEIKEEG 251
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
166-335 |
1.08e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.36 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAQLSGSVLINSKErnlRRFRKLS-------CYIMQDDVLIANL 237
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvYPHGSYEGEILFDGEV---CRFKDIRdsealgiVIIHQELALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREammvaaNLKLG-----KNMISYAKVVV-VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPT 311
Cdd:NF040905 94 SIAE------NIFLGnerakRGVIDWNETNRrARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180
....*....|....*....|....
gi 161076684 312 SGLDSSTCFQLISLLRSLARGGRT 335
Cdd:NF040905 168 AALNEEDSAALLDLLLELKAQGIT 191
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
145-381 |
1.24e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 68.96 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTL---MNILagykTAQLSGSVLIN----SKERNL 217
Cdd:PRK13633 5 IKCKNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNAL----LIPSEGKVYVDgldtSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 218 RRFRKLSCYIMQ--DDVLIANLTVREAMMVAANLKLGKNMISYAkvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIA 295
Cdd:PRK13633 81 WDIRNKAGMVFQnpDNQIVATIVEEDVAFGPENLGIPPEEIRER----VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 296 LELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPSARLfeKFDHLYLLAQGQCVYEGRVK----- 369
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAV--EADRIIVMDSGKVVMEGTPKeifke 234
|
250 260
....*....|....*....|
gi 161076684 370 -------GL-VPYLSSLGYE 381
Cdd:PRK13633 235 vemmkkiGLdVPQVTELAYE 254
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
145-371 |
1.65e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.04 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDSHRRGFKTIlKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLIN-------SKERNL 217
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQAI-HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL-LKPTTGTVTVDditithkTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 218 RRFRKLSCYIMQ--DDVLIANLTVREAMMVAANLKLG-KNMISYAkvvvvEEILETIGLKESVNTLT-CNLSGGQRKRLS 293
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNlDEVKNYA-----HRLLMDLGFSRDVMSQSpFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 294 IALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLA-RGGRTIVCTIHQPS--ARLfekFDHLYLLAQGQCVYEGRVKG 370
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNevARY---ADEVIVMKEGSIVSQTSPKE 232
|
.
gi 161076684 371 L 371
Cdd:PRK13646 233 L 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
168-337 |
1.73e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 168 SVSGKFRN-------GEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFR-----KLsCYIMQD---DV 232
Cdd:COG1129 263 SVGGVVRDvsfsvraGEILGIAGLVGAGRTELARALFGADPAD-SGEIRLDGKPVRIRSPRdairaGI-AYVPEDrkgEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 233 LIANLTVREAMMVAANLKLGKNM-ISYAKVV-VVEEILETIGLK-ESVNTLTCNLSGG-QRKrLSIALELVNNPPVMFFD 308
Cdd:COG1129 341 LVLDLSIRENITLASLDRLSRGGlLDRRRERaLAEEYIKRLRIKtPSPEQPVGNLSGGnQQK-VVLAKWLATDPKVLILD 419
|
170 180
....*....|....*....|....*....
gi 161076684 309 EPTSGLDSSTCFQLISLLRSLARGGRTIV 337
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAEGKAVI 448
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
144-367 |
1.79e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.82 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSVTDSHrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLI---NSKERNLRRF 220
Cdd:PRK11176 341 DIEFRNVTFTYPGKE----VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-EGEILLdghDLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKlSCYIMQDDVLIANLTVREAMMVAANLKLGKNMI-SYAKVVVVEEILEtiGLKESVNTLT----CNLSGGQRKRLSIA 295
Cdd:PRK11176 416 RN-QVALVSQNVHLFNDTIANNIAYARTEQYSREQIeEAARMAYAMDFIN--KMDNGLDTVIgengVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076684 296 LELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIHQPSArlFEKFDHLYLLAQGQCVYEGR 367
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLST--IEKADEILVVEDGEIVERGT 561
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
164-338 |
2.25e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 164 TILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAQLSGSVLINSKE---RNLRRF-RKLSCYIMQDDVLIANLT 238
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTWDGEIYWSGSPlkaSNIRDTeRAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREAMMVAANLKLGKNMISYAKVVV-VEEILETIGLKESVNTLTC-NLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:TIGR02633 95 VAENIFLGNEITLPGGRMAYNAMYLrAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTE 174
|
170 180
....*....|....*....|..
gi 161076684 317 STCFQLISLLRSLARGGrtIVC 338
Cdd:TIGR02633 175 KETEILLDIIRDLKAHG--VAC 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
165-329 |
2.32e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.34 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTaQLSGSVLINSKE--RNLRRFRKLScYIMQDDVLIANLTVREa 242
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEH-QTSGHIRFHGTDvsRLHARDRKVG-FVFQHYALFRHMTVFD- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 243 mmvaaNLKLGKNMI-------SYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:PRK10851 94 -----NIAFGLTVLprrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170
....*....|....
gi 161076684 316 SSTCFQLISLLRSL 329
Cdd:PRK10851 169 AQVRKELRRWLRQL 182
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
166-323 |
2.42e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyKTAQLSGSVLINSKERNLRRFRK-LSC---YIMQD---DVLIANLT 238
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG-ALPRTSGYVTLDGHEVVTRSPQDgLANgivYISEDrkrDGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREAMMVAANLKLGKNMIS---YAKVVVVEEILETIGLKE-SVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGL 314
Cdd:PRK10762 347 VKENMSLTALRYFSRAGGSlkhADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170
....*....|..
gi 161076684 315 D---SSTCFQLI 323
Cdd:PRK10762 427 DvgaKKEIYQLI 438
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
133-344 |
2.51e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 133 ALSHLPQRPPVDIEfcdisySVTdsHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQ----LSGSV 208
Cdd:PRK11247 3 NTARLNQGTPLLLN------AVS--KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSagelLAGTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 209 LINSKERNLRrfrklscyIM-QDdvliANLTVREAMMVAANLKLGKNMISYAkvvvvEEILETIGLKESVNTLTCNLSGG 287
Cdd:PRK11247 75 PLAEAREDTR--------LMfQD----ARLLPWKKVIDNVGLGLKGQWRDAA-----LQALAAVGLADRANEWPAALSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 288 QRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPS 344
Cdd:PRK11247 138 QKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVS 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
152-337 |
4.96e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.08 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 152 YSVTDSHRRGfktiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQLSGSVLINSKERNLRR----FRKLSCYI 227
Cdd:TIGR02633 266 WDVINPHRKR----VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDIRNpaqaIRAGIAMV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 228 MQDdvlianltvREAMMVAANLKLGKNMI-----SYAKVVVVEEILETIGLKESVNTLTC----------NLSGGQRKRL 292
Cdd:TIGR02633 342 PED---------RKRHGIVPILGVGKNITlsvlkSFCFKMRIDAAAELQIIGSAIQRLKVktaspflpigRLSGGNQQKA 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 161076684 293 SIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIV 337
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAII 457
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
163-366 |
5.93e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.38 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN-----SKERNLRRFRKLSCYIMQ--DDVLIA 235
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT-SGKIIIDgvditDKKVKLSDIRKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAMMVAANLKLGKNMISYAkvvvVEEILETIGLKESV--NTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSG 313
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENR----VKRAMNIVGLDYEDykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 314 LDSSTCFQLISLLRSLARG-GRTIVCTIH--QPSARLFEKfdhLYLLAQGQCVYEG 366
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEyNMTIILVSHsmEDVAKLADR---IIVMNKGKCELQG 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
176-343 |
7.36e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYKTAqLSGSVLINSkeRNLRRfrklscyimQDDVLIANLT-------VREAMMVAAN 248
Cdd:PRK13538 27 GELVQIEGPNGAGKTSLLRILAGLARP-DAGEVLWQG--EPIRR---------QRDEYHQDLLylghqpgIKTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 249 LKLGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRS 328
Cdd:PRK13538 95 LRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
170
....*....|....*
gi 161076684 329 LARGGRTIVCTIHQP 343
Cdd:PRK13538 175 HAEQGGMVILTTHQD 189
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
174-331 |
9.29e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 9.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 174 RNGEITAIMGPSGAGKS----TLMNILAgyKTAQLSGSVLINSKE------RNLRRFR--KLScYIMQDDVLIAN--LTV 239
Cdd:PRK09473 40 RAGETLGIVGESGSGKSqtafALMGLLA--ANGRIGGSATFNGREilnlpeKELNKLRaeQIS-MIFQDPMTSLNpyMRV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 240 REAMMVAanLKLGKNMisyAKVVVVEE---ILETIGLKESVNTLTC---NLSGGQRKRLSIALELVNNPPVMFFDEPTSG 313
Cdd:PRK09473 117 GEQLMEV--LMLHKGM---SKAEAFEEsvrMLDAVKMPEARKRMKMyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 191
|
170
....*....|....*...
gi 161076684 314 LDSSTCFQLISLLRSLAR 331
Cdd:PRK09473 192 LDVTVQAQIMTLLNELKR 209
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
166-331 |
1.00e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSG---KFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSV------LINSKERNLRRFRKLSCYIMQDDVLIAN 236
Cdd:PRK15079 34 LKAVDGvtlRLYEGETLGVVGESGCGKSTFARAIIGLVKAT-DGEVawlgkdLLGMKDDEWRAVRSDIQMIFQDPLASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 --LTVREamMVAANLKLGKNMISYAKVVV-VEEILETIGLKESV-NTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTS 312
Cdd:PRK15079 113 prMTIGE--IIAEPLRTYHPKLSRQEVKDrVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170
....*....|....*....
gi 161076684 313 GLDSSTCFQLISLLRSLAR 331
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQR 209
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
174-341 |
1.41e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.47 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 174 RNGEITAIMGPSGAGKSTLMNILAGYKTAQLSGSVLINSKERNLRRFR--KLSCYIMQddvlIANLTVREAMMV------ 245
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRgsELQNYFTK----LLEGDVKVIVKPqyvdli 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 246 --AANLKLGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLI 323
Cdd:cd03236 100 pkAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170
....*....|....*...
gi 161076684 324 SLLRSLARGGRTIVCTIH 341
Cdd:cd03236 180 RLIRELAEDDNYVLVVEH 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
174-337 |
1.68e-11 |
|
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: 67.89 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 174 RNGEITAIMGPSGAGKSTLMNILAGyktaqlsgsVLI-N--------SKERNLRRFRK--LSCYIMQddvlIANLTVREA 242
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSG---------ELKpNlgdydeepSWDEVLKRFRGteLQDYFKK----LANGEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 243 M---MVaanlklgkNMISyaKVV---------------VVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPV 304
Cdd:COG1245 164 HkpqYV--------DLIP--KVFkgtvrellekvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190
....*....|....*....|....*....|....*.
gi 161076684 305 MFFDEPTSGLDsstCFQLI---SLLRSLARGGRTIV 337
Cdd:COG1245 234 YFFDEPSSYLD---IYQRLnvaRLIRELAEEGKYVL 266
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
161-332 |
1.70e-11 |
|
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: 67.89 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKtiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVlinskERNLrrfrKLSC---YIMQDdvliANL 237
Cdd:COG1245 353 GFS--LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPD-EGEV-----DEDL----KISYkpqYISPD----YDG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREAMMVAANLKLGKnmiSYAKvvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:COG1245 417 TVEEFLRSANTDDFGS---SYYK----TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170
....*....|....*
gi 161076684 318 TCFQLISLLRSLARG 332
Cdd:COG1245 490 QRLAVAKAIRRFAEN 504
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
158-378 |
2.62e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 158 HRRGFKTILKSVSGKFRNGEITAIMGPSGAGKS----TLMNILAGYKTAQLSGSVLINSKERNLRRFRKLSCYIMQDdVL 233
Cdd:PRK10261 24 QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRH-VR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 234 IANLTV--REAM-----------MVAANLKLGKNMISYAKVVVVEEILETIGLKESVNTLT---CNLSGGQRKRLSIALE 297
Cdd:PRK10261 103 GADMAMifQEPMtslnpvftvgeQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSrypHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 298 LVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEGRVKGLV----- 372
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapqh 262
|
....*.
gi 161076684 373 PYLSSL 378
Cdd:PRK10261 263 PYTRAL 268
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
166-341 |
3.00e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLSCYIMQDDVL-------IANLT 238
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPD-TGTIEWIFKDEKNKKKTKEKEKVLEKLVIqktrfkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 -VREAMMVA---ANLKLGKNMI---------SYAkvVVVEE-------ILETIGLKES-VNTLTCNLSGGQRKRLSIALE 297
Cdd:PRK13651 102 eIRRRVGVVfqfAEYQLFEQTIekdiifgpvSMG--VSKEEakkraakYIELVGLDESyLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 161076684 298 LVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIH 341
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
265-371 |
4.35e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.53 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 265 EEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPS 344
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYME 205
|
90 100
....*....|....*....|....*...
gi 161076684 345 ARlfEKFDH-LYLLAQGQCVYEGRVKGL 371
Cdd:NF000106 206 EA--EQLAHeLTVIDRGRVIADGKVDEL 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
178-315 |
4.73e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 178 ITAIMGPSGAGKSTLMNILAGYKTAQ-----LSGSVLINSKER-NL----RRFRklscYIMQDDVLIANLTVReammvaA 247
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQkgrivLNGRVLFDAEKGiCLppekRRIG----YVFQDARLFPHYKVR------G 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 248 NLKLG--KNMISYakvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:PRK11144 96 NLRYGmaKSMVAQ-----FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
159-317 |
5.40e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE---RNLRRFRKLSCYIMQDDVLIA 235
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT-SGTLLFEGEDistLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NlTVREAMMVAANLKLGK-NMISYAKVVVVEEILETIgLKESVNtltcNLSGGQRKRLSIALELVNNPPVMFFDEPTSGL 314
Cdd:PRK10247 95 D-TVYDNLIFPWQIRNQQpDPAIFLDDLERFALPDTI-LTKNIA----ELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
...
gi 161076684 315 DSS 317
Cdd:PRK10247 169 DES 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
159-329 |
5.52e-11 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 65.86 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGF--KTI-----LKSVSGKFRNGEITAIMGPSGAGKSTL-MNILagyktaQL---SGSVLINS------KERNLRRFR 221
Cdd:COG4172 288 KRGLfrRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTLgLALL------RLipsEGEIRFDGqdldglSRRALRPLR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 KLSCYIMQDDV--LIANLTVREamMVAANLKLGKNMISYAKVV-VVEEILETIGLKESvntlTCN-----LSGGQRKRLS 293
Cdd:COG4172 362 RRMQVVFQDPFgsLSPRMTVGQ--IIAEGLRVHGPGLSAAERRaRVAEALEEVGLDPA----ARHrypheFSGGQRQRIA 435
|
170 180 190
....*....|....*....|....*....|....*.
gi 161076684 294 IALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSL 329
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL 471
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
159-366 |
6.49e-11 |
|
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: 62.94 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAqlSGSVLINskernlrrfRKLSCYI-----MQDDv 232
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPD--SGTVTVR---------GRVSSLLglgggFNPE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 233 lianLTVRE-AMMVAANLKLGKNMISyakvVVVEEILETIGLKESVNTLTCNLSGGQRKRL--SIALELvnNPPVMFFDE 309
Cdd:cd03220 99 ----LTGREnIYLNGRLLGLSRKEID----EKIDEIIEFSELGDFIDLPVKTYSSGMKARLafAIATAL--EPDILLIDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 310 PTSGLDSStcFQL--ISLLRSLARGGRTIVCTIHQPSarLFEKF-DHLYLLAQGQCVYEG 366
Cdd:cd03220 169 VLAVGDAA--FQEkcQRRLRELLKQGKTVILVSHDPS--SIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
128-372 |
7.16e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.50 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 128 KKGTIALSHLPQRPPVDI-EFCdisYSVTDshrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMN-ILAGYKTAQls 205
Cdd:PRK10789 301 KDGSEPVPEGRGELDVNIrQFT---YPQTD------HPALENVNFTLKPGQMLGICGPTGSGKSTLLSlIQRHFDVSE-- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 206 GSVlinskernlrRFRKLSCYIMQDDVLIANLTVREAM------MVAANLKLGK-----NMISYAKVV--VVEEILE-TI 271
Cdd:PRK10789 370 GDI----------RFHDIPLTKLQLDSWRSRLAVVSQTpflfsdTVANNIALGRpdatqQEIEHVARLasVHDDILRlPQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 272 GLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIHQPSArLFEKf 351
Cdd:PRK10789 440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSA-LTEA- 516
|
250 260
....*....|....*....|.
gi 161076684 352 DHLYLLAQGQCVYEGRVKGLV 372
Cdd:PRK10789 517 SEILVMQHGHIAQRGNHDQLA 537
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
176-371 |
8.66e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRK-----LSCyIMQDDVLIANLTvreammVAANLK 250
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRD-AGSILYLGKEVTFNGPKSsqeagIGI-IHQELNLIPQLT------IAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 251 LGKNMIS----------YAKvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCF 320
Cdd:PRK10762 102 LGREFVNrfgridwkkmYAE---ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 161076684 321 QLISLLRSLARGGRTIVCTIHqpsaRLFEKF---DHLYLLAQGQCVYEGRVKGL 371
Cdd:PRK10762 179 SLFRVIRELKSQGRGIVYISH----RLKEIFeicDDVTVFRDGQFIAEREVADL 228
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
176-341 |
9.89e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE-RNLRRFRKLScYIMQDDVLIANLTVREAMMVAANL--KLG 252
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTaTRGDRSRFMA-YLGHLPGLKADLSTLENLHFLCGLhgRRA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 253 KNMISYAkvvvveeiLETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG 332
Cdd:PRK13543 115 KQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRG 186
|
....*....
gi 161076684 333 GRTIVCTIH 341
Cdd:PRK13543 187 GGAALVTTH 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
165-315 |
1.12e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.09 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINS--------KERNLrrfrklscyIM--QDDVLI 234
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERIT-SGEIWIGGrvvnelepADRDI---------AMvfQNYALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 235 ANLTVREAMmvAANLK---LGKNMISyAKVVVVEEILETIGL-----KEsvntltcnLSGGQRKRLSIALELVNNPPVMF 306
Cdd:PRK11650 89 PHMSVRENM--AYGLKirgMPKAEIE-ERVAEAARILELEPLldrkpRE--------LSGGQRQRVAMGRAIVREPAVFL 157
|
....*....
gi 161076684 307 FDEPTSGLD 315
Cdd:PRK11650 158 FDEPLSNLD 166
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
165-318 |
1.17e-10 |
|
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: 62.04 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLmnILAGYKTAQL-SGSVLINSKE------RNLRRfrKLSCyIMQDDVLIANl 237
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLEAeEGKIEIDGIDistiplEDLRS--SLTI-IPQDPTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVReammvaANLKLgKNMISYakvvvvEEILETIGLKESVNtltcNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:cd03369 97 TIR------SNLDP-FDEYSD------EEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
.
gi 161076684 318 T 318
Cdd:cd03369 160 T 160
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
159-329 |
1.43e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSKERNLRRFRKLSC---YIMQDDVLIA 235
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM-IEPTSGELLIDDHPLHFGDYSYRSQrirMIFQDPSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAMMVAANLKLGKNMISYAKVVVVEEILETIGL-KESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGL 314
Cdd:PRK15112 101 NPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170
....*....|....*
gi 161076684 315 DSSTCFQLISLLRSL 329
Cdd:PRK15112 181 DMSMRSQLINLMLEL 195
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
166-365 |
1.44e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRfrklSCYIMQDDVLIA--NLTVREAM 243
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAT-SGRIVFDGKDITDWQ----TAKIMREAVAIVpeGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 244 MVAANLKLGKnmiSYAKVVVVEEILETI-----GLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSST 318
Cdd:PRK11614 96 TVEENLAMGG---FFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 161076684 319 CFQLISLLRSLARGGRTIVcTIHQPSARLFEKFDHLYLLAQGQCVYE 365
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIF-LVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
174-332 |
1.80e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 174 RNGEITAIMGPSGAGKSTLMNILAGYKTAQLSGSVLINSKERNLRRFR--KLSCYIMQddvlIANLTVREAMmvaanlkl 251
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRgtELQNYFKK----LYNGEIKVVH-------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 252 gKN-MISYA-KVV---------------VVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGL 314
Cdd:PRK13409 165 -KPqYVDLIpKVFkgkvrellkkvdergKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170
....*....|....*...
gi 161076684 315 DSSTCFQLISLLRSLARG 332
Cdd:PRK13409 244 DIRQRLNVARLIRELAEG 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
153-331 |
1.83e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKS-TLMNIL-------AGYKTA--QLSGSVLINSKERNLRRFR- 221
Cdd:PRK15134 12 SVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppVVYPSGdiRFHGESLLHASEQTLRGVRg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 -KLScYIMQDDVLIAN-LTVREAMMvAANLKLGKNMISYAKVVVVEEILETIGLKESVNTLT---CNLSGGQRKRLSIAL 296
Cdd:PRK15134 92 nKIA-MIFQEPMVSLNpLHTLEKQL-YEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGERQRVMIAM 169
|
170 180 190
....*....|....*....|....*....|....*
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR 331
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQ 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
163-315 |
1.90e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.10 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTL------MNILAGYKTaqLSGSVLINSKerNLRRFRKLSCYIMQDDVLIAN 236
Cdd:PRK14239 18 KKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLNPEVT--ITGSIVYNGH--NIYSPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREAMMVAANLKLGKNMISYAKVVVVEEILET--IG------LKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFD 308
Cdd:PRK14239 94 QPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKslKGasiwdeVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
....*..
gi 161076684 309 EPTSGLD 315
Cdd:PRK14239 174 EPTSALD 180
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
166-342 |
2.20e-10 |
|
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: 61.19 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyKTAQLSGSVLINSK-------ERNLRRFRKLSCYIMQDDVLIaNLT 238
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTLEGKVHWSNKnesepsfEATRSRNRYSVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREammvaaNLKLGK--NMISYAKVVVVEEILETIGL-----KESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPT 311
Cdd:cd03290 95 VEE------NITFGSpfNKQRYKAVTDACSLQPDIDLlpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|...
gi 161076684 312 SGLDSSTCFQLIS--LLRSLARGGRTIVCTIHQ 342
Cdd:cd03290 169 SALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
161-331 |
3.46e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.55 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKFRNGEITAIMGPSGAGKS-TLMNI--LAGYKTAQLSGSVLINSK------ERNLRRFR--KLSCyIMQ 229
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIlrLLPDPAAHPSGSILFDGQdllglsERELRRIRgnRIAM-IFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 230 DDvlianltvreamMVAAN------------LKLGKNMISYAKVVVVEEILETIGLKESVNTLTC---NLSGGQRKRLSI 294
Cdd:COG4172 100 EP------------MTSLNplhtigkqiaevLRLHRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQRVMI 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 161076684 295 ALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLAR 331
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQR 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
163-380 |
5.34e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQL-SGSVLInsKERNLRRF----RKLSCYIM--QDDVLIA 235
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVtGGTVEF--KGKDLLELspedRAGEGIFMafQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 NLTVREAMMVAAN----LKLGKNMISYAKVVVVEEILETIGLKESVNTLTCNL--SGGQRKRLSIALELVNNPPVMFFDE 309
Cdd:PRK09580 92 GVSNQFFLQTALNavrsYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076684 310 PTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEGRVKgLVPYLSSLGY 380
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFT-LVKQLEEQGY 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
145-361 |
5.55e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYSVTDshrRGFKtiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE---RNLRRFR 221
Cdd:PRK10522 323 LELRNVTFAYQD---NGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ-SGEILLDGKPvtaEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 222 KLSCYIMQDDVLIANLTVREAMMVAANLklgknmisyakvvvVEEILETIGLKESVN-----TLTCNLSGGQRKRLSIAL 296
Cdd:PRK10522 397 KLFSAVFTDFHLFDQLLGPEGKPANPAL--------------VEKWLERLKMAHKLEledgrISNLKLSKGQKKRLALLL 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076684 297 ELVNNPPVMFFDEPTSglDSSTCF------QLISLLRSLargGRTIVCTIHQPSarLFEKFDHLYLLAQGQ 361
Cdd:PRK10522 463 ALAEERDILLLDEWAA--DQDPHFrrefyqVLLPLLQEM---GKTIFAISHDDH--YFIHADRLLEMRNGQ 526
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
159-372 |
6.01e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKT-------AQLSGSVLINSK---ERNLRRFRKLSCYIM 228
Cdd:PRK13547 11 RRH-RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgARVTGDVTLNGEplaAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 229 QDDVLIANLTVREAMMvaanlkLGK-------NMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVN- 300
Cdd:PRK13547 90 QAAQPAFAFSAREIVL------LGRypharraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 301 --------NPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTI-HQP--SARlfeKFDHLYLLAQGQCVYEGRVK 369
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPnlAAR---HADRIAMLADGAIVAHGAPA 240
|
...
gi 161076684 370 GLV 372
Cdd:PRK13547 241 DVL 243
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
161-327 |
6.29e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyktaqlsgsvLINSKERNLRRFRKLSC-YIMQDDVLIAN--L 237
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG----------LVAPDEGVIKRNGKLRIgYVPQKLYLDTTlpL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREAMMVAANLKlGKNMISYAKVVVVEEILETIGLKesvntltcnLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:PRK09544 85 TVNRFLRLRPGTK-KEDILPALKRVQAGHLIDAPMQK---------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170
....*....|...
gi 161076684 318 ---TCFQLISLLR 327
Cdd:PRK09544 155 gqvALYDLIDQLR 167
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
159-316 |
7.21e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.66 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLRRFRKLS-CYIMQDDVLIANL 237
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPT-EGQIFIDGEDVTHRSIQQRDiCMVFQSYALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREammvaaNLKLGKNMISYAKVVV---VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGL 314
Cdd:PRK11432 94 SLGE------NVGYGLKMLGVPKEERkqrVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
..
gi 161076684 315 DS 316
Cdd:PRK11432 168 DA 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
152-337 |
1.01e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 152 YSVTDSHRRgfktILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQLSGSVLINSKERNLRRFRKLS----CYI 227
Cdd:PRK13549 268 WDPVNPHIK----RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQAIaqgiAMV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 228 MQD---DVLIAnltvreAMMVAANLKLGkNMISYAKVVVVEEILETIGLKESVNTLTC----------NLSGGQRKRLSI 294
Cdd:PRK13549 344 PEDrkrDGIVP------VMGVGKNITLA-ALDRFTGGSRIDDAAELKTILESIQRLKVktaspelaiaRLSGGNQQKAVL 416
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 161076684 295 ALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIV 337
Cdd:PRK13549 417 AKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAII 459
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
163-348 |
1.04e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.75 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyktaqL----SGSVLINSKERNLrrF--RKLscYIMQDdvlian 236
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-----LwpygSGRIARPAGARVL--FlpQRP--YLPLG------ 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 lTVREAmmvaanlklgknmISYAKVV------VVEEILETIGLKESVNTLTCN------LSGGQRKRLSIALELVNNPPV 304
Cdd:COG4178 441 -TLREA-------------LLYPATAeafsdaELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDW 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 161076684 305 MFFDEPTSGLDSSTCFQLISLLRSLARGGrTIVCTIHQPSARLF 348
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREELPGT-TVISVGHRSTLAAF 549
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
169-329 |
1.23e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.52 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 169 VSGKFRNGEITAIMGPSGAGKSTLMNILAGyktaqL----SGSVLINSKE------RNLRRFRKLSCYIMQD--DVLIAN 236
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLR-----LeeptSGEILFDGQDitglsgRELRPLRRRMQMVFQDpyASLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 LTVREamMVAANLKLGKNMISYAKVVVVEEILETIGLK-ESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:COG4608 112 MTVGD--IIAEPLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170
....*....|....
gi 161076684 316 SSTCFQLISLLRSL 329
Cdd:COG4608 190 VSIQAQVLNLLEDL 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
166-401 |
1.39e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.80 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTL------MNILAgyKTAQLSGSVLINSKErnlrrfrklscyIMQDDVLIANLTV 239
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnrLNDLI--PGFRVEGKVTFHGKN------------LYAPDVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 240 REAMM----------VAANLKLGKNMISYAKVV--VVEEILETIGL----KESVNTLTCNLSGGQRKRLSIALELVNNPP 303
Cdd:PRK14243 92 RIGMVfqkpnpfpksIYDNIAYGARINGYKGDMdeLVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 304 VMFFDEPTSGLDSSTCFQLISLLRSLARgGRTIVCTIH--QPSARL--FEKFDHLYLLAQGqcvyeGRVKGLVPY-LSSL 378
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHnmQQAARVsdMTAFFNVELTEGG-----GRYGYLVEFdRTEK 245
|
250 260
....*....|....*....|...
gi 161076684 379 GYECPSYHNPADYVlevaSGEYG 401
Cdd:PRK14243 246 IFNSPQQQATRDYV----SGRFG 264
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
145-369 |
1.53e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.32 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDIS--YSVTDSHRRGFK--------------TILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YK-TaqlSG 206
Cdd:COG1134 5 IEVENVSksYRLYHEPSRSLKelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEpT---SG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 207 SVLINSKernlrrfrklscyimqddV--LIA-------NLTVRE-AMMVAANLKLGKNMISYakvvVVEEILETIGLKES 276
Cdd:COG1134 82 RVEVNGR------------------VsaLLElgagfhpELTGREnIYLNGRLLGLSRKEIDE----KFDEIVEFAELGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 277 VNTLTCNLSGGQRKRL--SIALELvnNPPVMFFDEPTSGLDSStcFQ--LISLLRSLARGGRTIVCTIHQPSArlFEKF- 351
Cdd:COG1134 140 IDQPVKTYSSGMRARLafAVATAV--DPDILLVDEVLAVGDAA--FQkkCLARIRELRESGRTVIFVSHSMGA--VRRLc 213
|
250
....*....|....*...
gi 161076684 352 DHLYLLAQGQCVYEGRVK 369
Cdd:COG1134 214 DRAIWLEKGRLVMDGDPE 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
153-315 |
1.74e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.20 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRRgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKE---RNLRRFRKLS-CYIM 228
Cdd:COG3845 264 SVRDDRGV---PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA-SGSIRLDGEDitgLSPRERRRLGvAYIP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 229 QD---DVLIANLTVREAMMVAA--NLKLGKN-MISYAKVV-VVEEILETIGLK-ESVNTLTCNLSGGQRKRLSIALELVN 300
Cdd:COG3845 340 EDrlgRGLVPDMSVAENLILGRyrRPPFSRGgFLDRKAIRaFAEELIEEFDVRtPGPDTPARSLSGGNQQKVILARELSR 419
|
170
....*....|....*
gi 161076684 301 NPPVMFFDEPTSGLD 315
Cdd:COG3845 420 DPKLLIAAQPTRGLD 434
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
176-331 |
1.84e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK------ERNLRRFRKLSCYIMQDDV--LIANLTVREAMMvaA 247
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQ-GGEIIFNGQridtlsPGKLQALRRDIQFIFQDPYasLDPRQTVGDSIM--E 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 248 NLKLGKNMISYAKVVVVEEILETIGLK-ESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLL 326
Cdd:PRK10261 427 PLRVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
....*
gi 161076684 327 RSLAR 331
Cdd:PRK10261 507 LDLQR 511
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
169-371 |
2.04e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 169 VSGKFRNGEITAIMGPSGAGKS----TLMNIL-AGykTAQLSGSVLINSKERNLRRFR-KLSCYIMQDDVLIAN--LTVR 240
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaAALGILpAG--VRQTAGRVLLDGKPVAPCALRgRKIATIMQNPRSAFNplHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 eAMMVAANLKLGKNmisyAKVVVVEEILETIGLKESVNTLTC---NLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:PRK10418 100 -THARETCLALGKP----ADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 318 TCFQLISLLRSLARG---GRTIVCTIHQPSARLfekFDHLYLLAQGQCVYEGRVKGL 371
Cdd:PRK10418 175 AQARILDLLESIVQKralGMLLVTHDMGVVARL---ADDVAVMSHGRIVEQGDVETL 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
160-341 |
2.36e-09 |
|
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: 60.59 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 160 RGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLIN--------SKERNLRRFR--KLSCYIMQ 229
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGV-LEPTSGEVNVRvgdewvdmTKPGPDGRGRakRYIGILHQ 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 230 DDVLIANLTVREAMMVAANLKLGKNMISYAKVVVveeiLETIGLKES-----VNTLTCNLSGGQRKRLSIALELVNNPPV 304
Cdd:TIGR03269 373 EYDLYPHRTVLDNLTEAIGLELPDELARMKAVIT----LKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190
....*....|....*....|....*....|....*...
gi 161076684 305 MFFDEPTSGLDSSTCFQLI-SLLRSLARGGRTIVCTIH 341
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSH 486
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
163-341 |
2.67e-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: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKT-----AQLSGSVLINskernlrrfrklscYIMQDDVLIANL 237
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKdfngeARPQPGIKVG--------------YLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREAMM---------------VAANL--------KLGKNMisyAKvvvVEEILETIG-------LKESVNTLTC----- 282
Cdd:TIGR03719 84 TVRENVEegvaeikdaldrfneISAKYaepdadfdKLAAEQ---AE---LQEIIDAADawdldsqLEIAMDALRCppwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076684 283 ---NLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTcfqlISLL-RSLARGGRTIVCTIH 341
Cdd:TIGR03719 158 dvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLeRHLQEYPGTVVAVTH 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
169-315 |
3.53e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 169 VSGKFRNGEITAIMGPSGAGKSTLMNILAGY-----KTAQLSGSVlINSKERNLRRfRklSCYIMQDDVLIANLTVREAM 243
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLlpaseGEAWLFGQP-VDAGDIATRR-R--VGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076684 244 MVAANL-KLGKNMISYAkvvvVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:NF033858 361 ELHARLfHLPAAEIAAR----VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
163-366 |
4.12e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 60.56 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLinsKERNLrrfrklsCYIMQDdVLIANLTVREA 242
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS-EGRVW---AERSI-------AYVPQQ-AWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 243 MMV-----AANLklgknmisyAKVVVVEEI----------LET-IGLKesvntlTCNLSGGQRKRLSIALELVNNPPVMF 306
Cdd:PTZ00243 741 ILFfdeedAARL---------ADAVRVSQLeadlaqlgggLETeIGEK------GVNLSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076684 307 FDEPTSGLDSSTCFQLIS--LLRSLArgGRTIVCTIHQpsARLFEKFDHLYLLAQGQCVYEG 366
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVEecFLGALA--GKTRVLATHQ--VHVVPRADYVVALGDGRVEFSG 863
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
144-366 |
4.38e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEFCDISYSVTDSHRRGFKTiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN--------SKER 215
Cdd:PRK13645 6 DIILDNVSYTYAKKTPFEFKA-LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISE-TGQTIVGdyaipanlKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 216 NLRRFRKLSCYIMQ--DDVLIANLTVREAMMVAANLKLGKNMIsYAKVvvvEEILETIGL-KESVNTLTCNLSGGQRKRL 292
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEA-YKKV---PELLKLVQLpEDYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076684 293 SIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARG-GRTIVCTIHQPSaRLFEKFDHLYLLAQGQCVYEG 366
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
145-363 |
1.15e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 58.66 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYS-VTDSHRRGFktILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK---ERNLRRF 220
Cdd:COG4615 328 LELRGVTYRyPGEDGDEGF--TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE-SGEILLDGQpvtADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 RKLSCYIMQDDVLIANLTVREAMMVAAnlklgknmisyakvvVVEEILETIGLKE--SVNT---LTCNLSGGQRKRLSIA 295
Cdd:COG4615 405 RQLFSAVFSDFHLFDRLLGLDGEADPA---------------RARELLERLELDHkvSVEDgrfSTTDLSQGQRKRLALL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 296 LELVNNPPVMFFDE------PTsgldsstcF------QLISLLRslaRGGRTIVCTIHQPsaRLFEKFDHLYLLAQGQCV 363
Cdd:COG4615 470 VALLEDRPILVFDEwaadqdPE--------FrrvfytELLPELK---ARGKTVIAISHDD--RYFDLADRVLKMDYGKLV 536
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
169-367 |
1.33e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 169 VSGKFRNGEITAIMGPSGAGKStlMNILAGYKTAQLSGSVLINSKERNLRRFRKLS------------CYIMQDDVLIAN 236
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISekerrnlvgaevAMIFQDPMTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 --LTVREAMMVAANLKLGKNMISYAKVVVveEILETIGLKESVNTLTC---NLSGGQRKRLSIALELVNNPPVMFFDEPT 311
Cdd:PRK11022 104 pcYTVGFQIMEAIKVHQGGNKKTRRQRAI--DLLNQVGIPDPASRLDVyphQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 312 SGLDSSTCFQLISLLRSLARGGRTIVCTIHQPSARLFEKFDHLYLLAQGQCVYEGR 367
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
159-458 |
1.36e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 57.74 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 159 RRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILaGYKTAQLSGSVLINS------KERNLRRFR-KLSCYIMQDD 231
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLL-NRLIEPTRGQVLIDGvdiakiSDAELREVRrKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 232 VLIANLTVREammvaaNLKLGKNMISYAKVVVVEEILET---IGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFD 308
Cdd:PRK10070 116 ALMPHMTVLD------NTAFGMELAGINAEERREKALDAlrqVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 309 EPTSGLDSSTCFQLI-SLLRSLARGGRTIVCTIHQPSARLfEKFDHLYLLAQGQCVYEGRVKGLVpylsslgyecpsyHN 387
Cdd:PRK10070 190 EAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVGTPDEIL-------------NN 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161076684 388 PA-DYVLEVASGeygdavpklVDavksgACKKYAHKDyvltLAQKGCNNDIIKGSGSGAENAMAILTLEDEK 458
Cdd:PRK10070 256 PAnDYVRTFFRG---------VD-----ISQVFSAKD----IARRTPNGLIRKTPGFGPRSALKLLQDEDRE 309
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
152-329 |
1.67e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.28 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 152 YSVtdshRRGF---KTILKSVSG-KFR--NGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLIN---------SKERN 216
Cdd:PRK11308 15 YPV----KRGLfkpERLVKALDGvSFTleRGKTLAVVGESGCGKSTLARLLTMIETPT-GGELYYQgqdllkadpEAQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 217 LRR-----F---------RKLSCYIMQDDVLIanltvreammvaaNLKLGKNmisyAKVVVVEEILETIGLK-ESVNTLT 281
Cdd:PRK11308 90 LRQkiqivFqnpygslnpRKKVGQILEEPLLI-------------NTSLSAA----ERREKALAMMAKVGLRpEHYDRYP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 161076684 282 CNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSL 329
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
165-318 |
2.03e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNIL-----------------------------------AGYKTA------- 202
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgdeeqnVGMKNVnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 203 -----------QLSGSVL---INSKERNLRRFRKLSCYIMQDDVLIaNLTVREammvaaNLKLGK------NMISYAKVV 262
Cdd:PTZ00265 1263 eggsgedstvfKNSGKILldgVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYE------NIKFGKedatreDVKRACKFA 1335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 263 VVEEILETIGLKESVNT--LTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSST 318
Cdd:PTZ00265 1336 AIDEFIESLPNKYDTNVgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
163-329 |
2.16e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.28 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK---ERNLRRFRKLSCYIMQD-DVLIANLT 238
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGDlltEENVWDIRHKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 239 VREAmmVAANLKlgKNMISYAKVVV-VEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:PRK13650 99 VEDD--VAFGLE--NKGIPHEEMKErVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170
....*....|..
gi 161076684 318 TCFQLISLLRSL 329
Cdd:PRK13650 175 GRLELIKTIKGI 186
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
158-355 |
3.82e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.52 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 158 HRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNilagyktaQLSGSVLINSKERNLRRFRKLSCYimqddvlianl 237
Cdd:cd03227 3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILD--------AIGLALGGAQSATRRRSGVKAGCI----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 tvreammVAAnlklgknmisyakvVVVEEILETIGLkesvntltcnlSGGQRKRLSIALEL----VNNPPVMFFDEPTSG 313
Cdd:cd03227 64 -------VAA--------------VSAELIFTRLQL-----------SGGEKELSALALILalasLKPRPLYILDEIDRG 111
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 161076684 314 LDSSTCFQLISLLRSLARGGRTIVCTIHQPsaRLFEKFDHLY 355
Cdd:cd03227 112 LDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
138-366 |
4.04e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 138 PQRPPVDIEFCDISYSVTDShrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQLSGSVLInskernl 217
Cdd:PLN03232 610 PGAPAISIKNGYFSWDSKTS-----KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI------- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 218 rrfRKLSCYIMQDDvLIANLTVREAMMVAANLKLGKnmisYAKVVVVEEILETIGL-----KESVNTLTCNLSGGQRKRL 292
Cdd:PLN03232 678 ---RGSVAYVPQVS-WIFNATVRENILFGSDFESER----YWRAIDVTALQHDLDLlpgrdLTEIGERGVNISGGQKQRV 749
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076684 293 SIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQpsARLFEKFDHLYLLAQGQCVYEG 366
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEGMIKEEG 821
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
176-344 |
4.33e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYKTAQLSGSVLINskernlrrfrklscyimqddvliANLTVREAMMVAANLKLGKNM 255
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-----------------------GEDILEEVLDQLLLIIVGGKK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 256 ISyakvvvveeiletiglkesvntltcnLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLIS------LLRSL 329
Cdd:smart00382 59 AS--------------------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLLK 112
|
170
....*....|....*
gi 161076684 330 ARGGRTIVCTIHQPS 344
Cdd:smart00382 113 SEKNLTVILTTNDEK 127
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
176-318 |
5.13e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAG--------------YKTAQL--------SGSVL------INSKERNLRRFRKLSCYI 227
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdLIVARLqqdpprnvEGTVYdfvaegIEEQAEYLKRYHDISHLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 228 MQD--DVLIANLTVREAMMVAANLKLGKNMISyakvvvveEILETIGLkeSVNTLTCNLSGGQRKRLSIALELVNNPPVM 305
Cdd:PRK11147 109 ETDpsEKNLNELAKLQEQLDHHNLWQLENRIN--------EVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDVL 178
|
170
....*....|...
gi 161076684 306 FFDEPTSGLDSST 318
Cdd:PRK11147 179 LLDEPTNHLDIET 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
152-337 |
5.60e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 152 YSVTDSHRRgfktILKSVSGKFRNGEITAIMGPSGAGKSTL-MNILAGYKTAQLSGSVLINSKERNLRRFRK-----LSc 225
Cdd:NF040905 266 YHPLHPERK----VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNISGTVFKDGKEVDVSTVSDaidagLA- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 226 YIMQDDV---LIANLTVREAMmVAANL-KLGKNMI--SYAKVVVVEEILETIGLKE-SVNTLTCNLSGGQRKRLSIALEL 298
Cdd:NF040905 341 YVTEDRKgygLNLIDDIKRNI-TLANLgKVSRRGVidENEEIKVAEEYRKKMNIKTpSVFQKVGNLSGGNQQKVVLSKWL 419
|
170 180 190
....*....|....*....|....*....|....*....
gi 161076684 299 VNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIV 337
Cdd:NF040905 420 FTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVI 458
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
145-357 |
6.89e-08 |
|
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: 52.93 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 145 IEFCDISYsVTDSHRrgfkTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyktaqL----SGSVLINSKERNLrrf 220
Cdd:cd03223 1 IELENLSL-ATPDGR----VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-----LwpwgSGRIGMPEGEDLL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 221 rklscYIMQDDVLIAnLTVREAmmvaanlklgknmISYA--KVvvveeiletiglkesvntltcnLSGGQRKRLSIALEL 298
Cdd:cd03223 68 -----FLPQRPYLPL-GTLREQ-------------LIYPwdDV----------------------LSGGEQQRLAFARLL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 299 VNNPPVMFFDEPTSGLDSSTCFQLISLLRSLargGRTIVCTIHQPSARLFekFDHLYLL 357
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHRPSLWKF--HDRVLDL 160
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
160-316 |
8.37e-08 |
|
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: 56.11 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 160 RGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyKTAQLSGSVLInskernlrrfrKLSCYIMQDDVLIANLTV 239
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA-EMDKVEGHVHM-----------KGSVAYVPQQAWIQNDSL 715
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 240 REAMMVAANL--KLGKNMISYAKVVVVEEILETiGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:TIGR00957 716 RENILFGKALneKYYQQVLEACALLPDLEILPS-GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
161-315 |
9.08e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 9.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKtiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSkernlrrfrKLSC---YIMQDdvliANL 237
Cdd:PRK13409 352 DFS--LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPD-EGEVDPEL---------KISYkpqYIKPD----YDG 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 238 TVREAMMVAANlKLGKNMISyakvvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:PRK13409 416 TVEDLLRSITD-DLGSSYYK-------SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
163-315 |
1.05e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKT-----AQLSGSVLINskernlrrfrklscYIMQDDVLIANL 237
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKefegeARPAPGIKVG--------------YLPQEPQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 238 TVREAMM---------------VAANL--------KLGKNMisyAKvvvVEEILETIG-------LKESVNTLTC----- 282
Cdd:PRK11819 86 TVRENVEegvaevkaaldrfneIYAAYaepdadfdALAAEQ---GE---LQEIIDAADawdldsqLEIAMDALRCppwda 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 161076684 283 ---NLSGGQRKRLSIALELVNNPPVMFFDEPTSGLD 315
Cdd:PRK11819 160 kvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
150-316 |
1.09e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.95 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 150 ISYSVTDSHRRGFKtiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyktaqlsgsvLINSKERNLRRFRKLSCYIMQ 229
Cdd:cd03237 1 YTYPTMKKTLGEFT--LEVEGGSISESEVIGILGPNGIGKTTFIKMLAG----------VLKPDEGDIEIELDTVSYKPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 230 DDVLIANLTVREAMMvaanlklGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDE 309
Cdd:cd03237 69 YIKADYEGTVRDLLS-------SITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
....*..
gi 161076684 310 PTSGLDS 316
Cdd:cd03237 142 PSAYLDV 148
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
139-340 |
2.83e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.71 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 139 QRPPVDIEfcDISYSVTDSHRRGfktiLKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK---ER 215
Cdd:PRK13635 2 KEEIIRVE--HISFRYPDAATYA----LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-AGTITVGGMvlsEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 216 NLRRFRKLSCYIMQD-DVLIANLTVREAmmVAANLKlgKNMISYAKVVV-VEEILETIGLKESVNTLTCNLSGGQRKRLS 293
Cdd:PRK13635 75 TVWDVRRQVGMVFQNpDNQFVGATVQDD--VAFGLE--NIGVPREEMVErVDQALRQVGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 161076684 294 IALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTI 340
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSI 197
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
166-371 |
4.32e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYkTAQLSGSVLINSKERNLrrfrKLSCYIMQDDVLIA----NLTVRE 241
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGI-YQKDSGSILFQGKEIDF----KSSKEALENGISMVhqelNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 242 AMMvaANLKLG----KNM-ISYAKV-----VVVEEILETIGLKESVNTltcnLSGGQRKRLSIALELVNNPPVMFFDEPT 311
Cdd:PRK10982 89 SVM--DNMWLGryptKGMfVDQDKMyrdtkAIFDELDIDIDPRAKVAT----LSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 312 SGLDSSTCFQLISLLRSLARGGRTIVCTIHQpSARLFEKFDHLYLLAQGQCVYEGRVKGL 371
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHK-MEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
166-344 |
4.45e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.78 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNIlAGYKTAQLSgsvLINSKERNlrrFRKLSCYIMQDDVLIA-NLTVreamm 244
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-GLYASGKAR---LISFLPKF---SRNKLIFIDQLQFLIDvGLGY----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 245 vaanLKLGKNMISyakvvvveeiletiglkesvntltcnLSGGQRKRLSIALEL-VNNPPVMF-FDEPTSGLDSSTCFQL 322
Cdd:cd03238 79 ----LTLGQKLST--------------------------LSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQL 128
|
170 180
....*....|....*....|..
gi 161076684 323 ISLLRSLARGGRTIVCTIHQPS 344
Cdd:cd03238 129 LEVIKGLIDLGNTVILIEHNLD 150
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
165-387 |
5.77e-07 |
|
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: 53.38 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyktaQLSGSvliNSKERNLRR--FRKLSCYIMQDdvlianlTVREA 242
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG----ELEPS---EGKIKHSGRisFSPQTSWIMPG-------TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 243 MMVAanlkLGKNMISYAKVVVVEEILETIG-LKESVNTLT----CNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSS 317
Cdd:TIGR01271 507 IIFG----LSYDEYRYTSVIKACQLEEDIAlFPEKDKTVLgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 161076684 318 TCFQLIS--LLRSLARGGRTIVCTihqpSARLFEKFDHLYLLAQGQCVYEG---RVKGLVPYLSSLGYECPSYHN 387
Cdd:TIGR01271 583 TEKEIFEscLCKLMSNKTRILVTS----KLEHLKKADKILLLHEGVCYFYGtfsELQAKRPDFSSLLLGLEAFDN 653
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
161-318 |
7.38e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyKTAQLSGSVLINSKER--NLRR-------FRKLSCYIMQDD 231
Cdd:PRK15064 12 GAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGG-DLEPSAGNVSLDPNERlgKLRQdqfafeeFTVLDTVIMGHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 232 VLIANLTVREAM-----------MVAANL--KLGKnMISYAKVVVVEEILETIGLKESV-NTLTCNLSGGQRKRLSIALE 297
Cdd:PRK15064 91 ELWEVKQERDRIyalpemseedgMKVADLevKFAE-MDGYTAEARAGELLLGVGIPEEQhYGLMSEVAPGWKLRVLLAQA 169
|
170 180
....*....|....*....|.
gi 161076684 298 LVNNPPVMFFDEPTSGLDSST 318
Cdd:PRK15064 170 LFSNPDILLLDEPTNNLDINT 190
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
165-342 |
8.94e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLI--NSKERNLRRFRKLSCYIMQDDVLIANLTVREA 242
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE-KGEILFerQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 243 MMVAANLKLGKnmisyakvVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQL 322
Cdd:PRK13540 95 CLYDIHFSPGA--------VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|
gi 161076684 323 ISLLRSLARGGRTIVCTIHQ 342
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
160-355 |
1.05e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 50.30 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 160 RGFKTILKSVSGKFRNGeITAIMGPSGAGKSTlmnILAGYKTAqLSGSVLINSKERNlrrfrklscyimQDDVLIANLTV 239
Cdd:cd03240 7 RNIRSFHERSEIEFFSP-LTLIVGQNGAGKTT---IIEALKYA-LTGELPPNSKGGA------------HDPKLIREGEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 240 REAMMVAANLKLGKNMISYAKVVVVEE------------ILETIGlkesvntltcNLSGGQRKRLSIALELV------NN 301
Cdd:cd03240 70 RAQVKLAFENANGKKYTITRSLAILENvifchqgesnwpLLDMRG----------RCSGGEKVLASLIIRLAlaetfgSN 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 302 PPVMFFDEPTSGLDSSTC-FQLISLLRSLAR-GGRTIVCTIHQPsaRLFEKFDHLY 355
Cdd:cd03240 140 CGILALDEPTTNLDEENIeESLAEIIEERKSqKNFQLIVITHDE--ELVDAADHIY 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
165-318 |
1.99e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 165 ILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAG-YKTAQlsGSVLINS----KERNLRRFRKLSCYIMQDDVLIAN--- 236
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERlYDPTE--GDIIINDshnlKDINLKWWRSKIGVVSQDPLLFSNsik 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 ---------LTVREAM-----------------------MVAANLKLGKNMISYAKVVVVEEILETIGLKESVN------ 278
Cdd:PTZ00265 478 nnikyslysLKDLEALsnyynedgndsqenknkrnscraKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDvskkvl 557
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 279 -------------TLT----CNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSST 318
Cdd:PTZ00265 558 ihdfvsalpdkyeTLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
284-396 |
4.76e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 284 LSGGQRKRLSIALELVN---NPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHqpSARLFEKFDHL------ 354
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH--NMHVVKVADYVlelgpe 887
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161076684 355 ------YLLAqgQCVYEGRV-------KGLVPYLSS------LGYECPSYHNPADYVLEVA 396
Cdd:PRK00635 888 ggnlggYLLA--SCSPEELIhlhtptaKALRPYLSSpqelpyLPDPSPKPPVPADITIKNA 946
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
341-394 |
5.64e-06 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 49.52 E-value: 5.64e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 341 HQPSARLFEKFDHLYLLAQ-GQCVYEGRVKGLVPYLSSLGYECPSYHNPADY---VLE 394
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHfidILE 58
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
166-401 |
1.46e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.78 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGY-----KTAQLSGSVLINSKERNLRRfrKLSCYIMQDDVLIANLTVR 240
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfeefeGKVKIDGELLTAENVWNLRR--KIGMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 241 EAMMVAANlklGKNMISYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCF 320
Cdd:PRK13642 101 DDVAFGME---NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 321 QLISLLRSLARGGRTIVCTIHQPSARLFEKfDHLYLLAQGQCVYEGRVKGL-------------VPYLSSL-------GY 380
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSITHDLDEAASS-DRILVMKAGEIIKEAAPSELfatsedmveigldVPFSSNLmkdlrknGF 256
|
250 260
....*....|....*....|.
gi 161076684 381 ECPSYHNPADYVLEVASGEYG 401
Cdd:PRK13642 257 DLPEKYLSEDELVELLADKLR 277
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
176-366 |
2.34e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGYKTAQLSGSVLInskernlrrfRKLSCYIMQDDvLIANLTVREAMMVAANLKLGKnm 255
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVI----------RGTVAYVPQVS-WIFNATVRDNILFGSPFDPER-- 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 256 isYAKVVVVE------EILETIGLKEsVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSL 329
Cdd:PLN03130 710 --YERAIDVTalqhdlDLLPGGDLTE-IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKD 786
|
170 180 190
....*....|....*....|....*....|....*..
gi 161076684 330 ARGGRTIVCTIHQpsARLFEKFDHLYLLAQGQCVYEG 366
Cdd:PLN03130 787 ELRGKTRVLVTNQ--LHFLSQVDRIILVHEGMIKEEG 821
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
616-754 |
2.42e-05 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 47.38 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 616 FVSLFTTFTAMMPTILTFPTEMSVFVREHLN--------YWYSLKAFYFAKTIADMPFQIVFSSVYVLVVYYLTSQPMEL 687
Cdd:pfam12698 159 YAYYLVGLILMIIILIGAAIIAVSIVEEKESrikerllvSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIPFGNL 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161076684 688 ERVsmfVLICVLNSLVAQSLGLLIGAGM-NIETGVFLGPVTTIPTILFSGFFVNFDTIPGYLQWVTYV 754
Cdd:pfam12698 239 GLL---LLLFLLYGLAYIALGYLLGSLFkNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSI 303
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
153-361 |
2.60e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 153 SVTDSHRRGFKTILKSVsgkfRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSKERNLR----RFRKLSCYIM 228
Cdd:PRK15439 270 TVEDLTGEGFRNISLEV----RAGEILGLAGVVGAGRTELAETLYGLRPAR-GGRIMLNGKEINALstaqRLARGLVYLP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 229 QDdvlianltvREAMMVAANLKLGKNMISY------------AKVVVVEEILETIGLK-----ESVNTLtcnlSGGQRKR 291
Cdd:PRK15439 345 ED---------RQSSGLYLDAPLAWNVCALthnrrgfwikpaRENAVLERYRRALNIKfnhaeQAARTL----SGGNQQK 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 161076684 292 LSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTihqpSARL--FEKF-DHLYLLAQGQ 361
Cdd:PRK15439 412 VLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI----SSDLeeIEQMaDRVLVMHQGE 480
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
166-337 |
9.49e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTaQLSGSVLINSKERNLRR--------F-------RKLSCYIMQD 230
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIRE-KSAGTITLHGKKINNHNaneainhgFalvteerRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 231 ---DVLIANLtvrEAMMVAANLKLGKNMISYAKVVVVEEILETIGLKESVNTLtcnlSGGQRKRLSIALELVNNPPVMFF 307
Cdd:PRK10982 343 igfNSLISNI---RNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSL----SGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190
....*....|....*....|....*....|
gi 161076684 308 DEPTSGLDSSTCFQLISLLRSLARGGRTIV 337
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDKGII 445
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
268-341 |
1.03e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 1.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161076684 268 LETIGLKESVNTLtcnlSGGQRKRLSIALEL---VNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIH 341
Cdd:TIGR00630 818 LGYIRLGQPATTL----SGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
160-330 |
1.18e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 160 RGFKTILKSVSGKFRNGeITAIMGPSGAGKSTLMN--------------------ILAGYKTAQLSGSVLINSKERNLRR 219
Cdd:COG0419 8 ENFRSYRDTETIDFDDG-LNLIVGPNGAGKSTILEairyalygkarsrsklrsdlINVGSEEASVELEFEHGGKRYRIER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 220 -------FRKLSCYIMQDdvLIANL----TVREAMMVAANLKLGKNMiSYAKVVVVEEILETIGLKESVNTLTCNLSGGQ 288
Cdd:COG0419 87 rqgefaeFLEAKPSERKE--ALKRLlgleIYEELKERLKELEEALES-ALEELAELQKLKQEILAQLSGLDPIETLSGGE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 161076684 289 RKRLSIAlELVNnppvMFFDepTSGLDSSTCFQLISLLRSLA 330
Cdd:COG0419 164 RLRLALA-DLLS----LILD--FGSLDEERLERLLDALEELA 198
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
161-355 |
1.21e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.99 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKFRNGeITAIMGPSGAGKStlmNILAGYKTaqlsgsVLINSKERNLRRFRklscyiMQDdvLIAN---- 236
Cdd:cd03278 8 GFKSFADKTTIPFPPG-LTAIVGPNGSGKS---NIIDAIRW------VLGEQSAKSLRGEK------MSD--VIFAgset 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 237 ---LTVREAMMVAANLKLGKNMISYAKvvvVEEILETIGLKESVNTLtcnLSGGQRKRLSIAL----ELVNNPPVMFFDE 309
Cdd:cd03278 70 rkpANFAEVTLTFDNSDGRYSIISQGD---VSEIIEAPGKKVQRLSL---LSGGEKALTALALlfaiFRVRPSPFCVLDE 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 161076684 310 PTSGLDSSTCFQLISLLRSLARGGRTIVCTiHQPsaRLFEKFDHLY 355
Cdd:cd03278 144 VDAALDDANVERFARLLKEFSKETQFIVIT-HRK--GTMEAADRLY 186
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
171-316 |
1.35e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 171 GKFRNGEITAIMGPSGAGKSTLMNILAGyktaqlsgsvlinskernlrrfrklscyimqddVLIANltvreammvaanlk 250
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAG---------------------------------QLIPN-------------- 52
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161076684 251 lgknmisyakvvvvEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDS 316
Cdd:cd03222 53 --------------GDNDEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
154-347 |
2.11e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.07 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 154 VTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNilAGYKTAQLSGSVLINSKERN---LRRFRKLSCYIMQd 230
Cdd:cd03289 8 LTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRLLNTEGDIQIDGVSWNsvpLQKWRKAFGVIPQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 231 DVLIANLTVReammvaanlklgKNMISYAKvVVVEEIL---ETIGLKESVNTLT-----------CNLSGGQRKRLSIAL 296
Cdd:cd03289 85 KVFIFSGTFR------------KNLDPYGK-WSDEEIWkvaEEVGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLAR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 161076684 297 ELVNNPPVMFFDEPTSGLDSSTcFQLISLLRSLARGGRTIVCTIHQPSARL 347
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPIT-YQVIRKTLKQAFADCTVILSEHRIEAML 201
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
176-198 |
2.43e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 43.16 E-value: 2.43e-04
10 20
....*....|....*....|...
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAG 198
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLP 107
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
266-388 |
2.51e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 266 EILETIGLKES---VNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQ 342
Cdd:PRK15093 138 ELLHRVGIKDHkdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISH 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 161076684 343 PSARLFEKFDHLYLLAQGQCVYEGRVKGLV-----PYLSSLGYECPSYHNP 388
Cdd:PRK15093 218 DLQMLSQWADKINVLYCGQTVETAPSKELVttphhPYTQALIRAIPDFGSA 268
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
161-207 |
2.57e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 42.53 E-value: 2.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 161076684 161 GFKTILKSVSGKfrngeITAIMGPSGAGKSTLMNILAG---YKTAQLSGS 207
Cdd:pfam03193 96 GIEALKELLKGK-----TTVLAGQSGVGKSTLLNALLPeldLRTGEISEK 140
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
154-323 |
3.28e-04 |
|
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: 44.52 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 154 VTDSHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILagYKTAQLSGSVLINSKERN---LRRFRKLSCYIMQd 230
Cdd:TIGR01271 1223 LTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL--LRLLSTEGEIQIDGVSWNsvtLQTWRKAFGVIPQ- 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 231 DVLIANLTVReammvaanlklgKNMISYAKVVVVE--EILETIGLKESVNTLT-----------CNLSGGQRKRLSIALE 297
Cdd:TIGR01271 1300 KVFIFSGTFR------------KNLDPYEQWSDEEiwKVAEEVGLKSVIEQFPdkldfvlvdggYVLSNGHKQLMCLARS 1367
|
170 180
....*....|....*....|....*.
gi 161076684 298 LVNNPPVMFFDEPTSGLDSSTcFQLI 323
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVT-LQII 1392
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
209-344 |
6.15e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 209 LINSKERNLRRFRKLSCYIM-----QDDVLIANLTVREAMMVAANLKLGKNMISYAKVVVVEEILETIGLKESVNtltcN 283
Cdd:pfam13304 161 LLLEDWAVLDLAADLALFPDlkellQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAF----E 236
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 161076684 284 LSGGQRK---RLSIALELVNNPPVMFFDEPTSGLDSSTCFQLISLLRSLARGGRTIVCTIHQPS 344
Cdd:pfam13304 237 LSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
176-207 |
2.17e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 40.96 E-value: 2.17e-03
10 20 30
....*....|....*....|....*....|....*
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAG---YKTAQLSGS 207
Cdd:PRK00098 164 GKVTVLAGQSGVGKSTLLNALAPdleLKTGEISEA 198
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
158-267 |
3.34e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 39.56 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 158 HRRGFKTI---LKSVSGKFRNGEITAIMGPSGAGKSTLMNILA---GYKTAQLSGSVLINSKERNLRRFRKLscYIMQDD 231
Cdd:pfam03215 24 HKRKIKDVqewLDAMFLENAKHRILLISGPSGCGKSTVIKELSkelGPKYREWSNPTSFRSPPNQVTDFRGD--CIVNSR 101
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 161076684 232 VLIANLTVREAMMVAANL----KLGKNMISYAKVVVVEEI 267
Cdd:pfam03215 102 FLSQMESFSEFELKGARYlvmqKRGKNAQGNKKLILIEDL 141
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
144-213 |
3.82e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 3.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 144 DIEfcDISYSVTDshrrgfKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLINSK 213
Cdd:PRK11147 321 EME--NVNYQIDG------KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQAD-SGRIHCGTK 381
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
176-337 |
4.04e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 176 GEITAIMGPSGAGKSTLMNILAGyKTAQLSGSvLINSKERNLR-RFRKLSCYIMQD------DVLIAN-----LTVREam 243
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAG-ELPLLSGE-RQSQFSHITRlSFEQLQKLVSDEwqrnntDMLSPGeddtgRTTAE-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 244 MVAANLKlgknmisyaKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQLI 323
Cdd:PRK10938 105 IIQDEVK---------DPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170
....*....|....
gi 161076684 324 SLLRSLARGGRTIV 337
Cdd:PRK10938 176 ELLASLHQSGITLV 189
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
163-344 |
4.09e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 163 KTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGYKTAQlSGSVLInsKERNLRRFRKLSC-YIMQddvliaNLTVRE 241
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPS-SGNIYY--KNCNINNIAKPYCtYIGH------NLGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 242 AMMVAANLKLGKNMisYAKVVVVEEILETIGLKESVNTLTCNLSGGQRKRLSIALELVNNPPVMFFDEPTSGLDSSTCFQ 321
Cdd:PRK13541 84 EMTVFENLKFWSEI--YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDL 161
|
170 180
....*....|....*....|...
gi 161076684 322 LISLLRSLARGGRTIVCTIHQPS 344
Cdd:PRK13541 162 LNNLIVMKANSGGIVLLSSHLES 184
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
166-203 |
4.34e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 4.34e-03
10 20 30
....*....|....*....|....*....|....*....
gi 161076684 166 LKSVSGKFRNGEITAIMGPSGAGKSTLMN-ILagYKTAQ 203
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINeTL--YKALA 661
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
172-202 |
5.31e-03 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 39.77 E-value: 5.31e-03
10 20 30
....*....|....*....|....*....|....*..
gi 161076684 172 KFRNGEI------TAIMGPSGAGKSTLMNILAGYKTA 202
Cdd:pfam12631 84 TADRGRIlregikVVIVGKPNVGKSSLLNALLGEERA 120
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
230-337 |
5.54e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 230 DDVLiaNLTVREAMMVAANLKlgknmisyakvvVVEEILET--------IGLKESVNTLtcnlSGGQRKRLSIALEL--V 299
Cdd:COG0178 783 ADVL--DMTVEEALEFFENIP------------KIARKLQTlqdvglgyIKLGQPATTL----SGGEAQRVKLASELskR 844
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 161076684 300 NNPPVMF-FDEPTSGL---DSStcfQLISLLRSLARGGRTIV 337
Cdd:COG0178 845 STGKTLYiLDEPTTGLhfhDIR---KLLEVLHRLVDKGNTVV 883
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
162-347 |
6.24e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.51 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 162 FKTILKSVSGKFRNGEITAIMGPSGAGKSTLMniLAGYKTAQL-SGSVLINS---KERNLRRFRKLSCYIMQDDVLIA-- 235
Cdd:cd03288 33 LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLS--LAFFRMVDIfDGKIVIDGidiSKLPLHTLRSRLSIILQDPILFSgs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 236 ---NL---------TVREAMMVAanlKLgKNMISYAKVvvveeiletiGLKESVNTLTCNLSGGQRKRLSIALELVNNPP 303
Cdd:cd03288 111 irfNLdpeckctddRLWEALEIA---QL-KNMVKSLPG----------GLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 161076684 304 VMFFDEPTSGLDSSTCFQLISLLRSlARGGRTIVCTIHQPSARL 347
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVSTIL 219
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
174-208 |
6.28e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 6.28e-03
10 20 30
....*....|....*....|....*....|....*
gi 161076684 174 RNGEITAIMGPSGAGKSTLMNILAGyKTAQLSGSV 208
Cdd:PRK01889 193 SGGKTVALLGSSGVGKSTLVNALLG-EEVQKTGAV 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-196 |
7.17e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 7.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161076684 129 KGTIALSHLPQRPPVDIEFCDISysVTDSHRRGFKTILKSVSgkfRNGeITAIMGPSGAGKSTLM-NIL 196
Cdd:PRK00635 920 SSPQELPYLPDPSPKPPVPADIT--IKNAYQHNLKHIDLSLP---RNA-LTAVTGPSASGKHSLVfDIL 982
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
157-208 |
7.81e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 7.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 161076684 157 SHRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMNILAGyKTAQLSGSV 208
Cdd:PRK15064 326 TKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-ELEPDSGTV 376
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
158-315 |
9.84e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 158 HRRGFKTILKSVSGKFRNGEITAIMGPSGAGKSTLMniLAGYKTAQL-SGSVLINSKE---RNLRRFRKLSCYIMQDDVL 233
Cdd:PTZ00243 1318 YREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLL--LTFMRMVEVcGGEIRVNGREigaYGLRELRRQFSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161076684 234 IANlTVREammvaaNLklgkNMISYAKVVVVEEILETIGLKESVNTLT-----------CNLSGGQRKRLSIALELVN-N 301
Cdd:PTZ00243 1396 FDG-TVRQ------NV----DPFLEASSAEVWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARALLKkG 1464
|
170
....*....|....
gi 161076684 302 PPVMFFDEPTSGLD 315
Cdd:PTZ00243 1465 SGFILMDEATANID 1478
|
|
| |
