|
Name |
Accession |
Description |
Interval |
E-value |
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-504 |
0e+00 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 1019.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAG 83
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQELHLIPEMTVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAK 163
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 164 IIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDNMQEVNHDALVQAMVGR 243
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRDQLVQAMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 244 ELGDIYGWQPREYGKERLRLDRVKAPGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIR 323
Cdd:PRK11288 241 EIGDIYGYRPRPLGEVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 324 KPAQAIQAGMMLCPEDRKAEGIIPVHSVRDNINISARRKHILAGCVINNAWEAQNADQHIKSLNIKTPGAEQLIMNLSGG 403
Cdd:PRK11288 321 SPRDAIRAGIMLCPEDRKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQLIMNLSGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 404 NQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGELLH 483
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAR 480
|
490 500
....*....|....*....|.
gi 490204990 484 EHANEQQALSLAMPKVSQAVA 504
Cdd:PRK11288 481 EQATERQALSLALPRTSAAVA 501
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-502 |
0e+00 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 744.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAG 83
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQELHLIPEMTVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAK 163
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 164 IIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDnMQEVNHDALVQAMVGR 243
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGP-VAELTEDELVRLMVGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 244 ELGDIYGWQPREYGKERLRLDRVKAPGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIR 323
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVLEVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 324 KPAQAIQAGMMLCPEDRKAEGIIPVHSVRDNINISARRKHILAGcVINNAWEAQNADQHIKSLNIKTPGAEQLIMNLSGG 403
Cdd:COG1129 320 SPRDAIRAGIAYVPEDRKGEGLVLDLSIRENITLASLDRLSRGG-LLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 404 NQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGELLH 483
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDR 478
|
490
....*....|....*....
gi 490204990 484 EHANEQQALSLAMPKVSQA 502
Cdd:COG1129 479 EEATEEAIMAAATGGAAAA 497
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-495 |
0e+00 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 534.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYvPTA---GSLQIQGQQMTFTHTTEAL 80
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 81 NAGVAIIYQELHLIPEMTVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALAR 160
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 161 NAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTfDNMQEVNHDALVQAM 240
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT-RPAAGMTEDDIITMM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 241 VGRELGDIYGWQPREYGKERLRLDRVKAPGVRQP-------VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSR-ITAGQ 312
Cdd:PRK13549 240 VGRELTALYPREPHTIGEVILEVRNLTAWDPVNPhikrvddVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 313 VYIDGEAIDIRKPAQAIQAGMMLCPEDRKAEGIIPVHSVRDNINISARRKHILAGcVINNAWEAQNADQHIKSLNIKTPG 392
Cdd:PRK13549 320 IFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNITLAALDRFTGGS-RIDDAAELKTILESIQRLKVKTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 393 AEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVM 472
Cdd:PRK13549 399 PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
|
490 500
....*....|....*....|...
gi 490204990 473 REGEIAGELLHEHANEQQALSLA 495
Cdd:PRK13549 479 HEGKLKGDLINHNLTQEQVMEAA 501
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-504 |
6.92e-176 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 504.15 E-value: 6.92e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGV 84
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQELHLIPEMTVAENIYLGQLP-HKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAK 163
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFvNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 164 IIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDnMQEVNHDALVQAMVGR 243
Cdd:PRK10762 162 VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAERE-VADLTEDSLIEMMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 244 ELGDIYGWQPREYGKERLRLDRVKAPGVRQpVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIR 323
Cdd:PRK10762 241 KLEDQYPRLDKAPGEVRLKVDNLSGPGVND-VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 324 KPAQAIQAGMMLCPEDRKAEGIIPVHSVRDNINISARRKHILAGCVINNAWEAQNADQHIKSLNIKTPGAEQLIMNLSGG 403
Cdd:PRK10762 320 SPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 404 NQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGELLH 483
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTR 479
|
490 500
....*....|....*....|.
gi 490204990 484 EHANEQQALSLAMPKVSQAVA 504
Cdd:PRK10762 480 EQATQEKLMAAAVGKLNRVNQ 500
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-496 |
3.24e-163 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 471.82 E-value: 3.24e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAG 83
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQELHLIPEMTVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAK 163
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 164 IIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDNmQEVNHDALVQAMVGR 243
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDT-AETSEEELAELMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 244 ELGDIYGWQPREYGKERLRLDRVKAPGVR-----QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGE 318
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVENLSVRDDRgvpalKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 319 AIDIRKPAQAIQAGMMLCPEDRKAEGIIPVHSVRDNINISA-RRKHILAGCVINNAWEAQNADQHIKSLNIKTPGAEQLI 397
Cdd:COG3845 321 DITGLSPRERRRLGVAYIPEDRLGRGLVPDMSVAENLILGRyRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 398 MNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
490
....*....|....*....
gi 490204990 478 AGELLHEHANEQQaLSLAM 496
Cdd:COG3845 481 VGEVPAAEATREE-IGLLM 498
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-496 |
5.31e-163 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 471.20 E-value: 5.31e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYvPTA---GSLQIQGQQMTFTHTTEALNAGV 84
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQELHLIPEMTVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKI 164
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 165 IAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFD-NMQEVNHDALVQAMVGR 243
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDcRADEVTEDRIIRGMVGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 244 ELGDIYGWQPREYGKERLRldrVKAPGVRQP----------VSLSVRSGEIVGLFGLVGAGRSELMKGLFG---GSRITa 310
Cdd:NF040905 241 DLEDRYPERTPKIGEVVFE---VKNWTVYHPlhperkvvddVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsyGRNIS- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 311 GQVYIDGEAIDIRKPAQAIQAGMMLCPEDRKAEGIIPVHSVRDNINISARRKhILAGCVINNAWEAQNADQHIKSLNIKT 390
Cdd:NF040905 317 GTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKGYGLNLIDDIKRNITLANLGK-VSRRGVIDENEEIKVAEEYRKKMNIKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 391 PGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIV 470
Cdd:NF040905 396 PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIY 475
|
490 500
....*....|....*....|....*.
gi 490204990 471 VMREGEIAGELLHEHANeQQALSLAM 496
Cdd:NF040905 476 VMNEGRITGELPREEAS-QERIMRLI 500
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-497 |
1.64e-154 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 450.01 E-value: 1.64e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmTFTHTTEALNA-- 82
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI--NYNKLDHKLAAql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 GVAIIYQELHLIPEMTVAENIYLGQLPHKG----GIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKAL 158
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 159 ARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDnMQEVNHDALVQ 238
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGM-VSDVSNDDIVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 239 AMVGRELGDIYGWQPREYG----------KERLRLDRVKApgvrQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRI 308
Cdd:PRK09700 240 LMVGRELQNRFNAMKENVSnlahetvfevRNVTSRDRKKV----RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 309 TAGQVYIDGEAIDIRKPAQAIQAGMMLCPEDRKAEGIIPVHSVRDNINISARRKhiLAGC-----VINNAWEAQNADQHI 383
Cdd:PRK09700 316 AGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLK--DGGYkgamgLFHEVDEQRTAENQR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 384 KSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVL 463
Cdd:PRK09700 394 ELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEII 473
|
490 500 510
....*....|....*....|....*....|....*
gi 490204990 464 GVADRIVVMREGEIAGELLH-EHANEQQALSLAMP 497
Cdd:PRK09700 474 TVCDRIAVFCEGRLTQILTNrDDMSEEEIMAWALP 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-496 |
1.78e-147 |
|
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: 431.56 E-value: 1.78e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYvPTA---GSLQIQGQQMTFTHTTEALNAGV 84
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQELHLIPEMTVAENIYLG-QLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPET-PLKYLSIGQWQMVEIAKALARNA 162
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 163 KIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDnMQEVNHDALVQAMVG 242
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKD-MSTMSEDDIITMMVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 243 RELGDIYGWQPREYGKERLRLDRVKAPGVRQP-------VSLSVRSGEIVGLFGLVGAGRSELMKGLFGG-SRITAGQVY 314
Cdd:TIGR02633 240 REITSLYPHEPHEIGDVILEARNLTCWDVINPhrkrvddVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 315 IDGEAIDIRKPAQAIQAGMMLCPEDRKAEGIIPVHSVRDNINISARRKHILAGcVINNAWEAQNADQHIKSLNIKTPGAE 394
Cdd:TIGR02633 320 INGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKM-RIDAAAELQIIGSAIQRLKVKTASPF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 395 QLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMRE 474
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGE 478
|
490 500
....*....|....*....|..
gi 490204990 475 GEIAGELLHEHANEQQALSLAM 496
Cdd:TIGR02633 479 GKLKGDFVNHALTQEQVLAAAL 500
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-495 |
2.81e-138 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 407.96 E-value: 2.81e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 12 GITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVAIIYQEL 91
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 92 HLIPEMTVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPT 171
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 172 SSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTfDNMQEVNHDALVQAMVGRELGDIY-- 249
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT-QPLAGLTMDKIIAMMVGRSLTQRFpd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 250 -GWQPREYGKERLRLDRVKAPGVrQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQA 328
Cdd:PRK10982 242 kENKPGEVILEVRNLTSLRQPSI-RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 329 IQAGMMLCPEDRKAEGIIPVHSVRDNINISARRKHILAGCVINNAWEAQNADQHIKSLNIKTPGAEQLIMNLSGGNQQKA 408
Cdd:PRK10982 321 INHGFALVTEERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 409 ILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGELLHEHANE 488
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGIVDTKTTTQ 480
|
....*..
gi 490204990 489 QQALSLA 495
Cdd:PRK10982 481 NEILRLA 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-495 |
8.87e-122 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 366.30 E-value: 8.87e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGV 84
Cdd:PRK15439 9 PPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQELHLIPEMTVAENIYLGqLPHKGGIVNRsllnyeagLQ--LQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNA 162
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFG-LPKRQASMQK--------MKqlLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 163 KIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGrYVRTFDNMQEVNHDALVQAM-- 240
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDG-TIALSGKTADLSTDDIIQAItp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 241 VGRELG---------DIYGWQPRE-YGKERLRLDRVKAPGVRQpVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITA 310
Cdd:PRK15439 239 AAREKSlsasqklwlELPGNRRQQaAGAPVLTVEDLTGEGFRN-ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 311 GQVYIDGEAIDIRKPAQAIQAGMMLCPEDRKAEGIIPVHSVRdnINISARRKHILaGCVINNAWEAQNADQHIKSLNIKT 390
Cdd:PRK15439 318 GRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDAPLA--WNVCALTHNRR-GFWIKPARENAVLERYRRALNIKF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 391 PGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIV 470
Cdd:PRK15439 395 NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVL 474
|
490 500
....*....|....*....|....*
gi 490204990 471 VMREGEIAGELLHEHANEQQALSLA 495
Cdd:PRK15439 475 VMHQGEISGALTGAAINVDTIMRLA 499
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
257-477 |
5.59e-79 |
|
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: 244.65 E-value: 5.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 257 GKERLRLDRVKAPGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMLC 336
Cdd:cd03215 1 GEPVLEVRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 337 PEDRKAEGIIPVHSVRDNINISARrkhilagcvinnaweaqnadqhikslniktpgaeqlimnLSGGNQQKAILGRWLSE 416
Cdd:cd03215 81 PEDRKREGLVLDLSVAENIALSSL---------------------------------------LSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 417 EMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-224 |
1.67e-72 |
|
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: 226.93 E-value: 1.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVAII 87
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQelhlipemtvaeniylgqlphkggivnrsllnyeaglqlqhlgldidpetplkyLSIGQWQMVEIAKALARNAKIIAF 167
Cdd:cd03216 81 YQ------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 168 DEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRT 224
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-477 |
2.45e-50 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 179.71 E-value: 2.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFPG--VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGnYVP----TAGSLQIQGQQMTfTHTTE 78
Cdd:COG1123 2 TPLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPhggrISGEVLLDGRDLL-ELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 79 ALNAGVAIIYQE--LHLIPeMTVAENIYLGQLPHKggiVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAK 156
Cdd:COG1123 80 LRGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 157 ALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDNMQEVNHDA 235
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 236 LVQAMVGRELGDIYGWQPREYGKERLRLDRV-------KAPGVR--QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGS 306
Cdd:COG1123 236 ALAAVPRLGAARGRAAPAAAAAEPLLEVRNLskrypvrGKGGVRavDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 307 RITAGQVYIDGEAIDIRKPAQAiqagmmlcPEDRKAEGII---------PVHSVRDNINISARRKHILAGcvinnAWEAQ 377
Cdd:COG1123 316 RPTSGSILFDGKDLTKLSRRSL--------RELRRRVQMVfqdpysslnPRMTVGDIIAEPLRLHGLLSR-----AERRE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 378 NADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFAS 456
Cdd:COG1123 383 RVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFIS 462
|
490 500
....*....|....*....|.
gi 490204990 457 SDLPEVLGVADRIVVMREGEI 477
Cdd:COG1123 463 HDLAVVRYIADRVAVMYDGRI 483
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-220 |
4.32e-47 |
|
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: 164.06 E-value: 4.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAG 83
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQELHLIPEMTVAENIYLGQLPHKGGIVNRSLLNY------------EAGLQLQHLGLDIDPETPLKYLSIGQWQM 151
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLprarreereareRAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 152 VEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
12-220 |
6.20e-47 |
|
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: 162.99 E-value: 6.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 12 GITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVAIIYQEL 91
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 92 HLIPEMTVAENIYLGQLPHKG-GIVNRSLLNYEAGLQ------LQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKI 164
Cdd:cd03219 85 RLFPELTVLENVMVAAQARTGsGLLLARARREEREAReraeelLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 165 IAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-236 |
3.60e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 158.30 E-value: 3.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAgVAII 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRR-IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENI-YLGQLPHKGGIVNRSLLNyEAglqLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIA 166
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFARLYGLPRKEARERID-EL---LELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 167 FDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRyVRTFDNMQEVNHDAL 236
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGR-IVADGTPDELKARLL 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-220 |
1.13e-44 |
|
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: 157.33 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtfTHTTEALNAGVAII 87
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV--RKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENI-YLGQLpHKggiVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIA 166
Cdd:COG4555 80 PDERGLYDRLTVRENIrYFAEL-YG---LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 167 FDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-172 |
2.58e-44 |
|
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: 153.19 E-value: 2.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFThTTEALNAGVAIIYQELHLIPEMTVAEN 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 103 IYLGQLPHKggiVNRSLLNYEAGLQLQHLGLDIDPETPLKY----LSIGQWQMVEIAKALARNAKIIAFDEPTS 172
Cdd:pfam00005 80 LRLGLLLKG---LSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-220 |
2.13e-40 |
|
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: 143.31 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtFTHTTEALNAgVAII 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRR-IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIylgqlphkggivnrsllnyeaglqlqhlgldidpetplkYLSIGQWQMVEIAKALARNAKIIAF 167
Cdd:cd03230 79 PEEPSLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490204990 168 DEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-222 |
8.52e-38 |
|
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: 137.80 E-value: 8.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTealnagvAII 87
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN-------RIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 Y--QELHLIPEMTVAEN-IYLGQLphKGgiVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKI 164
Cdd:cd03269 74 YlpEERGLYPKMKVIDQlVYLAQL--KG--LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 165 IAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-220 |
2.59e-37 |
|
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: 136.44 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 9 SFHGITMTFPG--VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAI 86
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT-KLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQElhliPE-----MTVAENI--YLGQLPHKGGIVNRSLLNYeaglqLQHLGLDIDPETPLKYLSIGQWQMVEIAKALA 159
Cdd:cd03225 80 VFQN----PDdqffgPTVEEEVafGLENLGLPEEEIEERVEEA-----LELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 160 RNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-220 |
3.90e-36 |
|
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: 133.41 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthTTEALNAGVAII 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT---GVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIylgQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAF 167
Cdd:cd03259 78 FQDYALFPHLTVAENI---AFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 168 DEPTSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-226 |
4.12e-36 |
|
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: 134.23 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFP-GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTE--ALNAGV 84
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQELHLIPEMTVAENIYLGQLPHKGGIvnRSLLN------YEAGLQ-LQHLGLDIDPETPLKYLSIGQWQMVEIAKA 157
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTW--RSLFGlfpkeeKQRALAaLERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 158 LARNAKIIAFDEPTSSL---SAREIDNLFRVIRelRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVrtFD 226
Cdd:cd03256 159 LMQQPKLILADEPVASLdpaSSRQVMDLLKRIN--REEGITVIVSLHQVDLAREYADRIVGLKDGRIV--FD 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-230 |
7.55e-36 |
|
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: 132.63 E-value: 7.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG--VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNaGVA 85
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQ-SLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIPEMTVAENIYL-GQLphKGgiVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKI 164
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFyARL--KG--LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 165 IAFDEPTSSLSAREIDNLFRVIRELRQeGRVIIYVSHRMEEIFALSDAITVFKDGRyVRTFDNMQE 230
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGK-LRCIGSPQE 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-220 |
4.45e-35 |
|
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: 130.69 E-value: 4.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQ---QMTFTHTTEAL 80
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 81 NAGVAIIYQELHLIPEMTVAENIYLGQLPhkGGIVNRSLLNYEAGLqLQHLGLDIDPETPLKYLSIGQWQMVEIAKALAR 160
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLL--AGVPKKERRERAEEL-LERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 161 NAKIIAFDEPTSSL---SAREIDNLFRVIRelRQEGRVIIYVSHRMeEIFALSDAITVFKDGR 220
Cdd:cd03255 158 DPKIILADEPTGNLdseTGKEVMELLRELN--KEAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-220 |
2.11e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 129.01 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFP----GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthtteAL 80
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS------SL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 81 NAG---------VAIIYQELHLIPEMTVAENIYLGQLPHKGGIVNRSLLNYEAglqLQHLGLD--ID--PETplkyLSIG 147
Cdd:COG1136 76 SERelarlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERAREL---LERVGLGdrLDhrPSQ----LSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 148 QWQMVEIAKALARNAKIIAFDEPTSSL---SAREIdnlFRVIREL-RQEGRVIIYVSHRmEEIFALSDAITVFKDGR 220
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLdskTGEEV---LELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-220 |
2.42e-34 |
|
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: 126.59 E-value: 2.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 9 SFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNaGVAIIY 88
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR-RIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 89 QelhlipemtvaeniylgqlphkggivnrsllnyeaglqlqhlgldidpetplkyLSIGQWQMVEIAKALARNAKIIAFD 168
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 169 EPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-220 |
2.45e-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: 127.30 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQ-MTFTHTTEALNAGVAI 86
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIPEMTVAENIYLGqlphkggivnrsllnyeaglqlqhlgldidpetplkyLSIGQWQMVEIAKALARNAKIIA 166
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 167 FDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-220 |
1.17e-33 |
|
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: 127.85 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAII 87
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIYLGQLPHKGG----------IVNRSLlnyeAGLQLQHLGldidpETPLKYLSIGQWQMVEIAKA 157
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLfgrpsaedreAVEEAL----ERTGLEHLA-----DRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 158 LARNAKIIAFDEPTSSLsareiD-----NLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG1120 152 LAQEPPLLLLDEPTSHL-----DlahqlEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGR 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-220 |
1.24e-33 |
|
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: 127.06 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFP-GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAgVAI 86
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQ--ELHLIpEMTVAENI-----YLGqLPHK--GGIVNRSLlnyeAGLQLQHLgLDIDPETplkyLSIGQWQMVEIAKA 157
Cdd:COG1122 80 VFQnpDDQLF-APTVEEDVafgpeNLG-LPREeiRERVEEAL----ELVGLEHL-ADRPPHE----LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 158 LARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-220 |
2.68e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 126.75 E-value: 2.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthtteALNA- 82
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT------GLPPe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 --GVAIIYQELHLIPEMTVAENIYLGqLPHKGgiVNRS--------LLNYeagLQLQHLGlDIDPETplkyLSIGQWQMV 152
Cdd:COG3842 76 krNVGMVFQDYALFPHLTVAENVAFG-LRMRG--VPKAeirarvaeLLEL---VGLEGLA-DRYPHQ----LSGGQQQRV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 153 EIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGR 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
275-477 |
4.64e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 122.86 E-value: 4.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEaiDIRKPAQAIQAGMMLCPEDRkaeGIIPVHSVRDN 354
Cdd:COG1131 19 VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE--DVARDPAEVRRRIGYVPQEP---ALYPDLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARrkhiLAGcvINNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:COG1131 94 LRFFAR----LYG--LPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490204990 435 KHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG1131 167 RRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-201 |
6.71e-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: 121.43 E-value: 6.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtfTHTTEALNAGVAII 87
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI--RDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENI-YLGQLphKGGIVNRSLLNyEAglqLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIA 166
Cdd:COG4133 81 GHADGLKPELTVRENLrFWAAL--YGLRADREAID-EA---LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 490204990 167 FDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSH 201
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
273-478 |
1.13e-31 |
|
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: 121.89 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEaiDIRKPAQAIQAGMMLCPEDRkaeGIIPVHSVR 352
Cdd:COG4555 18 KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE--DVRKEPREARRQIGVLPDER---GLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISARrkhiLAGcvINNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDV 432
Cdd:COG4555 93 ENIRYFAE----LYG--LFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 433 GAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:COG4555 166 MARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-220 |
1.64e-31 |
|
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: 119.41 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG--VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVA 85
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR-DLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIpEMTVAENIylgqlphkggivnrsllnyeaglqlqhlgldidpetplkyLSIGQWQMVEIAKALARNAKII 165
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 166 AFDEPTSSL---SAREIdnlFRVIRELRQeGRVIIYVSHRMEEIfALSDAITVFKDGR 220
Cdd:cd03228 119 ILDEATSALdpeTEALI---LEALRALAK-GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-226 |
4.52e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.96 E-value: 4.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFP----GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTftht 76
Cdd:COG1116 1 MSAAAPALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 77 teALNAGVAIIYQELHLIPEMTVAENIYLGqLPHKGgiVNRSllnyEAGLQLQHL----GLDiDPETplKY---LSIGQW 149
Cdd:COG1116 77 --GPGPDRGVVFQEPALLPWLTVLDNVALG-LELRG--VPKA----ERRERARELlelvGLA-GFED--AYphqLSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 150 QMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRV-IIYVSHRMEEIFALSDAITVFKD--GRYVRTFD 226
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKtVLFVTHDVDEAVFLADRVVVLSArpGRIVEEID 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-222 |
5.55e-31 |
|
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: 125.79 E-value: 5.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 2 QQSTPYLSFHGITMTFP-----GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHT 76
Cdd:COG1123 255 AAAEPLLEVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 77 TE--ALNAGVAIIYQ--ELHLIPEMTVAENIYLGQLPHkgGIVNRSLLNYEAGLQLQHLGLdiDPETPLKY---LSIGQW 149
Cdd:COG1123 335 RSlrELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLH--GLLSRAERRERVAELLERVGL--PPDLADRYpheLSGGQR 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 150 QMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-220 |
1.43e-30 |
|
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: 118.13 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthTTEALNAGVAII 87
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT---DLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIYLGQLPHKGG--IVNRSLLNYEAGLQLQHLgLDIDPetplKYLSIGQWQMVEIAKALARNAKII 165
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPkdEIDERVREVAELLQIEHL-LDRKP----KQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 166 AFDEPTSSLSAReidnlFRV-----IRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03301 153 LMDEPLSNLDAK-----LRVqmraeLKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-222 |
4.89e-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: 116.55 E-value: 4.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 12 GITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQmtFTHTTEALN-AGVAIIYQE 90
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEALRrIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 91 LHliPEMTVAENIYLGQ----LPHKggIVNRsLLNYeaglqlqhLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIA 166
Cdd:cd03268 83 FY--PNLTARENLRLLArllgIRKK--RIDE-VLDV--------VGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 167 FDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-217 |
6.39e-30 |
|
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: 116.09 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 9 SFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQmtfthtTEALNAGVAIIY 88
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP------LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 89 QELHLIPEM--TVAENIYLGQLPHKGGIVNRSLLNYEAGLQ-LQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKII 165
Cdd:cd03235 75 QRRSIDRDFpiSVRDVVLMGLYGHKGLFRRLSKADKAKVDEaLERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 166 AFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFK 217
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-234 |
6.70e-30 |
|
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: 116.38 E-value: 6.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 19 GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVAIIYQELHLIPEMT 98
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGRRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 99 VAENIYLGQLPHKGGIVNRSL-------------LNYEAGLqlqhlgldidpetplkyLSIGQWQMVEIAKALARNAKII 165
Cdd:cd03224 92 VEENLLLGAYARRRAKRKARLervyelfprlkerRKQLAGT-----------------LSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 166 AFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRyVRTFDNMQEVNHD 234
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR-VVLEGTAAELLAD 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-220 |
7.75e-30 |
|
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: 114.84 E-value: 7.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 6 PYLSFHGITmtfpGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVA 85
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELH---LIPEMTVAENIYLGQLphkggivnrsllnyeaglqlqhlgldidpetplkyLSIGQWQMVEIAKALARNA 162
Cdd:cd03215 79 YVPEDRKregLVLDLSVAENIALSSL-----------------------------------LSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 163 KIIAFDEPTsslsaREID-----NLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03215 124 RVLILDEPT-----RGVDvgakaEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-227 |
1.51e-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: 115.26 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthtteALNAG 83
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQELHLIPEMTVAENIYLGqLPHKGgiVNRSLLNYEAGLQLQHLGLDidpETPLKY---LSIGQWQMVEIAKALAR 160
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALG-LELQG--VPKAEARERAEELLELVGLS---GFENAYphqLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 161 NAKIIAFDEPTSSLSA--REI--DNLFRVireLRQEGRVIIYVSHRMEEIFALSDAITVF--KDGRYVRTFDN 227
Cdd:cd03293 149 DPDVLLLDEPFSALDAltREQlqEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEVEV 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-221 |
3.49e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.19 E-value: 3.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmtfthTTEALNAG 83
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK------PPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQELHLIPE--MTVAENIYLGQLPHKG----------GIVNRSLlnyEAgLQLQHLGldidpETPLKYLSIGQWQM 151
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRDVVLMGRYGRRGlfrrpsradrEAVDEAL---ER-VGLEDLA-----DRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 152 VEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRY 221
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
275-484 |
4.31e-29 |
|
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: 4.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMLCPEDRkaeGIIPVHSVRDN 354
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGR---RIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 inisarrkhILAGCVINNAWEAQNADQHIKSL------NIKTPGAeqlimNLSGGNQQKAILGRWLSEEMKVILLDEPTR 428
Cdd:cd03224 96 ---------LLLGAYARRRAKRKARLERVYELfprlkeRRKQLAG-----TLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 429 GIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI-----AGELLHE 484
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVvlegtAAELLAD 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
4.38e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.47 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFPGVK--ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTE 78
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 79 ALNAgVAIIYQElhliPE-----MTVAENIYLGqLPHKggIVNRSLLN---YEAGLQLQHLG-LDIDPEtplkYLSIGQW 149
Cdd:PRK13632 81 IRKK-IGIIFQN----PDnqfigATVEDDIAFG-LENK--KVPPKKMKdiiDDLAKKVGMEDyLDKEPQ----NLSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 150 QMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEG-RVIIYVSHRMEEIFaLSDAITVFKDGRYVRT 224
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI-LADKVIVFSEGKLIAQ 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-222 |
4.48e-29 |
|
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: 114.00 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqMTFTHTTEALNAGVAIIYQELHLIPEMTV 99
Cdd:cd03266 18 VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRRLGFVSDSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 100 AENI-YLGQLPHKGGIVNRSLLNYEAGLqlqhlgLDIDP--ETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSA 176
Cdd:cd03266 96 RENLeYFAGLYGLKGDELTARLEELADR------LGMEEllDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 177 REIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-239 |
5.21e-29 |
|
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: 120.25 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFP-GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAI 86
Cdd:COG4988 337 IELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS-DLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIPeMTVAENIYLGQlPHkggiVNRSLLNY---EAGL-----QLQHlGLDidpeTPL----KYLSIGQWQMVEI 154
Cdd:COG4988 416 VPQNPYLFA-GTIRENLRLGR-PD----ASDEELEAaleAAGLdefvaALPD-GLD----TPLgeggRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 155 AKALARNAKIIAFDEPTSSL---SAREIdnlFRVIRELRQeGRVIIYVSHRMEEIfALSDAITVFKDGRYVrtfdnmQEV 231
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLdaeTEAEI---LQALRRLAK-GRTVILITHRLALL-AQADRILVLDDGRIV------EQG 553
|
....*...
gi 490204990 232 NHDALVQA 239
Cdd:COG4988 554 THEELLAK 561
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-220 |
9.19e-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: 113.01 E-value: 9.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTT-EALNAGVAI 86
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQHLGLDidpETPLKY---LSIGQWQMVEIAKALARNAK 163
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKG--MSKAEAEERALELLEKVGLA---DKADAYpaqLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 164 IIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-231 |
1.17e-28 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 113.58 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthTTEALNAGVAIIYQELHLIPEMTVAEN 102
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT---NLPPEKRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 103 IYLG---QLPHKGGIvNRSLLNYEAGLQLQHLgLDIDPETplkyLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREI 179
Cdd:cd03299 92 IAYGlkkRKVDKKEI-ERKVLEIAEMLGIDHL-LNRKPET----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490204990 180 DNLFRVIRELRQEGRV-IIYVSHRMEEIFALSDAITVFKDGRYVRtFDNMQEV 231
Cdd:cd03299 166 EKLREELKKIRKEFGVtVLHVTHDFEEAWALADKVAIMLNGKLIQ-VGKPEEV 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
275-477 |
1.46e-28 |
|
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: 112.60 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKPAQAIQAGMMLCPEDRkaegIIPVH-SVRD 353
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--YSIRTDRKAARQSLGYCPQFD----ALFDElTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 354 NINISARRKHilagcvINNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQK-----AILGrwlseEMKVILLDEPTR 428
Cdd:cd03263 95 HLRFYARLKG------LPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKlslaiALIG-----GPSVLLLDEPTS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 429 GIDVGAKHEIYNVIYALaASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03263 163 GLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-239 |
1.57e-28 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 113.15 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 3 QSTPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTE--AL 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 81 NAGVAIIYQELHLIPEMTVAENIylgQLP---HKGgiVNRSLLNYEAGLQLQHLGLdidPETPLKY---LSIGqwqM--- 151
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENV---AFPlreHTD--LSEAEIRELVLEKLELVGL---PGAADKMpseLSGG---Mrkr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 152 VEIAKALARNAKIIAFDEPTSSL---SAREIDNLfrvIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRyVRTFDN 227
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLdpiTSAVIDEL---IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGK-IIAEGT 225
|
250
....*....|....
gi 490204990 228 MQEVNH--DALVQA 239
Cdd:COG1127 226 PEELLAsdDPWVRQ 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-222 |
1.76e-28 |
|
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: 112.60 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAG 83
Cdd:cd03257 2 LEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 --VAIIYQELH--LIPEMTVAENIYLGQLPHKGGIvNRSLLNYEAGLQLQHLGLdiDPETPLKY---LSIGQWQMVEIAK 156
Cdd:cd03257 82 keIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGL--PEEVLNRYpheLSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 157 ALARNAKIIAFDEPTSSL---SAREIDNLFrviRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03257 159 ALALNPKLLIADEPTSALdvsVQAQILDLL---KKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-222 |
1.82e-28 |
|
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: 112.66 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSG-----NYVPTAGSLQIQGQQ-MTFTHTTEALN 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 82 AGVAIIYQELHLIPeMTVAENIYLGQLPHkgGIVNRSLLNY--EAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALA 159
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLH--GIKLKEELDErvEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 160 RNAKIIAFDEPTSSL---SAREIDNLfrvIRELRQEGRVIIyVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03260 158 NEPEVLLLDEPTSALdpiSTAKIEEL---IAELKKEYTIVI-VTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
275-477 |
2.30e-28 |
|
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: 110.57 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEaiDIRKPAQAIQAGMMLCPEDRkaeGIIPVHSVRDN 354
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK--DIKKEPEEVKRRIGYLPEEP---SLYENLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INisarrkhilagcvinnaweaqnadqhikslniktpgaeqlimnLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:cd03230 94 LK-------------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490204990 435 KHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03230 131 RREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-220 |
2.69e-28 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 112.39 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTT-EALNAGVAI 86
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDiNKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQHLGLD--IDpetplKY---LSIGQWQMVEIAKALARN 161
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKVKK--MSKAEAEERAMELLERVGLAdkAD-----AYpaqLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 162 AKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEeiFA--LSDAITVFKDGR 220
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMG--FAreVADRVVFMDGGR 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-242 |
3.28e-28 |
|
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: 112.00 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGV 84
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQELHLIPEMTVAENIYLGQLPHKGGIVNRSLLN--YE------------AGlqlqhlgldidpetplkYLSIGQWQ 150
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLErvYElfprlkerrrqrAG-----------------TLSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 151 MVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDNMQE 230
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
250
....*....|..
gi 490204990 231 VNHDALVQAMVG 242
Cdd:COG0410 224 LADPEVREAYLG 235
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-222 |
3.94e-28 |
|
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: 111.19 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 11 HGITMTFP-GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEAlnagVAIIYQ 89
Cdd:cd03226 3 ENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS----IGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 90 EL-HLIPEMTVAENIYLG--QLPHKGGIVNRSLLNYE-AGLQLQHlgldidpetPLKyLSIGQWQMVEIAKALARNAKII 165
Cdd:cd03226 79 DVdYQLFTDSVREELLLGlkELDAGNEQAETVLKDLDlYALKERH---------PLS-LSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 166 AFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-226 |
5.30e-28 |
|
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: 111.52 E-value: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTE--ALN 81
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 82 AGVAIIYQELHLIPEMTVAENIylgQLPHKGGIVNRSLLNYEAGLQLQHLGL----DIDPETplkyLSIGQWQMVEIAKA 157
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENV---ALPLEIAGVPKAEIEERVLELLELVGLedkaDAYPAQ----LSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 158 LARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFD 226
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-220 |
8.17e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.89 E-value: 8.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHttealnagvaii 87
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 yqeLHLI---PE-------MTVAENI-YLGQLphKG---GIVNRSLLNYeaglqLQHLGLDIDPETPLKYLSIGQWQMVE 153
Cdd:COG4152 70 ---RRRIgylPEerglypkMKVGEQLvYLARL--KGlskAEAKRRADEW-----LERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 154 IAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-220 |
1.79e-27 |
|
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: 109.69 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 25 DISFDCyAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmTFTHTTEALNA-----GVAIIYQELHLIPEMTV 99
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT--VLFDSRKKINLppqqrKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 100 AENIYLGqLPHKGGIVNRSLLNYEAG-LQLQHLGldidpETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSARE 178
Cdd:cd03297 93 RENLAFG-LKRKRNREDRISVDELLDlLGLDHLL-----NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490204990 179 IDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03297 167 RLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
10-204 |
3.02e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 109.72 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 10 FHGITmtfpgvKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEA-----LNAGV 84
Cdd:PRK11124 11 FYGAH------QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDkaireLRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQELHLIPEMTVAENiyLGQLPHKGGIVNRSLLNYEAGLQLQHLGL-DIDPETPLkYLSIGQWQMVEIAKALARNAK 163
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQN--LIEAPCRVLGLSKDQALARAEKLLERLRLkPYADRFPL-HLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490204990 164 IIAFDEPTSSLSArEIDN-LFRVIRELRQEGRVIIYVSHRME 204
Cdd:PRK11124 162 VLLFDEPTAALDP-EITAqIVSIIRELAETGITQVIVTHEVE 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-239 |
7.86e-27 |
|
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: 114.55 E-value: 7.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG--VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVA 85
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR-QIDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIpEMTVAENIYLGqlphkggivnRSLLNYEAGLQ-LQHLGLD--IDpETPLKY----------LSIGQWQMV 152
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLG----------DPDATDEEIIEaARLAGLHdfIE-ALPMGYdtvvgeggsnLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 153 EIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQeGRVIIYVSHRMEEIfALSDAITVFKDGRYVrtfdnmQEVN 232
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI-RLADRIIVLDKGRIV------EDGT 692
|
....*..
gi 490204990 233 HDALVQA 239
Cdd:COG2274 693 HEELLAR 699
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-222 |
8.54e-27 |
|
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: 108.36 E-value: 8.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTE--ALNAGVA 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIPEMTVAENIYLGQLPHkgGIVNRSLLNYEAGLQLQHLGLdidPETPLKY---LSIGQWQMVEIAKALARNA 162
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREH--TRLSEEEIREIVLEKLEAVGL---RGAEDLYpaeLSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 163 KIIAFDEPTSSL---SAREIDNLfrvIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03261 156 ELLLYDEPTAGLdpiASGVIDDL---IRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-220 |
1.11e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 110.55 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthTTEALNAGVAII 87
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT---DLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIYLG----QLPhKGGI---VNRSLlnyeAGLQLQHLgLDIDPetplKYLSIGQWQMVEIAKALAR 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPlklrKVP-KAEIdrrVREAA----ELLGLEDL-LDRKP----KQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 161 NAKIIAFDEPTSSLsareiDNLFRV-----IRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG3839 151 EPKVFLLDEPLSNL-----DAKLRVemraeIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGR 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
269-480 |
1.70e-26 |
|
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: 105.20 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 269 PGVR--QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMmlcpedrkaegii 346
Cdd:cd03216 11 GGVKalDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 pvhsvrdninisarrkhilagcvinnaweaqnadqhikslniktpgaeQLIMNLSGGNQQKAILGRWLSEEMKVILLDEP 426
Cdd:cd03216 78 ------------------------------------------------AMVYQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 427 TRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-244 |
1.89e-26 |
|
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: 107.39 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGV-KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEaLNAGVAI 86
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE-LRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIPEMTVAENIYLgqLPhkggivnrSLLNY------EAGLQLQHLgLDIDPETPL-KY---LSIGQWQMVEIAK 156
Cdd:cd03295 80 VIQQIGLFPHMTVEENIAL--VP--------KLLKWpkekirERADELLAL-VGLDPAEFAdRYpheLSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 157 ALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYVR--TFDNMQEVNH 233
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQvgTPDEILRSPA 228
|
250
....*....|.
gi 490204990 234 DALVQAMVGRE 244
Cdd:cd03295 229 NDFVAEFVGAD 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-220 |
3.57e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.00 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAG 83
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQELHLIPEMTVAENIYLGQLPHkggiVNRSLLnyeAGL-------------------QLQHLGLDIDPETPLKYL 144
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLLVAQHQQ----LKTGLF---SGLlktpafrraesealdraatWLERVGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 145 SIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRV-IIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVtVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-220 |
4.64e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.70 E-value: 4.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQmTFTHTTeALNAGVAII 87
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-LFTNLP-PRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIYLG---QLPHKGGIVNR--SLLnyEAgLQLQHLGlDidpetplKY---LSIGQWQMVEIAKALA 159
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGlrvRPPSKAEIRARveELL--EL-VQLEGLA-D-------RYpsqLSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 160 RNAKIIAFDEPTSSLSA---REI-DNLFRVIRELrqeGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG1118 150 VEPEVLLLDEPFGALDAkvrKELrRWLRRLHDEL---GGTTVFVTHDQEEALELADRVVVMNQGR 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-220 |
5.44e-26 |
|
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: 105.78 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtftHTTEALNAGVAII 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI---TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIYLGqLPHKGgiVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAF 167
Cdd:cd03300 78 FQNYALFPHLTVFENIAFG-LRLKK--LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 168 DEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGK 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
275-483 |
5.54e-26 |
|
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: 105.83 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMLCPEDRkaeGIIPVHSVRDN 354
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGR---RIFPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISAR------------------------RKHILAGcvinnaweaqnadqhikslniktpgaeqlimNLSGGNQQKAIL 410
Cdd:COG0410 99 LLLGAYarrdraevradlervyelfprlkeRRRQRAG-------------------------------TLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 411 GRWLSEEMKVILLDEPTRGID---VgakHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI-----AGELL 482
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLApliV---EEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIvlegtAAELL 224
|
.
gi 490204990 483 H 483
Cdd:COG0410 225 A 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-220 |
7.13e-26 |
|
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: 104.05 E-value: 7.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 11 HGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmtfthttealnagvaiiyqE 90
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK--------------------D 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 91 LHLIPEMTVAENI-YLGQLphkggivnrslLNYeagLQLQHLGldidpETPLKYLSIGQWQMVEIAKALARNAKIIAFDE 169
Cdd:cd03214 63 LASLSPKELARKIaYVPQA-----------LEL---LGLAHLA-----DRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 170 PTSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-223 |
1.71e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.00 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtfTHTTEALNAgV 84
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL--SHVPPYQRP-I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQELHLIPEMTVAENIYLG----QLPhKGGIVNRsllnYEAGLQLQHLgLDIDPETPLKyLSIGQWQMVEIAKALAR 160
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGlkqdKLP-KAEIASR----VNEMLGLVHM-QEFAKRKPHQ-LSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 161 NAKIIAFDEPTSSLSAREIDNL-FRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVR 223
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-233 |
2.05e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.09 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 12 GITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHtteALNAGVAIIYQEL 91
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH---ARDRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 92 HLIPEMTVAENIYLG--QLPHK----GGIVNRSLLNYEAGLQLQHLGldidPETPLKyLSIGQWQMVEIAKALARNAKII 165
Cdd:PRK10851 84 ALFRHMTVFDNIAFGltVLPRRerpnAAAIKAKVTQLLEMVQLAHLA----DRYPAQ-LSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 166 AFDEPTSSLSAREIDNLFRVIRELRQEGRVI-IYVSHRMEEIFALSDAITVFKDG-----------------RYVRTFdn 227
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTsVFVTHDQEEAMEVADRVVVMSQGnieqagtpdqvwrepatRFVLEF-- 236
|
....*.
gi 490204990 228 MQEVNH 233
Cdd:PRK10851 237 MGEVNR 242
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
10-220 |
2.36e-25 |
|
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: 104.34 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 10 FHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEalnAGVAIIYQ 89
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 90 ELHLIPEMTVAENIYLG-------QLPHKGGIVNR--SLLNYeagLQLQHLGLDIDPEtplkyLSIGQWQMVEIAKALAR 160
Cdd:cd03296 82 HYALFRHMTVFDNVAFGlrvkprsERPPEAEIRAKvhELLKL---VQLDWLADRYPAQ-----LSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 161 NAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVI-IYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTtVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-477 |
2.79e-25 |
|
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: 109.12 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 13 ITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSG--NYVPTAGSL-------------------------- 64
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyverpskvgepcpvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 65 --QIQGQQMTFTHTTEALNAGV----AIIYQE-LHLIPEMTVAENIY--LGQLPHKGGIVNRSLLNYEAGLQLQHLGLDI 135
Cdd:TIGR03269 86 ggTLEPEEVDFWNLSDKLRRRIrkriAIMLQRtFALYGDDTVLDNVLeaLEEIGYEGKEAVGRAVDLIEMVQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 136 DPEtplkyLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAIT 214
Cdd:TIGR03269 166 ARD-----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 215 VFKDGRYVRTFDNMQEVNHDALVQAMVGR----ELG-DIYgwQPREYGKERLRLDR--VKAPgvrQPVSLSVRSGEIVGL 287
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAVFMEGVSEVEKecevEVGePII--KVRNVSKRYISVDRgvVKAV---DNVSLEVKEGEIFGI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 288 FGLVGAGRSELMKGLFGGSRITAGQVY--IDGEAIDIRKPaqaiqaGMMLCPEDRKAEGII-------PVHSVRDNINIS 358
Cdd:TIGR03269 316 VGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMTKP------GPDGRGRAKRYIGILhqeydlyPHRTVLDNLTEA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 359 ---------ARRKHILAgcvinnaweaqnadqhIKSLNIKTPGAEQLI----MNLSGGNQQKAILGRWLSEEMKVILLDE 425
Cdd:TIGR03269 390 iglelpdelARMKAVIT----------------LKMVGFDEEKAEEILdkypDELSEGERHRVALAQVLIKEPRIVILDE 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 426 PTRGID----VGAKHEIYNVIYALAASGVAVvfaSSDLPEVLGVADRIVVMREGEI 477
Cdd:TIGR03269 454 PTGTMDpitkVDVTHSILKAREEMEQTFIIV---SHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-222 |
6.68e-25 |
|
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: 103.88 E-value: 6.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 22 ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNA----GVAIIYQELHLIPEM 97
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRKELRElrrkKISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 98 TVAENIYLGqLPHKGgiVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSA- 176
Cdd:cd03294 118 TVLENVAFG-LEVQG--VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPl 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 177 --REI-DNLFRVIRELRqegRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03294 195 irREMqDELLRLQAELQ---KTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
275-477 |
1.72e-24 |
|
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: 101.74 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMlcpedRK--AEGIIPVHSVR 352
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIG-----RTfqIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISA---RRKHILAGCVINNAWEAQN-ADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTR 428
Cdd:cd03219 94 ENVMVAAqarTGSGLLLARARREEREARErAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 429 GIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03219 173 GLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
10-222 |
2.81e-24 |
|
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: 100.74 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 10 FHGITMTFPG--VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEaLNAGVAII 87
Cdd:cd03245 5 FRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIpEMTVAENIYLGQLPHK----------GGI---VNRSLLNYEagLQLQHLGldidpetplKYLSIGQWQMVEI 154
Cdd:cd03245 84 PQDVTLF-YGTLRDNITLGAPLADderilraaelAGVtdfVNKHPNGLD--LQIGERG---------RGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 155 AKALARNAKIIAFDEPTSSLsarEIDNLFRVIRELRQ--EGRVIIYVSHRMeEIFALSDAITVFKDGRYV 222
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAM---DMNSEERLKERLRQllGDKTLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-201 |
9.89e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.50 E-value: 9.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQ---QMTFTHTTEALNAGVAIIYQELHLIPEMTV 99
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKLSSAAKAELRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 100 AENIylgQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREI 179
Cdd:PRK11629 105 LENV---AMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180
....*....|....*....|...
gi 490204990 180 DNLFRVIREL-RQEGRVIIYVSH 201
Cdd:PRK11629 182 DSIFQLLGELnRLQGTAFLVVTH 204
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-222 |
1.49e-23 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 98.33 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 28 FDCY--AGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEalnAGVAIIYQELHLIPEMTVAENIYL 105
Cdd:cd03298 17 FDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---RPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 106 GQLPH-KGGIVNRSLLNYEAGlqlqHLGLD-IDPETPlKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLF 183
Cdd:cd03298 94 GLSPGlKLTAEDRQAIEVALA----RVGLAgLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490204990 184 RVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03298 169 DLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-239 |
1.94e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 103.71 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG-VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAI 86
Cdd:COG1132 340 IEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR-DLTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIpEMTVAENIYLG-----------------------QLPHkggivnrsllnyeaglqlqhlGLDidpeTPL-- 141
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYGrpdatdeeveeaakaaqahefieALPD---------------------GYD----TVVge 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 142 --KYLSIGQWQMVEIAKALARNAKIIAFDEPTSSL---SAREIdnlFRVIRELRQeGRVIIYVSHRMEEIfALSDAITVF 216
Cdd:COG1132 473 rgVNLSGGQRQRIAIARALLKDPPILILDEATSALdteTEALI---QEALERLMK-GRTTIVIAHRLSTI-RNADRILVL 547
|
250 260
....*....|....*....|...
gi 490204990 217 KDGRYVrtfdnmQEVNHDALVQA 239
Cdd:COG1132 548 DDGRIV------EQGTHEELLAR 564
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-220 |
2.07e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.56 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthTTEAL 80
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT---HVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 81 NAGVAIIYQELHLIPEMTVAENIYLG----QLPHKGgiVNRSLLNYEAGLQLQHLGlDIDPetplKYLSIGQWQMVEIAK 156
Cdd:PRK09452 85 NRHVNTVFQSYALFPHMTVFENVAFGlrmqKTPAAE--ITPRVMEALRMVQLEEFA-QRKP----HQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 157 ALARNAKIIAFDEPTSSLSAR-------EIDNLfrvireLRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKlrkqmqnELKAL------QRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-215 |
5.29e-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: 101.98 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGV-KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmTFTHTTEA-LNAGVA 85
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV--PLADADADsWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIPEmTVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDpeTPL----KYLSIGQWQMVEIAKALARN 161
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLD--TPIgeggAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 162 AKIIAFDEPTSSLSAREIDNLFRVIRELRQeGRVIIYVSHRmEEIFALSDAITV 215
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHR-LALAALADRIVV 528
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-208 |
6.14e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.47 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 10 FHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEAL---NAGvaI 86
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAG--M 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQHLGLDidpETPLKY---LSIGQWQMVEIAKALARNAK 163
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRVRG--ASKEEAEKQARELLAKVGLA---ERAHHYpseLSGGQQQRVAIARALAVKPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490204990 164 IIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEeiFA 208
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG--FA 199
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-222 |
7.14e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 7.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQElHLIPE-MTVAE 101
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS-MLSSRQLARRLALLPQH-HLTPEgITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 102 NIYLGQLPH----------KGGIVNRSLlnyeAGLQLQHLGldidpETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPT 171
Cdd:PRK11231 96 LVAYGRSPWlslwgrlsaeDNARVNQAM----EQTRINHLA-----DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490204990 172 SSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK11231 167 TYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-223 |
9.58e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 96.11 E-value: 9.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGqVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtfTHTTEALNAGVAII 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--LKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENI-YLGQLphkGGIVNRSLLNYEAGLqLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIA 166
Cdd:cd03264 78 PQEFGVYPNFTVREFLdYIAWL---KGIPSKEVKARVDEV-LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 167 FDEPTSSLSAREIDNLFRVIRELrQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVR 223
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-255 |
1.14e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.13 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtfTHTTEAL 80
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV--PARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 81 NAGVAIIYQELHLIPEMTVAENI-----YLGQLPHKGGIVNRSLLNYEAglqlqhlgLDIDPETPLKYLSIGQWQMVEIA 155
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLlvfgrYFGMSTREIEAVIPSLLEFAR--------LESKADARVSDLSGGMKRRLTLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 156 KALARNAKIIAFDEPTSSLS--AREIdnLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRyvrtfdNMQEVNH 233
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDphARHL--IWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR------KIAEGRP 256
|
250 260
....*....|....*....|..
gi 490204990 234 DALVQAMVGRELGDIYGWQPRE 255
Cdd:PRK13536 257 HALIDEHIGCQVIEIYGGDPHE 278
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-238 |
1.32e-22 |
|
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: 96.14 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 18 PGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQELHLIPEm 97
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 98 TVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHL--GLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLS 175
Cdd:cd03254 92 TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 176 AREIDNLFRVIRELRqEGRVIIYVSHRMEEIfALSDAITVFKDGRYVrtfdnmQEVNHDALVQ 238
Cdd:cd03254 172 TETEKLIQEALEKLM-KGRTSIIIAHRLSTI-KNADKILVLDDGKII------EEGTHDELLA 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-477 |
1.88e-22 |
|
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: 100.53 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKS----TLLKILSGNYVPTAGSLQIQGQQMtfTH 75
Cdd:COG4172 3 SMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL--LG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 76 TTEA-LNA----GVAIIYQE--LHLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQHLGLDiDPETPLK-Y---L 144
Cdd:COG4172 81 LSEReLRRirgnRIAMIFQEpmTSLNPLHTIGKQIAEVLRLHRG--LSGAAARARALELLERVGIP-DPERRLDaYphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 145 SIGQWQMVEIAKALARNAKI-IAfDEPTSSLSA---REIDNLfrvIRELRQE-GRVIIYVSH------RMeeifalSDAI 213
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLlIA-DEPTTALDVtvqAQILDL---LKDLQRElGMALLLITHdlgvvrRF------ADRV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 214 TVFKDGRYVRT------FDNMQevnHD---ALVQAMVGR-------------ELGDIYGWQPREYGKERLRLDRVKApgV 271
Cdd:COG4172 228 AVMRQGEIVEQgptaelFAAPQ---HPytrKLLAAEPRGdprpvppdappllEARDLKVWFPIKRGLFRRTVGHVKA--V 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 272 rQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRiTAGQVYIDGEAIDIRKPAQ------AIQagmM--------LCP 337
Cdd:COG4172 303 -DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrrRMQ---VvfqdpfgsLSP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 338 ----EDRKAEGIIpVHsvRDNINISARRKHILAgcvinnAWEAQNADqhikslniktPGAeqliMN-----LSGGNQQK- 407
Cdd:COG4172 378 rmtvGQIIAEGLR-VH--GPGLSAAERRARVAE------ALEEVGLD----------PAA----RHrypheFSGGQRQRi 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 408 AIlGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG4172 435 AI-ARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-222 |
1.92e-22 |
|
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: 95.76 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 18 PGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQELHLIPEm 97
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR-EVTLDSLRRAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 98 TVAENIYLGQL---------PHKGGIVNRSLLNYEAGLQLQhLGldidpETPLKyLSIGQWQMVEIAKALARNAKIIAFD 168
Cdd:cd03253 90 TIGYNIRYGRPdatdeevieAAKAAQIHDKIMRFPDGYDTI-VG-----ERGLK-LSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 169 EPTSSLSAREIDNLFRVIRELRQeGRVIIYVSHRMEEIfALSDAITVFKDGRYV 222
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTI-VNADKIIVLKDGRIV 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
271-476 |
2.20e-22 |
|
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: 94.18 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDirkpaqaiqagmmlcpedrkaegiipvhs 350
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT----------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 vRDNINISARRKHIlaGCVINNAweaqnadQHIKSLNIKtpgaEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:cd03229 66 -DLEDELPPLRRRI--GMVFQDF-------ALFPHLTVL----ENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490204990 431 DVGAKHEIYNVIYALAA-SGVAVVFASSDLPEVLGVADRIVVMREGE 476
Cdd:cd03229 132 DPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
275-476 |
3.47e-22 |
|
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: 94.46 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQ-AGMML-CPEDRkaegiIPVHSVR 352
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRkVGLVFqNPDDQ-----FFGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISARRKHIlagcviNNAWEAQNADQHIKSLNIKTPgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDV 432
Cdd:cd03225 95 EEVAFGLENLGL------PEEEIEERVEEALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490204990 433 GAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGE 476
Cdd:cd03225 168 AGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-231 |
3.70e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmtfTHTTEALNAGvaiiyqeLHliPEMTV 99
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSALLELGAG-------FH--PELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 100 AENIYLGqlphkGGIvnrsllnyeaglqlqhLGL---DIDP---------------ETPLKYLSIGqwQMVEIAKALARN 161
Cdd:COG1134 106 RENIYLN-----GRL----------------LGLsrkEIDEkfdeivefaelgdfiDQPVKTYSSG--MRARLAFAVATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 162 AK--IIAFDEptsSLSAReiDNLFR-----VIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRyVRTFDNMQEV 231
Cdd:COG1134 163 VDpdILLVDE---VLAVG--DAAFQkkclaRIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGR-LVMDGDPEEV 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-220 |
4.01e-22 |
|
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: 94.40 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 10 FHGITMTFP-GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTH--TTEALNAGVAI 86
Cdd:cd03292 3 FINVTKTYPnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgrAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIPEMTVAENIYLG----QLPHKggivnrsLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNA 162
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFAlevtGVPPR-------EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 163 KIIAFDEPTSSL---SAREIDNLFRVIrelRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03292 156 TILIADEPTGNLdpdTTWEIMNLLKKI---NKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
271-476 |
4.09e-22 |
|
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: 92.69 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQaiqagmmlcpedrkaegiipvhs 350
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE----------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 vrdninisaRRKHIlagcvinnaweaqnadqhikslniktpgaeQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:cd00267 71 ---------LRRRI------------------------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 431 DVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGE 476
Cdd:cd00267 112 DPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
275-480 |
5.81e-22 |
|
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: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKPAQAIQAGMMLCPEdrkAEGIIPVHSVRDN 354
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRRLGFVSD---STGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRkHILAGcvinnaweaQNADQHIKSLniktpgAEQLIMN---------LSGGNQQKAILGRWLSEEMKVILLDE 425
Cdd:cd03266 99 LEYFAGL-YGLKG---------DELTARLEEL------ADRLGMEelldrrvggFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 426 PTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-223 |
6.36e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.96 E-value: 6.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFP-GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthtteALNAG--- 83
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS------RLKRReip 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 -----VAIIYQELHLIPEMTVAENIYL-----GqlphkggiVNRSLLNYEAGLQLQHLGL----DIDPETplkyLSIGQW 149
Cdd:COG2884 76 ylrrrIGVVFQDFRLLPDRTVYENVALplrvtG--------KSRKEIRRRVREVLDLVGLsdkaKALPHE----LSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 150 QMVEIAKALARNAKIIAFDEPTSSL---SAREIDNLFrviRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVR 223
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLdpeTSWEIMELL---EEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-223 |
6.41e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.41 E-value: 6.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEAL 80
Cdd:PRK10535 2 TALLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVA-TLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 81 NA----GVAIIYQELHLIPEMTVAENIylgQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAK 156
Cdd:PRK10535 81 AQlrreHFGFIFQRYHLLSHLTAAQNV---EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 157 ALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRmEEIFALSDAITVFKDGRYVR 223
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-222 |
7.36e-22 |
|
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: 93.97 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 12 GITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqmtFTHTTEALN--AGVAIIYQ 89
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG----HDVVREPREvrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 90 ELHLIPEMTVAENIYLgqlphKGGI--VNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAF 167
Cdd:cd03265 81 DLSVDDELTGWENLYI-----HARLygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 168 DEPTSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
275-477 |
7.83e-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: 93.50 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIrkpaqAIQAGMMLCPEDRkaeGIIPVHSVRDN 354
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNRIGYLPEER---GLYPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARrkhiLAGCVINNAweAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:cd03269 91 LVYLAQ----LKGLKKEEA--RRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490204990 435 KHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03269 164 VELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
271-478 |
1.05e-21 |
|
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: 93.35 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQ-AIqaGMM-----LCPedrkaeg 344
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrNI--GMVfqdyaLFP------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 345 iipvH-SVRDNINISARRKHIlagcviNNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILL 423
Cdd:cd03259 86 ----HlTVAENIAFGLKLRGV------PKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 424 DEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-237 |
1.15e-21 |
|
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: 93.83 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG--VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVA 85
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR-DYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIPEmTVAENIYLGQLphkggivNRSLLNYEAGLQLQHLGLDIDpETPLKY----------LSIGQWQMVEIA 155
Cdd:cd03251 80 LVSQDVFLFND-TVAENIAYGRP-------GATREEVEEAARAANAHEFIM-ELPEGYdtvigergvkLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 156 KALARNAKIIAFDEPTSSL---SAREIDnlfRVIRELrQEGRVIIYVSHRMEEIfALSDAITVFKDGRYVrtfdnmQEVN 232
Cdd:cd03251 151 RALLKDPPILILDEATSALdteSERLVQ---AALERL-MKNRTTFVIAHRLSTI-ENADRIVVLEDGKIV------ERGT 219
|
....*
gi 490204990 233 HDALV 237
Cdd:cd03251 220 HEELL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
275-477 |
1.31e-21 |
|
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: 92.11 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQaiQAGMMlcpedrkaeGIIPvhsvrdn 354
Cdd:cd03214 18 LSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE--LARKI---------AYVP------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 inisarrkhilagcvinnaweaqnadQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:cd03214 80 --------------------------QALELLGL-AHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490204990 435 KHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03214 133 QIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-220 |
1.62e-21 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 91.51 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKA--LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEaLNAGVA 85
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE-LGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIPEmTVAENIylgqlphkggivnrsllnyeaglqlqhlgldidpetplkyLSIGQWQMVEIAKALARNAKII 165
Cdd:cd03246 80 YLPQDDELFSG-SIAENI----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 166 AFDEPTSSLsarEIDN---LFRVIRELRQEGRVIIYVSHRMEEIfALSDAITVFKDGR 220
Cdd:cd03246 119 VLDEPNSHL---DVEGeraLNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGR 172
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
275-472 |
1.98e-21 |
|
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: 92.60 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaidirKPAQAIQAGMMLCPEDRKAEGIIPVhSVRDN 354
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG------KPLEKERKRIGYVPQRRSIDRDFPI-SVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 InISARRKHILAGCVINNAWEAQnADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:cd03235 91 V-LMGLYGHKGLFRRLSKADKAK-VDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 490204990 435 KHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVM 472
Cdd:cd03235 168 QEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-220 |
2.80e-21 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 91.46 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 7 YLSFHGITMT-----FPGVKA-LSDISFDCYAGQVHALMGENGAGKSTLLKILSG--NYVPTAGSLQIQGQQMtfthTTE 78
Cdd:cd03213 3 TLSFRNLTVTvksspSKSGKQlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL----DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 79 ALNAGVAIIYQELHLIPEMTVAENIYlgqlphkggivnrsllnYEAGlqlqhlgldidpetpLKYLSIGQWQMVEIAKAL 158
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTLTVRETLM-----------------FAAK---------------LRGLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 159 ARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHR-MEEIFALSDAITVFKDGR 220
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGR 189
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-222 |
3.75e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.51 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 12 GITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQ----------GQQMTFThttEALN 81
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslSQQKGLI---RQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 82 AGVAIIYQELHLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARN 161
Cdd:PRK11264 85 QHVGFVFQNFNLFPHRTVLENIIEGPVIVKG--EPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 162 AKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-220 |
3.99e-21 |
|
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: 92.45 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAG-SLQIQGQQMTFTHTTEaLNAG 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWE-LRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQELHL-IPEMTVAENIYL----GQLphkgGIVN----------RSLLNYeagLQLQHLGldidpETPLKYLSIGQ 148
Cdd:COG1119 80 IGLVSPALQLrFPRDETVLDVVLsgffDSI----GLYReptdeqreraRELLEL---LGLAHLA-----DRPFGTLSQGE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 149 WQMVEIAKALARNAKIIAFDEPTSSL--SAREidNLFRVIRELRQEGRV-IIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLdlGARE--LLLALLDKLAAEGAPtLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-220 |
4.59e-21 |
|
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: 92.01 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqQMTFTHTTEALNAGVAIIYQELHLIPEMTV 99
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 100 AENIYLgqLPHKGGIVNRsllnyEAGLQLQHLG--LDIDPE--TPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLS 175
Cdd:cd03267 113 IDSFYL--LAAIYDLPPA-----RFKKRLDELSelLDLEELldTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 176 AREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03267 186 VVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-188 |
1.08e-20 |
|
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: 90.96 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 2 QQSTPYLSFHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthtt 77
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 78 eALN---------AGVAIIYQELHLIPEMTVAENIylgQLP-----HKGGIVN-RSLLNyEAGLQ--LQHLgldidPetp 140
Cdd:COG4181 78 -ALDedararlraRHVGFVFQSFQLLPTLTALENV---MLPlelagRRDARARaRALLE-RVGLGhrLDHY-----P--- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 141 lKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSARE----IDNLFRVIRE 188
Cdd:COG4181 145 -AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRE 195
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-220 |
1.16e-20 |
|
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: 90.67 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmtfTHTTEALNAGvaiiyqelhLIPEMTV 99
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR----VSSLLGLGGG---------FNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 100 AENIYLgqlphkggivNRSLLN---------YEAGLQLQHLGLDIDpeTPLKYLSIGqwQMVEIAKALARNAK--IIAFD 168
Cdd:cd03220 102 RENIYL----------NGRLLGlsrkeidekIDEIIEFSELGDFID--LPVKTYSSG--MKARLAFAIATALEpdILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 169 EptsSLSAReiDNLF-----RVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03220 168 E---VLAVG--DAAFqekcqRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-203 |
1.20e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 91.40 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 2 QQSTPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILsgNY--VPTAGSLQIQGQQMTFTHT--- 76
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCI--NLleTPDSGEIRVGGEEIRLKPDrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 77 ---------TEALNAGVAIIYQELHLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQHLGL----DIDPetplKY 143
Cdd:COG4598 81 elvpadrrqLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLG--RPKAEAIERAEALLAKVGLadkrDAYP----AH 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 144 LSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRM 203
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEM 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-220 |
1.26e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.75 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 6 PYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtftHTTEALNAG-- 83
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV---EALSARAASrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQELHLIPEMTVAENIYLGQLPHKGGIVNRSLLNYEAGLQ-LQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNA 162
Cdd:PRK09536 79 VASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERaMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 163 KIIAFDEPTSSLSA-REIDNLfRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PRK09536 159 PVLLLDEPTASLDInHQVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGR 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-239 |
1.56e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.34 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 19 GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQElhliPE-- 96
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKWVRSKVGLVFQD----PDdq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 ---MTVAENIYLGqlPHKGGIvNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSS 173
Cdd:PRK13647 92 vfsSTVWDDVAFG--PVNMGL-DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 174 LSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDNMQEVNHDALVQA 239
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQA 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-204 |
1.64e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.80 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEA------------LNAGVAIIY 88
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadknqlrlLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 89 QELHLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQHLGldIDPETPLKY---LSIGQWQMVEIAKALARNAKII 165
Cdd:PRK10619 99 QHFNLWSHMTVLENVMEAPIQVLG--LSKQEARERAVKYLAKVG--IDERAQGKYpvhLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 490204990 166 AFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRME 204
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
11-250 |
1.86e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.53 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 11 HGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEaLNAGVAIIYQE 90
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE-LAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 91 LHLIPEMTVAENIYLGQLPHKGG--------IVNRSllnyeaglqLQHLGLdidpeTPLKY-----LSIGQWQMVEIAKA 157
Cdd:COG4604 84 NHINSRLTVRELVAFGRFPYSKGrltaedreIIDEA---------IAYLDL-----EDLADryldeLSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 158 LARNAKIIAFDEPTSSLS---AREIdnlFRVIRELRQE-GRVIIYVSHrmeEI-FA--LSDAITVFKDGRyVRTFDNMQE 230
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDmkhSVQM---MKLLRRLADElGKTVVIVLH---DInFAscYADHIVAMKDGR-VVAQGTPEE 222
|
250 260
....*....|....*....|
gi 490204990 231 VnhdalvqaMVGRELGDIYG 250
Cdd:COG4604 223 I--------ITPEVLSDIYD 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
273-478 |
2.95e-20 |
|
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: 90.10 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI-DIRKPAQAIQAGMMlcPEDRKA-EGIipvhS 350
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaSLSRRELARRIAYV--PQEPPApFGL----T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNInISARRKHILAGCVINNAWEAQnADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:COG1120 92 VRELV-ALGRYPHLGLFGRPSAEDREA-VEEALERTGL-EHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 431 DVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:COG1120 169 DLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
275-478 |
5.09e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 89.38 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEaiDIRKPAQAIqaGMMlcPEDRKAEGIIPVhSVRDN 354
Cdd:COG1121 25 VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK--PPRRARRRI--GYV--PQRAEVDWDFPI-TVRDV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 InISARRKHILAGCVINNAWEAQnADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:COG1121 98 V-LMGRYGRRGLFRRPSRADREA-VDEALERVGL-EDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490204990 435 KHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:COG1121 175 EEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
281-479 |
5.69e-20 |
|
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: 88.12 E-value: 5.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 281 SGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI-DIRKpaqaiqaGMMLCPEDRKAeGII-------PVHSVR 352
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRK-------KINLPPQQRKI-GLVfqqyalfPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISARRKhilagcviNNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDV 432
Cdd:cd03297 94 ENLAFGLKRK--------RNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490204990 433 GAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIAG 479
Cdd:cd03297 165 ALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-220 |
5.90e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.66 E-value: 5.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 27 SFDCY--AGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEalnAGVAIIYQELHLIPEMTVAENIY 104
Cdd:COG3840 17 RFDLTiaAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RPVSMLFQENNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 105 LGQLPhkggivnrSL-LNYEAGLQLQH----LGL----DIDPETplkyLSIGQWQMVEIAKALARNAKIIAFDEPTSSLS 175
Cdd:COG3840 94 LGLRP--------GLkLTAEQRAQVEQalerVGLagllDRLPGQ----LSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 176 A---REIDNLfrvIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG3840 162 PalrQEMLDL---VDELCRErGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-220 |
8.54e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.55 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTpYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTeal 80
Cdd:PRK11432 1 MTQKN-FVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 81 NAGVAIIYQELHLIPEMTVAENIYLGqLPHKGgiVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALAR 160
Cdd:PRK11432 77 QRDICMVFQSYALFPHMSLGENVGYG-LKMLG--VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 161 NAKIIAFDEPTSSLSAreidNLFRV----IRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PRK11432 154 KPKVLLFDEPLSNLDA----NLRRSmrekIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
275-480 |
8.55e-20 |
|
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: 87.66 E-value: 8.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAiQAGMMLcpedrKAEGIIPVHSVRDN 354
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR-RIGALI-----EAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHIlagcvinnawEAQNADQHIKSLNIKTPGaEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:cd03268 93 LRLLARLLGI----------RKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 435 KHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:cd03268 162 IKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
275-480 |
1.11e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 87.81 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKPAQAIQAGMMLCPEDRKAEGIIpvhSVRDN 354
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPREVRRRIGIVFQDLSVDDEL---TGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARrkhiLAGcvINNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:cd03265 94 LYIHAR----LYG--VPGAERRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490204990 435 KHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:cd03265 167 RAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAE 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-222 |
1.15e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.01 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 6 PYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVA 85
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIPEMTVAENIYLGqlphkGGIVNRSllNYEAGLQLQHlglDIDPETPLK------YLSIGQWQMVEIAKALA 159
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMG-----GFFAERD--QFQERIKWVY---ELFPRLHERriqragTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 160 RNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
273-477 |
1.60e-19 |
|
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: 87.18 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEaiDIRKPAQAIQAGMmlcpedRKAEGII------ 346
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK--DLLKLSRRLRKIR------RKEIQMVfqdpms 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 ---PVHSVRDNINISARRKHILagcviNNAWEAQNAdqhIKSLNIKTPGAEQlIMN-----LSGGNQQKAILGRWLSEEM 418
Cdd:cd03257 94 slnPRMTIGEQIAEPLRIHGKL-----SKKEARKEA---VLLLLVGVGLPEE-VLNrypheLSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-220 |
1.61e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.09 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 9 SFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtftHTTEALNAGVAIIY 88
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM---NDVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 89 QELHLIPEMTVAENIYLG-QLPHKGGIVNRSLLNYEAG-LQLQHLgLDIDPetplKYLSIGQWQMVEIAKALARNAKIIA 166
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGlKLAGAKKEEINQRVNQVAEvLQLAHL-LDRKP----KALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 167 FDEPTSSLsareiDNLFRV-----IREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PRK11000 157 LDEPLSNL-----DAALRVqmrieISRLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
275-477 |
1.74e-19 |
|
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: 87.21 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMLCPED----RKAegiipvhS 350
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEasifRKL-------T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNINIsarrkhILAGCVINNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:cd03218 92 VEENILA------VLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490204990 431 DVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-253 |
1.81e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.09 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEAlNAG 83
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-SRARHA-RQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQELHLIPEMTVAENI-----YLGQLPHKGGIVNRSLLNYEAglqlqhlgLDIDPETPLKYLSIGQWQMVEIAKAL 158
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLlvfgrYFGLSAAAARALVPPLLEFAK--------LENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 159 ARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRyvrtfdNMQEVNHDALVQ 238
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR------KIAEGAPHALIE 227
|
250
....*....|....*
gi 490204990 239 AMVGRELGDIYGWQP 253
Cdd:PRK13537 228 SEIGCDVIEIYGPDP 242
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-220 |
2.00e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.57 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqmtFTHTTEALN-------AGVAIIYQELHL 93
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG----VDITDKKVKlsdirkkVGLVFQYPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 94 IPEmTVAENIYLGqlPHKGGIVNRSLLN--YEAglqLQHLGLDIDP---ETPLKyLSIGQWQMVEIAKALARNAKIIAFD 168
Cdd:PRK13637 97 FEE-TIEKDIAFG--PINLGLSEEEIENrvKRA---MNIVGLDYEDykdKSPFE-LSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490204990 169 EPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-222 |
2.58e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.30 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 2 QQSTPYlsfhgitmtfpGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqMTFTHTTE--- 78
Cdd:PRK13646 13 QKGTPY-----------EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD--ITITHKTKdky 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 79 --ALNAGVAIIYQ--ELHLIpEMTVAENIYLGqlPHKGGIVNRSLLNYEAGLQLQhLGL--DIDPETPLKyLSIGQWQMV 152
Cdd:PRK13646 80 irPVRKRIGMVFQfpESQLF-EDTVEREIIFG--PKNFKMNLDEVKNYAHRLLMD-LGFsrDVMSQSPFQ-MSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 153 EIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELR-QEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-223 |
2.79e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.96 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNA---GVAIIYQ--ELHLIp 95
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKlrkKVSLVFQfpEAQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 96 EMTVAENIYLGqlPHKGGIVNRSLlnYEAGLQ-LQHLGLDID--PETPLKyLSIGQWQMVEIAKALARNAKIIAFDEPTS 172
Cdd:PRK13641 100 ENTVLKDVEFG--PKNFGFSEDEA--KEKALKwLKKVGLSEDliSKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490204990 173 SLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVR 223
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
271-477 |
3.28e-19 |
|
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: 85.77 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIqaGMMLCPEDRkaegIIPVHS 350
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI--GYVMQDVDY----QLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNINISARRKHIlagcvinnawEAQNADQHIKSLNIKTPgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:cd03226 89 VREELLLGLKELDA----------GNEQAETVLKDLDLYAL-KERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490204990 431 DVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-238 |
3.52e-19 |
|
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: 86.44 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 18 PGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHtTEALNAGVAIIYQELHLIpEM 97
Cdd:cd03249 14 PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQIGLVSQEPVLF-DG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 98 TVAENIYLGQLPHKGGIVNRSLLNYEAglqlqHlglDIDPETPLKY----------LSIGQWQMVEIAKALARNAKIIAF 167
Cdd:cd03249 92 TIAENIRYGKPDATDEEVEEAAKKANI-----H---DFIMSLPDGYdtlvgergsqLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 168 DEPTSSL---SAREI-DNLFRVIRelrqeGRVIIYVSHRMEEIFAlSDAITVFKDGRYVrtfdnmQEVNHDALVQ 238
Cdd:cd03249 164 DEATSALdaeSEKLVqEALDRAMK-----GRTTIVIAHRLSTIRN-ADLIAVLQNGQVV------EQGTHDELMA 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
275-477 |
7.21e-19 |
|
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: 85.23 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKpaqaiqagmmlCPEDRKAE------GII-- 346
Cdd:cd03255 23 VSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDG--TDISK-----------LSEKELAAfrrrhiGFVfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 -----PVHSVRDNINISArrkhILAGcvINNAWEAQNADQHIKSLNIKTpGAEQLIMNLSGGNQQKAILGRWLSEEMKVI 421
Cdd:cd03255 90 sfnllPDLTALENVELPL----LLAG--VPKKERRERAEELLERVGLGD-RLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 422 LLDEPTRGIDVGAKHEIYNVIYALAA-SGVAVVFASSDlPEVLGVADRIVVMREGEI 477
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-220 |
1.05e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.22 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 6 PYLSFHGITMTFPGVK--ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAG 83
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS-EETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQElhliPE-----MTVAENIYLGqLPHKGgiVNRSLL--NYEAGLQLQHLG--LDIDPEtplkYLSIGQWQMVEI 154
Cdd:PRK13635 83 VGMVFQN----PDnqfvgATVQDDVAFG-LENIG--VPREEMveRVDQALRQVGMEdfLNREPH----RLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 155 AKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRV-IIYVSHRMEEIfALSDAITVFKDGR 220
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEA-AQADRVIVMNKGE 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-231 |
1.19e-18 |
|
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: 89.04 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKA--LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtFTHTTEALnaGVA 85
Cdd:COG4618 331 LSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL-SQWDREEL--GRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIY--QELHLIPEmTVAENIylgqlphkggivnrsllnyeAGLQlqhlglDIDPET-----------------PLKY--- 143
Cdd:COG4618 408 IGYlpQDVELFDG-TIAENI--------------------ARFG------DADPEKvvaaaklagvhemilrlPDGYdtr 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 144 -------LSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMeEIFALSDAITVF 216
Cdd:COG4618 461 igeggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP-SLLAAVDKLLVL 539
|
250
....*....|....*
gi 490204990 217 KDGRyVRTFDNMQEV 231
Cdd:COG4618 540 RDGR-VQAFGPRDEV 553
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
1.29e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQ----GQQMTFTHTTEA-----------LNAGV 84
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNpyskkiknfkeLRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQ--ELHLIPEmTVAENIYLGQLPHKggiVNRSLLNYEAGLQLQHLGLDID--PETPLKyLSIGQWQMVEIAKALAR 160
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIEKDIMFGPVALG---VKKSEAKKLAKFYLNKMGLDDSylERSPFG-LSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 161 NAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRT 224
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-282 |
2.39e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALN-----AGVAIIYQELHLIP 95
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpvrkkVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 96 EmTVAENIYLGqlPHKGGIvNRSLLNYEAGLQLQHLGLDID--PETPLKyLSIGQWQMVEIAKALARNAKIIAFDEPTSS 173
Cdd:PRK13643 100 E-TVLKDVAFG--PQNFGI-PKEKAEKIAAEKLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 174 LSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRT---FDNMQEVnhDALVQAMVGRELGDIYG 250
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCgtpSDVFQEV--DFLKAHELGVPKATHFA 252
|
250 260 270
....*....|....*....|....*....|....*
gi 490204990 251 WQPRE---YGKERLRLDRvkAPGVRQPVSLSVRSG 282
Cdd:PRK13643 253 DQLQKtgaVTFEKLPITR--AELVTLLTSLSVNSG 285
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
275-477 |
2.98e-18 |
|
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: 84.32 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGM-------MLCPEdrkaegiip 347
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIartfqnpRLFPE--------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 vHSVRDNINISA--RRKHILAGCVINNAWEAQN-------ADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEM 418
Cdd:COG0411 94 -LTVLENVLVAAhaRLGRGLLAALLRLPRARREerearerAEELLERVGL-ADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYALAA-SGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-220 |
3.43e-18 |
|
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: 82.36 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG--VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqmTFTHTTE-ALNAGV 84
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG---VPVSDLEkALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQELHLIpEMTVAENIylgqlphkggivnrsllnyeaGLQlqhlgldidpetplkyLSIGQWQMVEIAKALARNAKI 164
Cdd:cd03247 78 SVLNQRPYLF-DTTLRNNL---------------------GRR----------------FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 165 IAFDEPTSSLSAREIDNLFRVIRELrQEGRVIIYVSHRMEEIFALsDAITVFKDGR 220
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHM-DKILFLENGK 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
273-481 |
3.68e-18 |
|
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: 83.29 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPaqaiQAGMMLcPEDRkaegIIPVHSVR 352
Cdd:cd03293 21 EDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP----DRGYVF-QQDA----LLPWLTVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISARRKHILAGcvinnawEAQ-NADQHIKSLNIKtpGAEQL-IMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:cd03293 92 DNVALGLELQGVPKA-------EAReRAEELLELVGLS--GFENAyPHQLSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 431 DVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVM--REGEIAGEL 481
Cdd:cd03293 163 DALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEV 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-222 |
3.79e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 83.47 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSG---NYVPTAGSLQIQGQQMTFTHTTEAlnagVAIIYQELHLIPE 96
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQKC----VAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 MTVAENIY---LGQLPHKGGIVNRSLLnyEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSS 173
Cdd:cd03234 96 LTVRETLTytaILRLPRKSSDAIRKKR--VEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490204990 174 LSAREIDNLFRVIRELRQEGRVIIYVSHR-MEEIFALSDAITVFKDGRYV 222
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
275-480 |
4.07e-18 |
|
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: 83.32 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAgmmlcpedRKAEGIIPVH----- 349
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL--------RRRMGMLFQSgalfd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 --SVRDNINISARRKHILAGCVINNAweaqnADQHIKSLNIktPGAEQLiM--NLSGGNQQKAILGRWLSEEMKVILLDE 425
Cdd:cd03261 91 slTVFENVAFPLREHTRLSEEEIREI-----VLEKLEAVGL--RGAEDL-YpaELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 426 PTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-224 |
4.15e-18 |
|
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: 82.57 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 19 GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGN--YVPTAGSLQIQGQQMTFTHTTEALNAGVAIIYQELHLIPE 96
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 MTVAEniYLgqlphkggivnRSlLNYEaglqlqhlgldidpetplkyLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSA 176
Cdd:cd03217 92 VKNAD--FL-----------RY-VNEG--------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490204990 177 REIDNLFRVIRELRQEGRVIIYVSHRmEEIFAL--SDAITVFKDGRYVRT 224
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHY-QRLLDYikPDRVHVLYDGRIVKS 186
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-239 |
4.19e-18 |
|
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: 83.69 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 22 ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQElHLIPEMTVAE 101
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQVGVVLQE-NVLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 102 NIYLGQlphKGGIVNRslLNYEAGLQLQHlglDIDPETPLKY----------LSIGQWQMVEIAKALARNAKIIAFDEPT 171
Cdd:cd03252 95 NIALAD---PGMSMER--VIEAAKLAGAH---DFISELPEGYdtivgeqgagLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 172 SSLSAREIDNLFRVIRELrQEGRVIIYVSHRMEEIFAlSDAITVFKDGRYVrtfdnmQEVNHDALVQA 239
Cdd:cd03252 167 SALDYESEHAIMRNMHDI-CAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIV------EQGSHDELLAE 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
275-480 |
4.48e-18 |
|
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: 85.55 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIdirkpaQAIQAGMMLCPEDRKAeGII-------P 347
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL------FDSRKGIFLPPEKRRI-GYVfqearlfP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 VHSVRDNINISARRkhilagcvINNAWEAQNADQHIKSLNIKtPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPT 427
Cdd:TIGR02142 89 HLSVRGNLRYGMKR--------ARPSERRISFERVIELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 428 RGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-171 |
5.15e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 10 FHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqmtfthttealNAGVAIIYQ 89
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 90 ELHLIPEMTVAENIYLG------------QLPHKGGIVNRSLLNYEAgLQ------------------LQHLGL-DIDPE 138
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGdaelraleaeleELEAKLAEPDEDLERLAE-LQeefealggweaearaeeiLSGLGFpEEDLD 147
|
170 180 190
....*....|....*....|....*....|....
gi 490204990 139 TPLKYLSiGQWQM-VEIAKALARNAKIIAFDEPT 171
Cdd:COG0488 148 RPVSELS-GGWRRrVALARALLSEPDLLLLDEPT 180
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-226 |
5.15e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.94 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 10 FHGITMTFPGVK-ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIY 88
Cdd:PRK13657 337 FDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR-TVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 89 QELHLIpEMTVAENIYLGqlphKGGIVNRSLlnYEAGLQLQhlGLDIDPETPLKY----------LSIGQWQMVEIAKAL 158
Cdd:PRK13657 416 QDAGLF-NRSIEDNIRVG----RPDATDEEM--RAAAERAQ--AHDFIERKPDGYdtvvgergrqLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 159 ARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQeGRVIIYVSHRMEEIfALSDAITVFKDGRYVR--TFD 226
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTV-RNADRILVFDNGRVVEsgSFD 554
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
269-489 |
5.44e-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: 83.85 E-value: 5.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 269 PGVRQpVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDI--RKPAQAIQA---GMMLcpedrKAE 343
Cdd:cd03294 38 VGVND-VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsRKELRELRRkkiSMVF-----QSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 344 GIIPVHSVRDNINISARrkhiLAGcvINNAWEAQNADQHIKSLNIKtPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILL 423
Cdd:cd03294 112 ALLPHRTVLENVAFGLE----VQG--VPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 424 DEPTRGIDVGAKHEIYNVIYALAA-SGVAVVFASSDLPEVLGVADRIVVMREGEI-----AGELLHEHANEQ 489
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLvqvgtPEEILTNPANDY 256
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-220 |
6.85e-18 |
|
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: 87.38 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 18 PGVKALsDISFdcYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtfTHTTEALNAGVAIIYQELHLIPEM 97
Cdd:TIGR01257 944 PAVDRL-NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 98 TVAENI-YLGQLphKGGIVNRSLLNYEAglQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSL-- 174
Cdd:TIGR01257 1019 TVAEHIlFYAQL--KGRSWEEAQLEMEA--MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVdp 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490204990 175 -SAREIDNLFRVIRelrqEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:TIGR01257 1095 ySRRSIWDLLLKYR----SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-224 |
8.43e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 83.64 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTE---ALNAGVAIIYQ--ELHLIP 95
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 96 EmTVAENIYLGqlPHKGGiVNRSLLNYEAGLQLQHLGLDID--PETPLKyLSIGQWQMVEIAKALARNAKIIAFDEPTSS 173
Cdd:PRK13649 101 E-TVLKDVAFG--PQNFG-VSQEEAEALAREKLALVGISESlfEKNPFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490204990 174 LSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRT 224
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-220 |
1.03e-17 |
|
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: 82.13 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 10 FHGITMTF---PGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMT-FTHttEALNAGVA 85
Cdd:cd03248 14 FQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqYEH--KYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIPEmTVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLK--YLSIGQWQMVEIAKALARNAK 163
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKgsQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 164 IIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIyVSHRMEEIfALSDAITVFKDGR 220
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPERRTVLV-IAHRLSTV-ERADQILVLDGGR 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-220 |
1.10e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.98 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQG-----QQMTFthtteALNAGVaIIYQELHLI 94
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkRRKEF-----ARRIGV-VFGQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 95 PEMTVAEN------IYlgQLPHKggiVNRSLLNYEAGLqlqhlgLDIDP--ETPLKYLSIGQwQM-VEIAKALARNAKII 165
Cdd:COG4586 109 WDLPAIDSfrllkaIY--RIPDA---EYKKRLDELVEL------LDLGEllDTPVRQLSLGQ-RMrCELAAALLHRPKIL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 166 AFDEPT------SSLSAREidnlFrvIRELRQEGRV-IIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG4586 177 FLDEPTigldvvSKEAIRE----F--LKEYNRERGTtILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-197 |
1.40e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.07 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEA------LNAgvaiiyqelhLIPE 96
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNA----------MKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 MTVAENIYLGQlphkgGIVNRSLLNYEAGL---QLQHLGldidpETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSS 173
Cdd:PRK13539 88 LTVAENLEFWA-----AFLGGEELDIAAALeavGLAPLA-----HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*
gi 490204990 174 LSAREIDNLFRVIRE-LRQEGRVII 197
Cdd:PRK13539 158 LDAAAVALFAELIRAhLAQGGIVIA 182
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-222 |
1.44e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.97 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNA- 82
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT-ALSERELRAa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 --GVAIIYQELHLIPEMTVAENIylgQLPhkggivnrsllnyeaglqLQHLGLD---IDPE-TPL-----------KY-- 143
Cdd:COG1135 81 rrKIGMIFQHFNLLSSRTVAENV---ALP------------------LEIAGVPkaeIRKRvAELlelvglsdkadAYps 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 144 -LSIGQWQMVEIAKALARNAKIIAFDEPTSSL---SAREIDNLfrvIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKD 218
Cdd:COG1135 140 qLSGGQKQRVGIARALANNPKVLLCDEATSALdpeTTRSILDL---LKDINRElGLTIVLITHEMDVVRRICDRVAVLEN 216
|
....
gi 490204990 219 GRYV 222
Cdd:COG1135 217 GRIV 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
273-465 |
1.49e-17 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 80.99 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMmLCPEDrkaeGIIPVHSVR 352
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY-LGHAD----GLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISARrkhiLAGCVINNAweaqNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGR-WLSEEmKVILLDEPTRGID 431
Cdd:COG4133 94 ENLRFWAA----LYGLRADRE----AIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARlLLSPA-PLWLLDEPFTALD 163
|
170 180 190
....*....|....*....|....*....|....
gi 490204990 432 VGAKHEIYNVIYALAASGVAVVFASSDLPEVLGV 465
Cdd:COG4133 164 AAGVALLAELIAAHLARGGAVLLTTHQPLELAAA 197
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
275-477 |
1.86e-17 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 81.62 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDiRKPAQAIQAGMMLcpedrKAEGIIPVHSVRDN 354
Cdd:cd03296 21 VSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-DVPVQERNVGFVF-----QHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHILAGcvINNAWEAQNADQHIKSLNIKTPgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:cd03296 95 VAFGLRVKPRSER--PPEAEIRAKVHELLKLVQLDWL-ADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490204990 435 KHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03296 172 RKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-220 |
1.97e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 81.44 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVAII 87
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIYL---GQLPHKGGIVNR--SLLNYeagLQLQHLGldidpETPLKYLSIGQWQMVEIAKALARNA 162
Cdd:cd03218 81 PQEASIFRKLTVEENILAvleIRGLSKKEREEKleELLEE---FHITHLR-----KSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 163 KIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
275-477 |
2.28e-17 |
|
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: 81.10 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRkpaqaiqagmMLCPED-RKAEGIIPVH---- 349
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG--TDIR----------QLDPADlRRNIGYVPQDvtlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 --SVRDNINI---SARRKHILAgcVINNAWEAQNADQHIKSLN--IKTPGaeqliMNLSGGNQQKAILGRWLSEEMKVIL 422
Cdd:cd03245 91 ygTLRDNITLgapLADDERILR--AAELAGVTDFVNKHPNGLDlqIGERG-----RGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 423 LDEPTRGIDVGAKHEIYNVIYALAASGVAVVfaSSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGDKTLII--ITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
273-427 |
2.36e-17 |
|
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: 78.84 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDiRKPAQAIQAGMMLCPEDrkaEGIIPVHSVR 352
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQD---PQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 353 DNINISARRKHILagcvinNAWEAQNADQHIKSLNIKtPGAEQLIMN----LSGGNQQKAILGRWLSEEMKVILLDEPT 427
Cdd:pfam00005 78 ENLRLGLLLKGLS------KREKDARAEEALEKLGLG-DLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-497 |
2.62e-17 |
|
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: 81.39 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKP-AQAIQAGMMlcPEDrkAEGII-PVHSVR 352
Cdd:COG1124 24 VSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRVQMV--FQD--PYASLhPRHTVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNIN---ISARRKHILAGcvINNAWEAQNADQHIKSlniKTPGAeqlimnLSGGNQQKAILGRWLSEEMKVILLDEPTRG 429
Cdd:COG1124 100 RILAeplRIHGLPDREER--IAELLEQVGLPPSFLD---RYPHQ------LSGGQRQRVAIARALILEPELLLLDEPTSA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 430 IDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEI-----AGELL----HEHANEQQALSLAMP 497
Cdd:COG1124 169 LDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIveeltVADLLagpkHPYTRELLAASLAFE 246
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-220 |
2.99e-17 |
|
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: 80.94 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQI--QGQQMTFTHTTE----ALNAGVaIIY--QEL 91
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPreilALRRRT-IGYvsQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 92 HLIPEMT----VAEniylgQLPHKGgiVNRSLLNYEAGLQLQHLGL-----DIDPETplkyLSIGQWQMVEIAKALARNA 162
Cdd:COG4778 103 RVIPRVSaldvVAE-----PLLERG--VDREEARARARELLARLNLperlwDLPPAT----FSGGEQQRVNIARGFIADP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 163 KIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-224 |
3.73e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.66 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 13 ITMTFP-GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTT-EALNAGVAIIYQE 90
Cdd:PRK13639 7 LKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSlLEVRKTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 91 lhliPE-----MTVAENIYLGQLP---HKGGIVNRSLlnyEAglqLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNA 162
Cdd:PRK13639 87 ----PDdqlfaPTVEEDVAFGPLNlglSKEEVEKRVK---EA---LKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 163 KIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRT 224
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-224 |
4.06e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.88 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGN--YVPTAGSLQIQGQQMTFTHTTEALNAGVAIIYQ---ElhlIPEM 97
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLAFQypvE---IPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 98 TVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDpetplkYL--------SIGQWQMVEIAKALARNAKIIAFDE 169
Cdd:COG0396 93 SVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDED------FLdryvnegfSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 170 PTSSLsarEIDNLFRV---IRELRQEGRVIIYVSH--RM-EEIFAlsDAITVFKDGRYVRT 224
Cdd:COG0396 167 TDSGL---DIDALRIVaegVNKLRSPDRGILIITHyqRIlDYIKP--DFVHVLVDGRIVKS 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
273-477 |
5.82e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 79.47 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDiRKPAQAIQAGMMLCPedrkAEGIIPVHSVR 352
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS-AMPPPEWRRQVAYVP----QEPALWGGTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISARRKHIlagcvinnAWEAQNADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDV 432
Cdd:COG4619 92 DNLPFPFQLRER--------KFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 433 GAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG4619 164 ENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-244 |
5.86e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 5.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVAIIYQ---ELHLIPEM 97
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITEsrrDNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 98 TVAENIYLGQLPHKG------GIVNRSLLNYEAGLQLQHLGLDIDP-ETPLKYLSIGQWQMVEIAKALARNAKIIAFDEP 170
Cdd:PRK09700 357 SIAQNMAISRSLKDGgykgamGLFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 171 TSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDNMQEVNHDALVQAMVGRE 244
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWALPQE 510
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-224 |
6.49e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.36 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQ-------------Q 70
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyalseaE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 71 MTFTHTTE--------------ALNAGvAIIYQELhlipeMTVAENiylgqlpHKGGIvnRSllnyEAGLQLQHLGLD-- 134
Cdd:PRK11701 83 RRRLLRTEwgfvhqhprdglrmQVSAG-GNIGERL-----MAVGAR-------HYGDI--RA----TAGDWLERVEIDaa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 135 -IDpETPLKYlSIGQWQMVEIAKALARNAKIIAFDEPTS----SLSAREIDNLFRVIRELrqeGRVIIYVSHRMEEIFAL 209
Cdd:PRK11701 144 rID-DLPTTF-SGGMQQRLQIARNLVTHPRLVFMDEPTGgldvSVQARLLDLLRGLVREL---GLAVVIVTHDLAVARLL 218
|
250
....*....|....*
gi 490204990 210 SDAITVFKDGRYVRT 224
Cdd:PRK11701 219 AHRLLVMKQGRVVES 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-222 |
6.89e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.05 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 19 GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHT-TEALNAGVAIIYQEL-HLIPE 96
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKgLMKLRESVGMVFQDPdNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 MTVAENIYLG----QLPHKGgiVNRSLLNYEAGLQLQHLgldidPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTS 172
Cdd:PRK13636 98 ASVYQDVSFGavnlKLPEDE--VRKRVDNALKRTGIEHL-----KDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490204990 173 SLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
275-477 |
7.23e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKpAQAIQAGMMLCPEDR------KAEGIIPV 348
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS-ARAASRRVASVPQDTslsfefDVRQVVEM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 ----HSVRDNINISARRKhilagcVINNAWEAQNADQHikslniktpgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLD 424
Cdd:PRK09536 101 grtpHRSRFDTWTETDRA------AVERAMERTGVAQF----------ADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490204990 425 EPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK09536 165 EPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-201 |
7.30e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.16 E-value: 7.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAII 87
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA-AWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIYLGQLPHKGG------IVNRSLlnyeAGLQLQHLGldidpETPLKYLSIGQWQMVEIAKALA-- 159
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPHGSSaaqdrqIVREAL----ALVGLAHLA-----GRSYQTLSGGEQQRVQLARVLAql 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 160 -----RNAKIIAFDEPTSSLsareiD-----NLFRVIRELRQEGRVIIYVSH 201
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSAL-----DlahqhAVLRLARQLARRGGGVVAVLH 198
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-477 |
7.87e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 7.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTF----PGVKALSDISFDCYAGQVHALMGENGAGKS----TLLKIL--SGNYVPTAGSLQ-------IQGQQ 70
Cdd:PRK10261 13 LAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLrrrsrqvIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 71 MTFTHTTEALNAGVAIIYQE--LHLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQHLGLDIDPETPLKY---LS 145
Cdd:PRK10261 93 QSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQG--ASREEAMVEAKRMLDQVRIPEAQTILSRYphqLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 146 IGQWQMVEIAKALA-RNAKIIAfDEPTSSLSAREIDNLFRVIRELRQEGRV-IIYVSHRMEEIFALSDAITVFKDGRYVR 223
Cdd:PRK10261 171 GGMRQRVMIAMALScRPAVLIA-DEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 224 T------FDNMQEVNHDALVQAMvgRELGDIYGWQ-PReygkeRLRLDRVKAPGVRQP---------------------- 274
Cdd:PRK10261 250 TgsveqiFHAPQHPYTRALLAAV--PQLGAMKGLDyPR-----RFPLISLEHPAKQEPpieqdtvvdgepilqvrnlvtr 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 --------------------VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPA--QAIQAG 332
Cdd:PRK10261 323 fplrsgllnrvtrevhavekVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 333 MMLCPEDRKAEgIIPVHSVRDNInISARRKHILagcvINNAWEAQNADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGR 412
Cdd:PRK10261 403 IQFIFQDPYAS-LDPRQTVGDSI-MEPLRVHGL----LPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIAR 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 413 WLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK10261 477 ALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-476 |
8.95e-17 |
|
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: 83.30 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 33 GQVHALMGENGAGKSTLLKILSGNYVPTAGSLQ-----------IQGQQMtFTHTTEALNAGVAIIY--QELHLIPEMtv 99
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRGTEL-QDYFKKLANGEIKVAHkpQYVDLIPKV-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 100 aeniylgqlpHKGGIvnRSLLNY--EAG--------LQLQHLgLDIDpetpLKYLSIGQWQMVEIAKALARNAKIIAFDE 169
Cdd:COG1245 176 ----------FKGTV--RELLEKvdERGkldelaekLGLENI-LDRD----ISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 170 PTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSD-----------------------AITVFKDGrYVRTfD 226
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADyvhilygepgvygvvskpksvrvGINQYLDG-YLPE-E 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 227 NM---------------QEVNHDALVqamvgrELGDIYgwqpREYGKERLRLDrvkaPGvrqpvslSVRSGEIVGLFGLV 291
Cdd:COG1245 317 NVrirdepiefevhaprREKEEETLV------EYPDLT----KSYGGFSLEVE----GG-------EIREGEVLGIVGPN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 292 GAGRSELMKglfggsrITAGQVYIDGEAIDIR-----KPaQAIQAgmmlcpedrKAEGiipvhSVRDNInisarRKHIlA 366
Cdd:COG1245 376 GIGKTTFAK-------ILAGVLKPDEGEVDEDlkisyKP-QYISP---------DYDG-----TVEEFL-----RSAN-T 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 367 GCVINNAWEAqnadQHIKSLNIKtPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALA 446
Cdd:COG1245 428 DDFGSSYYKT----EIIKPLGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
|
490 500 510
....*....|....*....|....*....|.
gi 490204990 447 AS-GVAVVFASSDLPEVLGVADRIVVMrEGE 476
Cdd:COG1245 503 ENrGKTAMVVDHDIYLIDYISDRLMVF-EGE 532
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-222 |
9.45e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.42 E-value: 9.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 13 ITMTFP-GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVAIIYQEl 91
Cdd:PRK13644 7 VSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQN- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 92 hliPEM-----TVAENIYLGQ----LPhkgGIVNRSLLNyeagLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNA 162
Cdd:PRK13644 86 ---PETqfvgrTVEEDLAFGPenlcLP---PIEIRKRVD----RALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 163 KIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFAlSDAITVFKDGRYV 222
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIV 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
273-504 |
1.06e-16 |
|
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: 82.64 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMK---GLFGGSRITAGQVYIDGEaiDIRKPAQAI---QAGMM-------LCP-- 337
Cdd:COG1123 23 DGVSLTIAPGETVALVGESGSGKSTLALalmGLLPHGGRISGEVLLDGR--DLLELSEALrgrRIGMVfqdpmtqLNPvt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 338 -EDRKAEGIIpvhsvrdniNISARRKHILAgcvinnaweaqNADQHIKSLNIKTPgAEQLIMNLSGGNQQKAILGRWLSE 416
Cdd:COG1123 101 vGDQIAEALE---------NLGLSRAEARA-----------RVLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 417 EMKVILLDEPTRGIDVGAKHEIYNVIYALAA-SGVAVVFASSDLPEVLGVADRIVVMREGEI-----AGELLHEHANEQQ 490
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIvedgpPEEILAAPQALAA 239
|
250
....*....|....
gi 490204990 491 ALSLAMPKVSQAVA 504
Cdd:COG1123 240 VPRLGAARGRAAPA 253
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-222 |
1.15e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.00 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 10 FHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthtteALNAG-- 83
Cdd:PRK11153 4 LKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLT------ALSEKel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 ------VAIIYQELHLIPEMTVAENIylgQLP------HKGGIVNR--SLLNYeAGLQLQHlgldidpetpLKY---LSI 146
Cdd:PRK11153 78 rkarrqIGMIFQHFNLLSSRTVFDNV---ALPlelagtPKAEIKARvtELLEL-VGLSDKA----------DRYpaqLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 147 GQWQMVEIAKALARNAKIIAFDEPTSSL---SAREIDNLFRVI-RELrqeGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALdpaTTRSILELLKDInREL---GLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
275-478 |
1.35e-16 |
|
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: 79.15 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI------DIRKPAQAIqaGMMLcpedrKAEGIIPV 348
Cdd:cd03256 20 VSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkALRQLRRQI--GMIF-----QQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 HSVRDNINISA-RRKHILAGCVinNAW---EAQNADQHIKSLNIKTPgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLD 424
Cdd:cd03256 93 LSVLENVLSGRlGRRSTWRSLF--GLFpkeEKQRALAALERVGLLDK-AYQRADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 425 EPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-219 |
1.60e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.05 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILS--GNYVP---TAGSLQIQGQQMTFTHT-T 77
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSPRTdT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 78 EALNAGVAIIYQELHLIPeMTVAENIYLGQlpHKGGIVNRSLLNYEAGLQLQHLGL-----DIDPETPLKyLSIGQWQMV 152
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGL--RLKGIKDKQVLDEAVEKSLKGASIwdevkDRLHDSALG-LSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 153 EIAKALARNAKIIAFDEPTSSL---SAREIDNlfrVIRELRQEgRVIIYVSHRMEEIFALSDAITVFKDG 219
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALdpiSAGKIEE---TLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-222 |
1.83e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.99 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG--VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVA 85
Cdd:PRK11176 342 IEFRNVTFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR-DYTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIPEmTVAENIYLGQLPH--KGGIVNRSLLNYEAGL--QLQHlGLD--IDPETPLkyLSIGQWQMVEIAKALA 159
Cdd:PRK11176 421 LVSQNVHLFND-TIANNIAYARTEQysREQIEEAARMAYAMDFinKMDN-GLDtvIGENGVL--LSGGQRQRIAIARALL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 160 RNAKIIAFDEPTSSL---SAREIDnlfRVIRELrQEGRVIIYVSHRMEEIfALSDAITVFKDGRYV 222
Cdd:PRK11176 497 RDSPILILDEATSALdteSERAIQ---AALDEL-QKNRTSLVIAHRLSTI-EKADEILVVEDGEIV 557
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-248 |
1.84e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.20 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 19 GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGnYVPTAGSLQIQGQ---QMTFTHTTEALnagvAIIYQELHLiP 95
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIelrELDPESWRKHL----SWVGQNPQL-P 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 96 EMTVAENIYLGQLPHKGGIVNRSLLNYEAG--LQLQHLGLDidpeTPLK----YLSIGQWQMVEIAKALARNAKIIAFDE 169
Cdd:PRK11174 436 HGTLRDNVLLGNPDASDEQLQQALENAWVSefLPLLPQGLD----TPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 170 PTSSLSAReidNLFRVIRELRQ--EGRVIIYVSHRMEEIFALsDAITVFKDGRYVRTFDNMQEVNHDALVQAMVGRELGD 247
Cdd:PRK11174 512 PTASLDAH---SEQLVMQALNAasRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
.
gi 490204990 248 I 248
Cdd:PRK11174 588 I 588
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-222 |
1.99e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSG-----NYVPTAGSLQIQGQQMTFTHTTE 78
Cdd:PRK14271 18 AAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmndkvSGYRYSGDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 79 ALNAGVAIIYQELHLIPeMTVAENIYLGQLPHKggIVNRSLLNYEAGLQLQHLGL-----DIDPETPLKyLSIGQWQMVE 153
Cdd:PRK14271 98 EFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHK--LVPRKEFRGVAQARLTEVGLwdavkDRLSDSPFR-LSGGQQQLLC 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 154 IAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIyVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVII-VTHNLAQAARISDRAALFFDGRLV 241
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
269-478 |
2.04e-16 |
|
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: 77.84 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 269 PGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKpaqaiqagmmlcpedrkaegiIPV 348
Cdd:cd03369 21 PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--IDIST---------------------IPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 HSVRDNINISARRKHILAGCVINN--AWEAQNADQHIKSLNIKTPGaeqliMNLSGGNQQKAILGRWLSEEMKVILLDEP 426
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTIRSNldPFDEYSDEEIYGALRVSEGG-----LNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 427 TRGIDVGAKHEIYNVIYALaASGVAVVFASSDLPEVLGVaDRIVVMREGEIA 478
Cdd:cd03369 153 TASIDYATDALIQKTIREE-FTNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
274-478 |
2.27e-16 |
|
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: 78.00 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 274 PVSLSVRSGeIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKPAQAIQAGMMLCPEDRkaeGIIPVHSVRD 353
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPQKLRRRIGYLPQEF---GVYPNFTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 354 NINISARRKHIlagcviNNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVG 433
Cdd:cd03264 92 FLDYIAWLKGI------PSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490204990 434 AKHEIYNVIYALAASGVaVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:cd03264 165 ERIRFRNLLSELGEDRI-VILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-220 |
2.53e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFT-HTTEALNAGVAIIYQElhliPEmtvaE 101
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSkRGLLALRQQVATVFQD----PE----Q 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 102 NIYLGQLPHKGGIVNRSLLNYEA--------GLQL---QHLgldidPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEP 170
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNLGVPEAeitrrvdeALTLvdaQHF-----RHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490204990 171 TSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ 213
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-215 |
3.53e-16 |
|
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: 78.18 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 33 GQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQ---MTFTHTTEALNAGVAIIYQELHLI--PEmtvaeniYLGQ 107
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWdeiLDEFRGSELQNYFTKLLEGDVKVIvkPQ-------YVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 108 LPH--KGGIvnRSLLNY--EAGLQ---LQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREID 180
Cdd:cd03236 99 IPKavKGKV--GELLKKkdERGKLdelVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 490204990 181 NLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITV 215
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHC 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-222 |
3.92e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.69 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEaLNAGVAIIYQEL-HLIPEMT 98
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVGLVFQNPdDQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 99 VAENIYLGqlPHKGGIvNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSARE 178
Cdd:PRK13652 96 VEQDIAFG--PINLGL-DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490204990 179 IDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK13652 173 VKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-224 |
3.94e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIqGQQMTFTHTTE----ALNAGVAIIYQ--ElHLI 94
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkklkPLRKKVGIVFQfpE-HQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 95 PEMTVAENIYLGqlPHKGGI-VNRSLLNYEAGLQLQHLGLDIDPETPLKyLSIGQWQMVEIAKALARNAKIIAFDEPTSS 173
Cdd:PRK13634 99 FEETVEKDICFG--PMNFGVsEEDAKQKAREMIELVGLPEELLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 174 LSAR---EIDNLFrviRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYVRT 224
Cdd:PRK13634 176 LDPKgrkEMMEMF---YKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
7-220 |
4.45e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.31 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 7 YLsFHGITMTFpgvkalsdiSFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmTFTHTTEALNAgVAI 86
Cdd:PRK10771 9 WL-YHHLPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRP-VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIPEMTVAENIYLGQLPhkggivnrSL-LNYEAGLQLQHL----GL-DIDPETPLKyLSIGQWQMVEIAKALAR 160
Cdd:PRK10771 76 LFQENNLFSHLTVAQNIGLGLNP--------GLkLNAAQREKLHAIarqmGIeDLLARLPGQ-LSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 161 NAKIIAFDEPTSSLSA---REIDNLFRVIRELRQegRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PRK10771 147 EQPILLLDEPFSALDPalrQEMLTLVSQVCQERQ--LTLLMVSHSLEDAARIAPRSLVVADGR 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-249 |
4.69e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 18 PGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMT-FTHttEALNAGVAIIYQELHLIpE 96
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqYDH--HYLHRQVALVGQEPVLF-S 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 MTVAENIYLGQLPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLK--YLSIGQWQMVEIAKALARNAKIIAFDEPTSSL 174
Cdd:TIGR00958 569 GSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKgsQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 175 SArEIDNLFRVIRElrQEGRVIIYVSHRMEEIfALSDAITVFKDGRYVrtfdnmQEVNHDALvqamvgRELGDIY 249
Cdd:TIGR00958 649 DA-ECEQLLQESRS--RASRTVLLIAHRLSTV-ERADQILVLKKGSVV------EMGTHKQL------MEDQGCY 707
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-477 |
5.43e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.61 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDiRKPAQAIqaGMMlcPEDRkaeGIIPVHSVRDN 354
Cdd:COG4152 20 VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-PEDRRRI--GYL--PEER---GLYPKMKVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHIlagcvinNAWEA-QNADQHIKSLNIKtPGAEQLIMNLSGGNQQK-----AILGrwlseEMKVILLDEPTR 428
Cdd:COG4152 92 LVYLARLKGL-------SKAEAkRRADEWLERLGLG-DRANKKVEELSKGNQQKvqliaALLH-----DPELLILDEPFS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 429 GIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG4152 159 GLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
261-477 |
6.07e-16 |
|
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: 75.72 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 261 LRLDRV--KAPGVRQPV----SLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMM 334
Cdd:cd03246 1 LEVENVsfRYPGAEPPVlrnvSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 335 LCPEDRKAEGiipvhSVRDNInisarrkhilagcvinnaweaqnadqhikslniktpgaeqlimnLSGGNQQKAILGRWL 414
Cdd:cd03246 81 LPQDDELFSG-----SIAENI--------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 415 SEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDlPEVLGVADRIVVMREGEI 477
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
275-482 |
6.52e-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: 77.12 E-value: 6.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPaqaiqagmmlcpeDR----KAEGIIPVHS 350
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP-------------DRmvvfQNYSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNINISARRkhILAGcvINNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:TIGR01184 71 VRENIALAVDR--VLPD--LSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 431 DVGAKHEIYNVIYALAA-SGVAVVFASSDLPEVLGVADRIVVMREGEIA--GELL 482
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEeHRVTVLMVTHDVDEALLLSDRVVMLTNGPAAniGQIL 200
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-227 |
7.14e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.75 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 13 ITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSG---------NYVPTAG-SLQIQGQqmtFTHTTEALNA 82
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagSHIELLGrTVQREGR---LARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 GVAIIYQELHLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQH-------LGLDIDPETPLKYLSIGQWQMVEIA 155
Cdd:PRK09984 87 NTGYIFQQFNLVNRLSVLENVLIGALGSTP--FWRTCFSWFTREQKQRalqaltrVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 156 KALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQ-EGRVIIYVSHRM-------EEIFALSDAiTVFKDGRyVRTFDN 227
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVdyalrycERIVALRQG-HVFYDGS-SQQFDN 242
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-206 |
1.05e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.98 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVP---TAGSLQIQGQQMTfthtteALNA-- 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLT------ALPAeq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 -GVAIIYQELHLIPEMTVAENIYLGqLPHKGGIVNRSLLNYEAglqLQHLGL----DIDPETplkyLSIGQWQMVEIAKA 157
Cdd:COG4136 76 rRIGILFQDDLLFPHLSVGENLAFA-LPPTIGRAQRRARVEQA---LEEAGLagfaDRDPAT----LSGGQRARVALLRA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490204990 158 LARNAKIIAFDEPTSSLSAREIDNlFR--VIRELRQEGRVIIYVSHRMEEI 206
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAALRAQ-FRefVFEQIRQRGIPALLVTHDEEDA 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-201 |
1.13e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPY----LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHT 76
Cdd:PRK10575 1 MQEYTNHsdttFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE-SWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 77 TEALNAGVAIIYQELHLIPEMTVAENIYLGQLPHKG-----GIVNRSllNYEAGLQLqhLGLdidpeTPLKY-----LSI 146
Cdd:PRK10575 80 SKAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHGalgrfGAADRE--KVEEAISL--VGL-----KPLAHrlvdsLSG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 147 GQWQMVEIAKALARNAKIIAFDEPTSSLS-AREIDNLFRVIRELRQEGRVIIYVSH 201
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLH 206
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-222 |
1.15e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.61 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILsgN----YVPTA---GSLQIQGQQMtFTHTT--EALNAGVAIIYQEL 91
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCL--NrmndLIPGArveGEILLDGEDI-YDPDVdvVELRRRVGMVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 92 HLIPeMTVAENIYLGqlPHKGGIVNRSLLNY-------EAGL------QLQHLGLDidpetplkyLSIGQWQMVEIAKAL 158
Cdd:COG1117 102 NPFP-KSIYDNVAYG--LRLHGIKSKSELDEiveeslrKAALwdevkdRLKKSALG---------LSGGQQQRLCIARAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 159 ARNAKIIAFDEPTSSL---SAREIDNLfrvIRELRQEGRVIIyVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:COG1117 170 AVEPEVLLMDEPTSALdpiSTAKIEEL---ILELKKDYTIVI-VTHNMQQAARVSDYTAFFYLGELV 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-205 |
1.30e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.66 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtfthttEALNAGVAII 87
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------EGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIYLG-QLphkGGiVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIA 166
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGlQL---AG-VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490204990 167 FDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEE 205
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEE 191
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-220 |
1.38e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.08 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEaLNAGVAIIYQElhliPE-----M 97
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD-IRHKIGMVFQN----PDnqfvgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 98 TVAENIYLGqLPHKGgiVNRSLLNYEAGLQLQHLGL-DIDPETPLKyLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSA 176
Cdd:PRK13650 98 TVEDDVAFG-LENKG--IPHEEMKERVNEALELVGMqDFKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490204990 177 REIDNLFRVIRELRQE-GRVIIYVSHRMEEIfALSDAITVFKDGR 220
Cdd:PRK13650 174 EGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
275-480 |
1.46e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 76.77 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQ--AIQAGMMLCPEDRKAeGIIPVHSVR 352
Cdd:TIGR02769 30 VSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrAFRRDVQLVFQDSPS-AVNPRMTVR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISARrkHILAgcvINNAWEAQNADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDV 432
Cdd:TIGR02769 109 QIIGEPLR--HLTS---LDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 433 GAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:TIGR02769 184 VLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-213 |
1.50e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmtfthtteaLNAGV 84
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----------LRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 aiIYQELHLIPEM--TVAENIYLgqlphKGGIVNRSLLNYEAGLQLQHLgldidPETPLKYLSIGQWQMVEIAKALARNA 162
Cdd:PRK09544 72 --VPQKLYLDTTLplTVNRFLRL-----RPGTKKEDILPALKRVQAGHL-----IDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 163 KIIAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAI 213
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEV 191
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
8-220 |
1.73e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.76 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVK--ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGS---LQIQGQQMTfTHTTEALNA 82
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLT-AKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 GVAIIYQElhliPE-----MTVAENIYLG----QLPHKG--GIVNRSLlnYEAGLqlqhlgLDIDPETPlKYLSIGQWQM 151
Cdd:PRK13640 85 KVGIVFQN----PDnqfvgATVGDDVAFGlenrAVPRPEmiKIVRDVL--ADVGM------LDYIDSEP-ANLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 152 VEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIfALSDAITVFKDGR 220
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGK 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
261-475 |
2.65e-15 |
|
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: 79.29 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 261 LRLDRVKA--PGVRQP----VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIdiRKPAQAIQAGMM 334
Cdd:TIGR01257 1938 LRLNELTKvySGTSSPavdrLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 335 LCPEdrkAEGIIPVHSVRDNINISARRKHILAGCVinnaweAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWL 414
Cdd:TIGR01257 2016 YCPQ---FDAIDDLLTGREHLYLYARLRGVPAEEI------EKVANWSIQSLGL-SLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 415 SEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREG 475
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-234 |
3.25e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEAL 80
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS-TLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 81 NAGVAIIYQELHLIPEmTVAEN-IYLGQLPHKGGIVNRSLLNyeaglqLQHLGLdidPETPLKY----LSIGQWQMVEIA 155
Cdd:PRK10247 80 RQQVSYCAQTPTLFGD-TVYDNlIFPWQIRNQQPDPAIFLDD------LERFAL---PDTILTKniaeLSGGEKQRISLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 156 KALARNAKIIAFDEPTSSLSAREIDNLFRVI-RELRQEGRVIIYVSHRMEEIFALSDAITVFKDGryvrtfDNMQEVNHD 234
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIhRYVREQNIAVLWVTHDKDEINHADKVITLQPHA------GEMQEARYE 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-239 |
3.33e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAII 87
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-DWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIYLGQLPHKGG------IVNRSLlnyeAGLQLQHLGldidpETPLKYLSIGQWQMVEIAKALAR- 160
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHGLSraeddaLVAAAL----AQVDLAHLA-----GRDYPQLSGGEQQRVQLARVLAQl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 161 -----NAKIIAFDEPTSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGRY--------VRTFD 226
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLvadgtpaeVLTPE 232
|
250
....*....|....
gi 490204990 227 NMQEV-NHDALVQA 239
Cdd:PRK13548 233 TLRRVyGADVLVQP 246
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
275-477 |
4.75e-15 |
|
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: 74.21 E-value: 4.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDirkpaqaiqagmMLCPEDR------KAEGIIPV 348
Cdd:cd03301 19 LNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT------------DLPPKDRdiamvfQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 HSVRDNINISARRKHIlagcvinnawEAQNADQHIKSLnIKTPGAEQLIMN----LSGGNQQKAILGRWLSEEMKVILLD 424
Cdd:cd03301 87 MTVYDNIAFGLKLRKV----------PKDEIDERVREV-AELLQIEHLLDRkpkqLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 425 EPTRGID----VGAKHEIYNVIYALaasGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03301 156 EPLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
7.35e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.79 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFPGVKA--LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTE 78
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT-DDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 79 ALNAGVAIIYQElhliPE-----MTVAENIYLG----QLPHKG--GIVNRSL-----LNYEaglqlqhlglDIDPETplk 142
Cdd:PRK13648 80 KLRKHIGIVFQN----PDnqfvgSIVKYDVAFGlenhAVPYDEmhRRVSEALkqvdmLERA----------DYEPNA--- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 143 yLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRV-IIYVSHRMEEIfALSDAITVFKDG 219
Cdd:PRK13648 143 -LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItIISITHDLSEA-MEADHVIVMNKG 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
275-478 |
7.72e-15 |
|
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: 77.18 E-value: 7.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKpaqaiqagmmLCPED-RKAEGIIPVH---- 349
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG--IDLRQ----------IDPASlRRQIGVVLQDvflf 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 --SVRDNI---NISARRKHILAGCvinnawEAQNADQHIKSLniktP-GAEQLIM----NLSGGNQQKAILGRWLSEEMK 419
Cdd:COG2274 562 sgTIRENItlgDPDATDEEIIEAA------RLAGLHDFIEAL----PmGYDTVVGeggsNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 420 VILLDEPTRGIDVGAKHEIYNVIYALAAsGVAVVFASSDLpEVLGVADRIVVMREGEIA 478
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIV 688
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-226 |
9.42e-15 |
|
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: 76.76 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQ-GQQMTFTHTTEALNAGVA-----IIYQELHL 93
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGRGRAkryigILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 94 IPEMTVAEN----IYLgQLPHKggivnrsLLNYEAGLQLQHLGLDIDPETPL--KY---LSIGQWQMVEIAKALARNAKI 164
Cdd:TIGR03269 377 YPHRTVLDNlteaIGL-ELPDE-------LARMKAVITLKMVGFDEEKAEEIldKYpdeLSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 165 IAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFD 226
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-238 |
1.05e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.40 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 2 QQSTPYLSFHGITMTFPG--VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEA 79
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 80 LNAGVAIIYQELHLIPEmTVAENIYLGQlPHKggivnrsllNYEAGLQ-LQHLGLD--IDPETPL--------KYLSIGQ 148
Cdd:PRK11160 412 LRQAISVVSQRVHLFSA-TLRDNLLLAA-PNA---------SDEALIEvLQQVGLEklLEDDKGLnawlgeggRQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 149 WQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQeGRVIIYVSHR---MEEIfalsDAITVFKDGRYVrtf 225
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRltgLEQF----DRICVMDNGQII--- 552
|
250
....*....|...
gi 490204990 226 dnmQEVNHDALVQ 238
Cdd:PRK11160 553 ---EQGTHQELLA 562
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
273-481 |
1.09e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 73.97 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMK---GLfggSRITAGQVYIDGEAIdiRKPAQAIqaGMMLcPEDRkaegIIPVH 349
Cdd:COG1116 28 DDVSLTVAAGEFVALVGPSGCGKSTLLRliaGL---EKPTSGEVLVDGKPV--TGPGPDR--GVVF-QEPA----LLPWL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 SVRDNINISARRKHIlagcviNNAWEAQNADQHIKSLNIKtpGAEQ-LIMNLSGGNQQKAILGRWLSEEMKVILLDEPTR 428
Cdd:COG1116 96 TVLDNVALGLELRGV------PKAERRERARELLELVGLA--GFEDaYPHQLSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 429 GIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVM--REGEIAGEL 481
Cdd:COG1116 168 ALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEI 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
275-487 |
1.14e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.64 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAiQAGMMLcpedrKAEGIIPVHSVRDN 354
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR-PINMMF-----QSYALFPHMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHiLAGCVINNAWEAQNADQHIKSLNIKTPgaeqliMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:PRK11607 112 IAFGLKQDK-LPKAEIASRVNEMLGLVHMQEFAKRKP------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 435 KHEI-YNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAG----ELLHEHAN 487
Cdd:PRK11607 185 RDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQigepEEIYEHPT 242
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-277 |
1.22e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 3 QSTPyLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLqiqgqqMTFTHTTEALNA 82
Cdd:PRK11247 9 QGTP-LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 GVAIIYQELHLIPEMTVAENIYLGQlphKGGIVNRSLlnyEAglqLQHLGL-DIDPETPLKyLSIGQWQMVEIAKALARN 161
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGL---KGQWRDAAL---QA---LAAVGLaDRANEWPAA-LSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 162 AKIIAFDEPTSSLsareiDNLFRV-----IREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGRyvrtfdnmqevnhda 235
Cdd:PRK11247 152 PGLLLLDEPLGAL-----DALTRIemqdlIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK--------------- 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490204990 236 lvqamVGRELG-DIYgwQPREYGKERLR------LDRVKAPGVRQPVSL 277
Cdd:PRK11247 212 -----IGLDLTvDLP--RPRRRGSARLAeleaevLQRVMSRGESEPTRL 253
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-201 |
1.27e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.00 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTF--THTTEALNAGVAIIYQELH--LIP 95
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadPEAQKLLRQKIQIVFQNPYgsLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 96 EMTVaeniylGQLPHKGGIVNRSLLNYE----AGLQLQHLGLdiDPETPLKY---LSIGQWQMVEIAKALARNAKIIAFD 168
Cdd:PRK11308 108 RKKV------GQILEEPLLINTSLSAAErrekALAMMAKVGL--RPEHYDRYphmFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 490204990 169 EPTSSL--SAR-EIDNLFrviRELRQE-GRVIIYVSH 201
Cdd:PRK11308 180 EPVSALdvSVQaQVLNLM---MDLQQElGLSYVFISH 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
275-477 |
1.83e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 74.41 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMK---GLfggSRITAGQVYIDGEAIDIRKPAQAIQAGMM-----LCPedrkaegii 346
Cdd:COG1118 21 VSLEIASGELVALLGPSGSGKTTLLRiiaGL---ETPDSGRIVLNGRDLFTNLPPRERRVGFVfqhyaLFP--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 pvH-SVRDNINISARRKHIlagcviNNAWEAQNADQHIKSLNIktPG-AEQLIMNLSGGNQQKAILGRWLSEEMKVILLD 424
Cdd:COG1118 89 --HmTVAENIAFGLRVRPP------SKAEIRARVEELLELVQL--EGlADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 425 EPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-476 |
1.89e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 33 GQVHALMGENGAGKSTLLKILSGNYVPTAGSLQ-----------IQGQQMtFTHTTEALNAGVAIIY--QELHLIPEmtv 99
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdevlkrFRGTEL-QNYFKKLYNGEIKVVHkpQYVDLIPK--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 100 aeniYLgqlphKGGIvnRSLL--NYEAGLQ---LQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSL 174
Cdd:PRK13409 175 ----VF-----KGKV--RELLkkVDERGKLdevVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 175 SAREIDNLFRVIRELrQEGRVIIYVSHRMEEIFALSD-----------------------AITVFKDGrYVRTfDNMQ-- 229
Cdd:PRK13409 244 DIRQRLNVARLIREL-AEGKYVLVVEHDLAVLDYLADnvhiaygepgaygvvskpkgvrvGINEYLKG-YLPE-ENMRir 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 230 -------------EVNHDALVqamvgrELGDIYgwqpREYGKERLRLDrvkaPGvrqpvslSVRSGEIVGLFGLVGAGRS 296
Cdd:PRK13409 321 pepiefeerpprdESERETLV------EYPDLT----KKLGDFSLEVE----GG-------EIYEGEVIGIVGPNGIGKT 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 297 ELMKGLFGGSRITAGQVYIDgeaIDIR-KPaQAIQAgmmlcpedrKAEGiipvhSVRDNI-NISARrkhilagcvINNAW 374
Cdd:PRK13409 380 TFAKLLAGVLKPDEGEVDPE---LKISyKP-QYIKP---------DYDG-----TVEDLLrSITDD---------LGSSY 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 375 EAQNAdqhIKSLNIKtPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAA-SGVAVV 453
Cdd:PRK13409 433 YKSEI---IKPLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEeREATAL 508
|
490 500
....*....|....*....|...
gi 490204990 454 FASSDLPEVLGVADRIVVMrEGE 476
Cdd:PRK13409 509 VVDHDIYMIDYISDRLMVF-EGE 530
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-220 |
2.47e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.21 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 19 GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEA--LNAGVAIIYQELHLIPE 96
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 MTVAENIylgQLPHKGGIVNRSLLNYEAGLQLQHLG-LDIDPETPLKyLSIGQWQMVEIAKALARNAKIIAFDEPTSSLS 175
Cdd:PRK10908 94 RTVYDNV---AIPLIIAGASGDDIRRRVSAALDKVGlLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490204990 176 AREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PRK10908 170 DALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
275-477 |
2.98e-14 |
|
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: 71.79 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAI---QAGMmlcpedrkaegiipvhsV 351
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqKVGM-----------------V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 352 RDNINISARRKhilagcVINNAWEAQnadqhIKSLNIKTPGAEQLIM-----------------NLSGGNQQKAILGRWL 414
Cdd:cd03262 82 FQQFNLFPHLT------VLENITLAP-----IKVKGMSKAEAEERALellekvgladkadaypaQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 415 SEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
275-477 |
3.57e-14 |
|
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: 71.98 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMLCPEDRKAEGIIPVHSVRDN 354
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 inisarrKHILAgcvINNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:cd03267 120 -------AAIYD---LPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490204990 435 KHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03267 189 QENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
267-477 |
3.92e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 267 KAPGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMLCPEDrkaEGII 346
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE---ASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 PVHSVRDNINISARRKHILagcviNNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEP 426
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRDDL-----SAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490204990 427 TRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
275-480 |
4.32e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.83 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMLCPEDRKaegIIPVHSVRDN 354
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRR---VFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISArrkhILAgcvinnawEAQNADQHIKSLNIKTPGAE----QLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:PRK11614 101 LAMGG----FFA--------ERDQFQERIKWVYELFPRLHerriQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490204990 431 DVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-202 |
5.66e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtfTHTTEALNAGVAIIYQELHLIPEMTVAEN 102
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 103 IYLGQLPHKGGIVNRSLLNYeagLQLQHLgLDIdpetPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNL 182
Cdd:PRK13540 95 CLYDIHFSPGAVGITELCRL---FSLEHL-IDY----PCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|
gi 490204990 183 FRVIRELRQEGRVIIYVSHR 202
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSHQ 186
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
271-496 |
5.93e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.03 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQ--AIQAGMMLCPEDrkAEGII-P 347
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkAFRRDIQMVFQD--SISAVnP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 VHSVRDNINISARrkHILAgcvINNAWEAQNADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPT 427
Cdd:PRK10419 105 RKTVREIIREPLR--HLLS---LDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 428 RGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEI-----AGELLHEHANEQQALSLAM 496
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetqpVGDKLTFSSPAGRVLQNAV 254
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-217 |
6.75e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.61 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSgNYVPTAGSLQIQGQQMTFTHTT--- 77
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRVEFFNQNIyer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 78 ----EALNAGVAIIYQELHLIPeMTVAENI-----YLGQLP--HKGGIVNRSLLNYEAGLQLQH----LGLDidpetplk 142
Cdd:PRK14258 80 rvnlNRLRRQVSMVHPKPNLFP-MSVYDNVaygvkIVGWRPklEIDDIVESALKDADLWDEIKHkihkSALD-------- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 143 yLSIGQWQMVEIAKALARNAKIIAFDEPTSSL---SAREIDNLFRVIReLRQEGRVIIyVSHRMEEIFALSDAITVFK 217
Cdd:PRK14258 151 -LSGGQQQRLCIARALAVKPKVLLMDEPCFGLdpiASMKVESLIQSLR-LRSELTMVI-VSHNLHQVSRLSDFTAFFK 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
275-477 |
9.10e-14 |
|
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: 70.83 E-value: 9.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPaqaIQAGMMLCPEDRkaeGIIPVHSVRDN 354
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYVPQNY---ALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKhilagcVINNAWEAQNADQHIKSLNI-----KTPGaeqlimNLSGGNQQKAILGRWLSEEMKVILLDEPTRG 429
Cdd:cd03299 92 IAYGLKKR------KVDKKEIERKVLEIAEMLGIdhllnRKPE------TLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 430 IDVGAKHE-IYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03299 160 LDVRTKEKlREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
273-472 |
1.04e-13 |
|
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: 73.47 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAiqagmmlcpedRKAEGIIPVH--- 349
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-----------RDQIAWVPQHpfl 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 ---SVRDNINISARRKhilAGCVINNAWEAQNADQHIKSL--NIKTPGAEQLIMnLSGGNQQKAILGRWLSEEMKVILLD 424
Cdd:TIGR02857 408 fagTIAENIRLARPDA---SDAEIREALERAGLDEFVAALpqGLDTPIGEGGAG-LSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490204990 425 EPTRGIDVGAKHEIYNVIYALaASGVAVVFASSDlPEVLGVADRIVVM 472
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-222 |
1.12e-13 |
|
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: 73.18 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTL-LKILsgNYVPTAGSLQIQGQQMTfTHTTEALNA---GVAIIYQELH--L 93
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL--RLIPSEGEIRFDGQDLD-GLSRRALRPlrrRMQVVFQDPFgsL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 94 IPEMTVAEniylgqlphkggIVnrsllnyEAGLQLQHLGLD----------------IDPETPLKY---LSIGQWQMVEI 154
Cdd:COG4172 376 SPRMTVGQ------------II-------AEGLRVHGPGLSaaerrarvaealeevgLDPAARHRYpheFSGGQRQRIAI 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 155 AKALARNAKIIAFDEPTSSL--SAR-EIDNLFrviRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALdvSVQaQILDLL---RDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
265-484 |
1.13e-13 |
|
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: 70.59 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 265 RVKAPGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQ-AIQAGMMLcpedrkAE 343
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWlRRQVGVVL------QE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 344 GIIPVHSVRDNINIS----ARRKHILAgcvinnaweAQNADQHikSLNIKTP-GAEQLI----MNLSGGNQQKAILGRWL 414
Cdd:cd03252 85 NVLFNRSIRDNIALAdpgmSMERVIEA---------AKLAGAH--DFISELPeGYDTIVgeqgAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 415 SEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSdLPEVLGvADRIVVMREGEIAGELLHE 484
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHR-LSTVKN-ADRIIVMEKGRIVEQGSHD 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
273-477 |
1.23e-13 |
|
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: 70.34 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIdIRKPAQAIQAGMMLcpedrKAEGIIPVHSVR 352
Cdd:cd03300 17 DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVF-----QNYALFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISARRKHIlagcviNNAWEAQNADQHIKSLNIKTPgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDV 432
Cdd:cd03300 91 ENIAFGLRLKKL------PKAEIKERVAEALDLVQLEGY-ANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 433 GAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03300 164 KLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-477 |
1.36e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 24 SDISFDCYAGQVHALMGENGAGKS-TLLKIL----SGNYVPTAGSLQIQGQQMTftHTTEALNAGV-----AIIYQE--L 91
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFHGESLL--HASEQTLRGVrgnkiAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 92 HLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQHLGLDIDPETPLKY---LSIGQWQMVEIAKALARNAKIIAFD 168
Cdd:PRK15134 104 SLNPLHTLEKQLYEVLSLHRG--MRREAARGEILNCLDRVGIRQAAKRLTDYphqLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 169 EPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDNMQEVN---HDALVQAMVGRE 244
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSaptHPYTQKLLNSEP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 245 LGDiygwqPREYGKERLRLDRVKAPGVRQPV------------------SLSVRSGEIVGLFGLVGAGRSELMKGLFggs 306
Cdd:PRK15134 262 SGD-----PVPLPEPASPLLDVEQLQVAFPIrkgilkrtvdhnvvvkniSFTLRPGETLGLVGESGSGKSTTGLALL--- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 307 RITA--GQVYIDGEAIDIRKPAQaiqagmMLcPEDRKAEGII--PVHSVRDNINIsarrKHILA-GCVINNAW--EAQNA 379
Cdd:PRK15134 334 RLINsqGEIWFDGQPLHNLNRRQ------LL-PVRHRIQVVFqdPNSSLNPRLNV----LQIIEeGLRVHQPTlsAAQRE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 380 DQHIKSLN---------IKTPGAeqlimnLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-G 449
Cdd:PRK15134 403 QQVIAVMEevgldpetrHRYPAE------FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQ 476
|
490 500
....*....|....*....|....*...
gi 490204990 450 VAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK15134 477 LAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-222 |
1.54e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNA-----GVAIIYQELHLIPEM 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklrkEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 98 TVAENIYLGQLPHkgGIVNRSLLNYEAGLQLQHLGLDIDP----ETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSS 173
Cdd:PRK14246 106 SIYDNIAYPLKSH--GIKEKREIKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 174 LSAREIDNLFRVIRELRQEGRVIIyVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVI-VSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
273-476 |
1.76e-13 |
|
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: 68.56 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKpaqaiqagmmlcpedrkaegiIPVHSVR 352
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG--VDLRD---------------------LDLESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISARRKHILAGCVINNaweaqnadqhikslniktpgaeqlImnLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDV 432
Cdd:cd03228 76 KNIAYVPQDPFLFSGTIREN------------------------I--LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490204990 433 GAKHEIYNVIYALAAsGVAVVFASSDLpEVLGVADRIVVMREGE 476
Cdd:cd03228 130 ETEALILEALRALAK-GKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-220 |
1.80e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.50 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTF-PG----VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtfTHTTEalna 82
Cdd:COG1101 2 LELKNLSKTFnPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV--TKLPE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 gvaiiYQELHLI------------PEMTVAENIYLGQLPHKGGIVNRSLLNYEAGL---QLQHLGLDID--PETPLKYLS 145
Cdd:COG1101 76 -----YKRAKYIgrvfqdpmmgtaPSMTIEENLALAYRRGKRRGLRRGLTKKRRELfreLLATLGLGLEnrLDTKVGLLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 146 IGQWQMVEIAKALARNAKIIAFDEPTSSL---SAREIDNLF-RVIRElrqEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALdpkTAALVLELTeKIVEE---NNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-222 |
1.95e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSgNYVPT----AGSLQIQGQQMTfthtTEALNAGVAIIYQELHLIPEMT 98
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPID----AKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 99 VAENIYLG---QLPHKGGIVNRSLLNYEAglqLQHLGLD------IDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDE 169
Cdd:TIGR00955 116 VREHLMFQahlRMPRRVTKKEKRERVDEV---LQALGLRkcantrIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 170 PTSSLSAREIDNLFRVIRELRQEGRVIIYVSHR-MEEIFALSDAITVFKDGRYV 222
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVA 246
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-201 |
2.29e-13 |
|
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: 68.92 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmtfthtteALNAGVAII 87
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT---------PLAEQRDEP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLI-------PEMTVAENiyLGQLPHKGGIVNRSLLNyeaglQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALAR 160
Cdd:TIGR01189 72 HENILYLghlpglkPELSALEN--LHFWAAIHGGAQRTIED-----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490204990 161 NAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSH 201
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
275-477 |
2.56e-13 |
|
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: 69.13 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSEL------MKGLFGGSRITaGQVYIDGEaiDIRKPAQAIQagmmlcpEDRKAEGII-- 346
Cdd:cd03260 19 ISLDIPKGEITALIGPSGCGKSTLlrllnrLNDLIPGAPDE-GEVLLDGK--DIYDLDVDVL-------ELRRRVGMVfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 ---PVH-SVRDNINISAR-----RKHILAGCV-----INNAWEAQNADQHIKSLniktpgaeqlimnlSGGNQQKAILGR 412
Cdd:cd03260 89 kpnPFPgSIYDNVAYGLRlhgikLKEELDERVeealrKAALWDEVKDRLHALGL--------------SGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 413 WLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASgVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-227 |
2.58e-13 |
|
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: 69.06 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTF-PGVK-ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVA 85
Cdd:cd03244 3 IEFKNVSLRYrPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-KIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 IIYQELHLIpEMTVAENI-YLGQlpHKGGIVNRSLLnyEAGL----QLQHLGLDIDPETPLKYLSIGQWQMVEIAKALAR 160
Cdd:cd03244 82 IIPQDPVLF-SGTIRSNLdPFGE--YSDEELWQALE--RVGLkefvESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 161 NAKIIAFDEPTSSLSaREIDNL-FRVIRElRQEGRVIIYVSHRMEEIFAlSDAITVFKDGRyVRTFDN 227
Cdd:cd03244 157 KSKILVLDEATASVD-PETDALiQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGR-VVEFDS 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
275-477 |
2.63e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.67 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSE---LMKGLFggsRITAGQVYIDGEaiDI-RKP----AQAiqaGMMLCPED----RKA 342
Cdd:COG1137 22 VSLEVNQGEIVGLLGPNGAGKTTtfyMIVGLV---KPDSGRIFLDGE--DItHLPmhkrARL---GIGYLPQEasifRKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 343 egiipvhSVRDNI-------NIS-ARRKHILagcvinnaweaqnaDQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWL 414
Cdd:COG1137 94 -------TVEDNIlavlelrKLSkKEREERL--------------EELLEEFGI-THLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 415 SEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG1137 152 ATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
275-472 |
2.64e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.41 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEaidiRKPAqaiqagmmLCPEDRKAEGIIPVhSVRDN 354
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----ARVA--------YVPQRSEVPDSLPL-TVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISA-------RRKHILAGCVINNAWEAQnadqHIKSLniktpgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPT 427
Cdd:NF040873 78 VAMGRwarrglwRRLTRDDRAAVDDALERV----GLADL------AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490204990 428 RGIDVGAKHEIYNVIYALAASGVAVVFASSDlPEVLGVADRIVVM 472
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHD-LELVRRADPCVLL 191
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-226 |
2.95e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.50 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQI-------QGQQMTFTHTTEALNAG---------- 83
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknKKKTKEKEKVLEKLVIQktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 ------VAIIYQ--ELHLIpEMTVAENIYLGqlPHKGGIVNRSLLNyEAGLQLQHLGLDID--PETPLKyLSIGQWQMVE 153
Cdd:PRK13651 101 keirrrVGVVFQfaEYQLF-EQTIEKDIIFG--PVSMGVSKEEAKK-RAAKYIELVGLDESylQRSPFE-LSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 154 IAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVR---TFD 226
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKdgdTYD 251
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
275-484 |
3.20e-13 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 69.18 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKPAQaiqagmmlcPEDRKAEGIIPVHSV--- 351
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG--QDIREVTL---------DSLRRAIGVVPQDTVlfn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 352 ---RDNI---NISARRKHILAGCvinnawEAQNADQHIKSLNIK--TPGAEQLIMnLSGGNQQKAILGRWLSEEMKVILL 423
Cdd:cd03253 89 dtiGYNIrygRPDATDEEVIEAA------KAAQIHDKIMRFPDGydTIVGERGLK-LSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 424 DEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSdLPEVLGvADRIVVMREGEIAGELLHE 484
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHR-LSTIVN-ADKIIVLKDGRIVERGTHE 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
261-491 |
3.47e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 69.01 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 261 LRLDRVKapgVRQPV-----SLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQaiqagmml 335
Cdd:COG3840 2 LRLDDLT---YRYGDfplrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 336 cpedRkaegiiPV-----------H-SVRDNI--NISARRKhiLagcvinNAWEAQNADQHIKSLNI-----KTPGAeql 396
Cdd:COG3840 71 ----R------PVsmlfqennlfpHlTVAQNIglGLRPGLK--L------TAEQRAQVEQALERVGLaglldRLPGQ--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 397 imnLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREG 475
Cdd:COG3840 130 ---LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADG 206
|
250 260
....*....|....*....|.
gi 490204990 476 EIA-----GELLHEHANEQQA 491
Cdd:COG3840 207 RIAadgptAALLDGEPPPALA 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-220 |
3.61e-13 |
|
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: 68.26 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVK-----ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqmtfthttealna 82
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 GVAIIYQElHLIPEMTVAENIYLGQlPhkggivnrslLN---YEAGLQLQHLGLDID--PETPLKY-------LSIGQWQ 150
Cdd:cd03250 67 SIAYVSQE-PWIQNGTIRENILFGK-P----------FDeerYEKVIKACALEPDLEilPDGDLTEigekginLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 151 MVEIAKALARNAKIIAFDEPTSSLSAREIDNLF-RVIRELRQEGRVIIYVSHRMeEIFALSDAITVFKDGR 220
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
275-478 |
4.28e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.97 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKPAQAI-----QAGMM-----LCPEDRKAEG 344
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDErlirqEAGMVfqqfyLFPHLTALEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 345 II--PVHsVRDNINISARRkhiLAGCVINNAWEAQNADqHIKSlniktpgaeqlimNLSGGNQQKAILGRWLSEEMKVIL 422
Cdd:PRK09493 98 VMfgPLR-VRGASKEEAEK---QARELLAKVGLAERAH-HYPS-------------ELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 423 LDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
275-478 |
4.38e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 69.69 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI--------DIRKpaqaiQAGMML-CPEDRKAEGI 345
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkvklsDIRK-----KVGLVFqYPEYQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 346 IpvhsvrdninisarRKHILAGCVINNAWEAQNADQHIKSLNI----------KTPgaeqliMNLSGGNQQK-AILGRwL 414
Cdd:PRK13637 101 I--------------EKDIAFGPINLGLSEEEIENRVKRAMNIvgldyedykdKSP------FELSGGQKRRvAIAGV-V 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 415 SEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-202 |
5.33e-13 |
|
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: 71.24 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 6 PYLSFHGITMTFPG-VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEaLNAGV 84
Cdd:TIGR02868 333 PTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE-VRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 85 AIIYQELHLIpEMTVAENIYLGqlphKGGIVNRSLLNYEAGLQLQHL------GLDIDPETPLKYLSIGQWQMVEIAKAL 158
Cdd:TIGR02868 412 SVCAQDAHLF-DTTVRENLRLA----RPDATDEELWAALERVGLADWlralpdGLDTVLGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 159 ARNAKIIAFDEPTSSLSAREIDnlfRVIRELRQ--EGRVIIYVSHR 202
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETAD---ELLEDLLAalSGRTVVLITHH 529
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
275-480 |
5.98e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.15 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMkGLFGG-SRITAGQVYIDGEAIdirkpaqaiqAGMmlcPEDRKAE------GII- 346
Cdd:COG1136 27 VSLSIEAGEFVAIVGPSGSGKSTLL-NILGGlDRPTSGEVLIDGQDI----------SSL---SERELARlrrrhiGFVf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 ------PVHSVRDNINISARrkhiLAGcvINNAWEAQNADQHIKSLNI-----KTPGAeqlimnLSGGNQQKAILGRWLS 415
Cdd:COG1136 93 qffnllPELTALENVALPLL----LAG--VSRKERRERARELLERVGLgdrldHRPSQ------LSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 416 EEMKVILLDEPTRGIDVGAKHEIYNVIYALAA-SGVAVVFASSDlPEVLGVADRIVVMREGEIAGE 480
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-223 |
6.42e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.45 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 22 ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQG---QQMTFTHTTEALNAGVAIIYQELHLIPEMT 98
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 99 VAENIYLGQLPHKGGIVNRSLLNYEAglqLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLsare 178
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDA---LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL---- 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490204990 179 iDNLFR------VIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVR 223
Cdd:PRK10070 196 -DPLIRtemqdeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-239 |
7.28e-13 |
|
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: 71.00 E-value: 7.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQELHLIPEmTVAEN 102
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR-DVTQASLRAAIGIVPQDTVLFND-TIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 103 IYLGQLphkggivNRSLLNYEAGLQLQHLGLDID--P---ETP-----LKyLSIGQWQMVEIAKALARNAKIIAFDEPTS 172
Cdd:COG5265 452 IAYGRP-------DASEEEVEAAARAAQIHDFIEslPdgyDTRvgergLK-LSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 173 SL---SAREI-DNLFRVIRelrqeGRVIIYVSHRmeeifaLS-----DAITVFKDGRYVrtfdnmQEVNHDALVQA 239
Cdd:COG5265 524 ALdsrTERAIqAALREVAR-----GRTTLVIAHR------LStivdaDEILVLEAGRIV------ERGTHAELLAQ 582
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
274-475 |
8.60e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.04 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 274 PVSLSVRSGEIVGLFGLVGAGRSEL---MKGLFGGSritaGQVYIDGEAI-DIRKPAQAIQAGMmLCPEDRKAeGIIPVH 349
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLlarMAGLLPGS----GSIQFAGQPLeAWSAAELARHRAY-LSQQQTPP-FAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 -----SVRDNINISARRKHIlagcvinnaweaqnaDQHIKSLNIkTPGAEQLIMNLSGGNQQK-----AILGRW--LSEE 417
Cdd:PRK03695 88 qyltlHQPDKTRTEAVASAL---------------NEVAEALGL-DDKLGRSVNQLSGGEWQRvrlaaVVLQVWpdINPA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 418 MKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREG 475
Cdd:PRK03695 152 GQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-217 |
9.61e-13 |
|
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: 70.58 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 2 QQSTPYLSFHGITMTFPGVKaLSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSlqiqgqqmtfthtteaLN 81
Cdd:COG1245 336 KEEETLVEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE----------------VD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 82 AGVAIIY--QELHLIPEMTVAEniYLGQlpHKGGIVNRSLLNYEAglqLQHLGLDIDPETPLKYLSIGQWQMVEIAKALA 159
Cdd:COG1245 399 EDLKISYkpQYISPDYDGTVEE--FLRS--ANTDDFGSSYYKTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLS 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 160 RNAKIIAFDEPTSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFK 217
Cdd:COG1245 472 RDADLYLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
256-477 |
1.00e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.12 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 256 YGKERlrldrvkapgVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLfggSRI---TAGQVYIDGEAIDIRKPAQAIQAG 332
Cdd:PRK11231 12 YGTKR----------ILNDLSLSLPTGKITALIGPNGCGKSTLLKCF---ARLltpQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 333 MMLCPEDRKAEGIipvhSVRDNI------------NISARRKHIlagcvINNAWEaqnaDQHIKSLniktpgAEQLIMNL 400
Cdd:PRK11231 79 ALLPQHHLTPEGI----TVRELVaygrspwlslwgRLSAEDNAR-----VNQAME----QTRINHL------ADRRLTDL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 401 SGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-201 |
1.10e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAG-QVHaLMGENGAGKSTLLKILSGnYVPTAGSLQIQGQQM-TFTHTTEALNAgvAIIYQELHLIPEMTVA 100
Cdd:PRK03695 12 LGPLSAEVRAGeILH-LVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLeAWSAAELARHR--AYLSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 101 E--NIYLGQLPHKGGIvnRSLLNYEAGLqlqhLGLDIDPETPLKYLSIGQWQMVEIAKALAR-------NAKIIAFDEPT 171
Cdd:PRK03695 88 QylTLHQPDKTRTEAV--ASALNEVAEA----LGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPM 161
|
170 180 190
....*....|....*....|....*....|
gi 490204990 172 SSLSAREIDNLFRVIRELRQEGRVIIYVSH 201
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSH 191
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-222 |
1.10e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.28 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEAlNAGVAIIYQElhliPEMTV 99
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYR-SQRIRMIFQD----PSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 100 AENIYLGQLPHKGGIVNRSLLNYEAGLQ----LQHLGLDIDPETPLKY-LSIGQWQMVEIAKALARNAKIIAFDEPTSSL 174
Cdd:PRK15112 101 NPRQRISQILDFPLRLNTDLEPEQREKQiietLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 175 SAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK15112 181 DMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-201 |
1.17e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGnYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQELHLIPEMTVAEN 102
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLS-DWSAAELARHRAYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 103 IYLGQLPHKGGIVNRSLLNYEAGLqlqhLGLDIDPETPLKYLSIGQWQMVEIAKALAR-------NAKIIAFDEPTSSLS 175
Cdd:COG4138 90 LALHQPAGASSEAVEQLLAQLAEA----LGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
170 180
....*....|....*....|....*.
gi 490204990 176 AREIDNLFRVIRELRQEGRVIIYVSH 201
Cdd:COG4138 166 VAQQAALDRLLRELCQQGITVVMSSH 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-219 |
1.21e-12 |
|
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: 66.50 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 6 PYLSFHGITMTFPGVKA----LSDISFDCYAGQVHALMGENGAGKSTLLKILSG--NYVPTAGSLQIQGQQ--MTFTHTT 77
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGkrqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPldKNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 78 ealnagvAIIYQELHLIPEMTVAENIYLGQLphkggivnrsllnyeaglqlqhlgldidpetpLKYLSIGQWQMVEIAKA 157
Cdd:cd03232 82 -------GYVEQQDVHSPNLTVREALRFSAL--------------------------------LRGLSVEQRKRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 158 LARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHR-MEEIFALSDAITVFKDG 219
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQpSASIFEKFDRLLLLKRG 185
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
275-477 |
1.44e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAiQAGMMLcpedRKAEGII-------P 347
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSD-KAIREL----RRNVGMVfqqynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 VHSVRDNInISARRKhiLAGCVINNAweAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPT 427
Cdd:PRK11124 96 HLTVQQNL-IEAPCR--VLGLSKDQA--LARAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490204990 428 RGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK11124 170 AALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
275-488 |
1.83e-12 |
|
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: 66.94 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLfggSRI---TAGQVYIDGEAIDIRKPAQ-------AIQAgmmlcpedrkaEG 344
Cdd:cd03295 20 LNLEIAKGEFLVLIGPSGSGKTTTMKMI---NRLiepTSGEIFIDGEDIREQDPVElrrkigyVIQQ-----------IG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 345 IIPVHSVRDNINISARRKHilagcvinnaWEAQNADQHIKSLnIKTPG------AEQLIMNLSGGNQQKAILGRWLSEEM 418
Cdd:cd03295 86 LFPHMTVEENIALVPKLLK----------WPKEKIRERADEL-LALVGldpaefADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEIA-----GELLHEHANE 488
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVqvgtpDEILRSPAND 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-222 |
2.18e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEAL 80
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 81 NAgVAIIYQELHLIPEMTVAENIYLGQLPHKGGIVNRSLLNYEA-GLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALA 159
Cdd:PRK10253 81 RR-IGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 160 RNAKIIAFDEPTSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-217 |
2.22e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSfhGITMTF-PGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQmtfthTTEA 79
Cdd:PRK15056 2 MQQAGIVVN--DVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-----TRQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 80 LNAG-VAIIYQ--ELHLIPEMTVAENIYLGQLPHKG----------GIVNRSLLNYEAgLQLQHlgldidpeTPLKYLSI 146
Cdd:PRK15056 75 LQKNlVAYVPQseEVDWSFPVLVEDVVMMGRYGHMGwlrrakkrdrQIVTAALARVDM-VEFRH--------RQIGELSG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 147 GQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFK 217
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
273-477 |
2.22e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 68.18 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMK---GLFggsRITAGQVYIDGEAIDiRKPaqaiqagmmlcPEDRkaeGIIPV- 348
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRmiaGLE---DPTSGEILIGGRDVT-DLP-----------PKDR---NIAMVf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 -------H-SVRDNINISARRKHIlagcvinnawEAQNADQHIKS----LNI-----KTPGAeqlimnLSGGNQQKAILG 411
Cdd:COG3839 82 qsyalypHmTVYENIAFPLKLRKV----------PKAEIDRRVREaaelLGLedlldRKPKQ------LSGGQRQRVALG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 412 RWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-224 |
2.23e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.86 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSG--NYVPTA---GSLQIQGQQMtFTHTTEALNA 82
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDI-FKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 GVAIIYQELHLIPEMTVAENIYLGQLphkggiVNRsLLNYEAGLQLQ--------HLGLDIDP--ETPLKYLSIGQWQMV 152
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLK------LNR-LVKSKKELQERvrwalekaQLWDEVKDrlDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 153 EIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEgRVIIYVSHRMEEIFALSDAITVFKDGRYVRT 224
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-233 |
3.06e-12 |
|
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: 69.66 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 5 TPYLSFHGITMTFPGVK--ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMtFTHTTEalna 82
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISD---- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 83 gvaiIYQELHLIPEMTVAENIYLGQ----LPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKAL 158
Cdd:TIGR01257 2010 ----VHQNMGYCPQFDAIDDLLTGRehlyLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 159 ARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGryvrTFDNMQEVNH 233
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG----AFQCLGTIQH 2156
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
275-478 |
3.52e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 67.82 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDiRKPAQAIQAGMM-----LCPedrkaegiipvH 349
Cdd:COG3842 24 VSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPEKRNVGMVfqdyaLFP-----------H 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 -SVRDNI------------NISARRKHILAGCvinnaweaqnadqHIKSLniktpgAEQLIMNLSGGNQQKAILGRWLSE 416
Cdd:COG3842 92 lTVAENVafglrmrgvpkaEIRARVAELLELV-------------GLEGL------ADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 417 EMKVILLDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
275-477 |
4.44e-12 |
|
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: 65.51 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI-DIRKPAQAI---QAGMMLcpEDRKaegIIPVHS 350
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsDLRGRAIPYlrrKIGVVF--QDFR---LLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNINISARrkhilagCVINNAWEAQNADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:cd03292 95 VYENVAFALE-------VTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490204990 431 DVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-222 |
4.62e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.65 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 22 ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVAIIYQEL-HLIPEMTVA 100
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPdNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 101 ENIYLGqlPHKGGI--------VNRSLLN---YEAGLQLQHLgldidpetplkyLSIGQWQMVEIAKALARNAKIIAFDE 169
Cdd:PRK13633 105 EDVAFG--PENLGIppeeirerVDESLKKvgmYEYRRHAPHL------------LSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 170 PTSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIfALSDAITVFKDGRYV 222
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGKVV 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
275-480 |
4.88e-12 |
|
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: 65.68 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAgmmlcpedRKAEGIIPVH----- 349
Cdd:cd03258 24 VSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA--------RRRIGMIFQHfnlls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 --SVRDNINISARrkhiLAGcvinnaWEAQNADQHIKSLnIKTPG----AEQLIMNLSGGNQQKAILGRWLSEEMKVILL 423
Cdd:cd03258 96 srTVFENVALPLE----IAG------VPKAEIEERVLEL-LELVGledkADAYPAQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 424 DEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:cd03258 165 DEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
275-475 |
5.28e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.75 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMlcPEdrkAEGIIPVHSVRDN 354
Cdd:PRK13537 26 LSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV--PQ---FDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHILAGcvinnawEAQNADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:PRK13537 101 LLVFGRYFGLSAA-------AARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490204990 435 KHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREG 475
Cdd:PRK13537 174 RHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-238 |
5.98e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.82 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 14 TMTFPGVK--ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQEL 91
Cdd:PRK10789 320 QFTYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 92 HLIPEmTVAENIYLGQlPhkggivNRSLLNYEAGLQLQHLGLDIdPETPLKY----------LSIGQWQMVEIAKALARN 161
Cdd:PRK10789 399 FLFSD-TVANNIALGR-P------DATQQEIEHVARLASVHDDI-LRLPQGYdtevgergvmLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 162 AKIIAFDEptsSLSAREIDNLFRVIRELRQ--EGRVIIYVSHRMEeifALSDA--ITVFKDGRYvrtfdnMQEVNHDALV 237
Cdd:PRK10789 470 AEILILDD---ALSAVDGRTEHQILHNLRQwgEGRTVIISAHRLS---ALTEAseILVMQHGHI------AQRGNHDQLA 537
|
.
gi 490204990 238 Q 238
Cdd:PRK10789 538 Q 538
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
275-477 |
6.04e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAiQAGMMLcpedRKAEGII-------P 347
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSE-KAIRLL----RQKVGMVfqqynlwP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 VHSVRDNInISARRKhiLAGcvINNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPT 427
Cdd:COG4161 96 HLTVMENL-IEAPCK--VLG--LSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490204990 428 RGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG4161 170 AALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
273-478 |
6.55e-12 |
|
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: 64.98 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMK---GLFGGSRITAGQVYIDGEAidiRKPAQAIQAGMMLCPEDRKAEGIipvh 349
Cdd:cd03234 24 NDVSLHVESGQVMAILGSSGSGKTTLLDaisGRVEGGGTTSGQILFNGQP---RKPDQFQKCVAYVRQDDILLPGL---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 SVRDNINISARRKhiLAGCVINNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRG 429
Cdd:cd03234 97 TVRETLTYTAILR--LPRKSSDAIRKKRVEDVLLRDLAL-TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490204990 430 IDVGAKHEIYNVIYALAASGVAVVFA----SSDLPEVLgvaDRIVVMREGEIA 478
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTihqpRSDLFRLF---DRILLLSSGEIV 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-201 |
6.78e-12 |
|
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: 63.24 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLqiqgqqmtfthttealnagvaii 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 yqelhlipemTVAENIYLGQLPHkggivnrsllnyeaglqlqhlgldidpetplkyLSiGQWQM-VEIAKALARNAKIIA 166
Cdd:cd03221 58 ----------TWGSTVKIGYFEQ---------------------------------LS-GGEKMrLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*
gi 490204990 167 FDEPTSSLSAREIDNLfrvIRELRQEGRVIIYVSH 201
Cdd:cd03221 94 LDEPTNHLDLESIEAL---EEALKEYPGTVILVSH 125
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-280 |
7.11e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.82 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 35 VHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNA---GVAIIYQELHLIPEMTVAENIYLGQLPhk 111
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPekrRIGYVFQDARLFPHYKVRGNLRYGMAK-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 112 ggiVNRSLLNYEAG-LQLQHLgLDIDPETplkyLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSA---REidnLFRVIR 187
Cdd:PRK11144 104 ---SMVAQFDKIVAlLGIEPL-LDRYPGS----LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkRE---LLPYLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 188 ELRQEGRV-IIYVSHRMEEIFALSDAITVFKDGRyVRTFDNMQEV-NHDAL--------------VQ--------AMVGR 243
Cdd:PRK11144 173 RLAREINIpILYVSHSLDEILRLADRVVVLEQGK-VKAFGPLEEVwASSAMrpwlpkeeqssilkVTvlehhphyAMTAL 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490204990 244 ELGDIYGW---QPREYGkERLRLdRVKAPGV----RQPVSLSVR 280
Cdd:PRK11144 252 ALGDQHLWvnkLDAPLG-TALRI-RIQASDVslvlQPPQQSSIR 293
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
273-480 |
8.06e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 8.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAID-------IRK----PAQAIQAGMMLCPEdRK 341
Cdd:PRK10575 28 HPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswsskafARKvaylPQQLPAAEGMTVRE-LV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 342 AEGIIPVHSVRDNINISARRKhilagcvinnaweaqnADQHIKSLNIKtPGAEQLIMNLSGGNQQKAILGRWLSEEMKVI 421
Cdd:PRK10575 107 AIGRYPWHGALGRFGAADREK----------------VEEAISLVGLK-PLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 422 LLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQ 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-219 |
1.09e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 64.27 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 18 PGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSL---QIQGQQMTFTHTTEALNAGVAIIYQELHLI 94
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 95 pEMTVAENIYLGQLPHKGgivnrsllNYEAGLQLQHLGLDID-----PETPLKY----LSIGQWQMVEIAKALARNAKII 165
Cdd:cd03290 92 -NATVEENITFGSPFNKQ--------RYKAVTDACSLQPDIDllpfgDQTEIGErginLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 166 AFDEPTSSLSAREIDNLFR--VIRELRQEGRVIIYVSHRMEEIfALSDAITVFKDG 219
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-240 |
1.26e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.70 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLK----ILSGNYVPTAGSLQIQGQ---QMTFTHTTEALNAGVAIIYQE-- 90
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaicgITKDNWHVTADRFRWNGIdllKLSPRERRKIIGREIAMIFQEps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 91 LHLIPEMTV----AENIYLGQLphKGGIVNRSLLNYEAGLQLQH-LGLDiDPETPLK-Y---LSIGQWQMVEIAKALARN 161
Cdd:COG4170 100 SCLDPSAKIgdqlIEAIPSWTF--KGKWWQRFKWRKKRAIELLHrVGIK-DHKDIMNsYpheLTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 162 AKIIAFDEPTSSLSAREIDNLFRVIRELRQ-EGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDNMQEVNH------D 234
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSphhpytK 256
|
....*.
gi 490204990 235 ALVQAM 240
Cdd:COG4170 257 ALLRSM 262
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
275-489 |
1.45e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.62 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIdirkPAQAIQAgmmlcpedRKAEGIIPV------ 348
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLA--------RARIGVVPQfdnldl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 -HSVRDNI-------NISARRKHILAGCVINNAWEAQNADQHIKslniktpgaeqlimNLSGGNQQKAILGRWLSEEMKV 420
Cdd:PRK13536 128 eFTVRENLlvfgryfGMSTREIEAVIPSLLEFARLESKADARVS--------------DLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 421 ILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREG-EIAGELLHEHANEQ 489
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHALIDEH 263
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
23-239 |
1.48e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.67 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQM-TFTHttEALNAGVAIIYQELHLIPEmTVAE 101
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLsSLSH--SVLRQGVAMVQQDPVVLAD-TFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 102 NIYLGQlphkgGIVNRSLLNYEAGLQLQHL--GLDIDPETPL----KYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLS 175
Cdd:PRK10790 434 NVTLGR-----DISEEQVWQALETVQLAELarSLPDGLYTPLgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 176 AREIDNLFRVIRELRQEGRVIIyVSHRMEEIFAlSDAITVFKDGRYVrtfdnmQEVNHDALVQA 239
Cdd:PRK10790 509 SGTEQAIQQALAAVREHTTLVV-IAHRLSTIVE-ADTILVLHRGQAV------EQGTHQQLLAA 564
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
260-491 |
1.52e-11 |
|
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: 66.71 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 260 RLRLDRVKA--PGVRQPV----SLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRK-PAQAIQAG 332
Cdd:COG4987 333 SLELEDVSFryPGAGRPVldglSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG--VDLRDlDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 333 MMLCPEDrkaegiipVH----SVRDNINIsARrkhilagcviNNA-----WEA-QNA--DQHIKSLniktP-GAEQLI-- 397
Cdd:COG4987 411 IAVVPQR--------PHlfdtTLRENLRL-AR----------PDAtdeelWAAlERVglGDWLAAL----PdGLDTWLge 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 398 --MNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAsGVAVVFASSDLPEvLGVADRIVVMREG 475
Cdd:COG4987 468 ggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAG-LERMDRILVLEDG 545
|
250
....*....|....*.
gi 490204990 476 EIAGELLHEHANEQQA 491
Cdd:COG4987 546 RIVEQGTHEELLAQNG 561
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-220 |
1.53e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.63 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPG-VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthTTEALNAGVAI 86
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN---ELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIPEMTVAENIYLG----QLPhKGGIVNRSLlnyEAG--LQLQHLgLDIDPetplKYLSIGQWQMVEIAKALAR 160
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGlkirGMP-KAEIEERVA---EAAriLELEPL-LDRKP----RELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 161 NAKIIAFDEPTSSLSAReidnlFRV-----IREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAK-----LRVqmrleIQRLhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
275-477 |
1.59e-11 |
|
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: 65.46 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMK---GLFGGSRITAGQVYIDGEAIDIRKPAQAIQAgmmlcpedRKAE-GII---- 346
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARailGLLPPPGITSGEILFDGEDLLKLSEKELRKI--------RGREiQMIfqdp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 -----PVHSVRDNInISARRKHILAGcviNNAWEAQnADQHIKSLNIktPGAEQlIMN-----LSGGNQQKAILGRWLSE 416
Cdd:COG0444 96 mtslnPVMTVGDQI-AEPLRIHGGLS---KAEARER-AIELLERVGL--PDPER-RLDrypheLSGGMRQRVMIARALAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 417 EMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG0444 168 EPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-245 |
1.69e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.73 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQElhliPE--- 96
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT-AENVWNLRRKIGMVFQN----PDnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 --MTVAENIYLGQlpHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKyLSIGQWQMVEIAKALARNAKIIAFDEPTSSL 174
Cdd:PRK13642 95 vgATVEDDVAFGM--ENQGIPREEMIKRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 175 SAREIDNLFRVIRELRQEGRV-IIYVSHRMEEIfALSDAITVFKDGRYVR---------TFDNMQEVNHDALVQAMVGRE 244
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLtVLSITHDLDEA-ASSDRILVMKAGEIIKeaapselfaTSEDMVEIGLDVPFSSNLMKD 250
|
.
gi 490204990 245 L 245
Cdd:PRK13642 251 L 251
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-201 |
1.90e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 33 GQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTE--ALNA-GVAIIYQELHLIPEMTVAENIylgQLP 109
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraKLRAkHVGFVFQSFMLIPTLNALENV---ELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 110 H--KGGIVNRSLLNYEAGLQLQHLGLDIDpETPLKyLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIR 187
Cdd:PRK10584 113 AllRGESSRQSRNGAKALLEQLGLGKRLD-HLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170
....*....|....*
gi 490204990 188 EL-RQEGRVIIYVSH 201
Cdd:PRK10584 191 SLnREHGTTLILVTH 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
20-217 |
2.13e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHA-----LMGENGAGKSTLLKILSGNYVPTAGSlqiqgqqmtfthtteaLNAGVAIIY--QELH 92
Cdd:PRK13409 347 TKKLGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGE----------------VDPELKISYkpQYIK 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 93 LIPEMTVAEniYLGQLPhkgGIVNRSLLNYE--AGLQLQHLgLDidpeTPLKYLSIGQWQMVEIAKALARNAKIIAFDEP 170
Cdd:PRK13409 411 PDYDGTVED--LLRSIT---DDLGSSYYKSEiiKPLQLERL-LD----KNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490204990 171 TSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFK 217
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIaEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-222 |
2.31e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTT--EALNAGVAIIYQELH--LIP 95
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDPYasLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 96 EMTVAENIYLGQLPHkggivnrSLLNYEAGLQ-----LQHLGLdiDPETPLKY---LSIGQWQMVEIAKALARNAKIIAF 167
Cdd:PRK10261 417 RQTVGDSIMEPLRVH-------GLLPGKAAAArvawlLERVGL--LPEHAWRYpheFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 168 DEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
275-478 |
2.69e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.02 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQ-AIQAGMMlcpedrkaegiiPVHS--- 350
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElARRRAVL------------PQHSsls 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 ----VRDNINISarrkhiLAGCVINNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWL------SEEMKV 420
Cdd:PRK13548 89 fpftVEEVVAMG------RAPHGLSRAEDDALVAAALAQVDL-AHLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 421 ILLDEPTRGIDVGAKHEIYNVIYALA-ASGVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-238 |
2.81e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.02 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQ---QMTFTHTT 77
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 78 EAlNAGVAIIYQELHLIPEMTVAENIYL-----GQLPhkggivnRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMV 152
Cdd:PRK11831 81 TV-RKRMSMLFQSGALFTDMNVFDNVAYplrehTQLP-------APLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 153 EIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYVR--TFDNMQ 229
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAhgSAQALQ 232
|
....*....
gi 490204990 230 EvNHDALVQ 238
Cdd:PRK11831 233 A-NPDPRVR 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-432 |
3.54e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 9 SFHGITMTFPGVKA-LSDISFDCYAGQVHALMGENGAGKSTLLKILSGnyVPTagslQIQGQQMTfthtteALNAGVAII 87
Cdd:TIGR03719 6 TMNRVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDK----DFNGEARP------QPGIKVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENIYLGqLPHKGGIVNR----------------SLLNYEAGLQ--LQHLGL-DID------------ 136
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEG-VAEIKDALDRfneisakyaepdadfdKLAAEQAELQeiIDAADAwDLDsqleiamdalrc 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 137 --PETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELrqEGRVIIyVSH------------- 201
Cdd:TIGR03719 153 ppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVA-VTHdryfldnvagwil 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 202 -------------------------RMEEIFALSDAITVFKDGRYVRT---------------FDNM-----QEVNHDAL 236
Cdd:TIGR03719 230 eldrgrgipwegnysswleqkqkrlEQEEKEESARQKTLKRELEWVRQspkgrqakskarlarYEELlsqefQKRNETAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 237 VQAMVGRELGDI----------YGwqpreygkERLRLDRvkapgvrqpVSLSVRSGEIVGLFGLVGAGRSELMkglfggs 306
Cdd:TIGR03719 310 IYIPPGPRLGDKvieaenltkaFG--------DKLLIDD---------LSFKLPPGGIVGVIGPNGAGKSTLF------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 307 RITAGQVYIDGEAIDIrkpAQAIQAGMMlcpeDRKAEGIIPVHSVRDniNISARRKHILAGCVInnaweaQNADQHIKSL 386
Cdd:TIGR03719 366 RMITGQEQPDSGTIEI---GETVKLAYV----DQSRDALDPNKTVWE--EISGGLDIIKLGKRE------IPSRAYVGRF 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 490204990 387 NIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDV 432
Cdd:TIGR03719 431 NFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
17-222 |
3.74e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 17 FPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVAIIYQELHLIPE 96
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 MTVAENIyLGQLPHKGGIvNRSLLNYEAGLQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSA 176
Cdd:PRK10895 93 LSVYDNL-MAVLQIRDDL-SAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 177 REIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK10895 171 ISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-222 |
3.75e-11 |
|
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: 62.28 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 16 TFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGN---YVPTAGSLQ---IQGQQMTFTHTTEalnagvaIIY- 88
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHyngIPYKEFAEKYPGE-------IIYv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 89 --QELHlIPEMTVAENIylgqlphkggivnrsllnyEAGLQLQhlGLDIdpetpLKYLSIGQWQMVEIAKALARNAKIIA 166
Cdd:cd03233 89 seEDVH-FPTLTVRETL-------------------DFALRCK--GNEF-----VRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 167 FDEPTSSL---SAREIDNLFRVI-RELRqeGRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:cd03233 142 WDNSTRGLdssTALEILKCIRTMaDVLK--TTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
275-484 |
4.07e-11 |
|
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: 63.02 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKpaqaiqagmmlcpedrkaegiIPVHSVRDN 354
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG--HDVRD---------------------YTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHILAGCVINN---------------AWEAQNADQHIKSLniktP-GAEQLI----MNLSGGNQQKAILGRWL 414
Cdd:cd03251 78 IGLVSQDVFLFNDTVAENiaygrpgatreeveeAARAANAHEFIMEL----PeGYDTVIgergVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 415 SEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSdLPEVLGvADRIVVMREGEIAGELLHE 484
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHR-LSTIEN-ADRIVVLEDGKIVERGTHE 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-222 |
4.67e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 2 QQSTPYLSFHGITMTFPGVK-----------ALSDISFDCYAGQVHALMGENGAGKST----LLKILsgnyvPTAGSLQI 66
Cdd:PRK15134 270 EPASPLLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 67 QGQQMTFTHTTEAL--NAGVAIIYQELH--LIPEMTVAeniylgQLPHKGGIVNRSLLNYEAGLQ-----LQHLGLDidP 137
Cdd:PRK15134 345 DGQPLHNLNRRQLLpvRHRIQVVFQDPNssLNPRLNVL------QIIEEGLRVHQPTLSAAQREQqviavMEEVGLD--P 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 138 ETPLKY---LSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRV-IIYVSHRMEEIFALSDAI 213
Cdd:PRK15134 417 ETRHRYpaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLaYLFISHDLHVVRALCHQV 496
|
....*....
gi 490204990 214 TVFKDGRYV 222
Cdd:PRK15134 497 IVLRQGEVV 505
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-226 |
5.36e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.70 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIqgqqmtfthttealNAGVAII 87
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--------------GETVKIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 Y--QELH-LIPEMTVAENIylgqLPHKGGIVNRSLLNYeaglqLQHLGLD-IDPETPLKYLSIGQWQMVEIAKALARNAK 163
Cdd:COG0488 382 YfdQHQEeLDPDKTVLDEL----RDGAPGGTEQEVRGY-----LGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 164 IIAFDEPTSSL--SAREIDNLFrvireLRQ-EGRVIIyVSHRMEEIFALSDAITVFKDGRyVRTFD 226
Cdd:COG0488 453 VLLLDEPTNHLdiETLEALEEA-----LDDfPGTVLL-VSHDRYFLDRVATRILEFEDGG-VREYP 511
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
275-478 |
5.39e-11 |
|
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: 62.51 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKpaqaiqagmmlcpedrkaegiIPVHSVRDN 354
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDG--VDISK---------------------IGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHILAGCVINNA-----------WEAQnADQHIKSLNIKTPGAEQLIM-----NLSGGNQQKAILGRWLSEEM 418
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLdpfgeysdeelWQAL-ERVGLKEFVESLPGGLDTVVeeggeNLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYAlAASGVAVVFASSDLPEVLGvADRIVVMREGEIA 478
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-222 |
5.60e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.49 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSlQIQGQ-----QMTFTHTTEALNAGVAIIYQ--ELHL 93
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDyaipaNLKKIKEVKRLRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 94 IPEmTVAENIYLGQLpHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLKyLSIGQWQMVEIAKALARNAKIIAFDEPTSS 173
Cdd:PRK13645 104 FQE-TIEKDIAFGPV-NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490204990 174 LSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-201 |
6.47e-11 |
|
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: 61.74 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmtfthtteALNAGVAIIYQELHlipemtvaen 102
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---------PLDFQRDSIARGLL---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 103 iYLGqlpHKGGIvnRSLLNYEAGLQLQH--------------LGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFD 168
Cdd:cd03231 77 -YLG---HAPGI--KTTLSVLENLRFWHadhsdeqveealarVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170 180 190
....*....|....*....|....*....|...
gi 490204990 169 EPTSSLSAREIDNLFRVIRELRQEGRVIIYVSH 201
Cdd:cd03231 151 EPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
275-480 |
8.86e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.40 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAiqagmmlcpEDRKAEGIipVHSVRDN 354
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLL---------EVRKTVGI--VFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHILAGCVINNAWEAQNADQHIKSlNIKTPGAE----QLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:PRK13639 90 QLFAPTVEEDVAFGPLNLGLSKEEVEKRVKE-ALKAVGMEgfenKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490204990 431 DVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
275-475 |
1.63e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.54 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDiRKPAQAIQagmmlcpedRKaeGIipvhsVRDN 354
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-GLPGHQIA---------RM--GV-----VRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHIlagcVINNAWEAQNadQHIKSlNI-----KTPG---AEQLIM---------------------NLSGGNQ 405
Cdd:PRK11300 87 QHVRLFREMT----VIENLLVAQH--QQLKT-GLfsgllKTPAfrrAESEALdraatwlervgllehanrqagNLAYGQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 406 QKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREG 475
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
275-490 |
2.07e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.30 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAgmmLCPEDRKAEGIipvhsVRDN 354
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKG---LIRQLRQHVGF-----VFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARR---KHILAGCVINNAWEAQNADQHIKSLNIKT--PGAEQLI-MNLSGGNQQKAILGRWLSEEMKVILLDEPTR 428
Cdd:PRK11264 94 FNLFPHRtvlENIIEGPVIVKGEPKEEATARARELLAKVglAGKETSYpRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 429 GIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIA--GELLHEHANEQQ 490
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVeqGPAKALFADPQQ 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
275-477 |
2.18e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 60.78 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKpaqaiqagmmlcpedrkaegiipvhsvrdn 354
Cdd:COG1126 20 ISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSK------------------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHIlaG------------CVINNAWEAQnadqhIKSLNIKTPGAEQLIM-----------------NLSGGNQ 405
Cdd:COG1126 70 KDINKLRRKV--GmvfqqfnlfphlTVLENVTLAP-----IKVKKMSKAEAEERAMellervgladkadaypaQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 406 QK-AIlGRWLSEEMKVILLDEPTRGID---VGakhEIYNVIYALAASGVAVV-------FASSdlpevlgVADRIVVMRE 474
Cdd:COG1126 143 QRvAI-ARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVvvthemgFARE-------VADRVVFMDG 211
|
...
gi 490204990 475 GEI 477
Cdd:COG1126 212 GRI 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
263-475 |
2.35e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 60.53 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 263 LDRVKAPGVRQpVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYI--DGEAIDIrkpAQAIQAGMMlcpEDR 340
Cdd:COG4778 19 QGGKRLPVLDG-VSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDL---AQASPREIL---ALR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 341 KAE-G-------IIPVHSVRDninisarrkhILAGCVINNAWEAQNADQHIKS----LNIKtpgaEQLiMNL-----SGG 403
Cdd:COG4778 92 RRTiGyvsqflrVIPRVSALD----------VVAEPLLERGVDREEARARAREllarLNLP----ERL-WDLppatfSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 404 NQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREG 475
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-216 |
2.35e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 22 ALSDISFDCYAGQVHALMGENGAGKSTLLKILS--GNYVPTA---GSLQIQGQQMTFTHTTEA-LNAGVAIIYQELHLIP 95
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlNDLIPGFrveGKVTFHGKNLYAPDVDPVeVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 96 EmTVAENIYLGQ--LPHKGG---IVNRSL----LNYEAGLQLQHLGLDidpetplkyLSIGQWQMVEIAKALARNAKIIA 166
Cdd:PRK14243 105 K-SIYDNIAYGAriNGYKGDmdeLVERSLrqaaLWDEVKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490204990 167 FDEPTSSL---SAREIDNLfrvIRELRQEGRVIIyVSHRMEEIFALSDaITVF 216
Cdd:PRK14243 175 MDEPCSALdpiSTLRIEEL---MHELKEQYTIII-VTHNMQQAARVSD-MTAF 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
275-477 |
2.51e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.16 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAID------IRKpaqaiQAGMMLCPEDRKAEGIipv 348
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkenlkeIRK-----KIGIIFQNPDNQFIGA--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 hSVRDNI-----NISARRKHILAgcVINNAWEAQNADQHIKslniKTPgaeqliMNLSGGNQQKAILGRWLSEEMKVILL 423
Cdd:PRK13632 100 -TVEDDIafgleNKKVPPKKMKD--IIDDLAKKVGMEDYLD----KEP------QNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 424 DEPTRGIDVGAKHEIYNVIYALAASGVAVVFA-SSDLPEVLgVADRIVVMREGEI 477
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKL 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
275-478 |
2.53e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 62.27 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDiRKPAQAIQAGMMLcpedrKAEGIIPVHSVRDN 354
Cdd:PRK09452 33 LDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRHVNTVF-----QSYALFPHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRkhilagcvinnaweaqnadQHIKSLNIKTPGAEQLIM------------NLSGGNQQKAILGRWLSEEMKVIL 422
Cdd:PRK09452 107 VAFGLRM-------------------QKTPAAEITPRVMEALRMvqleefaqrkphQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 423 LDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
265-477 |
3.07e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.79 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 265 RVKAPGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKP---AQAIQAGMMLCPEDRK 341
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 342 aegiIPVHSVRDNINISARRKHILAGCV---INNAWEAQNAdQHIKslniktpgaEQLIMNLSGGNQQKAILGRWLSEEM 418
Cdd:PRK13638 90 ----IFYTDIDSDIAFSLRNLGVPEAEItrrVDEALTLVDA-QHFR---------HQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-432 |
3.12e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 38 LMGENGAGKSTLLKILSGNYVPTAGSLQIQG-------QQ--------MTFTHTTEALnAGVAIIYQELHLIPEMtvaen 102
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlQQdpprnvegTVYDFVAEGI-EEQAEYLKRYHDISHL----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 103 iyLGQLPhkggivNRSLLNYEAGLQ--LQHLG--------------LDIDPETPLKYLSiGQWQ-MVEIAKALARNAKII 165
Cdd:PRK11147 108 --VETDP------SEKNLNELAKLQeqLDHHNlwqlenrinevlaqLGLDPDAALSSLS-GGWLrKAALGRALVSNPDVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 166 AFDEPTSSLSAREIDNLFRVIRELRQEgrvIIYVSH------RM-EEIFALSDAITVFKDGRYVRTFDNMQE-VNHDALV 237
Cdd:PRK11147 179 LLDEPTNHLDIETIEWLEGFLKTFQGS---IIFISHdrsfirNMaTRIVDLDRGKLVSYPGNYDQYLLEKEEaLRVEELQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 238 QAMVGRELGDIYGW--------QPREYGKERL-------RLDRVKAPG-VRQPVSLSVRSGEIV---------------- 285
Cdd:PRK11147 256 NAEFDRKLAQEEVWirqgikarRTRNEGRVRAlkalrreRSERREVMGtAKMQVEEASRSGKIVfemenvnyqidgkqlv 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 286 -------------GLFGLVGAGRSELMKGLFGGSRITAGQVYIdGEAIDIrkpAQAIQAGMMLCPE----DRKAEGiipv 348
Cdd:PRK11147 336 kdfsaqvqrgdkiALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEV---AYFDQHRAELDPEktvmDNLAEG---- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 hsvRDNINISARRKHILAgcvinnawEAQNADQHIKslNIKTPgaeqlIMNLSGGNQQKAILGRWLSEEMKVILLDEPTR 428
Cdd:PRK11147 408 ---KQEVMVNGRPRHVLG--------YLQDFLFHPK--RAMTP-----VKALSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
....
gi 490204990 429 GIDV 432
Cdd:PRK11147 470 DLDV 473
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
276-473 |
3.20e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.05 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 276 SLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDirkpaQAIQAGMM-LCPEDRKAEGIIPVhsVRDN 354
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-----QALQKNLVaYVPQSEEVDWSFPV--LVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHiLAGCVINNAWEAQNADQHIKSLNIKTPGAEQlIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGA 434
Cdd:PRK15056 100 VVMMGRYGH-MGWLRRAKKRDRQIVTAALARVDMVEFRHRQ-IGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 490204990 435 KHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMR 473
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-245 |
3.42e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.86 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 11 HGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQ-----------------QMTF 73
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklnraqrkafrrdiQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 74 THTTEALNagvaiiyqelhliPEMTVAENI-----YLGQLPHKGGIVNRSLLNYEAGLQLQHLglDIDPETplkyLSIGQ 148
Cdd:PRK10419 96 QDSISAVN-------------PRKTVREIIreplrHLLSLDKAERLARASEMLRAVDLDDSVL--DKRPPQ----LSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 149 WQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSH--RMEEIFAlsDAITVFKDGRYVRTf 225
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHdlRLVERFC--QRVMVMDNGQIVET- 233
|
250 260
....*....|....*....|
gi 490204990 226 dnmQEVNHDALVQAMVGREL 245
Cdd:PRK10419 234 ---QPVGDKLTFSSPAGRVL 250
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
275-477 |
4.25e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 60.63 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKpaqaiqAGMMlcpEDRKAEGIipVHSVRDN 354
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR------KGLM---KLRESVGM--VFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHILAGCVINNAWEAQNADQHIKSLNIKTpGAEQL----IMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:PRK13636 94 QLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRT-GIEHLkdkpTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490204990 431 DVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
261-478 |
4.27e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 59.43 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 261 LRLDRVKAPGVRQPV--SLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQaiQAGMMLCPE 338
Cdd:cd03298 1 VRLDKIRFSYGEQPMhfDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 339 DrkaeGIIPVHSVRDNINIsARRKHILAGCVINNAWEAQNADQHIKSLNIKTPGAeqlimnLSGGNQQKAILGRWLSEEM 418
Cdd:cd03298 79 N----NLFAHLTVEQNVGL-GLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGE------LSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
275-477 |
5.32e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMK---GLFGGSRITAGQVYIDGEAI--------DIRKpaQAIQAGMMLcpedrKAE 343
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRhlsGLITGDKSAGSHIELLGRTVqregrlarDIRK--SRANTGYIF-----QQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 344 GIIPVHSVRDNINISAR-RKHILAGCVinnAW----EAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEM 418
Cdd:PRK09984 96 NLVNRLSVLENVLIGALgSTPFWRTCF---SWftreQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
271-480 |
5.34e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.00 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLfggSRITA---GQVYIDGEAIDiRKPAQAIQAGMMLCPEDRKAEGIIP 347
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTL---SRLMTpahGHVWLDGEHIQ-HYASKEVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 VHSvrdninISARRKHilAGCVINNAWEAQNADQHIKSLNIK--TPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDE 425
Cdd:PRK10253 98 VQE------LVARGRY--PHQPLFTRWRKEDEEAVTKAMQATgiTHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 426 PTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-218 |
5.39e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFThttealnagvaiiyqelhliPEMTVAEN 102
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG--------------------REASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 103 IY-LGQLPHKGGIVNRSLLNyEAGLQLqhlgldidpeTPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSL---SARE 178
Cdd:COG2401 106 IGrKGDFKDAVELLNAVGLS-DAVLWL----------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLdrqTAKR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490204990 179 IDnlFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKD 218
Cdd:COG2401 175 VA--RNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-431 |
5.79e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 27 SFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQgqqmtFTHTT----EALNAGVAIIYQELH--LIPE---- 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ-----FSHITrlsfEQLQKLVSDEWQRNNtdMLSPgedd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 --MTVAENIylgQLPHKGgivNRSLLNYEAGLQLQHLgLDidpeTPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSL 174
Cdd:PRK10938 98 tgRTTAEII---QDEVKD---PARCEQLAQQFGITAL-LD----RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 175 SAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDNmQEVNHDALVQAMVGRE-LGDIYGWQP 253
Cdd:PRK10938 167 DVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGER-EEILQQALVAQLAHSEqLEGVQLPEP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 254 REYGkERLRLDRVKAP-----GVRQ----PV----SLSVRSGEIVGLFGLVGAGRSELM--------KG------LFGGS 306
Cdd:PRK10938 246 DEPS-ARHALPANEPRivlnnGVVSyndrPIlhnlSWQVNPGEHWQIVGPNGAGKSTLLslitgdhpQGysndltLFGRR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 307 RITagqvyidGEAI-DIRKPAQAIQAGMMLcpEDRkaegiipvhsvrdnINISARRKhILAGC-----VINNAWEAQN-- 378
Cdd:PRK10938 325 RGS-------GETIwDIKKHIGYVSSSLHL--DYR--------------VSTSVRNV-ILSGFfdsigIYQAVSDRQQkl 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 490204990 379 ADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGID 431
Cdd:PRK10938 381 AQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
273-484 |
6.54e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.12 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRK----PAQAIQAGMMLcpedrKAEGIIPV 348
Cdd:PRK10908 19 QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrevPFLRRQIGMIF-----QDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 HSVRDNINISArrkhILAGCVINNAWEAQNADQHIKSLNIKtpgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTR 428
Cdd:PRK10908 94 RTVYDNVAIPL----IIAGASGDDIRRRVSAALDKVGLLDK---AKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 429 GIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGELLHE 484
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-242 |
6.73e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 15 MTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNY------------VPTAGSLQIQGQQ------------ 70
Cdd:PTZ00265 1176 ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNDMTNEQDYQgdeeqnvgmknv 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 71 ---------------MTFTHTTEALNAGV--------------AIIYQELHLIpEMTVAENIYLGQLPHKGGIVNRSLLN 121
Cdd:PTZ00265 1256 nefsltkeggsgedsTVFKNSGKILLDGVdicdynlkdlrnlfSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKF 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 122 YEAGLQLQHLGLDIDPET-PL-KYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEG-RVIIY 198
Cdd:PTZ00265 1335 AAIDEFIESLPNKYDTNVgPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIIT 1414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490204990 199 VSHRMEEIfALSDAITVF----KDGRYVRTfdnmqEVNHDALVQAMVG 242
Cdd:PTZ00265 1415 IAHRIASI-KRSDKIVVFnnpdRTGSFVQA-----HGTHEELLSVQDG 1456
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
275-485 |
8.78e-10 |
|
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: 58.78 E-value: 8.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKpaqaiqagmmlcpedrkaegiIPVHSVRDN 354
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG--IDIRD---------------------ISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHILAGCVINN-AWEAQNADQHIKSLNIKTPGAEQLIM---------------NLSGGNQQKAILGRWLSEEM 418
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENiRLGRPNATDEEVIEAAKEAGAHDFIMklpngydtvlgenggNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSdlPEVLGVADRIVVMREGEIAGELLHEH 485
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHR--LSTIKNADKILVLDDGKIIEEGTHDE 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-220 |
9.12e-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: 58.58 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQELHLIpEMTVA 100
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS-TIPLEDLRSSLTIIPQDPTLF-SGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 101 ENiylgqLPHKGGIVNRSLlnYEAgLQLQHLGLDidpetplkyLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREID 180
Cdd:cd03369 100 SN-----LDPFDEYSDEEI--YGA-LRVSEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490204990 181 NLFRVIRELRQeGRVIIYVSHRMEEIfALSDAITVFKDGR 220
Cdd:cd03369 163 LIQKTIREEFT-NSTILTIAHRLRTI-IDYDKILVMDAGE 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
271-477 |
9.71e-10 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 57.71 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaidirKPAQAIQAgmmlcpedrkaegiipvhS 350
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG------VPVSDLEK------------------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNINISARRKHILAGCVINNaweaqnadqhikslniktpgaeqLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGI 430
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNN-----------------------LGRRFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 431 DVGAKHEIYNVIYAlAASGVAVVFASSDLpevLGV--ADRIVVMREGEI 477
Cdd:cd03247 130 DPITERQLLSLIFE-VLKDKTLIWITHHL---TGIehMDKILFLENGKI 174
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
275-498 |
1.02e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.04 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAiQAGMMLcpedrKAEGIIPVHSVRDN 354
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER-GVGMVF-----QSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARrkhiLAGcvINNAWEAQNADQHIKSLNI-----KTPGAeqlimnLSGGNQQKAILGRWLSEEMKVILLDEPTRG 429
Cdd:PRK11000 96 MSFGLK----LAG--AKKEEINQRVNQVAEVLQLahlldRKPKA------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 430 ID----VGAKHEIYNVIYALaasGVAVVFASSDLPEVLGVADRIVVMREGEIAG-----ELLHEHANEQQALSLAMPK 498
Cdd:PRK11000 164 LDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQvgkplELYHYPANRFVAGFIGSPK 238
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
275-478 |
1.03e-09 |
|
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: 57.95 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFG--GSRITAGQVYIDGEAIDIRKPAQAIqaGMmlCPEDrkaEGIIPVHSVR 352
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKII--GY--VPQD---DILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 353 DNINISARRKHILAGcvinnawEAqnadqhiKSLNIktpgAEQLIMNLSggnqqkailgrwlseemkVILLDEPTRGIDV 432
Cdd:cd03213 101 ETLMFAAKLRGLSGG-------ER-------KRVSI----ALELVSNPS------------------LLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490204990 433 GAKHEIYNVIYALAASGVAVVF----ASSdlpEVLGVADRIVVMREGEIA 478
Cdd:cd03213 145 SSALQVMSLLRRLADTGRTIICsihqPSS---EIFELFDKLLLLSQGRVI 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
275-477 |
1.10e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMlcpedRKAEGII-------P 347
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKL-----RKEVGMVfqqpnpfP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 VHSVRDNI-------NISARR--KHILAGCVINNAWEAQNADQhikslnIKTPGAEqlimnLSGGNQQKAILGRWLSEEM 418
Cdd:PRK14246 104 HLSIYDNIayplkshGIKEKReiKKIVEECLRKVGLWKEVYDR------LNSPASQ-----LSGGQQQRLTIARALALKP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYALAASgVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
376-503 |
1.37e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.48 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 376 AQNADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFA 455
Cdd:PRK13631 153 KKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVI 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 456 SSDLPEVLGVADRIVVMREGEI--AGELLHEHANEQ--QALSLAMPKVSQAV 503
Cdd:PRK13631 233 THTMEHVLEVADEVIVMDKGKIlkTGTPYEIFTDQHiiNSTSIQVPRVIQVI 284
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
8-193 |
1.46e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.50 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthtteALN----AG 83
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT------HLPmhkrAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIY--QELHLIPEMTVAENIY----LGQLPHKGgIVNR--SLLNYeagLQLQHLGldidpETPLKYLSIGQWQMVEIA 155
Cdd:COG1137 78 LGIGYlpQEASIFRKLTVEDNILavleLRKLSKKE-REERleELLEE---FGITHLR-----KSKAYSLSGGERRRVEIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490204990 156 KALARNAKIIAFDEPTSS---LSAREIDNLfrvIRELRQEG 193
Cdd:COG1137 149 RALATNPKFILLDEPFAGvdpIAVADIQKI---IRHLKERG 186
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
275-477 |
1.54e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.71 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEaiDIRKpaqaiqagmmLCPEDRKAeGIIPVH----- 349
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSR----------LHARDRKV-GFVFQHyalfr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 --SVRDNI----NISARRKHIlagcviNNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILL 423
Cdd:PRK10851 88 hmTVFDNIafglTVLPRRERP------NAAAIKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 424 DEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
276-488 |
1.55e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.66 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 276 SLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAGMMLCPEDRKAEGIIPVHSVRDNI 355
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 356 NISARrkhiLAGcvINNAWEAQNADQHIKSLNIKTPgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAK 435
Cdd:PRK10070 128 AFGME----LAG--INAEERREKALDALRQVGLENY-AHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 436 HEIYNVIYALAASGV-AVVFASSDLPEVLGVADRIVVMREGEIA-----GELLHEHANE 488
Cdd:PRK10070 201 TEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVqvgtpDEILNNPAND 259
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
8-202 |
2.09e-09 |
|
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: 56.39 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKAL-SDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQqmtfthttealnAGVAI 86
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG------------EDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQElhliPEMTvaeniyLGQLphkggivnRSLLNYeaglqlqhlgldidpetPL-KYLSIGQWQMVEIAKALARNAKII 165
Cdd:cd03223 69 LPQR----PYLP------LGTL--------REQLIY-----------------PWdDVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*..
gi 490204990 166 AFDEPTSSLSAreiDNLFRVIRELRQEGRVIIYVSHR 202
Cdd:cd03223 114 FLDEATSALDE---ESEDRLYQLLKELGITVISVGHR 147
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-211 |
2.14e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 20 VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqmtfTHTTEALN-----AGVAIIYQElHLI 94
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND-----SHNLKDINlkwwrSKIGVVSQD-PLL 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 95 PEMTVAENI-----------YLGQLPHKGGIVNRSLLNYEAGLQLQHLGL------------------------------ 133
Cdd:PTZ00265 472 FSNSIKNNIkyslyslkdleALSNYYNEDGNDSQENKNKRNSCRAKCAGDlndmsnttdsneliemrknyqtikdsevvd 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 134 --------DIDPETPLKY----------LSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELR-QEGR 194
Cdd:PTZ00265 552 vskkvlihDFVSALPDKYetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENR 631
|
250 260
....*....|....*....|...
gi 490204990 195 VIIYVSHRME------EIFALSD 211
Cdd:PTZ00265 632 ITIIIAHRLStiryanTIFVLSN 654
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
273-480 |
2.55e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.10 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI------DIRKpaqaiQAGMMLCPEDRKAEGIi 346
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseetvwDVRR-----QVGMVFQNPDNQFVGA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 pvhSVRDNI-----NISARRKHILagcvinnaweaQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVI 421
Cdd:PRK13635 98 ---TVQDDVafgleNIGVPREEMV-----------ERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 422 LLDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGvADRIVVMREGEIAGE 480
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-213 |
3.17e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.74 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 24 SDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqmtfthttEALNAGVAIIYQEL----HL--I-PE 96
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG---------EPIRRQRDEYHQDLlylgHQpgIkTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 MTVAENI-YLGQLphkggivnRSLLNYEAGLQ-LQHLGLDIDPETPLKYLSIGQWQMVeiakALAR----NAKIIAFDEP 170
Cdd:PRK13538 89 LTALENLrFYQRL--------HGPGDDEALWEaLAQVGLAGFEDVPVRQLSAGQQRRV----ALARlwltRAPLWILDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490204990 171 TSSLSAREIDNLFRVIRELRQEGRVIIYVSHRmeEIFALSDAI 213
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTHQ--DLPVASDKV 197
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
275-501 |
4.99e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.34 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIdGEaidirkpaQAIQAGMMlcPED----RKAEGII---P 347
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GE--------RVITAGKK--NKKlkplRKKVGIVfqfP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 VHSVRDniniSARRKHILAGcVINNAWEAQNADQHIKSLnIKTPGAEQLIM-----NLSGGNQQK-AILGRwLSEEMKVI 421
Cdd:PRK13634 95 EHQLFE----ETVEKDICFG-PMNFGVSEEDAKQKAREM-IELVGLPEELLarspfELSGGQMRRvAIAGV-LAMEPEVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 422 LLDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEIAG----ELLHEHANEQQALSLAM 496
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLqgtpREIFADPDELEAIGLDL 247
|
....*
gi 490204990 497 PKVSQ 501
Cdd:PRK13634 248 PETVK 252
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-224 |
5.71e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 6 PYLSFHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKSTLLKILSG----NYVPTAGSLQ---IQGQQMTFT 74
Cdd:PRK15093 2 PLLDIRNLTIEFKTsdgwVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADRMRfddIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 75 HTTEALNAGVAIIYQELH--LIPEMTVAENIyLGQLP---HKGGIVNRSLLNYEAGLQLQH-LGL----DIDPETPLKyL 144
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQscLDPSERVGRQL-MQNIPgwtYKGRWWQRFGWRKRRAIELLHrVGIkdhkDAMRSFPYE-L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 145 SIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQ-EGRVIIYVSHRMEEIFALSDAITVFKDGRYVR 223
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
.
gi 490204990 224 T 224
Cdd:PRK15093 240 T 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-234 |
5.86e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 57.79 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTE--ALNAGVAIIYQE--LHLIPE 96
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwrAVRSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 MTVAEniylgqlphkggIVNRSLLNYEAGLQLQHL-----------GLdiDPETPLKY---LSIGQWQMVEIAKALARNA 162
Cdd:PRK15079 115 MTIGE------------IIAEPLRTYHPKLSRQEVkdrvkammlkvGL--LPNLINRYpheFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 163 KIIAFDEPTSSLSAR---EIDNLfrvIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKDGRYVR--TFDnmqEVNHD 234
Cdd:PRK15079 181 KLIICDEPVSALDVSiqaQVVNL---LQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVElgTYD---EVYHN 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
275-480 |
6.49e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.03 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRS---ELMKGLFggsRITAGQVYIDGEaidiRKPAQAI-----QAGMMLCPEDRKAEGIi 346
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSttaRLIDGLF---EEFEGKVKIDGE----LLTAENVwnlrrKIGMVFQNPDNQFVGA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 pvhSVRDNINISARRKHILAGCVINNAWEAQNAdqhIKSLNIKTPGAEQLimnlSGGNQQKAILGRWLSEEMKVILLDEP 426
Cdd:PRK13642 98 ---TVEDDVAFGMENQGIPREEMIKRVDEALLA---VNMLDFKTREPARL----SGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 427 TRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVlGVADRIVVMREGEIAGE 480
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEIIKE 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
285-480 |
7.30e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 56.73 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 285 VGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI---DIRkpaqaiqagmmlcpEDRKAEGIIPVHSvrDNINISARR 361
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkeNIR--------------EVRKFVGLVFQNP--DDQIFSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 362 KHILAGCVINNAWEAQNADQHIKSLnIKTPGAEQLI----MNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHE 437
Cdd:PRK13652 97 EQDIAFGPINLGLDEETVAHRVSSA-LHMLGLEELRdrvpHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490204990 438 IYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:PRK13652 176 LIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
275-477 |
7.33e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.42 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEaiDIRKpaQAIQagmmlcpeDR------KAEGIIPV 348
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTH--RSIQ--------QRdicmvfQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 HSVRDNI------------NISARRKHILAgCVINNAWEAQNADQhikslniktpgaeqlimnLSGGNQQKAILGRWLSE 416
Cdd:PRK11432 93 MSLGENVgyglkmlgvpkeERKQRVKEALE-LVDLAGFEDRYVDQ------------------ISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 417 EMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
259-478 |
8.70e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.41 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 259 ERLRLDRVKA--PGVRQP------VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIdiRKPAQaiq 330
Cdd:COG4525 2 SMLTVRHVSVryPGGGQPqpalqdVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--TGPGA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 331 agmmlcpeDR----KAEGIIPVHSVRDNINISARrkhiLAGcvINNAWEAQNADQHIKSLNIKtpGAEQ-LIMNLSGGNQ 405
Cdd:COG4525 77 --------DRgvvfQKDALLPWLNVLDNVAFGLR----LRG--VPKAERRARAEELLALVGLA--DFARrRIWQLSGGMR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 406 QKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVM--REGEIA 478
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIV 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
275-480 |
1.35e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.86 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDG-------EAIDIRKpaqaiQAGMMLCPEDRKAEGIIP 347
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeeNLWDIRN-----KAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 VHSVR---DNINISAR--RKHILAGCVINNAWEAQNADQHIkslniktpgaeqlimnLSGGNQQKAILGRWLSEEMKVIL 422
Cdd:PRK13633 104 EEDVAfgpENLGIPPEeiRERVDESLKKVGMYEYRRHAPHL----------------LSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 423 LDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGvADRIVVMREGEIAGE 480
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-226 |
1.60e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGN--YVPTAGSLQIQGQQMTFTHTTE 78
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 79 ALNAGVAIIYQELHLIPemtvaeniylgqlphkgGIVNRSLLNYEAGLQLQHLGL-DIDPETPLKYL------------- 144
Cdd:CHL00131 81 RAHLGIFLAFQYPIEIP-----------------GVSNADFLRLAYNSKRKFQGLpELDPLEFLEIIneklklvgmdpsf 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 145 ---------SIGQWQMVEIAKALARNAKIIAFDEPTSSLsarEIDNLFRV---IRELRQEGRVIIYVSH--RMEEiFALS 210
Cdd:CHL00131 144 lsrnvnegfSGGEKKRNEILQMALLDSELAILDETDSGL---DIDALKIIaegINKLMTSENSIILITHyqRLLD-YIKP 219
|
250
....*....|....*.
gi 490204990 211 DAITVFKDGRYVRTFD 226
Cdd:CHL00131 220 DYVHVMQNGKIIKTGD 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
269-494 |
1.69e-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: 57.26 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 269 PGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIrkPAQA-IQagmmlcpEDRKAEGIIP 347
Cdd:TIGR00957 651 PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYV--PQQAwIQ-------NDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 VHSVRDNinisaRRKHILAGCvinnaweAQNADQHIKSLNIKTPGAEQLImNLSGGNQQKAILGRWLSEEMKVILLDEPT 427
Cdd:TIGR00957 722 GKALNEK-----YYQQVLEAC-------ALLPDLEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 428 RGIDVG-AKHEIYNVIYALA----ASGVAVVFASSDLPEVlgvaDRIVVMREGEIA---------------GELLHEHAN 487
Cdd:TIGR00957 789 SAVDAHvGKHIFEHVIGPEGvlknKTRILVTHGISYLPQV----DVIIVMSGGKISemgsyqellqrdgafAEFLRTYAP 864
|
....*..
gi 490204990 488 EQQALSL 494
Cdd:TIGR00957 865 DEQQGHL 871
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
271-477 |
1.80e-08 |
|
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: 55.17 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDI-------RKPAQAIQagmmlcpedrkaE 343
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkylhSKVSLVGQ------------E 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 344 GIIPVHSVRDNINISarrkhiLAGCVINNAWEAQ---NADQHIKSL--NIKTpGAEQLIMNLSGGNQQKAILGRWLSEEM 418
Cdd:cd03248 97 PVLFARSLQDNIAYG------LQSCSFECVKEAAqkaHAHSFISELasGYDT-EVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSdlPEVLGVADRIVVMREGEI 477
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHR--LSTVERADQILVLDGGRI 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
275-480 |
1.96e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 56.71 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMK---GLFggsRITAGQVYIDGeaIDIRKpaqaiqagmmLCPED-RKAEGIIP--V 348
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNlllRFY---DPTSGRILIDG--VDIRD----------LTLESlRRQIGVVPqdT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 H----SVRDNI---NISARRKHILAgcvinnAWEAQNADQHIKSLniktP-GAEQLI----MNLSGGNQQK-----AILG 411
Cdd:COG1132 424 FlfsgTIRENIrygRPDATDEEVEE------AAKAAQAHEFIEAL----PdGYDTVVgergVNLSGGQRQRiaiarALLK 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 412 RwlseeMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFA---SSdlpeVLGvADRIVVMREGEIAGE 480
Cdd:COG1132 494 D-----PPILILDEATSALDTETEALIQEALERLMKGRTTIVIAhrlST----IRN-ADRILVLDDGRIVEQ 555
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
249-477 |
2.11e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.51 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 249 YGWQPREYGKERLRLDrvkapgvrqpVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIR----- 323
Cdd:PRK13643 9 YTYQPNSPFASRALFD----------IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqke 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 324 -KPAQAIQAGMMLCPEDRKAEGII--PVHSVRDNINISARRKHILAGcvinnaweaqnadQHIKSLNIKTPGAEQLIMNL 400
Cdd:PRK13643 79 iKPVRKKVGVVFQFPESQLFEETVlkDVAFGPQNFGIPKEKAEKIAA-------------EKLEMVGLADEFWEKSPFEL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 401 SGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK13643 146 SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
265-433 |
2.76e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.67 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 265 RVKAPGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKpaqaiqAGMMlcpEDRKAEG 344
Cdd:PLN03130 1248 RPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG--CDISK------FGLM---DLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 345 IIPVH------SVRdnINISARRKHilagcviNNA--WEA-QNAdqHIKSLNIKTP---------GAEqlimNLSGGNQQ 406
Cdd:PLN03130 1317 IIPQApvlfsgTVR--FNLDPFNEH-------NDAdlWESlERA--HLKDVIRRNSlgldaevseAGE----NFSVGQRQ 1381
|
170 180
....*....|....*....|....*..
gi 490204990 407 KAILGRWLSEEMKVILLDEPTRGIDVG 433
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVR 1408
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
271-477 |
2.96e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQaiqagmmLCPEDRKAEGII---- 346
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADA-------LAQLRREHFGFIfqry 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 ---PVHSVRDNINISArrkhILAGcvINNAWEAQNADQHIKSLniktpGAEQLI----MNLSGGNQQKAILGRWLSEEMK 419
Cdd:PRK10535 96 hllSHLTAAQNVEVPA----VYAG--LERKQRLLRAQELLQRL-----GLEDRVeyqpSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 420 VILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDlPEVLGVADRIVVMREGEI 477
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
277-470 |
2.97e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 277 LSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIR---KPAQAIQAGMMlcpeDRKAEGIIPV----- 348
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqDPPRNVEGTVY----DFVAEGIEEQaeylk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 --HSVRD---------NINISARRKHILAgcvINNAWEAQN-ADQHIKSLNIKtpgAEQLIMNLSGGNQQKAILGRWLSE 416
Cdd:PRK11147 100 ryHDISHlvetdpsekNLNELAKLQEQLD---HHNLWQLENrINEVLAQLGLD---PDAALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 417 EMKVILLDEPTRGIDVGAKHEIYNviYALAASGvAVVFASSDLPEVLGVADRIV 470
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEG--FLKTFQG-SIIFISHDRSFIRNMATRIV 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
204-459 |
3.07e-08 |
|
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: 56.21 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 204 EEIFALSDAITvfKDGRYVRTFDNMQEVNHDALVQAMVGRELGDIYGWQPREYGKERLRLDRVKAPGVRQPVSLSVRSGE 283
Cdd:TIGR02868 285 EAFAALPAAAQ--QLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 284 IVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDiRKPAQAIQAGMMLCPEDrkaegiipVH----SVRDNINISA 359
Cdd:TIGR02868 363 RVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS-SLDQDEVRRRVSVCAQD--------AHlfdtTVRENLRLAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 360 rrkhilAGCVINNAWEAQNADQ---HIKSLniktPGAEQLIMN-----LSGGNQQKAILGRWLSEEMKVILLDEPTRGID 431
Cdd:TIGR02868 434 ------PDATDEELWAALERVGladWLRAL----PDGLDTVLGeggarLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
250 260
....*....|....*....|....*...
gi 490204990 432 VGAKHEIYNVIYAlAASGVAVVFASSDL 459
Cdd:TIGR02868 504 AETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
275-477 |
3.57e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFG---------GSRITaGQVYIDGEaidirkPAQAIQAGMMLCpedRKAegI 345
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggaprGARVT-GDVTLNGE------PLAAIDAPRLAR---LRA--V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 346 IPvHSVRDNINISARrKHILAGCV--INNAWEAQNADQHIKSLNIKTPGAEQL----IMNLSGGNQQKAILGR-----WL 414
Cdd:PRK13547 88 LP-QAAQPAFAFSAR-EIVLLGRYphARRAGALTHRDGEIAWQALALAGATALvgrdVTTLSGGELARVQFARvlaqlWP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 415 SEEMKV----ILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGV-ADRIVVMREGEI 477
Cdd:PRK13547 166 PHDAAQppryLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAI 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
399-477 |
4.36e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.71 E-value: 4.36e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 399 NLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-224 |
4.59e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 21 KALSDISFDCYAGQVHALMGENGAGKS-TLLKILSGNYVP---TAGSLQIQGQQMTFTHTTEA---LNAGVAIIYQE--L 91
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERrnlVGAEVAMIFQDpmT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 92 HLIPEMTVAENIYLGQLPHKGGivNRSLLNYEAGLQLQHLGLDiDPETPLKY----LSIGQWQMVEIAKALARNAKIIAF 167
Cdd:PRK11022 101 SLNPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQVGIP-DPASRLDVyphqLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 168 DEPTSSLSAREIDNLFRVIREL-RQEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRT 224
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
275-477 |
4.96e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.45 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIR---KPAQAIQAGMMLC---PEDRKAEgiipv 348
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnKNLKKLRKKVSLVfqfPEAQLFE----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 HSVRDNINISARRkhilAGCVINNAWEAqnADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTR 428
Cdd:PRK13641 101 NTVLKDVEFGPKN----FGFSEDEAKEK--ALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 429 GIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
275-477 |
5.99e-08 |
|
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: 53.55 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQ-VYI-----DGEAI-DIRK------PAQAiqagmmlcpedrk 341
Cdd:COG1119 22 ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgerrGGEDVwELRKriglvsPALQ------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 342 aEGIIPVHSVRDNInISA------RRKHIlagcvinNAWEAQNADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLS 415
Cdd:COG1119 89 -LRFPRDETVLDVV-LSGffdsigLYREP-------TDEQRERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 416 EEMKVILLDEPTRGIDVGAKHEIYNVIYALAASG-VAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-231 |
6.22e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.75 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 18 PGVK-ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthttealNAGVAIIYQELHLIPE 96
Cdd:PLN03232 1246 PGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--------KFGLTDLRRVLSIIPQ 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 97 M------TVAENIYLGQLPHKGGIvnrsllnYEAgLQLQHL---------GLDIDPETPLKYLSIGQWQMVEIAKALARN 161
Cdd:PLN03232 1318 SpvlfsgTVRFNIDPFSEHNDADL-------WEA-LERAHIkdvidrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 162 AKIIAFDEPTSSLSAReIDNLFRviRELRQEGR--VIIYVSHRMEEIFAlSDAITVFKDGRyVRTFDNMQEV 231
Cdd:PLN03232 1390 SKILVLDEATASVDVR-TDSLIQ--RTIREEFKscTMLVIAHRLNTIID-CDKILVLSSGQ-VLEYDSPQEL 1456
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
275-469 |
7.80e-08 |
|
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: 52.50 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPaqAIQAGMMLCPEdrkAEGIIPVHSVRDN 354
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYLGH---APGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INIsarrkhilagcvinnaWEAQNADQHIKSL--NIKTPGAEQLIMN-LSGGNQQKAILGRWLSEEMKVILLDEPTRGID 431
Cdd:cd03231 94 LRF----------------WHADHSDEQVEEAlaRVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 490204990 432 VGAKHEIYNVIYALAASGVAVVFASS-DLPEVLGVADRI 469
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-222 |
8.65e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSG--------NYVPTAGSLQIQGQQMTFTHTTEaLNAGVAIIYQELHLI 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAAIDAPR-LARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 95 PEMTVAENIYLGQLPH----------KGGIVNRSLLNYEAGlqlQHLGLDIDPetplkyLSIGQWQMVEIAKALA----- 159
Cdd:PRK13547 96 FAFSAREIVLLGRYPHarragalthrDGEIAWQALALAGAT---ALVGRDVTT------LSGGELARVQFARVLAqlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 160 ----RNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRV-IIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK13547 167 hdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-220 |
8.87e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 33 GQVHALMGENGAGKSTLLKILSGnyvptagslQIQGQQMTFT------HTTEALNAGVAIIYQELHLIPEMTVAENIYLG 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAG---------RIQGNNFTGTilannrKPTKQILKRTGFVTQDDILYPHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 107 QLPHKGGIVNRSLLNYEAGLQLQHLGL-----DIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDN 181
Cdd:PLN03211 165 SLLRLPKSLTKQEKILVAESVISELGLtkcenTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490204990 182 LFRVIRELRQEGRVIIYVSHR-MEEIFALSDAITVFKDGR 220
Cdd:PLN03211 245 LVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-231 |
1.03e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 22 ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFthtteALNAGvaiiyqelhLIPEMTVAE 101
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI-----AISAG---------LSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 102 NIYLGQLPHkgGIVNRSL--LNYEAgLQLQHLGLDIdpETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREI 179
Cdd:PRK13546 105 NIEFKMLCM--GFKRKEIkaMTPKI-IEFSELGEFI--YQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 180 DNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRyVRTFDNMQEV 231
Cdd:PRK13546 180 QKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK-LKDYGELDDV 230
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
33-216 |
1.07e-07 |
|
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: 51.80 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 33 GQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqmtfthttealnagVAIIYQelhlipemtvaeniylgqlPHKg 112
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG---------------ITPVYK-------------------PQY- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 113 givnrsllnyeaglqlqhlgldIDpetplkyLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQE 192
Cdd:cd03222 70 ----------------------ID-------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*
gi 490204990 193 G-RVIIYVSHRMEEIFALSDAITVF 216
Cdd:cd03222 121 GkKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-222 |
1.15e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 33 GQVHALMGENGAGKSTLLKIL----SGNYVptAGSLQIQG---QQMTFTHTTEalnagvaiiYQELHLI--PEMTVAEN- 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRISGfpkKQETFARISG---------YCEQNDIhsPQVTVRESl 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 103 IYLG--QLPHKGGIVNRSLLNYEAG--LQLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSARE 178
Cdd:PLN03140 975 IYSAflRLPKEVSKEEKMMFVDEVMelVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490204990 179 IDNLFRVIRELRQEGRVIIYVSHRME-EIFALSDAITVFKDGRYV 222
Cdd:PLN03140 1055 AAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLMKRGGQV 1099
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
261-480 |
1.17e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.07 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 261 LRLDRVK------APGVRQpVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKPAQaiqagmm 334
Cdd:PRK13644 2 IRLENVSysypdgTPALEN-INLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 335 lCPEDRKAEGII---PV-----HSVRDNINISARRKhILAGCVINNAWEAQNADQHIKSLNIKTPGAeqlimnLSGGNQQ 406
Cdd:PRK13644 72 -LQGIRKLVGIVfqnPEtqfvgRTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGLEKYRHRSPKT------LSGGQGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 407 KAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEvLGVADRIVVMREGEIAGE 480
Cdd:PRK13644 144 CVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLE 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
275-477 |
1.18e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.63 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEaiDIRKPAQAIQAGMMLCPEdrkaEGIIPVH-SVRD 353
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK--DIETNLDAVRQSLGMCPQ----HNILFHHlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 354 NINISARRKhilagcviNNAW-EAQ-NADQHIKSLNIKTPGAEQlIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGID 431
Cdd:TIGR01257 1023 HILFYAQLK--------GRSWeEAQlEMEAMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 432 VGAKHEIYNVIYALaASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:TIGR01257 1094 PYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
265-493 |
1.28e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 265 RVKAPGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKpaqaiqAGMMlcpEDRKAEG 344
Cdd:PLN03232 1245 RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD--CDVAK------FGLT---DLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 345 IIP----VHSVRDNINISARRKHILAGCvinnaWEAQNAdQHIKSLNIKTP---------GAEqlimNLSGGNQQKAILG 411
Cdd:PLN03232 1314 IIPqspvLFSGTVRFNIDPFSEHNDADL-----WEALER-AHIKDVIDRNPfgldaevseGGE----NFSVGQRQLLSLA 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 412 RWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSdLPEVLGvADRIVVMREGEIAgellhEHANEQQA 491
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHR-LNTIID-CDKILVLSSGQVL-----EYDSPQEL 1456
|
..
gi 490204990 492 LS 493
Cdd:PLN03232 1457 LS 1458
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
127-213 |
1.57e-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: 51.17 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 127 QLQHL---GLD-IDPETPLKYLSIGQWQMVEIAKALARNAK--IIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVS 200
Cdd:cd03238 67 QLQFLidvGLGyLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIE 146
|
90
....*....|...
gi 490204990 201 HRmEEIFALSDAI 213
Cdd:cd03238 147 HN-LDVLSSADWI 158
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
275-480 |
1.58e-07 |
|
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: 53.65 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFG--GSRITAGQVY----IDGEAIDIRKPAQAIQAgmmlCP------EDRKA 342
Cdd:TIGR03269 19 ISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIyhvaLCEKCGYVERPSKVGEP----CPvcggtlEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 343 EGIIPVHSVRDN----INISARRKHILAG--CVINNAWEAQN-----ADQHI-KSLN-IKTPGAEQLIM----NLSGGNQ 405
Cdd:TIGR03269 95 DFWNLSDKLRRRirkrIAIMLQRTFALYGddTVLDNVLEALEeigyeGKEAVgRAVDlIEMVQLSHRIThiarDLSGGEK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 406 QKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALA-ASGVAVVFaSSDLPEVLG-VADRIVVMREGEIAGE 480
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVL-TSHWPEVIEdLSDKAIWLENGEIKEE 250
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
275-467 |
1.63e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.73 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITaGQVYIDGEA-----------IDIRKPAQAIQagmMLCPEdrkaE 343
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVeffnqniyerrVNLNRLRRQVS---MVHPK----P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 344 GIIPVhSVRDNI----NISARRKHILAGCVINNAWEAQNADQHIKSLNIKTPgaeqliMNLSGGNQQKAILGRWLSEEMK 419
Cdd:PRK14258 98 NLFPM-SVYDNVaygvKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSA------LDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 420 VILLDEPTRGIDVGAKHEIYNVIYALA-ASGVAVVFASSDLPEVLGVAD 467
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-205 |
1.85e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 33 GQVHALMGENGAGKSTLLKILSGNY---VPTAGSLQIQGQ--QMTFTHTTEALNAgvaiiyQELHLiPEMTVAENI---- 103
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGRplDSSFQRSIGYVQQ------QDLHL-PTSTVRESLrfsa 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 104 YLGQLPH-----KGGIVNR--SLLNYE----AGLQLQHLGLDIDPEtplKYLSIGqwqmVEIAkalARNAKIIAFDEPTS 172
Cdd:TIGR00956 862 YLRQPKSvskseKMEYVEEviKLLEMEsyadAVVGVPGEGLNVEQR---KRLTIG----VELV---AKPKLLLFLDEPTS 931
|
170 180 190
....*....|....*....|....*....|....*...
gi 490204990 173 SLSAREIDNLFRVIRELRQEGRVIIYVSHR-----MEE 205
Cdd:TIGR00956 932 GLDSQTAWSICKLMRKLADHGQAILCTIHQpsailFEE 969
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
275-477 |
2.05e-07 |
|
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: 53.59 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIrkpaqaiqagmmlcpedrkaegiIPVHSVRDN 354
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD-----------------------IDRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKHILAGCVINN----AWEAQNADQHIKSLNIKTPGA--EQLIM-----------NLSGGNQQKAILGRWLSEE 417
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENlllgAKENVSQDEIWAACEIAEIKDdiENMPLgyqtelseegsSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 418 MKVILLDEPTRGIDVGAKHEIYNVIYALAASgvAVVFASSDLpEVLGVADRIVVMREGEI 477
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRL-SVAKQSDKIIVLDHGKI 686
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
253-477 |
2.51e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 53.18 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 253 PREYGKERLRLDRVKAPGVRQP----VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI-DIRkpAQ 327
Cdd:TIGR02203 325 ERARGDVEFRNVTFRYPGRDRPaldsISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYT--LA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 328 AIQAGMMLCPEDrkaegiipVH----SVRDNINISARRKHILAGcvINNAWEAQNADQHIKSL--NIKTPGAEQLImNLS 401
Cdd:TIGR02203 403 SLRRQVALVSQD--------VVlfndTIANNIAYGRTEQADRAE--IERALAAAYAQDFVDKLplGLDTPIGENGV-LLS 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 402 GGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSdLPEVLGvADRIVVMREGEI 477
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHR-LSTIEK-ADRIVVMDDGRI 545
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
271-477 |
2.72e-07 |
|
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: 51.83 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRK-PAQAIQAGMMLCPEDRkaegIIPVH 349
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG--IDISKlPLHTLRSRLSIILQDP----ILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 SVRdnINISARRKhilagCVINNAWEAQNADQ---HIKSL-----NIKTPGAEqlimNLSGGNQQKAILGRWLSEEMKVI 421
Cdd:cd03288 110 SIR--FNLDPECK-----CTDDRLWEALEIAQlknMVKSLpggldAVVTEGGE----NFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 422 LLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASsdLPEVLGVADRIVVMREGEI 477
Cdd:cd03288 179 IMDEATASIDMATENILQKVVMTAFADRTVVTIAH--RVSTILDADLVLVLSRGIL 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
275-477 |
3.53e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVyIDGEAidirkPAQAIQAGMMLCPEDRKaegIIPVHSVRDN 354
Cdd:PRK11247 31 LDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA-----PLAEAREDTRLMFQDAR---LLPWKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 INISARRKhilagcvinnaWEAQnADQHIKSLNIKT-----PGAeqlimnLSGGNQQKAILGRWLSEEMKVILLDEPTRG 429
Cdd:PRK11247 102 VGLGLKGQ-----------WRDA-ALQALAAVGLADranewPAA------LSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490204990 430 IDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK11247 164 LDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
271-480 |
3.56e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.51 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAiqagmMLCPEDRKAegiipVHS 350
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDG-----QLKVADKNQ-----LRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNINISARRKHILAG-CVINNAWEA-------------QNADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSE 416
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHmTVLENVMEApiqvlglskqearERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 417 EMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
275-478 |
3.77e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 52.74 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLF----GGSRItAGQVYIDGEAIDIRKpAQAIQAGMMlcpEDrkaEGIIPVHS 350
Cdd:TIGR00955 44 VSGVAKPGELLAVMGSSGAGKTTLMNALAfrspKGVKG-SGSVLLNGMPIDAKE-MRAISAYVQ---QD---DLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNINISArrkHILAGCVINNAWEAQNADQHIKSLNIKTP-----GAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDE 425
Cdd:TIGR00955 116 VREHLMFQA---HLRMPRRVTKKEKRERVDEVLQALGLRKCantriGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 426 PTRGIDVGAKHEIYNVIYALAASGVAVVFA----SSDLPEVLgvaDRIVVMREGEIA 478
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTihqpSSELFELF---DKIILMAEGRVA 246
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
275-476 |
3.97e-07 |
|
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: 50.55 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaidirkpaqaiqaGMMLCPEdrkaEGIIPVHSVRDN 354
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQ----EPWIQNGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 InisarrkhiLAGCVINNAW-----EAQNADQHIKSLniktPGAEQLI-----MNLSGGNQQKAILGRWLSEEMKVILLD 424
Cdd:cd03250 86 I---------LFGKPFDEERyekviKACALEPDLEIL----PDGDLTEigekgINLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490204990 425 EPTRGIDVG-AKHEIYNVIYALAASGVAVVFASSDLpEVLGVADRIVVMREGE 476
Cdd:cd03250 153 DPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-222 |
3.97e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.38 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 35 VHALMGENGAGKSTLLKILS-----GNYVPTAGSLQIQGQQMtFTHTTEALNA--GVAIIYQELHLIPEMTVAENIYLGq 107
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLFGRNI-YSPDVDPIEVrrEVGMVFQYPNPFPHLTIYDNVAIG- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 108 LPHKGGIVNRSLLNYEAGLQLQHLGLDIDPETPLK----YLSIGQWQMVEIAKALARNAKIIAFDEPTSSL---SAREID 180
Cdd:PRK14267 110 VKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILLMDEPTANIdpvGTAKIE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490204990 181 NLfrvIRELRQEgRVIIYVSHRMEEIFALSDAITVFKDGRYV 222
Cdd:PRK14267 190 EL---LFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-197 |
4.41e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALnag 83
Cdd:PRK13543 8 APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFM--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 vaiiyqelhlipemtvaenIYLGQLPH-KGGIVNRSLLNYEAGLQLQH-----------LGLDIDPETPLKYLSIGQWQM 151
Cdd:PRK13543 85 -------------------AYLGHLPGlKADLSTLENLHFLCGLHGRRakqmpgsalaiVGLAGYEDTLVRQLSAGQKKR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490204990 152 VEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIR-ELRQEGRVII 197
Cdd:PRK13543 146 LALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISaHLRGGGAALV 192
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
275-501 |
4.69e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.32 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI-------DIRKPAQAIqaGMML-CPEDRKAEgii 346
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdkYIRPVRKRI--GMVFqFPESQLFE--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 pvhsvrDNInisarRKHILAGcvinnaweAQNADQHIKSLNIKtpgAEQLIMNL--------------SGGNQQKAILGR 412
Cdd:PRK13646 101 ------DTV-----EREIIFG--------PKNFKMNLDEVKNY---AHRLLMDLgfsrdvmsqspfqmSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 413 WLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAA-SGVAVVFASSDLPEVLGVADRIVVMREGEIAGEL----LHEHAN 487
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTspkeLFKDKK 238
|
250
....*....|....
gi 490204990 488 EQQALSLAMPKVSQ 501
Cdd:PRK13646 239 KLADWHIGLPEIVQ 252
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-201 |
5.20e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 17 FPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLqiqgqqmtftHTTEALNagvaIIYQELH---L 93
Cdd:PRK11147 329 IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----------HCGTKLE----VAYFDQHraeL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 94 IPEMTVAENIYLGQlphKGGIVN---RSLLNYeagLQ--LQHlgldidPE---TPLKYLSIGQWQMVEIAKALARNAKII 165
Cdd:PRK11147 395 DPEKTVMDNLAEGK---QEVMVNgrpRHVLGY---LQdfLFH------PKramTPVKALSGGERNRLLLARLFLKPSNLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490204990 166 AFDEPTSSLsarEIDNLfrvirELRQE------GRVIIyVSH 201
Cdd:PRK11147 463 ILDEPTNDL---DVETL-----ELLEElldsyqGTVLL-VSH 495
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-220 |
5.28e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.65 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 1 MQQSTPYLSFHGITMTFPG----VKALSDISFDCYAGQVHALMGENGAGKS----TLLKILSGNYVpTAGSLQIQGQQMt 72
Cdd:PRK09473 6 QQQADALLDVKDLRVTFSTpdgdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 73 FTHTTEALN----AGVAIIYQE--LHLIPEMTVAENIYLGQLPHKGgiVNRSLLNYEAGLQLQHLGLdidPET------- 139
Cdd:PRK09473 84 LNLPEKELNklraEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKG--MSKAEAFEESVRMLDAVKM---PEArkrmkmy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 140 PLKYlSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQE-GRVIIYVSHRMEEIFALSDAITVFKD 218
Cdd:PRK09473 159 PHEF-SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYA 237
|
..
gi 490204990 219 GR 220
Cdd:PRK09473 238 GR 239
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-228 |
5.51e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVkALSDISFDCYAGQVHALMGENGAGKS----TLLKILSGNYVPTAGSLQIQGQQMtftHTTEALNAG 83
Cdd:PRK10418 5 IELRNIALQAAQP-LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 84 VAIIYQE-------LHLIPEMTVAENIYLGQLPhkggiVNRSLLNyeaglQLQHLGLDiDPETPLKY----LSIGQWQMV 152
Cdd:PRK10418 81 IATIMQNprsafnpLHTMHTHARETCLALGKPA-----DDATLTA-----ALEAVGLE-NAARVLKLypfeMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 153 EIAKALARNAKIIAFDEPTSSL----SAREIDNLFRVIRElrqEGRVIIYVSHRMEEIFALSDAITVFKDGRYVRTFDNM 228
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLdvvaQARILDLLESIVQK---RALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVE 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
400-477 |
5.74e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.16 E-value: 5.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 400 LSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-201 |
5.93e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFpGVKAL-SDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQI----------QGQ----QMT 72
Cdd:PRK15064 2 LSTANITMQF-GAKPLfENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdpnerlgklrQDQfafeEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 73 FTHTTEALNAGVAIIYQELHLI---PEMTVAENIYLGQLPHK----GGIVNRSllnyEAGLQLqhLGLDIDPET---PLK 142
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQERDRIyalPEMSEEDGMKVADLEVKfaemDGYTAEA----RAGELL--LGVGIPEEQhygLMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 143 YLSIGqWQM-VEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRElRQEGRVIIyvSH 201
Cdd:PRK15064 155 EVAPG-WKLrVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE-RNSTMIII--SH 210
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
271-492 |
6.30e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.03 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDiRKPAQAIQAGMMLCPEDrkaegiiPV-- 348
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQD-------PVvl 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 -HSVRDNI----NISARRkhilagcvinnAWEAQNADQ---HIKSL--NIKTPGAEQLiMNLSGGNQQKAILGRWLSEEM 418
Cdd:PRK10790 428 aDTFLANVtlgrDISEEQ-----------VWQALETVQlaeLARSLpdGLYTPLGEQG-NNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 419 KVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFAS--SDLPEvlgvADRIVVMREGEIAgellhEHANEQQAL 492
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHrlSTIVE----ADTILVLHRGQAV-----EQGTHQQLL 562
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
275-501 |
6.60e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.89 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAID------IRKpaqaiQAGMMLC-PEDRKAEGiip 347
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaenekwVRS-----KVGLVFQdPDDQVFSS--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 vhSVRDNINISARRKHILAGCVINNAWEAQNAdQHIKSLNIKTPgaeqliMNLSGGNQQKAILGRWLSEEMKVILLDEPT 427
Cdd:PRK13647 96 --TVWDDVAFGPVNMGLDKDEVERRVEEALKA-VRMWDFRDKPP------YHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 428 RGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI----AGELLHEHANEQQAlSLAMPKVSQ 501
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVlaegDKSLLTDEDIVEQA-GLRLPLVAQ 243
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
275-477 |
7.59e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.47 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFG----GSRITAGQVYIDGEAIDIRKPAQAIQAGMMLCPedRKAegIIPVHS 350
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGilpaGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNP--RSA--FNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNINISARRKHILAG-CVINNAWEA---QNADQHIKSLNIKtpgaeqlimnLSGGNQQKAILGRWLSEEMKVILLDEP 426
Cdd:PRK10418 98 MHTHARETCLALGKPADdATLTAALEAvglENAARVLKLYPFE----------MSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 427 TRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
278-498 |
7.83e-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: 50.48 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 278 SVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIrKPaQAIQAgmmlcpedrKAEGiipvhSVRDNIni 357
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-KP-QYIKA---------DYEG-----TVRDLL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 358 sarrKHILAGCVINNAWEAQNadqhIKSLNIKtPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHE 437
Cdd:cd03237 83 ----SSITKDFYTHPYFKTEI----AKPLQIE-QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 438 IYNVI--YALAASGVAVV----FASSDLpevlgVADRIVVMrEGEIAgelLHEHANEQQALSLAMPK 498
Cdd:cd03237 154 ASKVIrrFAENNEKTAFVvehdIIMIDY-----LADRLIVF-EGEPS---VNGVANPPQSLRSGMNR 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-103 |
1.10e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 9 SFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTFTHTTEALNAGVAIIY 88
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMP 82
|
90
....*....|....*..
gi 490204990 89 QEL--HLIPEMTVAENI 103
Cdd:NF033858 83 QGLgkNLYPTLSVFENL 99
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
258-478 |
1.17e-06 |
|
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: 49.45 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 258 KERLRLDRVKAPGVRQP---VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaidirKPAQAIQAGMm 334
Cdd:cd03220 21 KKLGILGRKGEVGEFWAlkdVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLGLGG- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 335 lcpedrkaeGIIPVHSVRDNINISAR-----RKHILAgcVINNAWE----AQNADQHIKslniktpgaeqlimNLSGGnq 405
Cdd:cd03220 94 ---------GFNPELTGRENIYLNGRllglsRKEIDE--KIDEIIEfselGDFIDLPVK--------------TYSSG-- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 406 QKAILGRWLSEEMK--VILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:cd03220 147 MKARLAFAIATALEpdILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
275-470 |
1.54e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGE----------AIDIRKPAqAIQAGMMLCPEDRKAEg 344
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrigyvpqklYLDTTLPL-TVNRFLRLRPGTKKED- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 345 IIPVhsvrdninisarRKHILAGCVInnaweaqnadqhikslniktpgaEQLIMNLSGGNQQKAILGRWLSEEMKVILLD 424
Cdd:PRK09544 101 ILPA------------LKRVQAGHLI-----------------------DAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490204990 425 EPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIV 470
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
273-477 |
1.74e-06 |
|
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: 48.80 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGgsrITAGQVYIDGE----AIDIRKPAQAIQAGMMLCPE-DRKaegiIP 347
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDihynGIPYKEFAEKYPGEIIYVSEeDVH----FP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 348 VHSVRDNINISARrkhilagCvinnaweaqNADQHIKSLniktpgaeqlimnlSGGNQQKAILGRWLSEEMKVILLDEPT 427
Cdd:cd03233 97 TLTVRETLDFALR-------C---------KGNEFVRGI--------------SGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 428 RGIDVGAKHEIYNVIYALA--ASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:cd03233 147 RGLDSSTALEILKCIRTMAdvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
275-478 |
1.85e-06 |
|
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: 48.68 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFG--GSRITAGQVYIDGEaiDIRKpaqaiqagmmLCPEDRKAEGI------- 345
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE--DITD----------LPPEERARLGIflafqyp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 346 IPVHSVRdninisarrkhilagcvinnaweaqNADqHIKSLNiktpgaeqliMNLSGGNQQKAILGRWLSEEMKVILLDE 425
Cdd:cd03217 87 PEIPGVK-------------------------NAD-FLRYVN----------EGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 426 PTRGIDVGAKHEIYNVIYALAASGVAVVFaSSDLPEVLG--VADRIVVMREGEIA 478
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLI-ITHYQRLLDyiKPDRVHVLYDGRIV 184
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
273-477 |
1.94e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.40 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI---DIRKPAQAIQ-----AGMMLCPEDRKAEG 344
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgDYSYRSQRIRmifqdPSTSLNPRQRISQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 345 I-IPVHsVRDNINISARRKHILagcvinnaweaqnadQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILL 423
Cdd:PRK15112 110 LdFPLR-LNTDLEPEQREKQII---------------ETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 424 DEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
401-477 |
2.02e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.15 E-value: 2.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 401 SGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
271-477 |
2.02e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.84 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAqaiqagmmlcpeDRkaeGIIPV-- 348
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA------------DR---DIAMVfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 ------H-SVRDNInisarrkhilagcvinnAWEAQNA-------DQHI----KSLNIktpgaEQLI----MNLSGGNQQ 406
Cdd:PRK11650 84 nyalypHmSVRENM-----------------AYGLKIRgmpkaeiEERVaeaaRILEL-----EPLLdrkpRELSGGQRQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490204990 407 KAILGRWLSEEMKVILLDEPTRGID----VGAKHEIYNVIYALAASGVAVvfaSSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRLKTTSLYV---THDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
8-236 |
2.59e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVK-ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfTHTTEALNAGVAI 86
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT-AEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IYQELHLIPEMtvaeniyLGQlphKGGIVNRSLL-NYEAGLQLQH-LGLDIDPETPLKyLSIGQWQMVEIAKALARNAKI 164
Cdd:PRK10522 402 VFTDFHLFDQL-------LGP---EGKPANPALVeKWLERLKMAHkLELEDGRISNLK-LSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 165 IAFDEptsslSAREIDNLFR------VIRELRQEGRVIIYVSHRmEEIFALSDAITVFKDGRYVR-TFDNMQEVNHDAL 236
Cdd:PRK10522 471 LLLDE-----WAADQDPHFRrefyqvLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSElTGEERDAASRDAV 543
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-197 |
2.73e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTA-GSLQIQGQqmtfthttealnagVAIIYQeLHLIPEMTVAE 101
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT--------------VAYVPQ-VSWIFNATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 102 NIYLGqLPHKGGIVNRSLlnyeAGLQLQHlGLDIDPETPLKY-------LSIGQWQMVEIAKALARNAKIIAFDEPTSSL 174
Cdd:PLN03130 698 NILFG-SPFDPERYERAI----DVTALQH-DLDLLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180
....*....|....*....|....*
gi 490204990 175 SAREIDNLF-RVIR-ELRQEGRVII 197
Cdd:PLN03130 772 DAHVGRQVFdKCIKdELRGKTRVLV 796
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
273-480 |
2.90e-06 |
|
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: 48.58 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMkGLFGG-SRITAGQVYIDGEAIDirkpaqaiqaGMmlcPEDRKAEGiipvhsv 351
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLL-GLLAGlDRPTSGTVRLAGQDLF----------AL---DEDARARL------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 352 rdninisaRRKHIlaGCVInnaweaQNAdQHIKSL----NIKTP-----------GAEQLI-------------MNLSGG 403
Cdd:COG4181 88 --------RARHV--GFVF------QSF-QLLPTLtaleNVMLPlelagrrdaraRARALLervglghrldhypAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 404 NQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDlPEVLGVADRIVVMREGEIAGE 480
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHD-PALAARCDRVLRLRAGRLVED 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
250-478 |
3.06e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.94 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 250 GWQPR---EYGKERLRLdRVKAPGVRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGeaIDIRKpa 326
Cdd:TIGR00957 1278 GWPPRgrvEFRNYCLRY-REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAK-- 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 327 qaiqagmmlcpedrkaegiIPVHSVRDNINISARRKHILAGCVINN-----------AWEAQNAdQHIKSLNIKTP---- 391
Cdd:TIGR00957 1353 -------------------IGLHDLRFKITIIPQDPVLFSGSLRMNldpfsqysdeeVWWALEL-AHLKTFVSALPdkld 1412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 392 -----GAEqlimNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVgakhEIYNVIYalaasgvAVVFASSDLPEVLGVA 466
Cdd:TIGR00957 1413 hecaeGGE----NLSVGQRQLVCLARALLRKTKILVLDEATAAVDL----ETDNLIQ-------STIRTQFEDCTVLTIA 1477
|
250 260
....*....|....*....|.
gi 490204990 467 ---------DRIVVMREGEIA 478
Cdd:TIGR00957 1478 hrlntimdyTRVIVLDKGEVA 1498
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
8-202 |
3.21e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.81 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKAL-SDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQI-QGQQMTFthttealnagva 85
Cdd:COG4178 363 LALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLF------------ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 86 iIYQELHLiPEMTVAENIYlgqLPHKGGIVNRSLLnyEAGLQ---LQHLGLDIDPETPL-KYLSIGQWQMVEIAKALARN 161
Cdd:COG4178 431 -LPQRPYL-PLGTLREALL---YPATAEAFSDAEL--REALEavgLGHLAERLDEEADWdQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490204990 162 AKIIAFDEPTSSLSAREIDNLFRVIRElRQEGRVIIYVSHR 202
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHR 543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
271-431 |
3.59e-06 |
|
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: 49.91 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFggsRI--TAGQVYIDGEAIDirkpAQAIQAGmmlcpedRKAEGIIPv 348
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL---RLlsTEGEIQIDGVSWN----SVTLQTW-------RKAFGVIP- 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 hsvrdninisaRRKHILAGCVINNA-WEAQNADQHI---------KSLNIKTPGAEQLIMN-----LSGGNQQKAILGRW 413
Cdd:TIGR01271 1299 -----------QKVFIFSGTFRKNLdPYEQWSDEEIwkvaeevglKSVIEQFPDKLDFVLVdggyvLSNGHKQLMCLARS 1367
|
170
....*....|....*...
gi 490204990 414 LSEEMKVILLDEPTRGID 431
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLD 1385
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
275-477 |
4.42e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI-------DIRKPAQaiQAGMML-CPEDRKAEGII 346
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknkDIKQIRK--KVGLVFqFPESQLFEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 --PVHSVRDNINIS-------ARRKHILAGCVinnaweaqnadqhiKSLNIKTPgaeqliMNLSGGNQQKAILGRWLSEE 417
Cdd:PRK13649 104 lkDVAFGPQNFGVSqeeaealAREKLALVGIS--------------ESLFEKNP------FELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 418 MKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
275-480 |
4.67e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.22 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI---------DIRKPAQAI-QAGMMLCPedrkaeg 344
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsrsrlyTVRKRMSMLfQSGALFTD------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 345 iipvHSVRDNINISARRKHILAGCVINNAweaqnadQHIKSLNIKTPGAEQLIMN-LSGGNQQKAILGRWLSEEMKVILL 423
Cdd:PRK11831 99 ----MNVFDNVAYPLREHTQLPAPLLHST-------VMMKLEAVGLRGAAKLMPSeLSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 424 DEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEIAGE 480
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAH 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-174 |
5.12e-06 |
|
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: 49.16 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIqgqqmtfthttealNAGVAII 87
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--------------GETVKLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQEL---HLIPEMTVAENI------------------YLGQLPHKGGivnrsllnyeaglqlqhlgldiDPETPLKYLSI 146
Cdd:TIGR03719 389 YVDQsrdALDPNKTVWEEIsggldiiklgkreipsraYVGRFNFKGS----------------------DQQKKVGQLSG 446
|
170 180
....*....|....*....|....*...
gi 490204990 147 GQWQMVEIAKALARNAKIIAFDEPTSSL 174
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
275-472 |
5.72e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.16 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQV------YIDGEAIDIRKPAQAIQagMMLcpEDrkaegiiPV 348
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdLLGMKDDEWRAVRSDIQ--MIF--QD-------PL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 HSVRDNINIsarrkhilaGCVINNAWE-------AQNADQHIKSLNIKTPGAEQLI----MNLSGGNQQKAILGRWLSEE 417
Cdd:PRK15079 109 ASLNPRMTI---------GEIIAEPLRtyhpklsRQEVKDRVKAMMLKVGLLPNLInrypHEFSGGQCQRIGIARALILE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 418 MKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVM 472
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-176 |
7.27e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 9 SFHGITMTFPGVKA-LSDISFDCYAGQVHALMGENGAGKSTLLKILSGnyVPTagslQIQGqqmtfthttEA-LNAGVAI 86
Cdd:PRK11819 8 TMNRVSKVVPPKKQiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--VDK----EFEG---------EArPAPGIKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 87 IY--QELHLIPEMTVAENIYLGqLPHKGGIVNR----------------SLLNYEAGLQ--LQHLGL-DID--------- 136
Cdd:PRK11819 73 GYlpQEPQLDPEKTVRENVEEG-VAEVKAALDRfneiyaayaepdadfdALAAEQGELQeiIDAADAwDLDsqleiamda 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490204990 137 -----PETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSA 176
Cdd:PRK11819 152 lrcppWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-234 |
7.50e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.54 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 19 GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqQMTFTHTTEALNAGvaiiyqelhlipemT 98
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-RISFSSQFSWIMPG--------------T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 99 VAENIYLGqlphkggiVNRSLLNYEAGLQLQHLGLDID--PE---TPLK----YLSIGQWQMVEIAKALARNAKIIAFDE 169
Cdd:cd03291 114 IKENIIFG--------VSYDEYRYKSVVKACQLEEDITkfPEkdnTVLGeggiTLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 170 PTSSLSAREIDNLFR--VIRELRQEGRviIYVSHRMEEIfALSDAITVFKDGR--YVRTFDNMQEVNHD 234
Cdd:cd03291 186 PFGYLDVFTEKEIFEscVCKLMANKTR--ILVTSKMEHL-KKADKILILHEGSsyFYGTFSELQSLRPD 251
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-234 |
8.31e-06 |
|
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: 48.75 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 19 GVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqQMTFTHTTEALNAGvaiiyqelhlipemT 98
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-RISFSPQTSWIMPG--------------T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 99 VAENIYLGqlphkggiVNRSLLNYEAGLQLQHLGLDID--PE---TPLK----YLSIGQWQMVEIAKALARNAKIIAFDE 169
Cdd:TIGR01271 503 IKDNIIFG--------LSYDEYRYTSVIKACQLEEDIAlfPEkdkTVLGeggiTLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 170 PTSSLSAREIDNLFR--VIRELRQEGRVIiyVSHRMEEIfALSDAITVFKDGR--YVRTFDNMQEVNHD 234
Cdd:TIGR01271 575 PFTHLDVVTEKEIFEscLCKLMSNKTRIL--VTSKLEHL-KKADKILLLHEGVcyFYGTFSELQAKRPD 640
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-213 |
8.52e-06 |
|
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: 45.81 E-value: 8.52e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 144 LSIGQWQMVEIAKALARNAK----IIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRmEEIFALSDAI 213
Cdd:cd03227 78 LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL-PELAELADKL 150
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-227 |
8.59e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPT-AGSLQIQGQQMTFTHTTEALNAgvaiiyqelhlipemTVAE 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVSWIFNA---------------TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 102 NIYLGQlphkggivnrsllNYEAG--------LQLQHlGLDIDPETPLKYL-------SIGQWQMVEIAKALARNAKIIA 166
Cdd:PLN03232 698 NILFGS-------------DFESErywraidvTALQH-DLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 167 FDEPTSSLSAREIDNLFR--VIRELRQEGRVII----YVSHRMEEIFALSDAItVFKDGRYVRTFDN 227
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDscMKDELKGKTRVLVtnqlHFLPLMDRIILVSEGM-IKEEGTFAELSKS 829
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-240 |
8.75e-06 |
|
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: 48.75 E-value: 8.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 16 TFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSgNYVPTAGSLQIQGQQMTfTHTTEALNAGVAIIYQEL---- 91
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWN-SVTLQTWRKAFGVIPQKVfifs 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 92 -----HLIPE--------MTVAENIYLG----QLPHKggivnrslLNYeaglQLQHLGLdidpetplkYLSIGQWQMVEI 154
Cdd:TIGR01271 1306 gtfrkNLDPYeqwsdeeiWKVAEEVGLKsvieQFPDK--------LDF----VLVDGGY---------VLSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 155 AKALARNAKIIAFDEPTSSLSAREidnlFRVIRE-LRQ--EGRVIIYVSHRMEEIFALSDAITVfkDGRYVRTFDNMQEV 231
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVT----LQIIRKtLKQsfSNCTVILSEHRVEALLECQQFLVI--EGSSVKQYDSIQKL 1438
|
250
....*....|.
gi 490204990 232 NHDA--LVQAM 240
Cdd:TIGR01271 1439 LNETslFKQAM 1449
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-226 |
9.25e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGQQMTfthttealNAGVAIIYQELHLIPEMTVaen 102
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA--------KIGLHDLRFKITIIPQDPV--- 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 103 IYLGQLPHK-GGIVNRSLLNYEAGLQLQHL---------GLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTS 172
Cdd:TIGR00957 1371 LFSGSLRMNlDPFSQYSDEEVWWALELAHLktfvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 173 SLSArEIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVfkDGRYVRTFD 226
Cdd:TIGR00957 1451 AVDL-ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVL--DKGEVAEFG 1501
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
261-475 |
1.20e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 47.00 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 261 LRLDRVKA--PG--VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDirkpAQAIQAGMMLc 336
Cdd:PRK11248 2 LQISHLYAdyGGkpALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE----GPGAERGVVF- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 337 pedrKAEGIIPVHSVRDNINISARrkhiLAGcvINNAWEAQNADQHIKSLNIKtpGAEQ-LIMNLSGGNQQKAILGRWLS 415
Cdd:PRK11248 77 ----QNEGLLPWRNVQDNVAFGLQ----LAG--VEKMQRLEIAHQMLKKVGLE--GAEKrYIWQLSGGQRQRVGIARALA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 416 EEMKVILLDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREG 475
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
275-504 |
1.51e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.65 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI------DIRKpaqaiQAGMMLCPEDRKAEGIipv 348
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwDIRH-----KIGMVFQNPDNQFVGA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 hSVRDNINISARRKHILAGCVINNAWEAQNAdqhIKSLNIKT--PGaeqlimNLSGGNQQKAILGRWLSEEMKVILLDEP 426
Cdd:PRK13650 98 -TVEDDVAFGLENKGIPHEEMKERVNEALEL---VGMQDFKErePA------RLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 427 TRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVlGVADRIVVMREGEIAG----ELLHEHANEQQALSLAMPKVSQ 501
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVEStstpRELFSRGNDLLQLGLDIPFTTS 246
|
...
gi 490204990 502 AVA 504
Cdd:PRK13650 247 LVQ 249
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
103-213 |
1.63e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 103 IYLGQLPHKGGIVNRSLLNYEAGLQ-LQHLGLD-IDPETPLKYLSIGQWQMVEIAKALARNAKIIAF--DEPTSSLSARE 178
Cdd:PRK00635 434 IFLSQLPSKSLSIEEVLQGLKSRLSiLIDLGLPyLTPERALATLSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQD 513
|
90 100 110
....*....|....*....|....*....|....*
gi 490204990 179 IDNLFRVIRELRQEGRVIIYVSHRmEEIFALSDAI 213
Cdd:PRK00635 514 THKLINVIKKLRDQGNTVLLVEHD-EQMISLADRI 547
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-95 |
1.81e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSG--NYVPTAGSLQIQGQQMTFTHTTEALNAGVA 85
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90
....*....|
gi 490204990 86 IIYQELHLIP 95
Cdd:PRK09580 82 MAFQYPVEIP 91
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
400-480 |
2.33e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 400 LSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASgVAVVFASSDLPEVLGVADRIVVMREGEIAG 479
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVE 242
|
.
gi 490204990 480 E 480
Cdd:PRK14271 243 E 243
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
8-201 |
2.53e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 8 LSFHGITMTFPGvKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqmtfTHTTEALNAGVAII 87
Cdd:PRK13541 2 LSLHQLQFNIEQ-KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKN-----CNINNIAKPYCTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 88 YQELHLIPEMTVAENiylgqLPHKGGIVNRSLLNYEAglqLQHLGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAF 167
Cdd:PRK13541 76 GHNLGLKLEMTVFEN-----LKFWSEIYNSAETLYAA---IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170 180 190
....*....|....*....|....*....|....
gi 490204990 168 DEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSH 201
Cdd:PRK13541 148 DEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
275-477 |
3.22e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.02 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEA-IDIRKpaqaiqaGMMLCPEDRKAeG-------II 346
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEK-------GICLPPEKRRI-GyvfqdarLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 347 PVHSVRDNINISARRKhilagcvinnawEAQNADQHIKSLNIKtPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEP 426
Cdd:PRK11144 89 PHYKVRGNLRYGMAKS------------MVAQFDKIVALLGIE-PLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490204990 427 TRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-206 |
3.43e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 22 ALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQIQGqqmtfTHTTEALNAGvaiiyqelhLIPEMTVAE 101
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----SAALIAISSG---------LNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 102 NIYLgqlphKGGIVnrsllnyeaGLQLQHLGlDIDPET------------PLKYLSIGQWQMVEIAKALARNAKIIAFDE 169
Cdd:PRK13545 105 NIEL-----KGLMM---------GLTKEKIK-EIIPEIiefadigkfiyqPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 490204990 170 PTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEI 206
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
401-472 |
4.66e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 4.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 401 SGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVM 472
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
269-493 |
5.45e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.59 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 269 PGVRQPV----SLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQaiqagmmlcpedrkaeg 344
Cdd:PRK11160 349 PDQPQPVlkglSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA----------------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 345 iipvhsVRDNINISARRKHILAGCVINN---AWEAQNADQHIKSLNikTPGAEQLIMN--------------LSGGNQQK 407
Cdd:PRK11160 412 ------LRQAISVVSQRVHLFSATLRDNlllAAPNASDEALIEVLQ--QVGLEKLLEDdkglnawlgeggrqLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 408 AILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAAsGVAVVFASSDLpevLGVA--DRIVVMREGEIAgellhEH 485
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRL---TGLEqfDRICVMDNGQII-----EQ 554
|
....*...
gi 490204990 486 ANEQQALS 493
Cdd:PRK11160 555 GTHQELLA 562
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
276-488 |
5.92e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.57 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 276 SLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQaiQAGMMLCPEDRkaegIIPVHSVRDNI 355
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENN----LFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 356 --------NISARRKHILAgcvinnaweaQNADQ-HIKSLNIKTPGAeqlimnLSGGNQQKAILGRWLSEEMKVILLDEP 426
Cdd:PRK10771 93 glglnpglKLNAAQREKLH----------AIARQmGIEDLLARLPGQ------LSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 427 TRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIA-----GELLHEHANE 488
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAwdgptDELLSGKASA 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
275-427 |
7.35e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.44 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDG---------------------EAIDIRKPAQAIQAGM 333
Cdd:COG0488 17 VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqeppldddltvldTVLDGDAELRALEAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 334 mlcpedRKAEgiipvHSVRDNINISARRKHILAGCVINNAWEAQN-ADQHIKSLNIKTPGAEQLIMNLSGGNQQKAILGR 412
Cdd:COG0488 97 ------EELE-----AKLAEPDEDLERLAELQEEFEALGGWEAEArAEEILSGLGFPEEDLDRPVSELSGGWRRRVALAR 165
|
170
....*....|....*
gi 490204990 413 WLSEEMKVILLDEPT 427
Cdd:COG0488 166 ALLSEPDLLLLDEPT 180
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-65 |
7.36e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 7.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 490204990 12 GITMTFPGVKALSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQ 65
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
399-477 |
7.49e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 44.41 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 399 NLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAA-SGVAVVFASSDLPEVLGvADRIVVMREGEI 477
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEANM-ADQVLVLDDGKL 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
275-486 |
8.85e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.93 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAgMMLCPEDRKAEGiipvHSVRDN 354
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ-VSYCAQTPTLFG----DTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 355 I-------NISARRKHILAGCvinnaweAQ-NADQHIkslniktpgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEP 426
Cdd:PRK10247 101 LifpwqirNQQPDPAIFLDDL-------ERfALPDTI---------LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 427 TRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEIAGELLHEHA 486
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEINHADKVITLQPHAGEMQEARYELA 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
275-445 |
8.89e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.00 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLfggSRI--------TAGQVYIDG--------EAIDIRKpaqaiQAGMMLcpe 338
Cdd:PRK14239 24 VSLDFYPNEITALIGPSGSGKSTLLRSI---NRMndlnpevtITGSIVYNGhniysprtDTVDLRK-----EIGMVF--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 339 drKAEGIIPVhSVRDNINISARRKHILAGCVINNAWEaqnadQHIKSLNIKTPGAEQL---IMNLSGGNQQKAILGRWLS 415
Cdd:PRK14239 93 --QQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVE-----KSLKGASIWDEVKDRLhdsALGLSGGQQQRVCIARVLA 164
|
170 180 190
....*....|....*....|....*....|
gi 490204990 416 EEMKVILLDEPTRGIDVGAKHEIYNVIYAL 445
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGL 194
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
275-501 |
1.02e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.35 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRS----ELMkGL--FGGsRITAGQVYIDGE---AIDIRKPAQAIQAGMMLCPEDrKAEGI 345
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIM-GLidYPG-RVMAEKLEFNGQdlqRISEKERRNLVGAEVAMIFQD-PMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 346 IPVHSVRDNInISARRKHiLAGcviNNAWEAQNADQHIKSLNIKTPGA--EQLIMNLSGGNQQKAILGRWLSEEMKVILL 423
Cdd:PRK11022 103 NPCYTVGFQI-MEAIKVH-QGG---NKKTRRQRAIDLLNQVGIPDPASrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 424 DEPTRGIDVGAKHEIYNVIYALA-ASGVAVVFASSDLPEVLGVADRIVVMREGEI-----AGELLHEHANE-QQALSLAM 496
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVvetgkAHDIFRAPRHPyTQALLRAL 257
|
....*
gi 490204990 497 PKVSQ 501
Cdd:PRK11022 258 PEFAQ 262
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
271-481 |
1.04e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 43.65 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDirKPAQAIQAGMmlcpEDRKAEGIIPVHS 350
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS--KLSSAAKAEL----RNQKLGFIYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNINIsarRKHILAGCVINNAWEAQNADQHIKSLniKTPGAEQLIMN----LSGGNQQKAILGRWLSEEMKVILLDEP 426
Cdd:PRK11629 98 LLPDFTA---LENVAMPLLIGKKKPAEINSRALEML--AAVGLEHRANHrpseLSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 427 TRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLpEVLGVADRIVVMREGEIAGEL 481
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELnRLQGTAFLVVTHDL-QLAKRMSRQLEMRDGRLTAEL 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
275-482 |
1.17e-04 |
|
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: 44.81 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEaiDIRKPAQAiqagmMLcpedRKAEGIIPVHSV--- 351
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ--DIRDVTQA-----SL----RAAIGIVPQDTVlfn 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 352 ---RDNI---NISARRKHILAgcvinnAWEAQNADQHIKSLniktP-GAEQLI----MNLSGGNQQKAILGRWLSEEMKV 420
Cdd:COG5265 446 dtiAYNIaygRPDASEEEVEA------AARAAQIHDFIESL----PdGYDTRVgergLKLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 421 ILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSdLPEVLGvADRIVVMREGEIA-----GELL 482
Cdd:COG5265 516 LIFDEATSALDSRTERAIQAALREVARGRTTLVIAHR-LSTIVD-ADEILVLEAGRIVergthAELL 580
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
98-213 |
1.21e-04 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 98 TVAE-NIYLGQLPHKGGIVNRslLNYEAGLQLQHLGLDIDPETplkyLSIGQWQMVEIAKALARN--AKIIAFDEPTSSL 174
Cdd:cd03270 97 TVTEiYDYLRLLFARVGIRER--LGFLVDVGLGYLTLSRSAPT----LSGGEAQRIRLATQIGSGltGVLYVLDEPSIGL 170
|
90 100 110
....*....|....*....|....*....|....*....
gi 490204990 175 SAREIDNLFRVIRELRQEGRVIIYVSHRmEEIFALSDAI 213
Cdd:cd03270 171 HPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHV 208
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-222 |
1.27e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 32 AGQVHALMGENGAGKSTLLKILSGNyvpTAGSLQIQGQQMTFTHTTEA-----LNAGVAIIYQ-ELHLiPEMTVAENIYL 105
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIASN---TDGFHIGVEGVITYDGITPEeikkhYRGDVVYNAEtDVHF-PHLTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 106 G---QLPHK--GGIVNRSLLNYEAGLQLQHLGLDIDPETP-----LKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSL- 174
Cdd:TIGR00956 162 AarcKTPQNrpDGVSREEYAKHIADVYMATYGLSHTRNTKvgndfVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLd 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490204990 175 --SAREIDNLFRVI-RELRQEGRVIIYvsHRMEEIFALSDAITVFKDGRYV 222
Cdd:TIGR00956 242 saTALEFIRALKTSaNILDTTPLVAIY--QCSQDAYELFDKVIVLYEGYQI 290
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
275-477 |
1.55e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.92 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGgsrI---TAGQVYIDGeaidirkpaqaiqagmmLCPEDRKAE--GIIPV- 348
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTG---IlvpTSGEVRVLG-----------------YVPFKRRKEfaRRIGVv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 ----------HSVRDNINISarrKHILAgcvINNAWEAQNADQHIKSLNI----KTPgaeqlIMNLSggnqqkaiLGrwl 414
Cdd:COG4586 101 fgqrsqlwwdLPAIDSFRLL---KAIYR---IPDAEYKKRLDELVELLDLgellDTP-----VRQLS--------LG--- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 415 sEEMK------------VILLDEPTRGIDVGAKHEIYNVIYAL-AASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG4586 159 -QRMRcelaaallhrpkILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
131-241 |
1.66e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 131 LGLDIDPETPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAReIDNLF-RVIRELRQEGRVIIyVSHRMEEIFAl 209
Cdd:PLN03130 1362 LGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR-TDALIqKTIREEFKSCTMLI-IAHRLNTIID- 1438
|
90 100 110
....*....|....*....|....*....|....
gi 490204990 210 SDAITVFKDGRyVRTFDNMQEV--NHDALVQAMV 241
Cdd:PLN03130 1439 CDRILVLDAGR-VVEFDTPENLlsNEGSAFSKMV 1471
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-220 |
1.81e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 4 STPYLSFHGITMTFPGVKAL-SDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSL--QIQGQQMTFT-HTTEA 79
Cdd:PLN03073 505 GPPIISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMAVFSqHHVDG 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 80 LNAGVAIIYQELHLIPemTVAEN---IYLGQLPHKGgivnrsllnyeaGLQLQhlgldidpetPLKYLSIGQWQMVEIAK 156
Cdd:PLN03073 585 LDLSSNPLLYMMRCFP--GVPEQklrAHLGSFGVTG------------NLALQ----------PMYTLSGGQKSRVAFAK 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490204990 157 ALARNAKIIAFDEPTSSLSAREIDNLFRVIrELRQEGrvIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAVEALIQGL-VLFQGG--VLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
273-477 |
1.85e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.64 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAgmmlcpedRKAEGIIPVH--- 349
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA--------RRQIGMIFQHfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 ----SVRDNINISARrkhiLAGcvinnaweaqnadqhIKSLNIKTPGAEQLIM------------NLSGGNQQKAILGRW 413
Cdd:PRK11153 94 lssrTVFDNVALPLE----LAG---------------TPKAEIKARVTELLELvglsdkadrypaQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 414 LSEEMKVILLDEPTRGIDvgakHEIYNVIYALAAS-----GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK11153 155 LASNPKVLLCDEATSALD----PATTRSILELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
275-477 |
4.22e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.05 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAI------DIRKpaqaiQAGMMLCPEDRKAEGIIPV 348
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnfeKLRK-----HIGIVFQNPDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 349 HSVR---DNINISARRKHILAGCVINNAWEAQNADQHIKSLniktpgaeqlimnlSGGNQQKAILGRWLSEEMKVILLDE 425
Cdd:PRK13648 103 YDVAfglENHAVPYDEMHRRVSEALKQVDMLERADYEPNAL--------------SGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490204990 426 PTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGvADRIVVMREGEI 477
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
24-220 |
4.95e-04 |
|
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: 41.44 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 24 SDISFDcyaGQVHALMGENGAGKSTLLKIL-------------SGNYVPT-AGSLQIQGQ-QMTFTHTTEAlnagvaiiy 88
Cdd:cd03240 16 SEIEFF---SPLTLIVGQNGAGKTTIIEALkyaltgelppnskGGAHDPKlIREGEVRAQvKLAFENANGK--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 89 qELHLIPEMTVAEN-IYLgqlpHKGGIvnRSLLnyeaglqlqhlgldidpETPLKYLSIGQWQMVEIA--KALAR----N 161
Cdd:cd03240 84 -KYTITRSLAILENvIFC----HQGES--NWPL-----------------LDMRGRCSGGEKVLASLIirLALAEtfgsN 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490204990 162 AKIIAFDEPTSSLSAREIDN-LFRVIRELR-QEGRVIIYVSHRMEEIFALSDAITVFKDGR 220
Cdd:cd03240 140 CGILALDEPTTNLDEENIEEsLAEIIEERKsQKNFQLIVITHDEELVDAADHIYRVEKDGR 200
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
273-477 |
5.42e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 42.52 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 273 QPVSLSVRSGEIVGLFGLVGAGRSELMKGLFG-----GSritagqVYIDGeaIDIRKpaqaiqagmmLCPED-RKA---- 342
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqGS------LKING--IELRE----------LDPESwRKHlswv 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 343 --EGIIPVHSVRDNI---NISARRKHILAgcVINNAWEAQNADQHIKSLNikTPGAEQLImNLSGGNQQKAILGRWLSEE 417
Cdd:PRK11174 429 gqNPQLPHGTLRDNVllgNPDASDEQLQQ--ALENAWVSEFLPLLPQGLD--TPIGDQAA-GLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 418 MKVILLDEPTRGIDVGAKHEIYNVIYAlAASGVAVVFASSDLpEVLGVADRIVVMREGEI 477
Cdd:PRK11174 504 CQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQL-EDLAQWDQIWVMQDGQI 561
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
400-476 |
6.27e-04 |
|
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: 40.12 E-value: 6.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490204990 400 LSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNviyALAASGVAVVFASSDLPEVLGVADRIVVMREGE 476
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE---ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
399-477 |
6.68e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.37 E-value: 6.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490204990 399 NLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASgVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
94-203 |
7.09e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 94 IPEMTV--AENIYLGQlPHkggIVNRslLNYEAGLQLQHLGLDidpeTPLKYLSIGQWQMVEIAKALARNAK---IIAFD 168
Cdd:PRK00635 768 ILEMTAyeAEKFFLDE-PS---IHEK--IHALCSLGLDYLPLG----RPLSSLSGGEIQRLKLAYELLAPSKkptLYVLD 837
|
90 100 110
....*....|....*....|....*....|....*
gi 490204990 169 EPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRM 203
Cdd:PRK00635 838 EPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM 872
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
399-493 |
8.64e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 399 NLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEIA 478
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRT 1437
|
90
....*....|....*
gi 490204990 479 GELLHEHANEQQALS 493
Cdd:PTZ00265 1438 GSFVQAHGTHEELLS 1452
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
271-476 |
1.05e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 41.00 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 271 VRQPVSLSVRSGEIVGLFGLVGAGRSELMkglfggsritagqvyidgeaidirkpaqaiqagMMLCPEDRKAEGIIPvHS 350
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLL---------------------------------MLILGELEPSEGKIK-HS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRdnINISARRKHILAGCVINNAWEAQNADQH-----IKSLNI-----KTPGAEQLIM-----NLSGGNQQKAILGRWLS 415
Cdd:cd03291 98 GR--ISFSSQFSWIMPGTIKENIIFGVSYDEYryksvVKACQLeeditKFPEKDNTVLgeggiTLSGGQRARISLARAVY 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490204990 416 EEMKVILLDEPTRGIDVGAKHEIY-NVIYALAASGVAVVFASSdlPEVLGVADRIVVMREGE 476
Cdd:cd03291 176 KDADLYLLDSPFGYLDVFTEKEIFeSCVCKLMANKTRILVTSK--MEHLKKADKILILHEGS 235
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
390-482 |
1.28e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 390 TPgaEQLIMNLSGGNQQKAILGRWLSEEMKVI--LLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDlPEVLGVAD 467
Cdd:PRK00635 469 TP--ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLAD 545
|
90
....*....|....*..
gi 490204990 468 RIVVM--REGEIAGELL 482
Cdd:PRK00635 546 RIIDIgpGAGIFGGEVL 562
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
275-477 |
1.30e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 40.45 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLfggSRI---TAGQVYIDGeaidiRKPAQ-AIQAGMMlcPEdrkaegiipvHS 350
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLI---AGIlepTSGRVEVNG-----RVSALlELGAGFH--PE----------LT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 351 VRDNINISARrkhilagcvINNAWEAQnadqhIKSLniktpgaEQLIMNLSGgnqqkaiLGRWLSEEMK----------- 419
Cdd:COG1134 105 GRENIYLNGR---------LLGLSRKE-----IDEK-------FDEIVEFAE-------LGDFIDQPVKtyssgmrarla 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490204990 420 ----------VILLDEptrGIDVG-----AKheIYNVIYALAASGVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG1134 157 favatavdpdILLVDE---VLAVGdaafqKK--CLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
275-477 |
1.37e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 40.83 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 275 VSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPAQAIQAgmmlcpedRKAEGIIPVH----- 349
Cdd:COG1135 24 VSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA--------RRKIGMIFQHfnlls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 350 --SVRDNINISARrkhiLAGcvinnaWEAQNADQHIKSLnIKTPG----AEQLIMNLSGGNQQK-AIlGRWLSEEMKVIL 422
Cdd:COG1135 96 srTVAENVALPLE----IAG------VPKAEIRKRVAEL-LELVGlsdkADAYPSQLSGGQKQRvGI-ARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 423 LDEPTRGIDVGAKHEIYNVIYALAAS-GVAVVFASSDLPEVLGVADRIVVMREGEI 477
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
400-484 |
1.45e-03 |
|
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: 39.61 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 400 LSGGNQQKAILGRWLSEEMK--VILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDlPEVLGVADRIVVM--REG 475
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN-LDVLSSADWIIDFgpGSG 166
|
....*....
gi 490204990 476 EIAGELLHE 484
Cdd:cd03238 167 KSGGKVVFS 175
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
379-480 |
1.69e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 379 ADQHIKSLNIkTPGAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSD 458
Cdd:NF000106 125 ADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQY 203
|
90 100
....*....|....*....|..
gi 490204990 459 LPEVLGVADRIVVMREGEIAGE 480
Cdd:NF000106 204 MEEAEQLAHELTVIDRGRVIAD 225
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
142-222 |
1.97e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 142 KYlSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEGRVIIYVSHRMEEIFALSDAITVFKDGRY 221
Cdd:NF000106 144 KY-SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
.
gi 490204990 222 V 222
Cdd:NF000106 223 I 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
282-475 |
3.27e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 40.25 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 282 GEIVGLFGLVGAGRSELMKGLFG---GSRITaGQVYIDGeaidiRKPAQAI--QAGM-----MLCPEDRKAEGIIPVHSV 351
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGriqGNNFT-GTILANN-----RKPTKQIlkRTGFvtqddILYPHLTVRETLVFCSLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 352 RDNINISARRKHILAGCVINNAWEAQNADQHIkslniktpgAEQLIMNLSGGNQQKAILGRWLSEEMKVILLDEPTRGID 431
Cdd:PLN03211 168 RLPKSLTKQEKILVAESVISELGLTKCENTII---------GNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490204990 432 VGAKHEIYNVIYALAASGVAVVfASSDLP--EVLGVADRIVVMREG 475
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIV-TSMHQPssRVYQMFDSVLVLSEG 283
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-66 |
3.91e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 3.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490204990 10 FHGITMTFpGVKAL-SDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSLQI 66
Cdd:PRK11819 327 AENLSKSF-GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
16-54 |
4.34e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.21 E-value: 4.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 490204990 16 TFPGVKALSDISFD-CYAGQVHALMGENGAGKSTLLKILS 54
Cdd:COG3950 7 TIENFRGFEDLEIDfDNPPRLTVLVGENGSGKTTLLEAIA 46
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
398-480 |
4.72e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490204990 398 MNLSGGNQQKAILGRWLSEEMKVILLDEPTRGIDVGAKHEIYNVIYALAASGVAVVFASSDLpEVLGVADRIVVMREGEI 477
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
|
...
gi 490204990 478 AGE 480
Cdd:PLN03232 818 KEE 820
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
144-219 |
5.46e-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: 38.74 E-value: 5.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490204990 144 LSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREIDNLFRVIRELRQEgRVIIYVSHRMEEIFAlSDAITVFKDG 219
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVSTILD-ADLVLVLSRG 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
274-326 |
5.93e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.18 E-value: 5.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490204990 274 PVSLSVRSGEIVGLFGLVGAGRSELMKGLFGGSRITAGQVYIDGEAIDIRKPA 326
Cdd:PRK10522 341 PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE 393
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
18-53 |
7.11e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.21 E-value: 7.11e-03
10 20 30
....*....|....*....|....*....|....*.
gi 490204990 18 PGVKALSDISFDCyagQVHALMGENGAGKSTLLKIL 53
Cdd:COG3910 25 PAVRNLEGLEFHP---PVTFFVGENGSGKSTLLEAI 57
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-64 |
9.17e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.61 E-value: 9.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490204990 23 LSDISFDCYAGQVHALMGENGAGKSTLLKILSGNYVPTAGSL 64
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| |
