|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-496 |
4.54e-74 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 242.66 E-value: 4.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 6 ITHLTFGFDKQVelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFP--LRPVYFPATISEQDQLTY 82
Cdd:COG0488 1 LENLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELePDSGEVSIPkgLRIGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 83 YALLEVADFELWELEREMNLIQLDP------------------------------QVLW----------QPYQTLSGGEQ 122
Cdd:COG0488 79 LDTVLDGDAELRALEAELEELEAKLaepdedlerlaelqeefealggweaearaeEILSglgfpeedldRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 123 TKVLLA-LLFTQenffP---LIDEPTNHLDLQGRQHVANYFQHKDG-FIVVSHDRQFLNQVTDHTLAIEKSQLVLYQGNF 197
Cdd:COG0488 159 RRVALArALLSE----PdllLLDEPTNHLDLESIEWLEEFLKNYPGtVLVVSHDRYFLDRVATRILELDRGKLTLYPGNY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 198 ATYEEQKELRDEFELAQNRKIKKEVSRLKrtaaekaEWSRsRETEKygkpsekgsggifdtgfigaraARTMKRSKTIeQ 277
Cdd:COG0488 235 SAYLEQRAERLEQEAAAYAKQQKKIAKEE-------EFIR-RFRAK----------------------ARKAKQAQSR-I 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 278 RMYDQIEVKEglLKDLEDVDRLTMSYHPSRHTQLLKMENLSLHYTEQEaLFAPLSFEVQRGTIVALTGPNGIGKSSVLHY 357
Cdd:COG0488 284 KALEKLEREE--PPRRDKTVEIRFPPPERLGKKVLELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 358 LLGTFAGQAnGELLR-PNVKISYVRQNYENNRG------TLQDFAE-ANQLDYSAFLnnlRKLGMERNVFQNQIEEMSMG 429
Cdd:COG0488 361 LAGELEPDS-GTVKLgETVKIGYFDQHQEELDPdktvldELRDGAPgGTEQEVRGYL---GRFLFSGDDAFKPVGVLSGG 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 430 QRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQTFLKNIGAQQIALK 496
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFE 503
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-187 |
1.44e-44 |
|
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: 153.37 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFP--LRPVYFPatiseqdql 80
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELePDEGIVTWGstVKIGYFE--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 81 tyyallevadfelweleremnliqldpqvlwqpyQtLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQ 160
Cdd:cd03221 70 ----------------------------------Q-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180
....*....|....*....|....*...
gi 2255859273 161 HKDG-FIVVSHDRQFLNQVTDHTLAIEK 187
Cdd:cd03221 115 EYPGtVILVSHDRYFLDQVATKIIELED 142
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-488 |
1.55e-38 |
|
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: 147.77 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 20 LFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEI------------QFP-LRP------------------ 67
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKDFNGEArpqpgikvgylpQEPqLDPtktvrenveegvaeikda 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 68 ------VY---------FPATISEQDQLTyyALLEVADfeLWELERE----MNLIQLDPqvlW-QPYQTLSGGEQTKVLL 127
Cdd:TIGR03719 100 ldrfneISakyaepdadFDKLAAEQAELQ--EIIDAAD--AWDLDSQleiaMDALRCPP---WdADVTKLSGGERRRVAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 128 ALLFTQENFFPLIDEPTNHLDLQG----RQHVANYfqhKDGFIVVSHDRQFLNQVTDHTLAIEKSQLVLYQGNFATYEEQ 203
Cdd:TIGR03719 173 CRLLLSKPDMLLLDEPTNHLDAESvawlERHLQEY---PGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 204 KELRdefeLAQNRkiKKEVSRLKRTAAEkAEWSRSRETEKYGKPSekgsggifdtgfigARAAR--TMKRSKTIEQRMYD 281
Cdd:TIGR03719 250 KQKR----LEQEE--KEESARQKTLKRE-LEWVRQSPKGRQAKSK--------------ARLARyeELLSQEFQKRNETA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 282 QIEVKEGllkdledvDRLTmsyhpsrhTQLLKMENLSLHYTEqEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLlgt 361
Cdd:TIGR03719 309 EIYIPPG--------PRLG--------DKVIEAENLTKAFGD-KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMI--- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 362 fAGQA---NGEL-LRPNVKISYVRQNYEN---NRGTLQDFAEAN--------QLDYSAFLNNLRKLGMERnvfQNQIEEM 426
Cdd:TIGR03719 369 -TGQEqpdSGTIeIGETVKLAYVDQSRDAldpNKTVWEEISGGLdiiklgkrEIPSRAYVGRFNFKGSDQ---QKKVGQL 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 427 SMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQTFLKNI 488
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRI 506
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-203 |
1.56e-36 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 141.36 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIQFP--LRPVYFPatiSEQDQL 80
Cdd:COG0488 316 LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpDSGTVKLGetVKIGYFD---QHQEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 81 ----TyyaLLEvadfELWEL---EREMNLIQL------DPQVLWQPYQTLSGGEQTKVLLALLFTQE-NFfpLI-DEPTN 145
Cdd:COG0488 391 dpdkT---VLD----ELRDGapgGTEQEVRGYlgrflfSGDDAFKPVGVLSGGEKARLALAKLLLSPpNV--LLlDEPTN 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2255859273 146 HLDLQGRQHVANYFQHKDG-FIVVSHDRQFLNQVTDHTLAIEKSQLVLYQGNFATYEEQ 203
Cdd:COG0488 462 HLDIETLEALEEALDDFPGtVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-485 |
2.61e-33 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 132.93 E-value: 2.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 10 TFGFDKQVellFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQF-------------PLRP-------- 67
Cdd:PRK11819 15 VVPPKKQI---LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvDKEFEGEARPapgikvgylpqepQLDPektvrenv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 68 -------------------------VYFPATISEQDQLTyyALLEVADfeLWELERE----MNLIQLDPqvlW-QPYQTL 117
Cdd:PRK11819 92 eegvaevkaaldrfneiyaayaepdADFDALAAEQGELQ--EIIDAAD--AWDLDSQleiaMDALRCPP---WdAKVTKL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 118 SGGEQTKVLLALLFTQENFFPLIDEPTNHLD------LQgrQHVANYfqhKDGFIVVSHDRQFLNQVTDHTLAIEKSQLV 191
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDaesvawLE--QFLHDY---PGTVVAVTHDRYFLDNVAGWILELDRGRGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 192 LYQGNFATYEEQKELRdefeLAQNRkiKKEVSRLKRTAAEkAEWSRSretekygkpSEKgsggifdtgfigARAARTMKR 271
Cdd:PRK11819 240 PWEGNYSSWLEQKAKR----LAQEE--KQEAARQKALKRE-LEWVRQ---------SPK------------ARQAKSKAR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 272 SKTIEQrMYDQIEVKEglLKDLEDV----DRLTmsyhpsrhTQLLKMENLSLHYTEQeALFAPLSFEVQRGTIVALTGPN 347
Cdd:PRK11819 292 LARYEE-LLSEEYQKR--NETNEIFippgPRLG--------DKVIEAENLSKSFGDR-LLIDDLSFSLPPGGIVGIIGPN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 348 GIGKSSvlhyLLGTFAGQA---NGEL-LRPNVKISYVRQnyenNRGTLQD----FAE-ANQLDY--------------SA 404
Cdd:PRK11819 360 GAGKST----LFKMITGQEqpdSGTIkIGETVKLAYVDQ----SRDALDPnktvWEEiSGGLDIikvgnreipsrayvGR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 405 FlnNLRklGMERnvfQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQTF 484
Cdd:PRK11819 432 F--NFK--GGDQ---QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWF 504
|
.
gi 2255859273 485 L 485
Cdd:PRK11819 505 L 505
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
312-497 |
2.95e-33 |
|
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: 122.94 E-value: 2.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEaLFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAgQANGELLR-PNVKISYVRQnyennrgt 390
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE-PDEGIVTWgSTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 391 lqdfaeanqldysaflnnlrklgmernvfqnqieeMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQ 470
Cdd:cd03221 71 -----------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE 115
|
170 180
....*....|....*....|....*..
gi 2255859273 471 KQPTMLIVEHDQTFLKNIGAQQIALKK 497
Cdd:cd03221 116 YPGTVILVSHDRYFLDQVATKIIELED 142
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-487 |
1.83e-30 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 125.06 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 1 MSTIKIT--HLTFGFDKqvelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLL-------GKYAYQGEI------QFPL 65
Cdd:PRK11147 1 MSLISIHgaWLSFSDAP----LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevllddGRIIYEQDLivarlqQDPP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 66 RPV------YFPATISEQDQL--TYYALL-----EVADFELWELEREMNliQLDPQVLWQ------------------PY 114
Cdd:PRK11147 77 RNVegtvydFVAEGIEEQAEYlkRYHDIShlvetDPSEKNLNELAKLQE--QLDHHNLWQlenrinevlaqlgldpdaAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 115 QTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQHKDGFIV-VSHDRQFLNQVTDHTLAIEKSQLVLY 193
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIfISHDRSFIRNMATRIVDLDRGKLVSY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 194 QGNFATYEEQKE--LRDEFElaQNRKIKKEVsrlkrtaAEKAEWSR----SRETEKYGKpsekgsggifdtgfigARAAR 267
Cdd:PRK11147 235 PGNYDQYLLEKEeaLRVEEL--QNAEFDRKL-------AQEEVWIRqgikARRTRNEGR----------------VRALK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 268 TMKrsktiEQRMyDQIEVKEGLLKDLEDVDRltmsyhpsRHTQLLKMENLSLHYtEQEALFAPLSFEVQRGTIVALTGPN 347
Cdd:PRK11147 290 ALR-----RERS-ERREVMGTAKMQVEEASR--------SGKIVFEMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPN 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 348 GIGKSSVLHYLLGTFagQANGELLRPNVK--ISYVRQNYEN---NRGTLQDFAEANQldySAFLNnlrklGMERNVF--- 419
Cdd:PRK11147 355 GCGKTTLLKLMLGQL--QADSGRIHCGTKleVAYFDQHRAEldpEKTVMDNLAEGKQ---EVMVN-----GRPRHVLgyl 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859273 420 ----------QNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQTFLKN 487
Cdd:PRK11147 425 qdflfhpkraMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDN 502
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
311-481 |
1.62e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.26 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALFaPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQangELLRPNVKISYVR 381
Cdd:COG1121 6 AIELENLTVSYGGRPVLE-DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGllpptsgtvRLFGK---PPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 382 QNYENNRG---TLQDFAEA------------NQLDYSAFLNNLRKLGMERnvFQN-QIEEMSMGQRKKVELAKSLAQEAE 445
Cdd:COG1121 82 QRAEVDWDfpiTVRDVVLMgrygrrglfrrpSRADREAVDEALERVGLED--LADrPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2255859273 446 LYIWDEPLNYLDVFNQKQLEDLL--LQKQP-TMLIVEHD 481
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLreLRREGkTILVVTHD 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
313-481 |
7.97e-27 |
|
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: 107.62 E-value: 7.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 313 KMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQangELLRPNVKISYVRQN 383
Cdd:cd03235 1 EVEDLTVSYGGHPVLED-VSFEVKPGEFLAIVGPNGAGKSTLLKAILGllkptsgsiRVFGK---PLEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 384 YENNR---------------GTLQDFAEANQLDYSAFLNNLRKLGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAELYI 448
Cdd:cd03235 77 RSIDRdfpisvrdvvlmglyGHKGLFRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 2255859273 449 WDEPLNYLDVFNQKQLEDLLLQKQP---TMLIVEHD 481
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHD 191
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
313-497 |
2.80e-25 |
|
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: 101.55 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 313 KMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELLRPNVKISYVRqnyennrgtlq 392
Cdd:cd00267 1 EIENLSFRYGGRTAL-DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG-LLKPTSGEILIDGKDIAKLP----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 393 dfaeanqldysaFLNNLRKLGMernVFQnqieeMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDL---LL 469
Cdd:cd00267 68 ------------LEELRRRIGY---VPQ-----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELlreLA 127
|
170 180
....*....|....*....|....*...
gi 2255859273 470 QKQPTMLIVEHDQTFLKNIGAQQIALKK 497
Cdd:cd00267 128 EEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-486 |
3.58e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 106.02 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 17 VELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLlgkyayQGEIQFPLRPVYFPATIS------EQDQLTYYALLEV-- 88
Cdd:PRK10636 13 VRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL------KNEISADGGSYTFPGNWQlawvnqETPALPQPALEYVid 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 89 ADFELWELEREMNLI--------------QLDPQVLW---------------------QPYQTLSGGEQTKVLLALLFTQ 133
Cdd:PRK10636 87 GDREYRQLEAQLHDAnerndghaiatihgKLDAIDAWtirsraasllhglgfsneqleRPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 134 ENFFPLIDEPTNHLDLQGRQHVANYFQHKDG-FIVVSHDRQFLNQVTDHTLAIEKSQLVLYQGNFATYEEQKELRdefeL 212
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGtLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATR----L 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 213 AQNRKI----KKEVSRLK------RTAAEKAEWSRSRetekygkpsekgsggifdtgfigaraARTMKRSKTIEQRMYDq 282
Cdd:PRK10636 243 AQQQAMyesqQERVAHLQsyidrfRAKATKAKQAQSR--------------------------IKMLERMELIAPAHVD- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 283 ievkegllkdleDVDRLTMSYHPSRHTQLLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF 362
Cdd:PRK10636 296 ------------NPFHFSFRAPESLPNPLLKMEKVSAGYGDRIIL-DSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGEL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 363 AGQANGELLRPNVKISYVRQN----YENNRGTLQDFAE-ANQLDYSAFLNNLRKLGMERNVFQNQIEEMSMGQRKKVELA 437
Cdd:PRK10636 363 APVSGEIGLAKGIKLGYFAQHqlefLRADESPLQHLARlAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLA 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2255859273 438 KSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQTFLK 486
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLR 491
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
313-481 |
1.06e-22 |
|
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: 95.19 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 313 KMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQANGELLRPNV--KISYVR 381
Cdd:cd03214 1 EVENLSVGYGGRTVL-DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGllkpssgeiLLDGKDLASLSPKELarKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 382 QNyennrgtlqdfaeanqldysaflnnLRKLGMERNVFQNqIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQ 461
Cdd:cd03214 80 QA-------------------------LELLGLAHLADRP-FNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180
....*....|....*....|....
gi 2255859273 462 KQLEDLL----LQKQPTMLIVEHD 481
Cdd:cd03214 134 IELLELLrrlaRERGKTVVMVLHD 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-189 |
2.00e-21 |
|
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: 90.77 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 5 KITHLTFGFDKQVelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFPLRPvyfpatiseqdqltyy 83
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLkPTSGEILIDGKD---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 84 alleVADFELWELEREmnlIQLDPQvlwqpyqtLSGGEQTKVLLALLFTQEnffP---LIDEPTNHLDLQGRQHVANYFQ 160
Cdd:cd00267 63 ----IAKLPLEELRRR---IGYVPQ--------LSGGQRQRVALARALLLN---PdllLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|...
gi 2255859273 161 --HKDG--FIVVSHDRQFLNQVTDHTLAIEKSQ 189
Cdd:cd00267 125 elAEEGrtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-481 |
2.29e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 97.19 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 34 LGLVGRNGRGKTTLLQLL-------LGKYA------------------------YQGEIQFPLRPVY-------FPATIS 75
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILsgelipnLGDYEeepswdevlkrfrgtelqnyfkklYNGEIKVVHKPQYvdlipkvFKGKVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 76 EqdqltyyaLLEVADfELWELEREMNLIQLDPqVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHV 155
Cdd:PRK13409 182 E--------LLKKVD-ERGKLDEVVERLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 156 ANYFQH---KDGFIVVSHDRQFLNQVTD--HTLaieksqlvlyqgnfatyeeqkelrdefelaqnrkikkevsrlkrtaa 230
Cdd:PRK13409 252 ARLIRElaeGKYVLVVEHDLAVLDYLADnvHIA----------------------------------------------- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 231 ekaewsrsretekYGKPsekGSGGIFdTGFIGARAArtmkrsktIEQRMydqievkEGLLKDlEDV----DRLTMSYHPS 306
Cdd:PRK13409 285 -------------YGEP---GAYGVV-SKPKGVRVG--------INEYL-------KGYLPE-ENMrirpEPIEFEERPP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 307 RHTQ----LLKMENLSLHYTEqealFaplSFEVQRGTI-----VALTGPNGIGKSsvlhyllgTFAGQANGEL------L 371
Cdd:PRK13409 332 RDESeretLVEYPDLTKKLGD----F---SLEVEGGEIyegevIGIVGPNGIGKT--------TFAKLLAGVLkpdegeV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 372 RPNVKISY----VRQNYEnnrGTLQDFAEANQLDY-SAFLNN--LRKLGMERnVFQNQIEEMSMGQRKKVELAKSLAQEA 444
Cdd:PRK13409 397 DPELKISYkpqyIKPDYD---GTVEDLLRSITDDLgSSYYKSeiIKPLQLER-LLDKNVKDLSGGELQRVAIAACLSRDA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2255859273 445 ELYIWDEPLNYLDVfNQ-----KQLEDLLLQKQPTMLIVEHD 481
Cdd:PRK13409 473 DLYLLDEPSAHLDV-EQrlavaKAIRRIAEEREATALVVDHD 513
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
311-481 |
3.78e-21 |
|
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: 92.80 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTFAGqangeLLRP---NV------------ 375
Cdd:COG1120 1 MLEAENLSVGYGGRPVL-DDVSLSLPPGEVTALLGPNGSGKST----LLRALAG-----LLKPssgEVlldgrdlaslsr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 376 -----KISYVRQNYENN----------------RGTLQDFAEAnqlDYSAFLNNLRKLGMERnvFQNQ-IEEMSMGQRKK 433
Cdd:COG1120 71 relarRIAYVPQEPPAPfgltvrelvalgryphLGLFGRPSAE---DREAVEEALERTGLEH--LADRpVDELSGGERQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 434 VELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL----LQKQPTMLIVEHD 481
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLrrlaRERGRTVVMVLHD 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-210 |
1.44e-20 |
|
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: 90.69 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGK-YAYQGEIQFPLRPV-------------- 68
Cdd:COG4555 2 IEVENLSKKYGKVPAL--KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlKPDSGSILIDGEDVrkeprearrqigvl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 69 ----YFPATISEQDQLTYYALL-----EVADFELWELEREMNLiqldPQVLWQPYQTLSGGEQTKVLLALLFTQENFFPL 139
Cdd:COG4555 80 pderGLYDRLTVRENIRYFAELyglfdEELKKRIEELIELLGL----EEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 140 IDEPTNHLDLQGRQHVANYFQH--KDGFIVV--SHDRQFLNQVTDHTLAIEKSQLVLYQGNFATYEE--QKELRDEF 210
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAlkKEGKTVLfsSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEigEENLEDAF 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
311-470 |
1.99e-20 |
|
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: 90.30 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF---AGQA--NGELLRPNV-----KISYV 380
Cdd:COG4555 1 MIEVENLSKKYGKVPAL-KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLkpdSGSIliDGEDVRKEPrearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 381 RQN---YENN--RGTLQDFAEANQLDYSAFLNN----LRKLGMERnvFQNQ-IEEMSMGQRKKVELAKSLAQEAELYIWD 450
Cdd:COG4555 80 PDErglYDRLtvRENIRYFAELYGLFDEELKKRieelIELLGLEE--FLDRrVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180
....*....|....*....|
gi 2255859273 451 EPLNYLDVFNQKQLEDLLLQ 470
Cdd:COG4555 158 EPTNGLDVMARRLLREILRA 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-481 |
2.81e-20 |
|
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: 93.81 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 1 MST-IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG----KYAYQGEIQFPLRPVY------ 69
Cdd:COG1123 1 MTPlLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllphGGRISGEVLLDGRDLLelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 70 ----------------FPATISEQDQLTYYALL---EVADFELWELEREMNLiqldPQVLWQPYQTLSGGEQTKVLLALL 130
Cdd:COG1123 81 rgrrigmvfqdpmtqlNPVTVGDQIAEALENLGlsrAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 131 FTQENFFPLIDEPTNHLDLQGRQHVANYF-----QHKDGFIVVSHDRQFLNQVTDHTLaieksqlVLYQGnfatyeEQKE 205
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLrelqrERGTTVLLITHDLGVVAEIADRVV-------VMDDG------RIVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 206 LRDEFELAQNRKIKKEVSRLKRTAAEKAEWSRSRETekygkpsekgsggifdtgfigaraartmkrsktieqrmydqiev 285
Cdd:COG1123 224 DGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEP-------------------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 286 kegllkdledvdrltmsyhpsrhtqLLKMENLSLHYT-----EQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG 360
Cdd:COG1123 260 -------------------------LLEVRNLSKRYPvrgkgGVRAV-DDVSLTLRRGETLGLVGESGSGKSTLARLLLG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 361 ---------TFAGQANGELLRPNVK-----ISYVRQNYE---NNRGTLQD-FAEAnqLDYSAFLNN----------LRKL 412
Cdd:COG1123 314 llrptsgsiLFDGKDLTKLSRRSLRelrrrVQMVFQDPYsslNPRMTVGDiIAEP--LRLHGLLSRaerrervaelLERV 391
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 413 GMERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQP--TMLIVEHD 481
Cdd:COG1123 392 GLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLrdLQRELglTYLFISHD 464
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-485 |
4.87e-20 |
|
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: 93.31 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 34 LGLVGRNGRGKTTLLQLL-------LGKYA------------------------YQGEIQFPLRPVY-------FPATIS 75
Cdd:COG1245 102 TGILGPNGIGKSTALKILsgelkpnLGDYDeepswdevlkrfrgtelqdyfkklANGEIKVAHKPQYvdlipkvFKGTVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 76 EqdqltyyaLLEVADfE---LWELEREMNLiqldPQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGR 152
Cdd:COG1245 182 E--------LLEKVD-ErgkLDELAEKLGL----ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 153 QHVANYFQH--KDG--FIVVSHDRQFLNQVTDHtlaIEksqlVLYqGNFATY----------------------EEQKEL 206
Cdd:COG1245 249 LNVARLIRElaEEGkyVLVVEHDLAILDYLADY---VH----ILY-GEPGVYgvvskpksvrvginqyldgylpEENVRI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 207 RDEfelaqnrKIKKEVSRLKRTA--AEKAEWSRSreTEKYGkpsekgsggifdtGFigaraartmkrsktieqrmydQIE 284
Cdd:COG1245 321 RDE-------PIEFEVHAPRREKeeETLVEYPDL--TKSYG-------------GF---------------------SLE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 285 VKEGllkdledvdrltmsyhpsrhtqllkmenlslhyteqealfaplsfEVQRGTIVALTGPNGIGKSsvlhyllgTFAG 364
Cdd:COG1245 358 VEGG---------------------------------------------EIREGEVLGIVGPNGIGKT--------TFAK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 365 QANGEL------LRPNVKISY----VRQNYEnnrGTLQDF-AEANQLDY-SAFLNN--LRKLGMERnVFQNQIEEMSMGQ 430
Cdd:COG1245 385 ILAGVLkpdegeVDEDLKISYkpqyISPDYD---GTVEEFlRSANTDDFgSSYYKTeiIKPLGLEK-LLDKNVKDLSGGE 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 431 RKKVELAKSLAQEAELYIWDEPLNYLDVfNQ-----KQLEDLLLQKQPTMLIVEHDQTFL 485
Cdd:COG1245 461 LQRVAIAACLSRDADLYLLDEPSAHLDV-EQrlavaKAIRRFAENRGKTAMVVDHDIYLI 519
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-193 |
6.32e-20 |
|
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: 87.11 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 5 KITHLTFGFDKQVelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFPLRPVyfpATISEQDQLTYY 83
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEILLDGKDL---ASLSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 84 ALLEVAdfelweLEReMNLIQLDPqvlwQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQ--- 160
Cdd:cd03214 76 AYVPQA------LEL-LGLAHLAD----RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRrla 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 2255859273 161 HKDGF--IVVSHDrqfLNQV---TDHTLAIEKSQLVLY 193
Cdd:cd03214 145 RERGKtvVMVLHD---LNLAaryADRVILLKDGRIVAQ 179
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
313-497 |
6.68e-20 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 87.91 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 313 KMENLSLHY-TEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHyLLGTFAGQANGELLRPNV------------KISY 379
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLR-LLNGLLGPTSGEVLVDGKdltklslkelrrKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 380 VRQNYEN----------------NRGTLQDfaEANQLDYSAflnnLRKLGMERnvFQNQ-IEEMSMGQRKKVELAKSLAQ 442
Cdd:cd03225 80 VFQNPDDqffgptveeevafgleNLGLPEE--EIEERVEEA----LELVGLEG--LRDRsPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859273 443 EAELYIWDEPLNYLDVFNQKQLEDLL--LQKQP-TMLIVEHDQTFLKNIGAQQIALKK 497
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLkkLKAEGkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
115-482 |
9.82e-20 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 92.62 E-value: 9.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 115 QTLSGGEQTKVLLA-LLFTQENFFpLIDEPTNHLDLQGRQHVANYF-QHKDGFIVVSHDRQFLNQVTDHTLAIEKSQLVL 192
Cdd:PLN03073 343 KTFSGGWRMRIALArALFIEPDLL-LLDEPTNHLDLHAVLWLETYLlKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 193 YQGNFATYEEQKElrdefelaqnrkikkEVSRLKRTAAEKAEWSRSRETEKYGKPSekgsggifdtgFIGARAARTMKRS 272
Cdd:PLN03073 422 YKGDYDTFERTRE---------------EQLKNQQKAFESNERSRSHMQAFIDKFR-----------YNAKRASLVQSRI 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 273 KTIEQRMY-DQIevkegllkdLEDVDRLTMSYHPSRHTQ--LLKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGI 349
Cdd:PLN03073 476 KALDRLGHvDAV---------VNDPDYKFEFPTPDDRPGppIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGI 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 350 GKSSVLHYLLGTFAGQANGELLRPNVKISYVRQNYENNrgtlQDFAeANQLDYSA----------FLNNLRKLGMERNVF 419
Cdd:PLN03073 547 GKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDG----LDLS-SNPLLYMMrcfpgvpeqkLRAHLGSFGVTGNLA 621
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 420 QNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQ 482
Cdd:PLN03073 622 LQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDE 684
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
312-481 |
1.09e-19 |
|
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: 86.30 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFaPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtfagqangeLLRP---NVKI---SYVRQNYE 385
Cdd:cd03230 1 IEVRNLSKRYGKKTALD-DISLTVEKGEIYGLLGPNGAGKTTLIKIILG---------LLKPdsgEIKVlgkDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 386 NNR--GTLqdfaeanqLDYSAFLNNLRklGMErNVfqnqieEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQ 463
Cdd:cd03230 71 VKRriGYL--------PEEPSLYENLT--VRE-NL------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180
....*....|....*....|.
gi 2255859273 464 LEDLLL---QKQPTMLIVEHD 481
Cdd:cd03230 134 FWELLRelkKEGKTILLSSHI 154
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-200 |
1.74e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 91.11 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 6 ITHLTFGFDKQVelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAY-QGEIQFplrpvyfpatiSEQDQLTYYA 84
Cdd:PRK15064 322 VENLTKGFDNGP--LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPdSGTVKW-----------SENANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 85 LLEVADFElweleREMNLIQL---------DPQVLW--------------QPYQTLSGGEQTKVLLALLFTQENFFPLID 141
Cdd:PRK15064 389 QDHAYDFE-----NDLTLFDWmsqwrqegdDEQAVRgtlgrllfsqddikKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 142 EPTNHLDLQGRQHVANYFQHKDG-FIVVSHDRQFLNQVTDHTLAIEKSQLVLYQGNFATY 200
Cdd:PRK15064 464 EPTNHMDMESIESLNMALEKYEGtLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
312-489 |
6.16e-19 |
|
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: 84.16 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQ----ANGELLRPNVKIS 378
Cdd:cd03229 1 LELKNVSKRYGQKTVLND-VSLNIEAGEIVALLGPSGSGKSTLLRCIAGleepdsgsiLIDGEdltdLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQNYennrgtlqdfaeanqldysAFLNNLrklgmerNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDV 458
Cdd:cd03229 80 MVFQDF-------------------ALFPHL-------TVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190
....*....|....*....|....*....|....*
gi 2255859273 459 FNQKQLEDLL--LQKQP--TMLIVEHDQTFLKNIG 489
Cdd:cd03229 134 ITRREVRALLksLQAQLgiTVVLVTHDLDEAARLA 168
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-496 |
6.47e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 89.57 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 1 MSTIKIThLTFGfdkqVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIQfpLRPVYFPATISeQDQ 79
Cdd:PRK15064 2 LSTANIT-MQFG----AKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEpSAGNVS--LDPNERLGKLR-QDQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 80 LTY--YALLEV---ADFELWELEREMNLIQLDPQV-------------------------------------LWQPYQTL 117
Cdd:PRK15064 74 FAFeeFTVLDTvimGHTELWEVKQERDRIYALPEMseedgmkvadlevkfaemdgytaearagelllgvgipEEQHYGLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 118 SG---GEQTKVLLA-LLFTQENFFpLIDEPTNHLDL---QGRQHVANyfQHKDGFIVVSHDRQFLNQVTDHTLAIEKSQL 190
Cdd:PRK15064 154 SEvapGWKLRVLLAqALFSNPDIL-LLDEPTNNLDIntiRWLEDVLN--ERNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 191 VLYQGNFATYEEQKELRDEFELAQNRKIKKEVSRLK----RTAAEKAE----WSRSRETEKYG----KPSekgsggifdt 258
Cdd:PRK15064 231 RVYPGNYDEYMTAATQARERLLADNAKKKAQIAELQsfvsRFSANASKakqaTSRAKQIDKIKleevKPS---------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 259 gfigaraartmkrsktieQRMYDQIEVKEGllKDLedvdrltmsyhpsrHTQLLKMENLSLHYtEQEALFAPLSFEVQRG 338
Cdd:PRK15064 301 ------------------SRQNPFIRFEQD--KKL--------------HRNALEVENLTKGF-DNGPLFKNLNLLLEAG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 339 TIVALTGPNGIGKSSVLHYLLGTFAGQANGELLRPNVKISYVRQNYEnnrgtlQDFAEanqlDYSAF--LNNLRKLG--- 413
Cdd:PRK15064 346 ERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHA------YDFEN----DLTLFdwMSQWRQEGdde 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 414 ------MERNVF-QNQIEE----MSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQ 482
Cdd:PRK15064 416 qavrgtLGRLLFsQDDIKKsvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDR 495
|
570
....*....|....
gi 2255859273 483 TFLKNIGAQQIALK 496
Cdd:PRK15064 496 EFVSSLATRIIEIT 509
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-191 |
1.12e-18 |
|
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: 89.05 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 3 TIKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQ-GEIQF---PLRPvYFPATISEQ- 77
Cdd:COG4987 333 SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsGSITLggvDLRD-LDEDDLRRRi 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 78 ---DQLTY-----------YALLEVADFELWE-LERemnlIQLDPQVLWQPY----------QTLSGGEQTKVLLALLFT 132
Cdd:COG4987 412 avvPQRPHlfdttlrenlrLARPDATDEELWAaLER----VGLGDWLAALPDgldtwlgeggRRLSGGERRRLALARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 133 QEnfFPLI--DEPTNHLDLQGRQHV-ANYFQHKDG--FIVVSHDRQFLNQVtDHTLAIEKSQLV 191
Cdd:COG4987 488 RD--APILllDEPTEGLDAATEQALlADLLEALAGrtVLLITHRLAGLERM-DRILVLEDGRIV 548
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
311-495 |
1.12e-18 |
|
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: 84.45 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEqEALFAPLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTFAGQAN---GELLRPNVKISYVRQNY--- 384
Cdd:COG4133 2 MLEAENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTT----LLRILAGLLPpsaGEVLWNGEPIRDAREDYrrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 385 -----------------EN------NRGTLQDFAEANQLdysaflnnLRKLGMERnvFQNQ-IEEMSMGQRKKVELAKSL 440
Cdd:COG4133 77 laylghadglkpeltvrENlrfwaaLYGLRADREAIDEA--------LEAVGLAG--LADLpVRQLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859273 441 AQEAELYIWDEPLNYLDVFNQKQLEDLL---LQKQPTMLIVEHDQTFLKniGAQQIAL 495
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIaahLARGGAVLLTTHQPLELA--AARVLDL 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
311-495 |
1.23e-18 |
|
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: 84.86 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQ----EALFaPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQ----ANGELLRP 373
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALD-DVSFSIKKGETLGLVGESGSGKSTLARAILGllkptsgsiIFDGKdllkLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 374 NVK-ISYVRQNYE---NNRGTLQD-FAEA----NQLDYSAF-----LNNLRKLGMERNVFQNQIEEMSMGQRKKVELAKS 439
Cdd:cd03257 80 RRKeIQMVFQDPMsslNPRMTIGEqIAEPlrihGKLSKKEArkeavLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 440 LAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQP--TMLIVEHDQTFLKNIgAQQIAL 495
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLkkLQEELglTLLFITHDLGVVAKI-ADRVAV 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
330-454 |
2.24e-18 |
|
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: 81.93 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 330 PLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQA--NGELLRPNVKISYVRQN---------YENNRG 389
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGllsptegtiLLDGQDltDDERKSLRKEIGYVFQDpqlfprltvRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859273 390 TLQDFAEANQLDYSAFLNNLRKLGME---RNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLN 454
Cdd:pfam00005 83 GLLLKGLSKREKDARAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-186 |
7.13e-18 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 82.14 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKqvELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFPLRPV------YF------ 70
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLpPSAGEVLWNGEPIrdaredYRrrlayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 71 ---PATISEQ---DQLTYYALL---EVADFELWELEREMNLIQLdpqvLWQPYQTLSGGEQTKVLLALLFTQEnfFPLI- 140
Cdd:COG4133 81 ghaDGLKPELtvrENLRFWAALyglRADREAIDEALEAVGLAGL----ADLPVRQLSAGQKRRVALARLLLSP--APLWl 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 141 -DEPTNHLDLQGRQHVANYF-QHKDG---FIVVSHDRQFLNqvTDHTLAIE 186
Cdd:COG4133 155 lDEPFTALDAAGVALLAELIaAHLARggaVLLTTHQPLELA--AARVLDLG 203
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
334-481 |
3.65e-17 |
|
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: 80.92 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 334 EVQRGTIVALTGPNGIGKSSVLHYLLGTFAgQANGELLRPNVKISYVRQNYE-NNRGTLQDF---AEANQLDYSAFLNNL 409
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLK-PDEGDIEIELDTVSYKPQYIKaDYEGTVRDLlssITKDFYTHPYFKTEI 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 410 RK-LGMERnVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQ----KQLEDLLLQKQPTMLIVEHD 481
Cdd:cd03237 100 AKpLQIEQ-ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFAENNEKTAFVVEHD 175
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
312-481 |
1.00e-16 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 79.30 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQA-----NGELLRPNV------KISYV 380
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSgevlvDGKDITKKNlrelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 381 RQNYEN----------------NRGtlQDFAEANQLDYSAflnnLRKLGME----RNVFqnqieEMSMGQRKKVELAKSL 440
Cdd:COG1122 81 FQNPDDqlfaptveedvafgpeNLG--LPREEIRERVEEA----LELVGLEhladRPPH-----ELSGGQKQRVAIAGVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2255859273 441 AQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQP-TMLIVEHD 481
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLkrLNKEGkTVIIVTHD 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-219 |
1.44e-16 |
|
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: 82.29 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKqvELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGK-YAYQGEIqfplrpvyfpaTISEQDQLTY 82
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeQPDSGTI-----------EIGETVKLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 83 Y-----AL-------LEVAD-FELWEL-EREM---------NLIQLDPQvlwQPYQTLSGGEQTKVLLALLFTQENFFPL 139
Cdd:TIGR03719 390 VdqsrdALdpnktvwEEISGgLDIIKLgKREIpsrayvgrfNFKGSDQQ---KKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 140 IDEPTNHLDLQGRQHVANYFQHKDG-FIVVSHDRQFLNQVTDHTLAIE-KSQLVLYQGNFATYEEQKELRDEFELAQNRK 217
Cdd:TIGR03719 467 LDEPTNDLDVETLRALEEALLNFAGcAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFSEYEEDKKRRLGEDADQPHR 546
|
..
gi 2255859273 218 IK 219
Cdd:TIGR03719 547 IK 548
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
312-481 |
1.57e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 78.28 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHY----TEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQangELLRPNVKIS 378
Cdd:cd03293 1 LEVRNVSKTYggggGAVTAL-EDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlerptsgevLVDGE---PVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQNY--------ENNRG---TLQDFAEANQLDYSAFLnnLRKLGMERnvFQNQ-IEEMSMGQRKKVELAKSLAQEAEL 446
Cdd:cd03293 77 YVFQQDallpwltvLDNVAlglELQGVPKAEARERAEEL--LELVGLSG--FENAyPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 2255859273 447 YIWDEPLNYLDVFNQKQLEDLLL----QKQPTMLIVEHD 481
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLdiwrETGKTVLLVTHD 191
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-145 |
1.74e-16 |
|
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: 76.53 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 21 FEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFPLRPVYFP---------ATISEQDQL---------- 80
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsPTEGTILLDGQDLTDDerkslrkeiGYVFQDPQLfprltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 81 TYYALL-----EVADFELWELEREMNLIQLDPQVLWQPYQTLSGGEQTKVLLA-LLFTQENFFpLIDEPTN 145
Cdd:pfam00005 81 RLGLLLkglskREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIArALLTKPKLL-LLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
312-480 |
1.89e-16 |
|
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: 77.04 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEA-LFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQA-----NG--------ELLRPNvkI 377
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSgeiliDGvdlrdldlESLRKN--I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 378 SYVRQNyennrgtlqdfaeanqldysAFLnnlrklgmernvFQNQIEE--MSMGQRKKVELAKSLAQEAELYIWDEPLNY 455
Cdd:cd03228 79 AYVPQD--------------------PFL------------FSGTIREniLSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180
....*....|....*....|....*..
gi 2255859273 456 LDVFNQKQLEDLL--LQKQPTMLIVEH 480
Cdd:cd03228 127 LDPETEALILEALraLAKGKTVIVIAH 153
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
311-481 |
2.28e-16 |
|
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: 78.69 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHY----TEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQ-----ANGELLR 372
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVL-KDVSLEVAPGESFGLVGESGSGKSTLLRALAGlerpwsgevTFDGRpvtrrRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 373 pnvKISYVRQNYE---NNRGTLQD-----FAEANQLDYSAFLNN-LRKLGMERNVFQNQIEEMSMGQRKKVELAKSLAQE 443
Cdd:COG1124 80 ---RVQMVFQDPYaslHPRHTVDRilaepLRIHGLPDREERIAElLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2255859273 444 AELYIWDEPLNYLDVFNQKQLEDLL--LQKQP--TMLIVEHD 481
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLkdLREERglTYLFVSHD 198
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
312-470 |
2.33e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 78.18 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQ---ANGELLRPnvKISY 379
Cdd:COG1131 1 IEVRGLTKRYGDKTAL-DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllrptsgevRVLGEdvaRDPAEVRR--RIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 380 VRQN---------YENnrgtLQDFAEANQLDYSAFLNN----LRKLGMERnvFQNQ-IEEMSMGQRKKVELAKSLAQEAE 445
Cdd:COG1131 78 VPQEpalypdltvREN----LRFFARLYGLPRKEARERidelLELFGLTD--AADRkVGTLSGGMKQRLGLALALLHDPE 151
|
170 180
....*....|....*....|....*
gi 2255859273 446 LYIWDEPLNYLDVFNQKQLEDLLLQ 470
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRE 176
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
312-470 |
3.24e-16 |
|
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: 77.32 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAnGELLRPNVKISYVRQN---Y-ENN 387
Cdd:cd03269 1 LEVENVTKRFGRVTAL-DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS-GEVLFDGKPLDIAARNrigYlPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 388 RGTLQDFAEANQLDYSAFLNNLRKLGMERNV-----------FQNQ-IEEMSMGQRKKVELAKSLAQEAELYIWDEPLNY 455
Cdd:cd03269 79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIdewlerlelseYANKrVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170
....*....|....*
gi 2255859273 456 LDVFNQKQLEDLLLQ 470
Cdd:cd03269 159 LDPVNVELLKDVIRE 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
331-481 |
8.37e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 75.73 E-value: 8.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAgQANGELLR-PNVKISYVRQNYENNRG---------TLQDFAEANQL 400
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR-PTSGTVRRaGGARVAYVPQRSEVPDSlpltvrdlvAMGRWARRGLW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 401 ------DYSAFLNNLRKLGMERnVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQ---K 471
Cdd:NF040873 90 rrltrdDRAAVDDALERVGLAD-LAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEehaR 168
|
170
....*....|
gi 2255859273 472 QPTMLIVEHD 481
Cdd:NF040873 169 GATVVVVTHD 178
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-186 |
1.11e-15 |
|
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: 76.68 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 27 TIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIQFPLRPV-YFPATISEQDQLTYYALL--EVADF---ELWELERe 99
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKpDEGDIEIELDTVsYKPQYIKADYEGTVRDLLssITKDFythPYFKTEI- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 100 MNLIQLDpQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQH-----KDGFIVVSHDRQF 174
Cdd:cd03237 100 AKPLQIE-QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRfaennEKTAFVVEHDIIM 178
|
170
....*....|..
gi 2255859273 175 LNQVTDHTLAIE 186
Cdd:cd03237 179 IDYLADRLIVFE 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-191 |
1.51e-15 |
|
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: 76.24 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQF---PLR------------- 66
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLdgrDLAslsrrelarriay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 67 -----PVYFPATI------------------SEQD-QLTYYALlevADFELWELERemnliqldpqvlwQPYQTLSGGEQ 122
Cdd:COG1120 80 vpqepPAPFGLTVrelvalgryphlglfgrpSAEDrEAVEEAL---ERTGLEHLAD-------------RPVDELSGGER 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2255859273 123 TKVLLALLFTQENffPLI--DEPTNHLDLQGRQHVANYFQ---HKDG--FIVVSHDrqfLNQ---VTDHTLAIEKSQLV 191
Cdd:COG1120 144 QRVLIARALAQEP--PLLllDEPTSHLDLAHQLEVLELLRrlaRERGrtVVMVLHD---LNLaarYADRLVLLKDGRIV 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-202 |
1.61e-15 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 79.44 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSswKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIQFP--LRPVYFPatiseQDQL 80
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGS--RIGLLGRNGAGKSTLIKLLAGELApVSGEIGLAkgIKLGYFA-----QHQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 81 TYyalLEVADFELWELERemnliqLDPQVLWQ------------------PYQTLSGGEQTKVLLALLFTQENFFPLIDE 142
Cdd:PRK10636 386 EF---LRADESPLQHLAR------LAPQELEQklrdylggfgfqgdkvteETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 143 PTNHLDLQGRQHVANYFQHKDG-FIVVSHDRQFLNQVTDHTLAIEKSQLVLYQGNFATYEE 202
Cdd:PRK10636 457 PTNHLDLDMRQALTEALIDFEGaLVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQ 517
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-189 |
2.35e-15 |
|
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: 74.81 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 5 KITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQFPLRPV--YFPATISEQ---- 77
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGlLGPTSGEVLVDGKDLtkLSLKELRRKvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 78 -----DQLTY--------YAL--LEVADFELWE-LEREMNLIQLDPQVLWQPYqTLSGGEQTKVLLA---------LLFt 132
Cdd:cd03225 81 fqnpdDQFFGptveeevaFGLenLGLPEEEIEErVEEALELVGLEGLRDRSPF-TLSGGQKQRVAIAgvlamdpdiLLL- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 133 qenffpliDEPTNHLDLQGRQHVANYFQ--HKDG--FIVVSHDRQFLNQVTDHTLAIEKSQ 189
Cdd:cd03225 159 --------DEPTAGLDPAGRRELLELLKklKAEGktIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
312-483 |
2.45e-15 |
|
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: 74.86 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF---AGQ--ANGELL--RPNVK--ISYVRQ 382
Cdd:cd03259 1 LELKGLSKTYGSVRAL-DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLErpdSGEilIDGRDVtgVPPERrnIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 383 NY---------EN------NRGTLQDFAEANQLDYsaflnnLRKLGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAELY 447
Cdd:cd03259 80 DYalfphltvaENiafglkLRGVPKAEIRARVREL------LELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2255859273 448 IWDEPLNYLDV----FNQKQLEDLLLQKQPTMLIVEHDQT 483
Cdd:cd03259 153 LLDEPLSALDAklreELREELKELQRELGITTIYVTHDQE 192
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-215 |
7.98e-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: 7.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIQF---PLR------------- 66
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRILIdgiDLRqidpaslrrqigv 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 67 ----PVYFPATISE-----QDQLTYYALLEVADfelweleremnLIQLDPQVLWQP--YQT--------LSGGEQTKVLL 127
Cdd:COG2274 554 vlqdVFLFSGTIREnitlgDPDATDEEIIEAAR-----------LAGLHDFIEALPmgYDTvvgeggsnLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 128 A---------LLFtqenffpliDEPTNHLDLQGRQHVANYFQHKDG---FIVVSHDRQFLNQVtDHTLAIEKSQLVlYQG 195
Cdd:COG2274 623 ArallrnpriLIL---------DEATSALDAETEAIILENLRRLLKgrtVIIIAHRLSTIRLA-DRIIVLDKGRIV-EDG 691
|
250 260
....*....|....*....|
gi 2255859273 196 NFATYEEQKELrdEFELAQN 215
Cdd:COG2274 692 THEELLARKGL--YAELVQQ 709
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-170 |
1.49e-14 |
|
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: 71.65 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIqfplrpvyfpaTISEQDqlty 82
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEI-----------LIDGVD---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 83 yalleVADFELWELEREMNLIQLDPQVLwqpYQT-----LSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVAN 157
Cdd:cd03228 66 -----LRDLDLESLRKNIAYVPQDPFLF---SGTireniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170
....*....|....*.
gi 2255859273 158 YFQHKDGF---IVVSH 170
Cdd:cd03228 138 ALRALAKGktvIVIAH 153
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-181 |
2.83e-14 |
|
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: 71.80 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 5 KITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG--KyAYQGEIQFPLRPV-------------- 68
Cdd:cd03235 1 EVEDLTVSYGGHPVL--EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllK-PTSGSIRVFGKPLekerkrigyvpqrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 69 ----YFPATISE-------------------QDQLTYYALLEVADFELWEleremnliqldpqvlwQPYQTLSGGEQTKV 125
Cdd:cd03235 78 sidrDFPISVRDvvlmglyghkglfrrlskaDKAKVDEALERVGLSELAD----------------RQIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 126 LLALLFTQENFFPLIDEPTNHLDLQGRQH----VANYFQHKDGFIVVSHDrqfLNQVTDH 181
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDiyelLRELRREGMTILVVTHD---LGLVLEY 198
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
315-496 |
3.04e-14 |
|
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: 71.52 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 315 ENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF---AGQ--------ANGELLRpnvKISYVRQN 383
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIkesSGSillngkpiKAKERRK---SIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 384 --------------YENNRGTLQDFAEANQLdysaflnnLRKLG----MERNVFqnqieEMSMGQRKKVELAKSLAQEAE 445
Cdd:cd03226 80 vdyqlftdsvreelLLGLKELDAGNEQAETV--------LKDLDlyalKERHPL-----SLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 446 LYIWDEPLNYLDVFNQKQLEDLL--LQKQ-PTMLIVEHDQTFLKNIGAQQIALK 496
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIreLAAQgKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
335-481 |
3.85e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.84 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 335 VQRGTIVALTGPNGIGKSSVLHYLLGT--------------------FAGQ---------ANGELlRPNVKISYVRQNYE 385
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGElipnlgdyeeepswdevlkrFRGTelqnyfkklYNGEI-KVVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 386 NNRGTLQDFAEanQLDYSAFLNNLRK-LGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQL 464
Cdd:PRK13409 175 VFKGKVRELLK--KVDERGKLDEVVErLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNV 251
|
170
....*....|....*....
gi 2255859273 465 EDLL--LQKQPTMLIVEHD 481
Cdd:PRK13409 252 ARLIreLAEGKYVLVVEHD 270
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
312-493 |
4.88e-14 |
|
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: 74.41 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQANGELLRPNV--KISYV 380
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGflppysgsiLINGVDLSDLDPASWrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 381 RQN--------YEN--------NRGTLQDFAEANQLDysAFLNNLRKlGMERnvfqnQIEE----MSMGQRKKVELAKSL 440
Cdd:COG4988 417 PQNpylfagtiRENlrlgrpdaSDEELEAALEAAGLD--EFVAALPD-GLDT-----PLGEggrgLSGGQAQRLALARAL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 441 AQEAELYIWDEPLNYLDVFNQKQLEDLLLQ--KQPTMLIVEHDQTFLKNigAQQI 493
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRlaKGRTVILITHRLALLAQ--ADRI 541
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
296-481 |
5.10e-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: 71.59 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 296 VDRLTMSYHPSRHTQLLKMENLSL---HYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtfagqangeLLR 372
Cdd:cd03267 3 VSNLSKSYRVYSKEPGLIGSLKSLfkrKYREVEAL-KGISFTIEKGEIVGFIGPNGAGKTTTLKILSG---------LLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 373 P-------NVKISYVRQNYENNRGTLQdFAEANQL-------------------DYSAFLNNLRKLG----MERNVFQnQ 422
Cdd:cd03267 73 PtsgevrvAGLVPWKRRKKFLRRIGVV-FGQKTQLwwdlpvidsfyllaaiydlPPARFKKRLDELSelldLEELLDT-P 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 423 IEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQ----KQPTMLIVEHD 481
Cdd:cd03267 151 VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEynreRGTTVLLTSHY 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-224 |
8.69e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.61 E-value: 8.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGF-DKqveLLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGK-YAYQGEIqfplrpvyfpaTISEQDQLT 81
Cdd:PRK11819 325 IEAENLSKSFgDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQeQPDSGTI-----------KIGETVKLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 82 YyalleV--------ADFELWEL-----------EREM---------NLIQLDPQvlwQPYQTLSGGEQTKVLLALLFTQ 133
Cdd:PRK11819 391 Y-----VdqsrdaldPNKTVWEEisggldiikvgNREIpsrayvgrfNFKGGDQQ---KKVGVLSGGERNRLHLAKTLKQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 134 ENFFPLIDEPTNHLDLQGRQHVANYFQHKDG-FIVVSHDRQFLNQVTDHTLAIE-KSQLVLYQGNFATYEEQKELRDEFE 211
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETLRALEEALLEFPGcAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEYEEDKKRRLGAD 542
|
250
....*....|....
gi 2255859273 212 LAQNRKIK-KEVSR 224
Cdd:PRK11819 543 AARPHRIKyKKLTR 556
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
333-481 |
1.21e-13 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 70.26 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 333 FEVQRGTIVALTGPNGIGKSSVLHYLLGTFAG-----QANGELLRPN-VKISYVRQNYE--------------NNR-GTL 391
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPakgtvKVAGASPGKGwRHIGYVPQRHEfawdfpisvahtvmSGRtGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 392 QDFAEANQLDYSAFLNNLRKLGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDL---L 468
Cdd:TIGR03771 81 GWLRRPCVADFAAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELfieL 159
|
170
....*....|...
gi 2255859273 469 LQKQPTMLIVEHD 481
Cdd:TIGR03771 160 AGAGTAILMTTHD 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-488 |
1.45e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.91 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQ---GEIQFPLRP------VYFPATI 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVL--KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsGRIIYHVALcekcgyVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 75 SEQ-------------------DQLTYYALLEVA-----DFELWELEREM-NLIQLDPQVLWQPYQT------------- 116
Cdd:TIGR03269 79 GEPcpvcggtlepeevdfwnlsDKLRRRIRKRIAimlqrTFALYGDDTVLdNVLEALEEIGYEGKEAvgravdliemvql 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 117 ----------LSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYF-----QHKDGFIVVSHDRQFLNQVTDH 181
Cdd:TIGR03269 159 shrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavkASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 182 TLAIEKSQlvlyqgnfatyeeqkelrdefelaqnrkIKKEvsrlkrtaaekaewsrsretekyGKPSEKgsggifdtgfi 261
Cdd:TIGR03269 239 AIWLENGE----------------------------IKEE-----------------------GTPDEV----------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 262 garAARTMKRSKTIEQrmYDQIEVKEgllkdledvdrltmsyhpsrhtQLLKMENLSLHY--TEQEALFA--PLSFEVQR 337
Cdd:TIGR03269 257 ---VAVFMEGVSEVEK--ECEVEVGE----------------------PIIKVRNVSKRYisVDRGVVKAvdNVSLEVKE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 338 GTIVALTGPNGIGKSSVLHYLLGTF---AGQAN-------------GELLRPNVK--ISYVRQNYE--NNRGTLQDFAEA 397
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLeptSGEVNvrvgdewvdmtkpGPDGRGRAKryIGILHQEYDlyPHRTVLDNLTEA 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 398 NQLDYSAFLN------NLRKLGME----RNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDL 467
Cdd:TIGR03269 390 IGLELPDELArmkaviTLKMVGFDeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHS 469
|
570 580
....*....|....*....|....*
gi 2255859273 468 LLQKQ----PTMLIVEHDQTFLKNI 488
Cdd:TIGR03269 470 ILKAReemeQTFIIVSHDMDFVLDV 494
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
312-493 |
1.80e-13 |
|
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: 72.94 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEA-LFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAnGELL---------RPNV---KIS 378
Cdd:COG2274 474 IELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS-GRILidgidlrqiDPASlrrQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQNYENNRGTLQD---FAEAnQLDYSAFLNNLRKLGMERNV------FQNQIEEM----SMGQRKKVELAKSLAQEAE 445
Cdd:COG2274 553 VVLQDVFLFSGTIREnitLGDP-DATDEEIIEAARLAGLHDFIealpmgYDTVVGEGgsnlSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2255859273 446 LYIWDEPLNYLDVFNQKQLEDLLLQ--KQPTMLIVEHDQTFLKNigAQQI 493
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIRL--ADRI 679
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
312-486 |
2.05e-13 |
|
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: 69.44 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHY----TEQEALFAPlSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQ-----ANGEL--L 371
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGV-SLSIEKGEFVAIVGPSGSGKSTLLNILGGldrptsgevRVDGTdisklSEKELaaF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 372 RpNVKISYVRQNY---------EN--------NRGTLQDFAEANQLdysaflnnLRKLGMErNVFQNQIEEMSMGQRKKV 434
Cdd:cd03255 80 R-RRHIGFVFQSFnllpdltalENvelplllaGVPKKERRERAEEL--------LERVGLG-DRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2255859273 435 ELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLL----QKQPTMLIVEHDQTFLK 486
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRelnkEAGTTIVVVTHDPELAE 205
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
338-481 |
2.11e-13 |
|
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: 70.09 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 338 GTIVALTGPNGIGKSSVLHYLLGT--------------------FAGQA---------NGELlRPNVKISYVRQNYENNR 388
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKlkpnlgkfddppdwdeildeFRGSElqnyftkllEGDV-KVIVKPQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 389 GTLQDFAEanQLDYSAFLNNLRKLGMERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDV---FNQKQLE 465
Cdd:cd03236 105 GKVGELLK--KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAARLI 182
|
170
....*....|....*.
gi 2255859273 466 DLLLQKQPTMLIVEHD 481
Cdd:cd03236 183 RELAEDDNYVLVVEHD 198
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
312-480 |
5.63e-13 |
|
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: 68.01 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtfagqangeLLRPN-----VKISYVRQNYEN 386
Cdd:cd03268 1 LKTNDLTKTYGKKRVL-DDISLHVKKGEIYGFLGPNGAGKTTTMKIILG---------LIKPDsgeitFDGKSYQKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 387 NR--GTLqdfaeanqLDYSAFLNNL---------RKLGMERNVFQNQIEEM--------------SMGQRKKVELAKSLA 441
Cdd:cd03268 71 LRriGAL--------IEAPGFYPNLtarenlrllARLLGIRKKRIDEVLDVvglkdsakkkvkgfSLGMKQRLGIALALL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2255859273 442 QEAELYIWDEPLNYLDVFNQKQLEDLLLQKQP---TMLIVEH 480
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSH 184
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
312-481 |
5.98e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.89 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLH---YLLGTFAGQ-----------ANGELLR----- 372
Cdd:PRK11231 3 LRTENLTVGYGTKRILND-LSLSLPTGKITALIGPNGCGKSTLLKcfaRLLTPQSGTvflgdkpismlSSRQLARrlall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 373 PNVK-----------ISYVRQNYENNRGTLQDfaEANQLDYSAflnnlrklgMER---NVFQNQ-IEEMSMGQRKKVELA 437
Cdd:PRK11231 82 PQHHltpegitvrelVAYGRSPWLSLWGRLSA--EDNARVNQA---------MEQtriNHLADRrLTDLSGGQRQRAFLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2255859273 438 KSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQ---PTMLIVEHD 481
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtqgKTVVTVLHD 197
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
312-496 |
1.08e-12 |
|
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: 67.59 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQANGELLRPNV-----KI 377
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvLIDGTDINKLKGKALrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 378 SYVRQNY---------ENN-----------RGTLQDFAEAnqlDYSAFLNNLRKLGMERNVFQnQIEEMSMGQRKKVELA 437
Cdd:cd03256 81 GMIFQQFnlierlsvlENVlsgrlgrrstwRSLFGLFPKE---EKQRALAALERVGLLDKAYQ-RADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 438 KSLAQEAELYIWDEPLNYLDVFNQKQLEDLLL----QKQPTMLIVEHDQTFLKNIGAQQIALK 496
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKrinrEEGITVIVSLHQVDLAREYADRIVGLK 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-199 |
1.34e-12 |
|
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: 69.79 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 2 STIKITHLTFGFDKQVELLfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQF----------------- 63
Cdd:COG4988 335 PSIELEDVSFSYPGGRPAL-DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSILIngvdlsdldpaswrrqi 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 64 ---PLRPVYFPATISE----------QDQLtyYALLEVADfeLWELeremnlIQLDPQVLwqpyQT--------LSGGEQ 122
Cdd:COG4988 414 awvPQNPYLFAGTIREnlrlgrpdasDEEL--EAALEAAG--LDEF------VAALPDGL----DTplgeggrgLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 123 TKVLLALLFTQENffPLI--DEPTNHLDLQGRQHV----ANYFQHKdGFIVVSHDRQFLNQVtDHTLAIEKSQLVLyQGN 196
Cdd:COG4988 480 QRLALARALLRDA--PLLllDEPTAHLDAETEAEIlqalRRLAKGR-TVILITHRLALLAQA-DRILVLDDGRIVE-QGT 554
|
...
gi 2255859273 197 FAT 199
Cdd:COG4988 555 HEE 557
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
312-480 |
1.71e-12 |
|
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: 65.14 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTFAGqangeLLRPN---VKIsyvrqnyennR 388
Cdd:cd03216 1 LELRGITKRFGGVKAL-DGVSLSVRRGEVHALLGENGAGKST----LMKILSG-----LYKPDsgeILV----------D 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 389 GTLQDFAEANQldysAflnnlRKLGMERnVFQnqieeMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL 468
Cdd:cd03216 61 GKEVSFASPRD----A-----RRAGIAM-VYQ-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI 125
|
170
....*....|....*
gi 2255859273 469 --LQKQP-TMLIVEH 480
Cdd:cd03216 126 rrLRAQGvAVIFISH 140
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-190 |
2.04e-12 |
|
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: 65.50 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIqfplrpvyfpatiseqdqlty 82
Cdd:cd03230 1 IEVRNLSKRYGKKTAL--DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGlLKPDSGEI--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 83 yallEVADFELWELEREMN-----LIQlDPQVLWQ--PYQTL--SGGEQTKVLLAL-LFTQENFFpLIDEPTNHLDLQGR 152
Cdd:cd03230 58 ----KVLGKDIKKEPEEVKrrigyLPE-EPSLYENltVRENLklSGGMKQRLALAQaLLHDPELL-ILDEPTSGLDPESR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2255859273 153 QHVANYFQH--KDG--FIVVSHDRQFLNQVTDHTLAIEKSQL 190
Cdd:cd03230 132 REFWELLRElkKEGktILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
336-481 |
3.35e-12 |
|
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: 68.66 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 336 QRGTIVALTGPNGIGKSSVLHYLLGT--------------------FAGQ---------ANGELlRPNVKISYV------ 380
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElkpnlgdydeepswdevlkrFRGTelqdyfkklANGEI-KVAHKPQYVdlipkv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 381 -----RQNYENN--RGTLQDFAEanqldysaflnnlrKLGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPL 453
Cdd:COG1245 176 fkgtvRELLEKVdeRGKLDELAE--------------KLGLE-NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|.
gi 2255859273 454 NYLDVF---NQKQLEDLLLQKQPTMLIVEHD 481
Cdd:COG1245 241 SYLDIYqrlNVARLIRELAEEGKYVLVVEHD 271
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
309-482 |
4.09e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.55 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 309 TQLLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELLRPNVKISYVRQNYENNR 388
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAG-FEQPTAGQIMLDGVDLSHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 389 GTLQDFA-------EANqldySAFlnNLRKLGMERNVFQNQIEEM-----------------SMGQRKKVELAKSLAQEA 444
Cdd:PRK11607 95 MMFQSYAlfphmtvEQN----IAF--GLKQDKLPKAEIASRVNEMlglvhmqefakrkphqlSGGQRQRVALARSLAKRP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2255859273 445 ELYIWDEPLNYLD--VFNQKQLE--DLLLQKQPTMLIVEHDQ 482
Cdd:PRK11607 169 KLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
312-481 |
6.11e-12 |
|
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: 67.70 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELLRPNVK------------ISY 379
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG-FVDPTEGSIAVNGVPladadadswrdqIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 380 VRQN--------YENNR-----GTLQDFAEANQLDYSAFLNNLRKLGMERNVFQNQiEEMSMGQRKKVELAKSLAQEAEL 446
Cdd:TIGR02857 401 VPQHpflfagtiAENIRlarpdASDAEIREALERAGLDEFVAALPQGLDTPIGEGG-AGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190
....*....|....*....|....*....|....*..
gi 2255859273 447 YIWDEPLNYLDVFNQKQLEDLLLQ--KQPTMLIVEHD 481
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRAlaQGRTVLLVTHR 516
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
332-481 |
1.37e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 332 SFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGEL----------LRPNVkISYVRQNYE---------------N 386
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMG-FVRLASGKIsilgqptrqaLQKNL-VAYVPQSEEvdwsfpvlvedvvmmG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 387 NRGTLQDFAEANQLDYSAFLNNLRKLGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLED 466
Cdd:PRK15056 105 RYGHMGWLRRAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIIS 183
|
170
....*....|....*...
gi 2255859273 467 LLLQ---KQPTMLIVEHD 481
Cdd:PRK15056 184 LLRElrdEGKTMLVSTHN 201
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-196 |
1.67e-11 |
|
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: 62.72 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFplrpvyfpatiseqdqlty 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLkPQQGEITL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 83 yallevADFELWELEREM-NLIQLDPQvlwQPY-----------QTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLD-L 149
Cdd:cd03247 62 ------DGVPVSDLEKALsSLISVLNQ---RPYlfdttlrnnlgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2255859273 150 QGRQHVANYFQHKDGFIVVshdrqflnQVTDHTLAIEKSQLVLYQGN 196
Cdd:cd03247 133 TERQLLSLIFEVLKDKTLI--------WITHHLTGIEHMDKILFLEN 171
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
312-480 |
1.78e-11 |
|
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: 62.62 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTE-QEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtfagqangeLLRP---NVKIsyvrqnyenn 387
Cdd:cd03246 1 LEVENVSFRYPGaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG---------LLRPtsgRVRL---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 388 rgtlqDFAEANQLDYSAFLNNLRKLGMERNVFQNQIEE--MSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLE 465
Cdd:cd03246 62 -----DGADISQWDPNELGDHVGYLPQDDELFSGSIAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170
....*....|....*...
gi 2255859273 466 DLLLQ---KQPTMLIVEH 480
Cdd:cd03246 137 QAIAAlkaAGATRIVIAH 154
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-177 |
1.98e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.41 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 20 LFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGK-YAYQGEIQF---PLR------------------PVYFPATISE- 76
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGElSPDSGEVRLngrPLAdwspaelarrravlpqhsSLSFPFTVEEv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 77 --------------QDQLTYYALLEVadfELWELERemnliqldpqvlwQPYQTLSGGEQTKVLLALLFTQ---ENFFP- 138
Cdd:PRK13548 97 vamgraphglsraeDDALVAAALAQV---DLAHLAG-------------RDYPQLSGGEQQRVQLARVLAQlwePDGPPr 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2255859273 139 --LIDEPTNHLDLQGRQHV---ANYFQHKDGF--IVVSHDrqfLNQ 177
Cdd:PRK13548 161 wlLLDEPTSALDLAHQHHVlrlARQLAHERGLavIVVLHD---LNL 203
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
312-493 |
2.71e-11 |
|
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: 62.87 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAP----LSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAgQANGELLRPNvKISYVRQ----- 382
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELE-KLSGSVSVPG-SIAYVSQepwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 383 NyennrGTLQD----FAEANQ------LDYSAFLNNLRKL--GMERNVFQNQIeEMSMGQRKKVELAKSLAQEAELYIWD 450
Cdd:cd03250 79 N-----GTIREnilfGKPFDEeryekvIKACALEPDLEILpdGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2255859273 451 EPLNYLD------VFNQKQLEDLLLQKqpTMLIVEHDQTFLKNigAQQI 493
Cdd:cd03250 153 DPLSAVDahvgrhIFENCILGLLLNNK--TRILVTHQLQLLPH--ADQI 197
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
310-481 |
2.72e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.95 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 310 QLLKMENLSLhyTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF-------AGQ--ANGELLRPN----VK 376
Cdd:PRK10418 3 QQIELRNIAL--QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrqtAGRvlLDGKPVAPCalrgRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 377 ISYVRQN-----------YENNRGTLQdfAEANQLDYSAFLNNLRKLGME--RNVFQNQIEEMS--MGQRKKVELAksLA 441
Cdd:PRK10418 81 IATIMQNprsafnplhtmHTHARETCL--ALGKPADDATLTAALEAVGLEnaARVLKLYPFEMSggMLQRMMIALA--LL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2255859273 442 QEAELYIWDEPLNYLDVFNQKQ----LEDLLLQKQPTMLIVEHD 481
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARildlLESIVQKRALGMLLVTHD 200
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-172 |
2.75e-11 |
|
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: 65.77 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 15 KQVELLFEDA-------NLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQF--------------------PLR 66
Cdd:TIGR02857 325 SGVSVAYPGRrpalrpvSFTVPPGERVALVGPSGAGKSTLLNLLLGfVDPTEGSIAVngvpladadadswrdqiawvPQH 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 67 PVYFPATISEQDQLtyyALLEVADFELWELEREMNLIQLDpQVLWQPYQT--------LSGGEQTKVLLALLFTQENFFP 138
Cdd:TIGR02857 405 PFLFAGTIAENIRL---ARPDASDAEIREALERAGLDEFV-AALPQGLDTpigeggagLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190
....*....|....*....|....*....|....*...
gi 2255859273 139 LIDEPTNHLDLQGRQHV----ANYFQHKDGfIVVSHDR 172
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVlealRALAQGRTV-LLVTHRL 517
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
313-481 |
3.19e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.56 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 313 KMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHY---LLGTFAGQ-----------ANGELLRpnvKIS 378
Cdd:COG4604 3 EIKNVSKRYGGKVVL-DDVSLTIPKGGITALIGPNGAGKSTLLSMisrLLPPDSGEvlvdgldvattPSRELAK---RLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQnyENN---------------------RGTLQDFAEANQ-LDYsaflnnlrkLGME--RNVFqnqIEEMSMGQRKKV 434
Cdd:COG4604 79 ILRQ--ENHinsrltvrelvafgrfpyskgRLTAEDREIIDEaIAY---------LDLEdlADRY---LDELSGGQRQRA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 435 ELAKSLAQEAElYIW-DEPLNYLDVFNQKQLEDLL------LQKqpTMLIVEHD 481
Cdd:COG4604 145 FIAMVLAQDTD-YVLlDEPLNNLDMKHSVQMMKLLrrladeLGK--TVVIVLHD 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-180 |
3.34e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.74 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 33 KLGLVGRNGRGKTTLLQLLLGKYAYQ-GEIQF--PLRPVYFpatiseqDQltYYALLE----VADfELWELEREMNLIQL 105
Cdd:PRK11147 347 KIALIGPNGCGKTTLLKLMLGQLQADsGRIHCgtKLEVAYF-------DQ--HRAELDpektVMD-NLAEGKQEVMVNGR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 106 DPQVL-------------WQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQG----RQHVANYfqhKDGFIVV 168
Cdd:PRK11147 417 PRHVLgylqdflfhpkraMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETlellEELLDSY---QGTVLLV 493
|
170
....*....|...
gi 2255859273 169 SHDRQFL-NQVTD 180
Cdd:PRK11147 494 SHDRQFVdNTVTE 506
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
327-470 |
3.53e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 327 LFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELLRPNVKISYVRQNY--------------------EN 386
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-LARPDAGEVLWQGEPIRRQRDEYhqdllylghqpgikteltalEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 387 nrgtLQDFAE-ANQLDYSAFLNNLRKLGMER--NVFQNQieeMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQ 463
Cdd:PRK13538 95 ----LRFYQRlHGPGDDEALWEALAQVGLAGfeDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
....*..
gi 2255859273 464 LEDLLLQ 470
Cdd:PRK13538 168 LEALLAQ 174
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
331-470 |
3.84e-11 |
|
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: 62.77 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF---AGQANGELLRPNVKISYVRQN---YENNRGTLQDFAEANQLDYSA 404
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLepdAGFATVDGFDVVKEPAEARRRlgfVSDSTGLYDRLTARENLEYFA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2255859273 405 FLNNLR-------------KLGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQ 470
Cdd:cd03266 104 GLYGLKgdeltarleeladRLGME-ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQ 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
325-470 |
3.95e-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: 62.51 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 325 EALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELLRPNVKISYVRQNYENN----------RGTLQdf 394
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG-LSPPLAGRVLLNGGPLDFQRDSIARGllylghapgiKTTLS-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 395 AEANQLDYSAF------LNNLRKLGMerNVFQNQI-EEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDL 467
Cdd:cd03231 90 VLENLRFWHADhsdeqvEEALARVGL--NGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
...
gi 2255859273 468 LLQ 470
Cdd:cd03231 168 MAG 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
312-497 |
4.68e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 62.38 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG----TfAGQA--NGELLR--PNVKISYVRQN 383
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeerpT-SGQVlvNGQDLSrlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 384 YennrGT-LQDFaeanQL--DYSAFLN---NLRKLGMERNVFQNQIEEM-----------------SMGQRKKVELAKSL 440
Cdd:COG2884 81 I----GVvFQDF----RLlpDRTVYENvalPLRVTGKSRKEIRRRVREVldlvglsdkakalphelSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 441 AQEAELYIWDEPLNYLDVFNQKQLEDLLL---QKQPTMLIVEHDQTFLKNIGAQQIALKK 497
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEeinRRGTTVLIATHDLELVDRMPKRVLELED 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-171 |
1.17e-10 |
|
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: 63.53 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 3 TIKITHLTFGFDKQVELLfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIQ------------------- 62
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVL-DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDpLQGEVTldgvpvssldqdevrrrvs 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 63 -FPLRPVYFPATISEQDQLtyyALLEVADFELWELEREMNLIQLdPQVLWQPYQT--------LSGGEQTKVLLALLFTQ 133
Cdd:TIGR02868 413 vCAQDAHLFDTTVRENLRL---ARPDATDEELWAALERVGLADW-LRALPDGLDTvlgeggarLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2255859273 134 EnfFPLI--DEPTNHLDLQ-GRQHVANYFQHKDGF--IVVSHD 171
Cdd:TIGR02868 489 D--APILllDEPTEHLDAEtADELLEDLLAALSGRtvVLITHH 529
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
326-480 |
1.43e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.45 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 326 ALFAPLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTFAG---QANGELLRPNVKISYVRQNYENN-------RGTLQDFA 395
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTT----LLRILAGllrPDSGEVRWNGTPLAEQRDEPHENilylghlPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 396 EANQLDysaFLNNLrkLGMERNVFQNQIEEM-------------SMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQK 462
Cdd:TIGR01189 90 ALENLH---FWAAI--HGGAQRTIEDALAAVgltgfedlpaaqlSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 2255859273 463 QLEDLL---LQKQPTMLIVEH 480
Cdd:TIGR01189 165 LLAGLLrahLARGGIVLLTTH 185
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-187 |
1.49e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.29 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 18 ELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAY-QGEIQFPL---------RPvYFPaTISEQDQLTY-YALL 86
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYgSGRIARPAgarvlflpqRP-YLP-LGTLREALLYpATAE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 87 EVADFELWELEREMNL----IQLDPQVLWQpyQTLSGGEQTKVLLA-LLFTQenffP---LIDEPTNHLDLQGRQHVANY 158
Cdd:COG4178 454 AFSDAELREALEAVGLghlaERLDEEADWD--QVLSLGEQQRLAFArLLLHK----PdwlFLDEATSALDEENEAALYQL 527
|
170 180 190
....*....|....*....|....*....|..
gi 2255859273 159 FQHKD---GFIVVSHdRQFLNQVTDHTLAIEK 187
Cdd:COG4178 528 LREELpgtTVISVGH-RSTLAAFHDRVLELTG 558
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
312-488 |
1.58e-10 |
|
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: 61.30 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQA-----NGEL---LRPN--VKISYVR 381
Cdd:cd03219 1 LEVRGLTKRFGGLVAL-DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSgsvlfDGEDitgLPPHeiARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 382 --QN---------YEN-----NRGTLQDFAEANQLDYSAFLNN-----LRKLGMERnVFQNQIEEMSMGQRKKVELAKSL 440
Cdd:cd03219 80 tfQIprlfpeltvLENvmvaaQARTGSGLLLARARREEREAREraeelLERVGLAD-LADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 441 AQEAELYIWDEPLNYLDVFNQKQLEDLLL---QKQPTMLIVEHDQTFLKNI 488
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRelrERGITVLLVEHDMDVVMSL 209
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
312-481 |
1.93e-10 |
|
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: 63.15 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAnGELLRPNVKISYVRQNYENNRGTL 391
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ-GEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 392 qdFAEANQLDYSAFLNNLR----------------KLGMERNV------FQNQIEEM----SMGQRKKVELAKSLAQEAE 445
Cdd:TIGR02868 414 --CAQDAHLFDTTVRENLRlarpdatdeelwaaleRVGLADWLralpdgLDTVLGEGgarlSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*...
gi 2255859273 446 LYIWDEPLNYLDVFNQKQLEDLLLQKQP--TMLIVEHD 481
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAALSgrTVVLITHH 529
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-191 |
1.98e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 61.28 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIQF---PLR------------- 66
Cdd:COG4559 2 LEAENLSVRLGGRT--LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTpSSGEVRLngrPLAawspwelarrrav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 67 -----PVYFPATISEQDQLTYYALLEVADFELWELEREMNLIQLDPqvLWQ-PYQTLSGGEQTKVLLALLFTQ----ENF 136
Cdd:COG4559 80 lpqhsSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAH--LAGrSYQTLSGGEQQRVQLARVLAQlwepVDG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 137 FP---LIDEPTNHLDLQGRQHV----ANYFQHKDGFIVVSHDrqfLN---QVTDHTLAIEKSQLV 191
Cdd:COG4559 158 GPrwlFLDEPTSALDLAHQHAVlrlaRQLARRGGGVVAVLHD---LNlaaQYADRILLLHQGRLV 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
311-480 |
3.10e-10 |
|
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: 60.48 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLH--------------YLLGTFAGQANGELLRPnvK 376
Cdd:COG1119 3 LLELRNVTVRRGGKTIL-DDISWTVKPGEHWAILGPNGAGKSTLLSlitgdlpptygndvRLFGERRGGEDVWELRK--R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 377 ISYV-----RQNYENNRG------------------TLQDFAEANQLdysaflnnLRKLGMERnvFQNQ-IEEMSMGQRK 432
Cdd:COG1119 80 IGLVspalqLRFPRDETVldvvlsgffdsiglyrepTDEQRERAREL--------LELLGLAH--LADRpFGTLSQGEQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 433 KVELAKSLAQEAELYIWDEPLNYLDVFNQKQ----LEDLLLQKQPTMLIVEH 480
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELllalLDKLAAEGAPTLVLVTH 201
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
312-481 |
3.87e-10 |
|
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: 59.89 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSS---VLHYLL---------GT--------FAGQANGELL 371
Cdd:cd03260 1 IELRDLNVYYGDKHALKD-ISLDIPKGEITALIGPSGCGKSTllrLLNRLNdlipgapdeGEvlldgkdiYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 372 RPNVKIsyVRQN--------YENNRGTLQDFAEAN--QLDYSAfLNNLRKLGMERNVFQNQIE-EMSMGQRKKVELAKSL 440
Cdd:cd03260 80 RRRVGM--VFQKpnpfpgsiYDNVAYGLRLHGIKLkeELDERV-EEALRKAALWDEVKDRLHAlGLSGGQQQRLCLARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2255859273 441 AQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQPTMLIVEHD 481
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIaeLKKEYTIVIVTHN 199
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-202 |
5.04e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 19 LLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKyayqgeiqfpLRPVYFPATISEQDQLTYYALLEVADFEL----- 93
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGE----------LQPSSGTVFRSAKVRMAVFSQHHVDGLDLssnpl 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 94 ------------WELEREMNLIQLDPQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVAN---Y 158
Cdd:PLN03073 593 lymmrcfpgvpeQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQglvL 672
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2255859273 159 FQhkDGFIVVSHDRQFLNQVTDHTLAIEKSQLVLYQGNFATYEE 202
Cdd:PLN03073 673 FQ--GGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
312-496 |
6.26e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.13 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQangellRPNVKISYVRQNYENNRG-- 389
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ------RGRVKVMGREVNAENEKWvr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 390 -----TLQD-----FAeANQLDYSAFlnNLRKLGMERNVFQNQIEE-----------------MSMGQRKKVELAKSLAQ 442
Cdd:PRK13647 79 skvglVFQDpddqvFS-STVWDDVAF--GPVNMGLDKDEVERRVEEalkavrmwdfrdkppyhLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 443 EAELYIWDEPLNYLDVFNQKQLEDLL--LQKQ-PTMLIVEHDQTFLKNIGAQQIALK 496
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILdrLHNQgKTVIVATHDVDLAAEWADQVIVLK 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
312-495 |
6.34e-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: 59.04 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQealfaPLSFEVQ--RGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELL-------------RPnvk 376
Cdd:cd03298 1 VRLDKIRFSYGEQ-----PMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAG-FETPQSGRVLingvdvtaappadRP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 377 ISYVRQnyENNRGTLQDFAE-----------ANQLDYSAFLNNLRKLGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAE 445
Cdd:cd03298 72 VSMLFQ--ENNLFAHLTVEQnvglglspglkLTAEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 446 LYIWDEPLNYLDVFNQKQLEDLLL----QKQPTMLIVEHDQTFLKNIGAQQIAL 495
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLdlhaETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
312-470 |
7.57e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.12 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF---AGQA--NGELLRPNV--KISYV---R 381
Cdd:COG4152 2 LELKGLTKRFGDKTAVDD-VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILapdSGEVlwDGEPLDPEDrrRIGYLpeeR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 382 QNYENNR--GTLQDFAEANQLDYSAFLNNLRKLgMERnvFQ------NQIEEMSMGQRKKVELAKSLAQEAELYIWDEPL 453
Cdd:COG4152 81 GLYPKMKvgEQLVYLARLKGLSKAEAKRRADEW-LER--LGlgdranKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170
....*....|....*..
gi 2255859273 454 NYLDVFNQKQLEDLLLQ 470
Cdd:COG4152 158 SGLDPVNVELLKDVIRE 174
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
316-464 |
7.90e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.46 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 316 NLSLHYTeqeALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAgQANGELlRPNVKISYVRQNYENNRGTLQD-- 393
Cdd:TIGR01271 433 NFSLYVT---PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELE-PSEGKI-KHSGRISFSPQTSWIMPGTIKDni 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 394 -------------FAEANQL--DYSAFLNNLRKLGMERNVfqnqieEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDV 458
Cdd:TIGR01271 508 ifglsydeyrytsVIKACQLeeDIALFPEKDKTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*.
gi 2255859273 459 FNQKQL 464
Cdd:TIGR01271 582 VTEKEI 587
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
311-482 |
8.40e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 58.90 E-value: 8.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALFAPL---SFEVQRGTIVALTGPNGIGKSSVLHyLLGT----------FAGQA-----NGEL-- 370
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALrgvSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGldrptsgevlIDGQDisslsERELar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 371 LRpNVKISYVRQNY---------EN--------NRGTLQDFAEANQLdysaflnnLRKLGMErNVFQNQIEEMSMGQRKK 433
Cdd:COG1136 83 LR-RRHIGFVFQFFnllpeltalENvalplllaGVSRKERRERAREL--------LERVGLG-DRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 434 VELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQP--TMLIVEHDQ 482
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLreLNRELgtTIVMVTHDP 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-180 |
8.64e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 34 LGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFPLRPVYFPATISEQDQLTYYALLE--VADFE---LW-ELEREMNLIQLd 106
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLkPDEGEVDPELKISYKPQYIKPDYDGTVEDLLRsiTDDLGssyYKsEIIKPLQLERL- 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2255859273 107 pqvLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQH-----KDGFIVVSHDRQFLNQVTD 180
Cdd:PRK13409 447 ---LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRiaeerEATALVVDHDIYMIDYISD 522
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
325-468 |
9.12e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.35 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 325 EALFAPLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTFAGqangeLLRP---NVKisyvrqnYENNRGTLQDFAEanQLD 401
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTT----LLRLIAG-----LLPPaagTIK-------LDGGDIDDPDVAE--ACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 402 YSAFLNNL-RKLGMERNV-----FQNQIE---------------------EMSMGQRKKVELAKSLAQEAELYIWDEPLN 454
Cdd:PRK13539 77 YLGHRNAMkPALTVAENLefwaaFLGGEEldiaaaleavglaplahlpfgYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|....
gi 2255859273 455 YLDVFNQKQLEDLL 468
Cdd:PRK13539 157 ALDAAAVALFAELI 170
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
311-491 |
1.23e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.67 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTE---QEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQANGEL-------L 371
Cdd:PRK11629 5 LLQCDNLCKRYQEgsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGldtptsgdvIFNGQPMSKLssaakaeL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 372 RpNVKISYVRQNYEnnrgTLQDF-----------------AEANQldysAFLNNLRKLGMERNVfQNQIEEMSMGQRKKV 434
Cdd:PRK11629 85 R-NQKLGFIYQFHH----LLPDFtalenvamplligkkkpAEINS----RALEMLAAVGLEHRA-NHRPSELSGGERQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 435 ELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL----LQKQPTMLIVEHDQTFLKNIGAQ 491
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLgelnRLQGTAFLVVTHDLQLAKRMSRQ 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
307-481 |
1.26e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.09 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 307 RHTQLLKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAgQANGELLRPNVKISYVRQNYEN 386
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK-PSSGRILFDGKPIDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 387 NRGTL----QDfaEANQLDYSAFLNNLR----KLGMERNVFQNQIEE-----------------MSMGQRKKVELAKSLA 441
Cdd:PRK13636 80 LRESVgmvfQD--PDNQLFSASVYQDVSfgavNLKLPEDEVRKRVDNalkrtgiehlkdkpthcLSFGQKKRVAIAGVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2255859273 442 QEAELYIWDEPLNYLDVFNQKQLEDLLLQKQP----TMLIVEHD 481
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelglTIIIATHD 201
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
311-457 |
1.44e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.87 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAG---------------QANGELLR--- 372
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHA-VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdksagshiellgrtvQREGRLARdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 373 -PNVKISYVRQNYE-NNRGTLQDFAEANQLDYSAF----------------LNNLRKLGMERNVFQnQIEEMSMGQRKKV 434
Cdd:PRK09984 83 kSRANTGYIFQQFNlVNRLSVLENVLIGALGSTPFwrtcfswftreqkqraLQALTRVGMVHFAHQ-RVSTLSGGQQQRV 161
|
170 180
....*....|....*....|...
gi 2255859273 435 ELAKSLAQEAELYIWDEPLNYLD 457
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLD 184
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
312-482 |
2.50e-09 |
|
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: 57.63 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELLRPNVKISYVRQNYENNRGTL 391
Cdd:cd03300 1 IELENVSKFYGGFVAL-DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAG-FETPTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 392 QDFAEANQLDYS---AFlnNLRKLGMERNVFQNQIEEM-----------------SMGQRKKVELAKSLAQEAELYIWDE 451
Cdd:cd03300 79 QNYALFPHLTVFeniAF--GLRLKKLPKAEIKERVAEAldlvqlegyanrkpsqlSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2255859273 452 PLNYLDVFNQK--QLEDLLLQKQ--PTMLIVEHDQ 482
Cdd:cd03300 157 PLGALDLKLRKdmQLELKRLQKElgITFVFVTHDQ 191
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-191 |
2.60e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 57.37 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLfEDANLTIDSswklG----LVGRNGRGKTTLLQLLLGKY-AYQGEIQFPLRPVyfpATISE-- 76
Cdd:COG2884 2 IRFENVSKRYPGGREAL-SDVSLEIEK----GefvfLTGPSGAGKSTLLKLLYGEErPTSGQVLVNGQDL---SRLKRre 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 77 ------------QD-----QLTYY---AL-LEVADFELWELEREMnliqldPQVLWQ----------PYQtLSGGEQTKV 125
Cdd:COG2884 74 ipylrrrigvvfQDfrllpDRTVYenvALpLRVTGKSRKEIRRRV------REVLDLvglsdkakalPHE-LSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 126 LL--ALLftqeNFFPLI--DEPTNHLDLQGRQHVANYFQ--HKDG--FIVVSHDRQFLNQVTDHTLAIEKSQLV 191
Cdd:COG2884 147 AIarALV----NRPELLlaDEPTGNLDPETSWEIMELLEeiNRRGttVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-180 |
3.15e-09 |
|
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: 59.41 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 34 LGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFPLRPVYFPATISEQDQLTYYALLEVADFEL----WELEREMNLIQLDPq 108
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDLKISYKPQYISPDYDGTVEEFLRSANTDDfgssYYKTEIIKPLGLEK- 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 109 VLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQ-----HKDGFIVVSHDRQFLNQVTD 180
Cdd:COG1245 448 LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRrfaenRGKTAMVVDHDIYLIDYISD 524
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
331-481 |
3.25e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 57.74 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQangEL--LRP-------------------------N 374
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGfyrptsgriLFDGR---DItgLPPhriarlgiartfqnprlfpeltvleN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 375 VKISYVRQNYENNRGTLQDF-----------AEANQLdysaflnnLRKLGMERnVFQNQIEEMSMGQRKKVELAKSLAQE 443
Cdd:COG0411 100 VLVAAHARLGRGLLAALLRLprarreerearERAEEL--------LERVGLAD-RADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2255859273 444 AELYIWDEP---LNYLDVfnqKQLEDLL--LQKQP--TMLIVEHD 481
Cdd:COG0411 171 PKLLLLDEPaagLNPEET---EELAELIrrLRDERgiTILLIEHD 212
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
35-191 |
3.28e-09 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 57.52 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 35 GLVGRNGRGKTTLLQLLLGKYA-YQGEIQFPLRPVYfpaTISEQDQLTYYALLEV-ADFELWELEREMNLIQLDP-QVLW 111
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRpDAGTVDLAGVDLH---GLSRRARARRVALVEQdSDTAVPLTVRDVVALGRIPhRSLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 112 -------------------------QPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYF--QHKDG 164
Cdd:TIGR03873 108 agdsphdaavvdralartelshladRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVreLAATG 187
|
170 180
....*....|....*....|....*....
gi 2255859273 165 FIVVS--HDRQFLNQVTDHTLAIEKSQLV 191
Cdd:TIGR03873 188 VTVVAalHDLNLAASYCDHVVVLDGGRVV 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
312-464 |
3.52e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 57.94 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTeqeALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFagQANGELLRPNVKISYVRQNYENNRGTL 391
Cdd:cd03291 40 LFFSNLCLVGA---PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGEL--EPSEGKIKHSGRISFSSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 392 QD---------------FAEANQL--DYSAFLNNLRKLGMERNVfqnqieEMSMGQRKKVELAKSLAQEAELYIWDEPLN 454
Cdd:cd03291 115 KEniifgvsydeyryksVVKACQLeeDITKFPEKDNTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170
....*....|
gi 2255859273 455 YLDVFNQKQL 464
Cdd:cd03291 189 YLDVFTEKEI 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
312-463 |
3.67e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 58.70 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAnGELL---RP--------------- 373
Cdd:PRK09536 4 IDVSDLSVEFGDTTVL-DGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA-GTVLvagDDvealsaraasrrvas 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 374 ---NVKISY---VRQNYENNRGT-LQDFAEANQLDYSAFLNNLRKLGMERnvFQNQ-IEEMSMGQRKKVELAKSLAQEAE 445
Cdd:PRK09536 82 vpqDTSLSFefdVRQVVEMGRTPhRSRFDTWTETDRAAVERAMERTGVAQ--FADRpVTSLSGGERQRVLLARALAQATP 159
|
170
....*....|....*...
gi 2255859273 446 LYIWDEPLNYLDVFNQKQ 463
Cdd:PRK09536 160 VLLLDEPTASLDINHQVR 177
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
309-481 |
4.64e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 309 TQLLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAnGELLR-PNVKISYVRQNYENN 387
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE-GVIKRnGKLRIGYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 388 rGTLqdfaeanQLDYSAFLN---NLRKL----GMER----NVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYL 456
Cdd:PRK09544 80 -TTL-------PLTVNRFLRlrpGTKKEdilpALKRvqagHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180
....*....|....*....|....*....
gi 2255859273 457 DVFNQKQLEDLLLQKQPTM----LIVEHD 481
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRELdcavLMVSHD 180
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
331-485 |
5.97e-09 |
|
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: 58.80 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQANGELLRPNVkiSYVRQNYENNRGTLQD---FAEANQLDY----- 402
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AYVPQQAWIQNDSLREnilFGKALNEKYyqqvl 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 403 --SAFLNNLRKL-GMERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL-----LQKQPT 474
Cdd:TIGR00957 735 eaCALLPDLEILpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpegVLKNKT 814
|
170
....*....|.
gi 2255859273 475 MLIVEHDQTFL 485
Cdd:TIGR00957 815 RILVTHGISYL 825
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
311-481 |
6.11e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 56.63 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELLRPNVKISyvrqNYENNRGT 390
Cdd:PRK11248 1 MLQISHLYADYGGKPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIAG-FVPYQHGSITLDGKPVE----GPGAERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 391 L-QDFA---EANQLDYSAF----------------LNNLRKLGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWD 450
Cdd:PRK11248 75 VfQNEGllpWRNVQDNVAFglqlagvekmqrleiaHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 2255859273 451 EPLNYLDVFNQKQLEDLLLQ------KQptMLIVEHD 481
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKlwqetgKQ--VLLITHD 188
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
311-480 |
7.52e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.13 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALFaplSFEVQRGTIVALTGPNGIGKSSVLHyLLGTFAGQANGELL-------------RPnVKI 377
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRF---DLTVERGERVAILGPSGAGKSTLLN-LIAGFLTPASGSLTlngqdhtttppsrRP-VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 378 SY----------VRQNY-----------ENNRGTLQDFAEanQLDYSAFLNNLRKlgmernvfqnqieEMSMGQRKKVEL 436
Cdd:PRK10771 76 LFqennlfshltVAQNIglglnpglklnAAQREKLHAIAR--QMGIEDLLARLPG-------------QLSGGQRQRVAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2255859273 437 AKSLAQEAELYIWDEPLNYLD-VFNQKQL---EDLLLQKQPTMLIVEH 480
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDpALRQEMLtlvSQVCQERQLTLLMVSH 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
311-481 |
7.59e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 56.62 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAgQANGELLRPNVKISYVRQNYENNRGT 390
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILK-PTSGEVLIKGEPIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 391 L---------QDFAEANQLDYsAF--LN--------------NLRKLGMERnvFQNQI-EEMSMGQRKKVELAKSLAQEA 444
Cdd:PRK13639 80 VgivfqnpddQLFAPTVEEDV-AFgpLNlglskeevekrvkeALKAVGMEG--FENKPpHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2255859273 445 ELYIWDEPLNYLDVFNQKQLEDLL--LQKQP-TMLIVEHD 481
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLydLNKEGiTIIISTHD 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
305-481 |
7.75e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.61 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 305 PSRHTQ--LLKMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAnGELLRPNVKISYVRq 382
Cdd:PRK11247 4 TARLNQgtPLLLNAVSKRYGERTVLNQ-LDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSA-GELLAGTAPLAEAR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 383 nyENNRGTLQDfaeANQLDYSAFLNNLrKLGMERNVFQNQIE----------------EMSMGQRKKVELAKSLAQEAEL 446
Cdd:PRK11247 81 --EDTRLMFQD---ARLLPWKKVIDNV-GLGLKGQWRDAALQalaavgladranewpaALSGGQKQRVALARALIHRPGL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2255859273 447 YIWDEPLNYLDVFN----QKQLEDLLLQKQPTMLIVEHD 481
Cdd:PRK11247 155 LLLDEPLGALDALTriemQDLIESLWQQHGFTVLLVTHD 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
297-488 |
8.49e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 297 DRLTMSYHPSRHtqLLKMENLSLHYteqealfaplsfevqrGTIVALTGPNGIGKSSVLHYLLGT---FAGQAngeLLRP 373
Cdd:TIGR03719 8 NRVSKVVPPKKE--ILKDISLSFFP----------------GAKIGVLGLNGAGKSTLLRIMAGVdkdFNGEA---RPQP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 374 NVKISY------------VRQNYENN----RGTLQDFAEANQLdYSAFLNNLRKLGMERNVFQNQIE-----------EM 426
Cdd:TIGR03719 67 GIKVGYlpqepqldptktVRENVEEGvaeiKDALDRFNEISAK-YAEPDADFDKLAAEQAELQEIIDaadawdldsqlEI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2255859273 427 SM-----------------GQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQTFLKNI 488
Cdd:TIGR03719 146 AMdalrcppwdadvtklsgGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNV 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
329-468 |
8.56e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 329 APLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQA----NGELLR--PNVKISYVR--------------------- 381
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGsiqfAGQPLEawSAAELARHRaylsqqqtppfampvfqyltl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 382 -----QNYENNRGTLQDFAEANQLDysaflnnlRKLGmeRNVFQnqieeMSMGQRKKVELAKSLAQ-------EAELYIW 449
Cdd:PRK03695 93 hqpdkTRTEAVASALNEVAEALGLD--------DKLG--RSVNQ-----LSGGEWQRVRLAAVVLQvwpdinpAGQLLLL 157
|
170
....*....|....*....
gi 2255859273 450 DEPLNYLDVFNQKQLEDLL 468
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLL 176
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-214 |
8.99e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.55 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 11 FGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFPLRPVYFP-----------ATI-SEQ 77
Cdd:PRK13638 7 LWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPLDYSkrgllalrqqvATVfQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 78 DQLTYYALLEvAD--FELWEL---EREMN------LIQLDPQVL-WQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTN 145
Cdd:PRK13638 87 EQQIFYTDID-SDiaFSLRNLgvpEAEITrrvdeaLTLVDAQHFrHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 146 HLDLQGR-QHVA---NYFQHKDGFIVVSHDRQFLNQVTDHTLAIEKSQlVLYQGNFATYEEQKELRDEFELAQ 214
Cdd:PRK13638 166 GLDPAGRtQMIAiirRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQ-ILTHGAPGEVFACTEAMEQAGLTQ 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-180 |
9.05e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.58 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 18 ELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQFPLRPVYFP------------------ATISEQD 78
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlSPPLAGRVLLNGGPLDFQrdsiargllylghapgikTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 79 QLTYYALLEvADFELWELEREMNLIQLDPqvlwQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANY 158
Cdd:cd03231 93 NLRFWHADH-SDEQVEEALARVGLNGFED----RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170 180
....*....|....*....|....
gi 2255859273 159 F-QH-KDGFIVVSHDRQFLNQVTD 180
Cdd:cd03231 168 MaGHcARGGMVVLTTHQDLGLSEA 191
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
312-481 |
1.06e-08 |
|
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: 55.77 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYL-------LGT--FAGQANGEL----LRPnvKIS 378
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrlieptSGEifIDGEDIREQdpveLRR--KIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQN--------YENNRGT---LQDFAEANQLDYSAFLnnLRKLGMERNVFQNQI-EEMSMGQRKKVELAKSLAQEAEL 446
Cdd:cd03295 79 YVIQQiglfphmtVEENIALvpkLLKWPKEKIRERADEL--LALVGLDPAEFADRYpHELSGGQQQRVGVARALAADPPL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 2255859273 447 YIWDEPLNYLDVFNQKQLEDLL--LQKQ--PTMLIVEHD 481
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFkrLQQElgKTIVFVTHD 195
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
331-468 |
1.08e-08 |
|
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: 54.86 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLG-TFAGQANGELL---------RPNVKISYVRQNyennrgtlqDFAEANQ- 399
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVSGEVLingrpldkrSFRKIIGYVPQD---------DILHPTLt 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 400 ----LDYSAflnNLRKLgmernvfqnqieemSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL 468
Cdd:cd03213 99 vretLMFAA---KLRGL--------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-187 |
1.20e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.27 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 18 ELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFPLRPVYFPATISeqdQLTYYA-------LLEVA 89
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLpPAAGTIKLDGGDIDDPDVAE---ACHYLGhrnamkpALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 90 D-FELW---------ELEREMNLIQLDPqVLWQPYQTLSGGEQTKVLLA-LLFTQENFFpLIDEPTNHLDLQGRQHVANY 158
Cdd:PRK13539 92 EnLEFWaaflggeelDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALArLLVSNRPIW-ILDEPTAALDAAAVALFAEL 169
|
170 180 190
....*....|....*....|....*....|.
gi 2255859273 159 FQH--KDGFIVVSHDRQFLNQVTDHTLAIEK 187
Cdd:PRK13539 170 IRAhlAQGGIVIAATHIPLGLPGARELDLGP 200
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
301-481 |
1.42e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.76 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 301 MSYHPSRhtqlLKMENLSLHYTEQeALFAPLSFEVQRGTIVALTGPNGIGKSSVLH-------------YLLGTFAGQ-A 366
Cdd:PRK10253 1 MTESVAR----LRGEQLTLGYGKY-TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRtlsrlmtpahghvWLDGEHIQHyA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 367 NGELLRpnvKISYVRQNYENNRG-TLQD------------FAEANQLDYSAFLNNLRKLGMERNVFQNqIEEMSMGQRKK 433
Cdd:PRK10253 76 SKEVAR---RIGLLAQNATTPGDiTVQElvargryphqplFTRWRKEDEEAVTKAMQATGITHLADQS-VDTLSGGQRQR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 434 VELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQ----KQPTMLIVEHD 481
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSElnreKGYTLAAVLHD 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-196 |
1.50e-08 |
|
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: 55.20 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHL--TFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLL-------GKYAYQG--------------- 59
Cdd:cd03257 2 LEVKNLsvSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILgllkptsGSIIFDGkdllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 60 -EIQF----P---LRPVYfpaTISEQ--DQLTYYALLEVADFELWELEREMNLIQLDPQVLWQ-PYQtLSGGEQTKVLLA 128
Cdd:cd03257 82 kEIQMvfqdPmssLNPRM---TIGEQiaEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHE-LSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 129 L-LFTQENFfpLI-DEPTNHLDLQGRQHVANYF-----QHKDGFIVVSHDRQFLNQVTDHTlaieksqLVLYQGN 196
Cdd:cd03257 158 RaLALNPKL--LIaDEPTSALDVSVQAQILDLLkklqeELGLTLLFITHDLGVVAKIADRV-------AVMYAGK 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
312-483 |
1.64e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 56.23 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQ-ANGelLRP---NvkIS 378
Cdd:COG3839 4 LELENVSKSYGGVEAL-KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGledptsgeiLIGGRdVTD--LPPkdrN--IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQNY---------EN------NRGTLQdfAEANQ--------LDYSAFLNnlRKLGmernvfqnqieEMSMGQRKKVE 435
Cdd:COG3839 79 MVFQSYalyphmtvyENiafplkLRKVPK--AEIDRrvreaaelLGLEDLLD--RKPK-----------QLSGGQRQRVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 436 LAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQ--PTMLIVEHDQT 483
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIkrLHRRlgTTTIYVTHDQV 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-189 |
1.76e-08 |
|
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: 54.54 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 36 LVGRNGRGKTTLLQLLlgKYAYQGEiqFPLR---PVYFPATISEQDQLTYYAL-LEVADFELWELEREMNLI-------Q 104
Cdd:cd03240 27 IVGQNGAGKTTIIEAL--KYALTGE--LPPNskgGAHDPKLIREGEVRAQVKLaFENANGKKYTITRSLAILenvifchQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 105 LDPQV-LWQPYQTLSGGEQTKVLLALLFTQENFFPL------IDEPTNHLDlqgRQHVANYF-------QHKDGF--IVV 168
Cdd:cd03240 103 GESNWpLLDMRGRCSGGEKVLASLIIRLALAETFGSncgilaLDEPTTNLD---EENIEESLaeiieerKSQKNFqlIVI 179
|
170 180
....*....|....*....|.
gi 2255859273 169 SHDRQFLnQVTDHTLAIEKSQ 189
Cdd:cd03240 180 THDEELV-DAADHIYRVEKDG 199
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
311-480 |
1.95e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.17 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYL--LGTfagqangelLRPNV----KISYVRQN- 383
Cdd:PRK14239 5 ILQVSDLSVYYNKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSInrMND---------LNPEVtitgSIVYNGHNi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 384 YENNRGTLQ-------DFAEANQLDYSAFLN---NLRKLGM-ERNVFQNQIEE---------------------MSMGQR 431
Cdd:PRK14239 75 YSPRTDTVDlrkeigmVFQQPNPFPMSIYENvvyGLRLKGIkDKQVLDEAVEKslkgasiwdevkdrlhdsalgLSGGQQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 432 KKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQPTMLIVEH 480
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLlgLKDDYTMLLVTR 205
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-180 |
2.32e-08 |
|
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: 55.07 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 34 LGLVGRNGRGKTTLLQLL-------LGKY-----------AYQG-EIQ--FP------LRPVYFPA---TISEQDQLTYY 83
Cdd:cd03236 29 LGLVGPNGIGKSTALKILagklkpnLGKFddppdwdeildEFRGsELQnyFTkllegdVKVIVKPQyvdLIPKAVKGKVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 84 ALLEVADfELWELEREMNLIQLDPqVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQ--- 160
Cdd:cd03236 109 ELLKKKD-ERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRela 186
|
170 180
....*....|....*....|.
gi 2255859273 161 -HKDGFIVVSHDRQFLNQVTD 180
Cdd:cd03236 187 eDDNYVLVVEHDLAVLDYLSD 207
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
312-482 |
2.73e-08 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 54.65 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQANGELLRPNVKISYVRQ 382
Cdd:cd03296 3 IEVRNVSKRFGDFVAL-DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlerpdsgtiLFGGEDATDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 383 NY---------ENNRGTLQ---DFAEANQLDYSAFLNNLRKLgMERNVFQNQI-EEMSMGQRKKVELAKSLAQEAELYIW 449
Cdd:cd03296 82 HYalfrhmtvfDNVAFGLRvkpRSERPPEAEIRAKVHELLKL-VQLDWLADRYpAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 2255859273 450 DEPLNYLDVFNQKQLEDLLLQKQP----TMLIVEHDQ 482
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQ 197
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-199 |
2.79e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 56.37 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFPLRP--------------- 67
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWdPQQGEILLNGQPiadyseaalrqaisv 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 68 ----VY-FPATISEQDQLtyyALLEVADFELWELEREMNLIQL--DPQVL--W------QpyqtLSGGEQTKVLLALLFT 132
Cdd:PRK11160 419 vsqrVHlFSATLRDNLLL---AAPNASDEALIEVLQQVGLEKLleDDKGLnaWlgeggrQ----LSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 133 QENFFPLIDEPTNHLDLQGRQHV-ANYFQHKDG--FIVVSHDRQFLNQVtDHTLAIEKSQLVLyQGNFAT 199
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQIlELLAEHAQNktVLMITHRLTGLEQF-DRICVMDNGQIIE-QGTHQE 559
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-149 |
3.09e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 55.62 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 1 MSTIKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIQFPLRPVYFP-------- 71
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVL--DGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVEALsaraasrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 72 -ATISEQDQLTY----YALLEV------ADFELWE------LEREMNLIQLDpQVLWQPYQTLSGGEQTKVLLALLFTQE 134
Cdd:PRK09536 79 vASVPQDTSLSFefdvRQVVEMgrtphrSRFDTWTetdraaVERAMERTGVA-QFADRPVTSLSGGERQRVLLARALAQA 157
|
170
....*....|....*
gi 2255859273 135 NFFPLIDEPTNHLDL 149
Cdd:PRK09536 158 TPVLLLDEPTASLDI 172
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
315-485 |
3.27e-08 |
|
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: 54.13 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 315 ENLSLHYTEQEAL-FAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF-------------AGQANGELLRPNvkISYV 380
Cdd:cd03245 6 RNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYkptsgsvlldgtdIRQLDPADLRRN--IGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 381 RQNYENNRGTLQD-------FAEANQLDYSA-------FLNNLRKlGMERnvfqnQIEE----MSMGQRKKVELAKSLAQ 442
Cdd:cd03245 84 PQDVTLFYGTLRDnitlgapLADDERILRAAelagvtdFVNKHPN-GLDL-----QIGErgrgLSGGQRQAVALARALLN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2255859273 443 EAELYIWDEPLNYLDVFNQKQLEDLLLQ--KQPTMLIVEHDQTFL 485
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQllGDKTLIIITHRPSLL 202
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
329-468 |
3.89e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.08 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 329 APLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQanGELL---RPNVKIS---------YVRQN-----------Y- 384
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ--GEILlngRPLSDWSaaelarhraYLSQQqsppfampvfqYl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 385 ----------ENNRGTLQDFAEANQLDysaflnnlRKLGmeRNVFQnqieeMSMGQRKKVELAKSLAQ-------EAELY 447
Cdd:COG4138 91 alhqpagassEAVEQLLAQLAEALGLE--------DKLS--RPLTQ-----LSGGEWQRVRLAAVLLQvwptinpEGQLL 155
|
170 180
....*....|....*....|.
gi 2255859273 448 IWDEPLNYLDVFNQKQLEDLL 468
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLL 176
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-148 |
4.08e-08 |
|
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: 53.81 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 18 ELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGK----YAYQGEIQF---PLRPVYFPATISEQDQ----------- 79
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRveggGTTSGQILFngqPRKPDQFQKCVAYVRQddillpgltvr 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255859273 80 --LTYYALL----EVADFELWELEREMNLIQL-DPQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLD 148
Cdd:cd03234 100 etLTYTAILrlprKSSDAIRKKRVEDVLLRDLaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
312-489 |
4.24e-08 |
|
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: 53.69 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQangELLRPNVKISYVR- 381
Cdd:cd03262 1 IEIKNLHKSFGDFHVL-KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLleepdsgtiIIDGL---KLTDDKKNINELRq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 382 ------QNY---------EN-------NRGTLQDFAEANQLDYsaflnnLRKLGME--RNVFQNQieeMSMGQRKKVELA 437
Cdd:cd03262 77 kvgmvfQQFnlfphltvlENitlapikVKGMSKAEAEERALEL------LEKVGLAdkADAYPAQ---LSGGQQQRVAIA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 438 KSLAQEAELYIWDEPLNYLDVFNQKQLEDL---LLQKQPTMLIVEHDQTFLKNIG 489
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVmkdLAEEGMTMVVVTHEMGFAREVA 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-176 |
4.32e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 20 LFEDANLTIdSSWKLGL-VGRNGRGKTTLLQLLLGKY---AYQGEIQFPLRPVYFPATISEQdqltYYALLEVAD-FELw 94
Cdd:COG2401 45 VLRDLNLEI-EPGEIVLiVGASGSGKSTLLRLLAGALkgtPVAGCVDVPDNQFGREASLIDA----IGRKGDFKDaVEL- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 95 elereMNLIQLDPQVLW-QPYQTLSGGEQTKVLLALLF-TQENFFpLIDEPTNHLDLQGRQHVANYFQ-----HKDGFIV 167
Cdd:COG2401 119 -----LNAVGLSDAVLWlRRFKELSTGQKFRFRLALLLaERPKLL-VIDEFCSHLDRQTAKRVARNLQklarrAGITLVV 192
|
....*....
gi 2255859273 168 VSHDRQFLN 176
Cdd:COG2401 193 ATHHYDVID 201
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
291-480 |
4.57e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.88 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 291 KDLEDVDR-----LTMSYHPSRHTQLLKMENLSLHYTEQ--EALFAPLSFEVQRGTIVALTGPNGIGKSSVLHyLLGTFA 363
Cdd:TIGR00958 453 KVFEYLDRkpnipLTGTLAPLNLEGLIEFQDVSFSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAA-LLQNLY 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 364 GQANGELLRPNV------------KISYVRQNYENNRGTLQD-------FAEANQLDYSAFLNNLRKLGME-RNVFQNQI 423
Cdd:TIGR00958 532 QPTGGQVLLDGVplvqydhhylhrQVALVGQEPVLFSGSVREniaygltDTPDEEIMAAAKAANAHDFIMEfPNGYDTEV 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 424 EE----MSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEH 480
Cdd:TIGR00958 612 GEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
312-360 |
4.62e-08 |
|
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: 53.59 E-value: 4.62e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2255859273 312 LKMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYLLG 360
Cdd:cd03224 1 LEVENLNAGYGKSQILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMG 48
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
312-487 |
5.85e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 55.24 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQ----ANG-ELLRPNVK-----ISYVR 381
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQgslkINGiELRELDPEswrkhLSWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 382 QNYENNRGTLQDF----------AEANQL----DYSAFLNNLrKLGMERNVfQNQIEEMSMGQRKKVELAKSLAQEAELY 447
Cdd:PRK11174 430 QNPQLPHGTLRDNvllgnpdasdEQLQQAlenaWVSEFLPLL-PQGLDTPI-GDQAAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2255859273 448 IWDEPLNYLDVFNQKQLEDLLLQ--KQPTMLIVEHDQTFLKN 487
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTHQLEDLAQ 549
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
311-365 |
6.89e-08 |
|
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: 53.45 E-value: 6.89e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 311 LLKMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQ 365
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGllpprsgsiRFDGE 65
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
331-481 |
6.98e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.06 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHY---LLGTFAGQAN--GELLRPNV----------KISYVRQNYENN---RGTLQ 392
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHfnaLLKPSSGTITiaGYHITPETgnknlkklrkKVSLVFQFPEAQlfeNTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 393 D-------FAEANQLDYSAFLNNLRKLGMERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLE 465
Cdd:PRK13641 106 DvefgpknFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
|
170
....*....|....*....
gi 2255859273 466 DLLLQKQP---TMLIVEHD 481
Cdd:PRK13641 186 QLFKDYQKaghTVILVTHN 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
312-483 |
7.08e-08 |
|
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: 53.03 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTFAG---QANGELLRPNVKISYVRQNYENNR 388
Cdd:cd03301 1 VELENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTT----TLRMIAGleePTSGRIYIGGRDVTDLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 389 GTLQDFA---EANQLDYSAFLNNLRK----------------LGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIW 449
Cdd:cd03301 76 MVFQNYAlypHMTVYDNIAFGLKLRKvpkdeidervrevaelLQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 2255859273 450 DEPLNYLD----VFNQKQLEDLLLQKQPTMLIVEHDQT 483
Cdd:cd03301 155 DEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQV 192
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
312-495 |
7.76e-08 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 52.94 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYteqEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELL-------------RPnvkIS 378
Cdd:TIGR01277 1 LALDKVRYEY---EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAG-FIEPASGSIKvndqshtglapyqRP---VS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQnyENNRGTLQDFAE--ANQLDYSAFLNNLRKLGMERNVFQNQI--------EEMSMGQRKKVELAKSLAQEAELYI 448
Cdd:TIGR01277 74 MLFQ--ENNLFAHLTVRQniGLGLHPGLKLNAEQQEKVVDAAQQVGIadyldrlpEQLSGGQRQRVALARCLVRPNPILL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 449 WDEPLNYLDvfnQKQLEDLLL-------QKQPTMLIVEHDQTFLKNIGAQQIAL 495
Cdd:TIGR01277 152 LDEPFSALD---PLLREEMLAlvkqlcsERQRTLLMVTHHLSDARAIASQIAVV 202
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-186 |
8.11e-08 |
|
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: 52.19 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLfeDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQFPLRPVYFPATIS-EQDQLT 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLN--DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPDSGSILIDGEDLTDLEDELpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 82 YYAlleVADFELW-ELEREMNLIQLdpqvlwqpyqtLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYF- 159
Cdd:cd03229 79 GMV---FQDFALFpHLTVLENIALG-----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLk 144
|
170 180 190
....*....|....*....|....*....|.
gi 2255859273 160 ----QHKDGFIVVSHDRQFLNQVTDHTLAIE 186
Cdd:cd03229 145 slqaQLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-186 |
8.85e-08 |
|
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: 52.19 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 34 LGLVGRNGRGKTTLLQLLLGKYAYQGE-IQFPL-RPVYFPATISeqdqltyyallevadfelweleremnliqldpqvlw 111
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDnDEWDGiTPVYKPQYID------------------------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 112 qpyqtLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQH-----KDGFIVVSHDRQFLNQVTDHTLAIE 186
Cdd:cd03222 72 -----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRlseegKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-155 |
9.14e-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: 53.16 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 20 LFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY--AYQGEIQ-----------FPLRP----------VYFPATIS- 75
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLppTYGNDVRlfgerrggedvWELRKriglvspalqLRFPRDETv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 76 EQ-------DQLTYYALLEVADFEL-WELEREMNLIQL-DpqvlwQPYQTLSGGEQTKVLLA--------LLftqenffp 138
Cdd:COG1119 98 LDvvlsgffDSIGLYREPTDEQRERaRELLELLGLAHLaD-----RPFGTLSQGEQRRVLIAralvkdpeLL-------- 164
|
170
....*....|....*..
gi 2255859273 139 LIDEPTNHLDLQGRQHV 155
Cdd:COG1119 165 ILDEPTAGLDLGARELL 181
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
315-486 |
9.32e-08 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 54.87 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 315 ENLSLHYTEQE--ALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAnGELLRPNV------------KISYV 380
Cdd:TIGR03375 467 RNVSFAYPGQEtpAL-DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTE-GSVLLDGVdirqidpadlrrNIGYV 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 381 RQNYENNRGTLQD--FAEANQLDYSAFLNNLRKLGMERNV------FQNQIEE----MSMGQRKKVELAKSLAQEAELYI 448
Cdd:TIGR03375 545 PQDPRLFYGTLRDniALGAPYADDEEILRAAELAGVTEFVrrhpdgLDMQIGErgrsLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2255859273 449 WDEPLNYLDVFNQKQLEDLL---LQKQpTMLIVEHDQTFLK 486
Cdd:TIGR03375 625 LDEPTSAMDNRSEERFKDRLkrwLAGK-TLVLVTHRTSLLD 664
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-195 |
9.53e-08 |
|
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: 54.52 E-value: 9.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFD----KQVELLfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-----------------------KYA 56
Cdd:COG1123 261 LEVRNLSKRYPvrgkGGVRAV-DDVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsilfdgkdltklsrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 57 YQGEIQ----------FPLRPVYfpATISEqdQLTYYALLEVAdfELWELERE-MNLIQLDPQVL-WQPYQtLSGGEQTK 124
Cdd:COG1123 340 LRRRVQmvfqdpysslNPRMTVG--DIIAE--PLRLHGLLSRA--ERRERVAElLERVGLPPDLAdRYPHE-LSGGQRQR 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2255859273 125 VLLALLFTQEnffP--LI-DEPTNHLDLQGRQHVANYF---QHKDGF--IVVSHDRQFLNQVTDHTlaieksqLVLYQG 195
Cdd:COG1123 413 VAIARALALE---PklLIlDEPTSALDVSVQAQILNLLrdlQRELGLtyLFISHDLAVVRYIADRV-------AVMYDG 481
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-188 |
1.08e-07 |
|
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: 51.39 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 19 LLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQFPL---------RPvYFPATiSEQDQLTYyallev 88
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWpWGSGRIGMPEgedllflpqRP-YLPLG-TLREQLIY------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 89 adfelweleremnliqldPqvlWQpyQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQ-HKDGFIV 167
Cdd:cd03223 87 ------------------P---WD--DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKeLGITVIS 143
|
170 180
....*....|....*....|.
gi 2255859273 168 VSHdRQFLNQVTDHTLAIEKS 188
Cdd:cd03223 144 VGH-RPSLWKFHDRVLDLDGE 163
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-171 |
1.12e-07 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 51.85 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 20 LFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQ-GEIQFP--LRPVY----------FPATISE---------- 76
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTsGTVRRAggARVAYvpqrsevpdsLPLTVRDlvamgrwarr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 77 --QDQLTYYALLEVADfelwELEReMNLIQLDPQvlwqPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQH 154
Cdd:NF040873 87 glWRRLTRDDRAAVDD----ALER-VGLADLAGR----QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180
....*....|....*....|.
gi 2255859273 155 VANYFQ--HKDG--FIVVSHD 171
Cdd:NF040873 158 IIALLAeeHARGatVVVVTHD 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
312-457 |
1.19e-07 |
|
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: 52.20 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGtIVALTGPNGIGKSSVLHyLLGTFAGQANGELLRPNVKISYVRQNYENNRGTL 391
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPG-MYGLLGPNGAGKTTLMR-ILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 392 -QDF-------AEAnQLDYSAFLNN-------------LRKLGMErNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWD 450
Cdd:cd03264 78 pQEFgvypnftVRE-FLDYIAWLKGipskevkarvdevLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
....*..
gi 2255859273 451 EPLNYLD 457
Cdd:cd03264 156 EPTAGLD 162
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
34-193 |
1.23e-07 |
|
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: 52.28 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 34 LGLVGRNGRGKTTLLQLLLGKYA-YQGEIQFPLRPV---------YFPA------TISEQDQLTYYALLevadfelwele 97
Cdd:cd03269 29 FGLLGPNGAGKTTTIRMILGIILpDSGEVLFDGKPLdiaarnrigYLPEerglypKMKVIDQLVYLAQL----------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 98 REMNLIQLDPQVL-W-----------QPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQHKDG- 164
Cdd:cd03269 98 KGLKKEEARRRIDeWlerlelseyanKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARa 177
|
170 180 190
....*....|....*....|....*....|..
gi 2255859273 165 ---FIVVSHDRQFLNQVTDHTLAIEKSQLVLY 193
Cdd:cd03269 178 gktVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-192 |
1.29e-07 |
|
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: 52.22 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQF----------PLR------ 66
Cdd:cd03268 1 LKTNDLTKTYGKKRVL--DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkPDSGEITFdgksyqknieALRrigali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 67 --PVYFPAtISEQDQLTYYA-LLEVADFELWELEREMNLIQLDPqvlwQPYQTLSGGEQTKVLLALLFTQENFFPLIDEP 143
Cdd:cd03268 79 eaPGFYPN-LTARENLRLLArLLGIRKKRIDEVLDVVGLKDSAK----KKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 144 TNHLDLQG----RQHVANYFQHKDGFIVVSHDRQFLNQVTDHTLAIEKSQLVL 192
Cdd:cd03268 154 TNGLDPDGikelRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
301-457 |
1.63e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 301 MSYHPSRHTQLLKMENLSLHYTEqEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF---AGQA--NGELLRPNV 375
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALAFSRNE-EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhveSGQIqiDGKTATRGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 376 KISYVRqnYENNRGTL-QDFAEANQLDYSAFLNNLRKLGMERNVF---------QNQIEEMSMGQRKKVELAKSLAQEAE 445
Cdd:PRK13543 80 RSRFMA--YLGHLPGLkADLSTLENLHFLCGLHGRRAKQMPGSALaivglagyeDTLVRQLSAGQKKRLALARLWLSPAP 157
|
170
....*....|..
gi 2255859273 446 LYIWDEPLNYLD 457
Cdd:PRK13543 158 LWLLDEPYANLD 169
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
321-481 |
1.83e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 321 YTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYL-------------------LGTFAGQANGELLRPNVKISYVR 381
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiydskikvdgkvlyFGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 382 QN-------YENNRGTLQDFAEANQLDYSAFLNN-LRKLGMERNVF---QNQIEEMSMGQRKKVELAKSLAQEAELYIWD 450
Cdd:PRK14246 99 PNpfphlsiYDNIAYPLKSHGIKEKREIKKIVEEcLRKVGLWKEVYdrlNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190
....*....|....*....|....*....|...
gi 2255859273 451 EPLNYLDVFNQKQLEDLL--LQKQPTMLIVEHD 481
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLIteLKNEIAIVIVSHN 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
310-481 |
1.91e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.32 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 310 QLLKMENLSLHYTEQEAL-FAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQA-----NGELLRP-NV-----KI 377
Cdd:PRK13635 4 EIIRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAgtitvGGMVLSEeTVwdvrrQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 378 SYVRQNYENNrgtlqdFAEANQLDYSAFlnNLRKLGMERNVFQNQIEE-----------------MSMGQRKKVELAKSL 440
Cdd:PRK13635 84 GMVFQNPDNQ------FVGATVQDDVAF--GLENIGVPREEMVERVDQalrqvgmedflnrephrLSGGQKQRVAIAGVL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2255859273 441 AQEAELYIWDEPLNYLD-VFNQKQLE---DLLLQKQPTMLIVEHD 481
Cdd:PRK13635 156 ALQPDIIILDEATSMLDpRGRREVLEtvrQLKEQKGITVLSITHD 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
313-481 |
2.01e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 52.30 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 313 KMENLSLHYTEQEAL-FAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQA-------------NGELLRPNVKIs 378
Cdd:PRK13632 9 KVENVSFSYPNSENNaLKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSgeikidgitiskeNLKEIRKKIGI- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 yVRQNYENNrgtlqdFAEANQLDYSAF-LNNLR---------------KLGMErNVFQNQIEEMSMGQRKKVELAKSLAQ 442
Cdd:PRK13632 88 -IFQNPDNQ------FIGATVEDDIAFgLENKKvppkkmkdiiddlakKVGME-DYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2255859273 443 EAELYIWDEPLNYLDVFNQKQLEDLL--LQKQ--PTMLIVEHD 481
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMvdLRKTrkKTLISITHD 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-191 |
2.07e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.10 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 35 GLVGRNGRGKTTLLQLLlGKY--AYQGEIQFPLRPV-------------YFPATISEQDQLTYYALLEVADFElW----- 94
Cdd:PRK10575 41 GLIGHNGSGKSTLLKML-GRHqpPSEGEILLDAQPLeswsskafarkvaYLPQQLPAAEGMTVRELVAIGRYP-Whgalg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 95 --------ELEREMNLIQLDPqVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQ---HKD 163
Cdd:PRK10575 119 rfgaadreKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHrlsQER 197
|
170 180 190
....*....|....*....|....*....|
gi 2255859273 164 GF--IVVSHDRQFLNQVTDHTLAIEKSQLV 191
Cdd:PRK10575 198 GLtvIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
324-457 |
2.49e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.50 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 324 QEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQANGELLRPNVKISYVRQNYENNRGTLQDFAEANQLDYS 403
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVELLNA 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859273 404 AFLNN----LRKlgmernvfqnqIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLD 457
Cdd:COG2401 122 VGLSDavlwLRR-----------FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-148 |
2.77e-07 |
|
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: 51.04 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELlfEDANLTIDSSWkLGLVGRNGRGKTTLLQLLLG-------------------KYAYQGEIQF- 63
Cdd:cd03264 1 LQLENLTKRYGKKRAL--DGVSLTLGPGM-YGLLGPNGAGKTTLMRILATltppssgtiridgqdvlkqPQKLRRRIGYl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 64 PLRPVYFPaTISEQDQLTYYALL-EVADFELW-ELEREMNLIQLDpQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLID 141
Cdd:cd03264 78 PQEFGVYP-NFTVREFLDYIAWLkGIPSKEVKaRVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
....*..
gi 2255859273 142 EPTNHLD 148
Cdd:cd03264 156 EPTAGLD 162
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-176 |
2.88e-07 |
|
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: 50.05 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 15 KQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQ----LLLGKYAYQGEIQFPLRPVYFPAtiseqdqltyyallevad 90
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaiglALGGAQSATRRRSGVKAGCIVAA------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 91 felweleREMNLIQLDPQvlwqpyqtLSGGEQTKVLLALLFTQENFFP----LIDEPTNHLDLQGRQHVANY----FQHK 162
Cdd:cd03227 67 -------VSAELIFTRLQ--------LSGGEKELSALALILALASLKPrplyILDEIDRGLDPRDGQALAEAilehLVKG 131
|
170
....*....|....
gi 2255859273 163 DGFIVVSHDRQFLN 176
Cdd:cd03227 132 AQVIVITHLPELAE 145
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-151 |
2.90e-07 |
|
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: 50.82 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 20 LFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQFPLRPVY------------------FPATISEQDQL 80
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGlLRPDSGEVRWNGTPLAeqrdephenilylghlpgLKPELSALENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 81 TYY-ALLEVADFELWELEREMNLIQLDPqvlwQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQG 151
Cdd:TIGR01189 95 HFWaAIHGGAQRTIEDALAAVGLTGFED----LPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
312-488 |
2.92e-07 |
|
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: 50.99 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtfagqangellrpnvkisyvRQNYENNRGTL 391
Cdd:cd03217 1 LEIKDLHVSVGGKEIL-KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--------------------HPKYEVTEGEI 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 392 QdFAEANQLDYSAFLNNLRKLGMernVFQNQIE---------------EMSMGQRKKVELAKSLAQEAELYIWDEPLNYL 456
Cdd:cd03217 60 L-FKGEDITDLPPEERARLGIFL---AFQYPPEipgvknadflryvneGFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190
....*....|....*....|....*....|....*
gi 2255859273 457 DVFNQKQLEDL---LLQKQPTMLIVEHDQTFLKNI 488
Cdd:cd03217 136 DIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
315-482 |
3.17e-07 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 52.46 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 315 ENLSLHYtEQEALFAPLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTFAG--QA-------NGELLRPNV-----KISYV 380
Cdd:COG1118 6 RNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTT----LLRIIAGleTPdsgrivlNGRDLFTNLpprerRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 381 RQNY---------EN--------------NRGTLQDFAEANQLDysaflnnlrklGMErNVFQNQIeemSMGQRKKVELA 437
Cdd:COG1118 81 FQHYalfphmtvaENiafglrvrppskaeIRARVEELLELVQLE-----------GLA-DRYPSQL---SGGQRQRVALA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2255859273 438 KSLAQEAELYIWDEPLNYLDVFNQKQLEDLL---LQKQP-TMLIVEHDQ 482
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLrrlHDELGgTTVFVTHDQ 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
331-481 |
3.67e-07 |
|
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: 50.76 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQrGTIVALTGPNGIGKSSVLHYLLG---TFAGQA--NGELL---RPNV-------KISYVRQNY---------EN 386
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGlekPDGGTIvlNGTVLfdsRKKInlppqqrKIGLVFQQYalfphlnvrEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 387 --------NRGTLQDFAEAnQLDYsaflnnlrkLGMERNVFQnQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDV 458
Cdd:cd03297 96 lafglkrkRNREDRISVDE-LLDL---------LGLDHLLNR-YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180
....*....|....*....|....*..
gi 2255859273 459 FN----QKQLEDLLLQKQPTMLIVEHD 481
Cdd:cd03297 165 ALrlqlLPELKQIKKNLNIPVIFVTHD 191
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
334-481 |
3.84e-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: 50.26 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 334 EVQRGTIVALTGPNGIGKSSVLHYLLGTfagqangelLRPNvkisyvrqnyennrgtlqdfAEANQLDysaflnnlrklg 413
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQ---------LIPN--------------------GDNDEWD------------ 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 414 MERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQ----KQLEDLLLQKQPTMLIVEHD 481
Cdd:cd03222 60 GITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEEGKKTALVVEHD 131
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-190 |
3.89e-07 |
|
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: 49.91 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIqfplrpvyfpatiseqdqlty 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRV--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 83 yaLLEVADFELWELEremnliQLDPQV--LWQPYQ---------TLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQG 151
Cdd:cd03246 60 --RLDGADISQWDPN------ELGDHVgyLPQDDElfsgsiaenILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2255859273 152 RQHVANYFQHKDGF----IVVSHDRQFLNQVtDHTLAIEKSQL 190
Cdd:cd03246 132 ERALNQAIAALKAAgatrIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
311-452 |
4.19e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.33 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF---AGQ--ANGELLRP-NVK------IS 378
Cdd:COG1129 4 LLEMRGISKSFGGVKALDG-VSLELRPGEVHALLGENGAGKSTLMKILSGVYqpdSGEilLDGEPVRFrSPRdaqaagIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQN---------YEN--------NRGTLQD---FAEANQLdysaflnnLRKLGMERNVFQnQIEEMSMGQRKKVELAK 438
Cdd:COG1129 83 IIHQElnlvpnlsvAENiflgreprRGGLIDWramRRRAREL--------LARLGLDIDPDT-PVGDLSVAQQQLVEIAR 153
|
170
....*....|....
gi 2255859273 439 SLAQEAELYIWDEP 452
Cdd:COG1129 154 ALSRDARVLILDEP 167
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-212 |
5.77e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.78 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 2 STIKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLL-------LGKYAYQGEiqfPL--------- 65
Cdd:PRK11231 1 MTLRTENLTVGYGTKRIL--NDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqSGTVFLGDK---PIsmlssrqla 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 66 RPVYF-------PATISEQD--------QLTYYALLEVADFELweLEREMNLIQLDpQVLWQPYQTLSGGEQTKVLLALL 130
Cdd:PRK11231 76 RRLALlpqhhltPEGITVRElvaygrspWLSLWGRLSAEDNAR--VNQAMEQTRIN-HLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 131 FTQENFFPLIDEPTNHLDLQGRQHVANYFQ--HKDG--FIVVSHDrqfLNQVT---DHTLAIEKSQLVlYQGnfaTYEE- 202
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRelNTQGktVVTVLHD---LNQASrycDHLVVLANGHVM-AQG---TPEEv 225
|
250
....*....|..
gi 2255859273 203 --QKELRDEFEL 212
Cdd:PRK11231 226 mtPGLLRTVFDV 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
334-483 |
5.84e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.57 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 334 EVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELLrpnvkISYVRQNY--ENNRG---TLQDFA---EANQLDYSAF 405
Cdd:PRK11000 25 DIHEGEFVVFVGPSGCGKSTLLRMIAG-LEDITSGDLF-----IGEKRMNDvpPAERGvgmVFQSYAlypHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 406 ---LNNLRKLGMERNVfqNQIEEM--------------SMGQRKKVELAKSLAQEAELYIWDEPLNYLDVF--NQKQLED 466
Cdd:PRK11000 99 glkLAGAKKEEINQRV--NQVAEVlqlahlldrkpkalSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrVQMRIEI 176
|
170
....*....|....*....
gi 2255859273 467 LLLQK--QPTMLIVEHDQT 483
Cdd:PRK11000 177 SRLHKrlGRTMIYVTHDQV 195
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
337-487 |
6.06e-07 |
|
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: 49.28 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 337 RGTIVALTGPNGIGKSSVLHYLLGTFAGQANGELLRPNVKISYvrqnyennrgtlqdfaeanqldYSAFLNnlrklgMER 416
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGC----------------------IVAAVS------AEL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859273 417 NVFQNQIeemSMGQRKKVELAKSLA----QEAELYIWDEPLNYLDVFNQKQLEDL---LLQKQPTMLIVEHDQTFLKN 487
Cdd:cd03227 72 IFTRLQL---SGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAileHLVKGAQVIVITHLPELAEL 146
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
315-481 |
6.28e-07 |
|
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: 50.45 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 315 ENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtfagqangeLLRPN------VKISYVRQNYENNR 388
Cdd:cd03265 4 ENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTT---------LLKPTsgratvAGHDVVREPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 389 G---TLQDFAEANQLdySAFLNNL---RKLGMERNVFQNQIEEM-----------------SMGQRKKVELAKSLAQEAE 445
Cdd:cd03265 74 RigiVFQDLSVDDEL--TGWENLYihaRLYGVPGAERRERIDELldfvglleaadrlvktySGGMRRRLEIARSLVHRPE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2255859273 446 LYIWDEPLNYLDVFNQKQL----EDLLLQKQPTMLIVEHD 481
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVweyiEKLKEEFGMTILLTTHY 191
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-214 |
7.17e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.32 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 25 NLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQGEIQFPLRPV--YFPAT-------ISEQD------------QLTYY 83
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLeaWSAAElarhrayLSQQQtppfampvfqylTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 84 ALLEVADFELwELEREMNLIQLDPQvLWQPYQTLSGGEQTKVLLALLFTQ-------ENFFPLIDEPTNHLDLQgrQHVA 156
Cdd:PRK03695 96 DKTRTEAVAS-ALNEVAEALGLDDK-LGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVA--QQAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 157 NY-----FQHKDGFIVVS-HDrqfLNqvtdHTLAIEKSQLVLYQGNFATYEEQKELRDEFELAQ 214
Cdd:PRK03695 172 LDrllseLCQQGIAVVMSsHD---LN----HTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQ 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
331-482 |
8.11e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 51.24 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQANGELLRPNVKISYVRQNYennrgTLqdFAEANQLD 401
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGlehqtsghiRFHGTDVSRLHARDRKVGFVFQHY-----AL--FRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 402 YSAF----------------------LNNLRKLGMERNVFQNQieeMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVF 459
Cdd:PRK10851 94 NIAFgltvlprrerpnaaaikakvtqLLEMVQLAHLADRYPAQ---LSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180
....*....|....*....|....*..
gi 2255859273 460 NQKQLEDLLLQKQP----TMLIVEHDQ 482
Cdd:PRK10851 171 VRKELRRWLRQLHEelkfTSVFVTHDQ 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
316-497 |
8.56e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.09 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 316 NLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYL--LGTFAGqanGELL-------RPNVKISYVRQN--- 383
Cdd:PRK09493 6 NVSKHFGPTQVLHN-IDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITS---GDLIvdglkvnDPKVDERLIRQEagm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 384 -------------YEN-------NRGTLQDFAEANQLDYsaflnnLRKLGMERNVfQNQIEEMSMGQRKKVELAKSLAQE 443
Cdd:PRK09493 82 vfqqfylfphltaLENvmfgplrVRGASKEEAEKQAREL------LAKVGLAERA-HHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 444 AELYIWDEPLNYLD------VFnqKQLEDlLLQKQPTMLIVEHDQTFLKNIGAQQIALKK 497
Cdd:PRK09493 155 PKLMLFDEPTSALDpelrheVL--KVMQD-LAEEGMTMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-173 |
8.72e-07 |
|
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: 49.93 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQF------PLRPVYFPATISE 76
Cdd:cd03300 1 IELENVSKFYGGFVAL--DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETPTSGEILLdgkditNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 77 QDqltyYAL---LEVAD---FEL-----------WELEREMNLIQLDPQVLWQPYQtLSGGEQTKVLLALLFTQENFFPL 139
Cdd:cd03300 79 QN----YALfphLTVFEniaFGLrlkklpkaeikERVAEALDLVQLEGYANRKPSQ-LSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 2255859273 140 IDEPTNHLDLQGRQHVA---NYFQHKDG--FIVVSHDRQ 173
Cdd:cd03300 154 LDEPLGALDLKLRKDMQlelKRLQKELGitFVFVTHDQE 192
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
312-488 |
1.04e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 49.95 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG-----------TFAGQANGELL-----RPNV 375
Cdd:TIGR01978 1 LKIKDLHVSVEDKEIL-KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsyevtsgtiLFKGQDLLELEpderaRAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 376 KISYvrQNYE-----NNRGTLQDFAEA-------NQLDYSAFLN----NLRKLGM-----ERNVfqNqiEEMSMGQRKKV 434
Cdd:TIGR01978 80 FLAF--QYPEeipgvSNLEFLRSALNArrsargeEPLDLLDFEKllkeKLALLDMdeeflNRSV--N--EGFSGGEKKRN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 435 ELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQ-KQPTM--LIVEHDQTFLKNI 488
Cdd:TIGR01978 154 EILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRlREPDRsfLIITHYQRLLNYI 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
331-495 |
1.08e-06 |
|
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: 49.81 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLGtfagqangeLLRPnvkisyvrqnyenNRGTL----QDFAEANQLDYSAFl 406
Cdd:cd03261 19 VDLDVRRGEILAIIGPSGSGKSTLLRLIVG---------LLRP-------------DSGEVlidgEDISGLSEAELYRL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 407 nnLRKLGM---------ERNVFQN--------------QIE---------------------EMSMGQRKKVELAKSLAQ 442
Cdd:cd03261 76 --RRRMGMlfqsgalfdSLTVFENvafplrehtrlseeEIReivlekleavglrgaedlypaELSGGMKKRVALARALAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 443 EAELYIWDEPLNYLDVFNQKQLEDLL--LQKQP--TMLIVEHDQTFLKNIgAQQIAL 495
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIrsLKKELglTSIMVTHDLDTAFAI-ADRIAV 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
311-481 |
1.09e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.89 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQANGELL------------RPNVKIS 378
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplhaRARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQN---------YENNRGTLQ---DFAEANQLDYSAFLNNLRKLGMERNvfqNQIEEMSMGQRKKVELAKSLAQEAEL 446
Cdd:PRK10895 82 YLPQEasifrrlsvYDNLMAVLQirdDLSAEQREDRANELMEEFHIEHLRD---SMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2255859273 447 YIWDEPLNYLD---VFNQKQLEDLLLQKQPTMLIVEHD 481
Cdd:PRK10895 159 ILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
311-488 |
1.23e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEqealfAPL----SFEVQRGTIVALTGPNGIGKSSVLHYLLGTFA---GQANGEllrPNVKISYVRQN 383
Cdd:PRK11147 3 LISIHGAWLSFSD-----APLldnaELHIEDNERVCLVGRNGAGKSTLMKILNGEVLlddGRIIYE---QDLIVARLQQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 384 YENN-RGTLQDF-----AEANQL--DYSAFLNNLRKLGMERNV-----FQNQIE-------------------------- 424
Cdd:PRK11147 75 PPRNvEGTVYDFvaegiEEQAEYlkRYHDISHLVETDPSEKNLnelakLQEQLDhhnlwqlenrinevlaqlgldpdaal 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 425 -EMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQTFLKNI 488
Cdd:PRK11147 155 sSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNM 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
311-481 |
1.29e-06 |
|
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: 50.84 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALFAP---LSFEVQRGTIVALTGPNGIGKS----SVLHyLLGTFAGQANGELLrpnvkisyvrqn 383
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAvkgVSFDIAAGETLALVGESGSGKSvtalSILR-LLPDPAAHPSGSIL------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 384 yennrgtlqdFAEANQLDYS-AFLNNLR--KLGMernVFQ-------------NQIEE---------------------- 425
Cdd:COG4172 73 ----------FDGQDLLGLSeRELRRIRgnRIAM---IFQepmtslnplhtigKQIAEvlrlhrglsgaaararalelle 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 426 -----------------MSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQPTM--LIVEHD 481
Cdd:COG4172 140 rvgipdperrldayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLkdLQRELGMalLLITHD 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-210 |
1.36e-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: 49.86 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 20 LFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-------KYAYQGEIQF-PLRPVYFPATISEQ-------DQLTYYA 84
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGelepsegKIKHSGRISFsSQFSWIMPGTIKENiifgvsyDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 85 LLEVADFElwelEREMNLIQLDPQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVanyFQHKDG 164
Cdd:cd03291 132 VVKACQLE----EDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI---FESCVC 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2255859273 165 FIVVSHDRQFLNQVTDHtLAIEKSQLVLYQGN---FATYEEQKELRDEF 210
Cdd:cd03291 205 KLMANKTRILVTSKMEH-LKKADKILILHEGSsyfYGTFSELQSLRPDF 252
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
311-480 |
1.58e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.59 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQE-ALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLlgTFAGQAN-GELLRPNVKI----------- 377
Cdd:PRK11160 338 SLTLNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL--TRAWDPQqGEILLNGQPIadyseaalrqa 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 378 -SYVRQNYENNRGTLQD---FAEANQLDySAFLNNLRKLGMERNVFQNQ-----IEE----MSMGQRKKVELAKSLAQEA 444
Cdd:PRK11160 416 iSVVSQRVHLFSATLRDnllLAAPNASD-EALIEVLQQVGLEKLLEDDKglnawLGEggrqLSGGEQRRLGIARALLHDA 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 2255859273 445 ELYIWDEPLNYLDVFNQKQLEDLLLQ--KQPTMLIVEH 480
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEhaQNKTVLMITH 532
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-210 |
1.99e-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: 50.68 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 13 FDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-------KYAYQGEIQF-PLRPVYFPATISEQ------- 77
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGelepsegKIKHSGRISFsPQTSWIMPGTIKDNiifglsy 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 78 DQLTYYALLEVAdfelwELEREMNLI-QLDPQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVa 156
Cdd:TIGR01271 514 DEYRYTSVIKAC-----QLEEDIALFpEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI- 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 157 nyFQHKDGFIVVSHDRQFLNQVTDHTLAIEKSqLVLYQGN---FATYEEQKELRDEF 210
Cdd:TIGR01271 588 --FESCLCKLMSNKTRILVTSKLEHLKKADKI-LLLHEGVcyfYGTFSELQAKRPDF 641
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-193 |
2.06e-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: 48.68 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 21 FEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAY-QGEIQFPLRPVYFPA-TISEQDQLT------YYALL------ 86
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPdSGTVTVRGRVSSLLGlGGGFNPELTgreniyLNGRLlglsrk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 87 -------EVADFElwELEREMNLiqldpqvlwqPYQTLSGGEQTKVLLAL-LFTQENFFpLIDEPTNHLDLQGRQHVANY 158
Cdd:cd03220 118 eidekidEIIEFS--ELGDFIDL----------PVKTYSSGMKARLAFAIaTALEPDIL-LIDEVLAVGDAAFQEKCQRR 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 2255859273 159 FQHKD----GFIVVSHDRQFLNQVTDHTLAIEKSQLVLY 193
Cdd:cd03220 185 LRELLkqgkTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
331-485 |
2.26e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFA-GQANGELLRPNV----KISY-----VRQN------YENNRGTLQDF 394
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELShAETSSVVIRGSVayvpQVSWifnatVRENilfgsdFESERYWRAID 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 395 AEANQLDYSAFL-NNLRKLGmERNVfqnqieEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQ--- 470
Cdd:PLN03232 716 VTALQHDLDLLPgRDLTEIG-ERGV------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKdel 788
|
170
....*....|....*
gi 2255859273 471 KQPTMLIVEHDQTFL 485
Cdd:PLN03232 789 KGKTRVLVTNQLHFL 803
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
310-486 |
2.32e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.13 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 310 QLLKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSvLHYLLGTFAGQANGELLRP-NVKISYVRQNYENNR 388
Cdd:TIGR00954 450 NGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGGRLTKPaKGKLFYVPQRPYMTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 389 GTLQD---------------FAEAnqlDYSAFLNNLrKLG--MERNV----FQNQIEEMSMGQRKKVELAKSLAQEAELY 447
Cdd:TIGR00954 529 GTLRDqiiypdssedmkrrgLSDK---DLEQILDNV-QLThiLEREGgwsaVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*....
gi 2255859273 448 IWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQTFLK 486
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWK 643
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-110 |
3.31e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 49.72 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 3 TIKITHLTFGFDKQvELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQ-GEIQFPLRPVyfpATISEQdqlt 81
Cdd:PRK10790 340 RIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTeGEIRLDGRPL---SSLSHS---- 411
|
90 100
....*....|....*....|....*....
gi 2255859273 82 yyallevadfelwELEREMNLIQLDPQVL 110
Cdd:PRK10790 412 -------------VLRQGVAMVQQDPVVL 427
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
332-452 |
3.47e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 332 SFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAnGEL---------------LRPNVKISYVRQNY-------EN--- 386
Cdd:PRK11288 24 SFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA-GSIlidgqemrfasttaaLAAGVAIIYQELHLvpemtvaENlyl 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255859273 387 ----------NRGTLQDFAEAnqldysaflnNLRKLGMERNVfQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEP 452
Cdd:PRK11288 103 gqlphkggivNRRLLNYEARE----------QLEHLGVDIDP-DTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
309-481 |
3.58e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.45 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 309 TQLLKMENLSLHYTeqeALFA--PLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELL--------RPNVKIS 378
Cdd:PRK11300 3 QPLLSVSGLMMRFG---GLLAvnNVNLEVREQEIVSLIGPNGAGKTTVFNCLTG-FYKPTGGTILlrgqhiegLPGHQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 ---YVR--QN---------YEN---------NRGTLQDF--------AEANQLDYSAFLnnLRKLGMeRNVFQNQIEEMS 427
Cdd:PRK11300 79 rmgVVRtfQHvrlfremtvIENllvaqhqqlKTGLFSGLlktpafrrAESEALDRAATW--LERVGL-LEHANRQAGNLA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859273 428 MGQRKKVELAKSLAQEAELYIWDEP---LNYLDVFNQKQLEDLLL-QKQPTMLIVEHD 481
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPaagLNPKETKELDELIAELRnEHNVTVLLIEHD 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-215 |
3.81e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.46 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 25 NLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQGEIQF---PLR-----------------PVYFPATISE-------- 76
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKIngiELReldpeswrkhlswvgqnPQLPHGTLRDnvllgnpd 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 77 --QDQLtyYALLEVADfeLWELEREMNLiQLDPQVLWQPyQTLSGGEQTKVLLA-LLFTQENFFpLIDEPTNHLDLQGRQ 153
Cdd:PRK11174 450 asDEQL--QQALENAW--VSEFLPLLPQ-GLDTPIGDQA-AGLSVGQAQRLALArALLQPCQLL-LLDEPTASLDAHSEQ 522
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 154 HVANYFQ---HKDGFIVVSHDRQFLNQVtDHTLAIEKSQLVlYQGNFATYEEQKELRDEFeLAQN 215
Cdd:PRK11174 523 LVMQALNaasRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIV-QQGDYAELSQAGGLFATL-LAHR 584
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
309-457 |
4.15e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 48.65 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 309 TQLLKMENLSLHYTEQeALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAN-----GELL-----RPNVKIS 378
Cdd:PRK13537 5 VAPIDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsislcGEPVpsrarHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQnYEN------NRGTLQDFAEANQLDYS---AFLNNLRKLGMERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIW 449
Cdd:PRK13537 84 VVPQ-FDNldpdftVRENLLVFGRYFGLSAAaarALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
....*...
gi 2255859273 450 DEPLNYLD 457
Cdd:PRK13537 163 DEPTTGLD 170
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
331-481 |
4.55e-06 |
|
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: 47.50 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLGTF---AGQA--NGELLRPNVK-----ISYVRQNyennrGTLQDFAEANQ- 399
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELrptSGTAyiNGYSIRTDRKaarqsLGYCPQF-----DALFDELTVREh 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 400 LDYSAFLNNLRKLGMERNV-----------FQN-QIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDL 467
Cdd:cd03263 96 LRFYARLKGLPKSEIKEEVelllrvlgltdKANkRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDL 175
|
170
....*....|....*.
gi 2255859273 468 LL--QKQPTMLIVEHD 481
Cdd:cd03263 176 ILevRKGRSIILTTHS 191
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-157 |
5.38e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.11 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 19 LLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQFPLRPvyfpatISEQDQLTYYALlevadfeLW--- 94
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlARPDAGEVLWQGEP------IRRQRDEYHQDL-------LYlgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 95 ------ELEREMNLI-------QLDPQVLWQ-------------PYQTLSGGEQTKVLLA-LLFTQEnffPL--IDEPTN 145
Cdd:PRK13538 82 qpgiktELTALENLRfyqrlhgPGDDEALWEalaqvglagfedvPVRQLSAGQQRRVALArLWLTRA---PLwiLDEPFT 158
|
170 180
....*....|....*....|
gi 2255859273 146 HLDLQG--------RQHVAN 157
Cdd:PRK13538 159 AIDKQGvarleallAQHAEQ 178
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
315-481 |
6.11e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.87 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 315 ENLSLHYTE-QEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQANGE---------LLRPNV-----KISY 379
Cdd:PRK13640 9 KHVSFTYPDsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNskitvdgitLTAKTVwdireKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 380 VRQNYENNrgtlqdFAEANQLDYSAFlnNLRKLGMERN----VFQNQIEEMSM-------------GQRKKVELAKSLAQ 442
Cdd:PRK13640 89 VFQNPDNQ------FVGATVGDDVAF--GLENRAVPRPemikIVRDVLADVGMldyidsepanlsgGQKQRVAIAGILAV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2255859273 443 EAELYIWDEPLNYLDVFNQKQLEDLLLQ----KQPTMLIVEHD 481
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKlkkkNNLTVISITHD 203
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
311-472 |
7.12e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.48 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALF--------APLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAnGELLRPNVKISYVRQ 382
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS-GELLIDDHPLHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 383 NYENN--RGTLQDFAEA--------NQLDYSAFLNN--------------LRKLGMERNVFQNQIEEMSMGQRKKVELAK 438
Cdd:PRK15112 83 SYRSQriRMIFQDPSTSlnprqrisQILDFPLRLNTdlepeqrekqiietLRQVGLLPDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190
....*....|....*....|....*....|....
gi 2255859273 439 SLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQ 472
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQ 196
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
305-469 |
7.29e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 305 PSRHTQLLKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQaNGELLRPNvKISYVRQNY 384
Cdd:PTZ00243 653 SERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS-EGRVWAER-SIAYVPQQA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 385 ---------------ENNRGTLQDFAEANQLDysaflNNLRKL--GMERNVFQNQIEeMSMGQRKKVELAKSLAQEAELY 447
Cdd:PTZ00243 731 wimnatvrgnilffdEEDAARLADAVRVSQLE-----ADLAQLggGLETEIGEKGVN-LSGGQKARVSLARAVYANRDVY 804
|
170 180
....*....|....*....|...
gi 2255859273 448 IWDEPLNYLDV-FNQKQLEDLLL 469
Cdd:PTZ00243 805 LLDDPLSALDAhVGERVVEECFL 827
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
311-481 |
7.95e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 47.80 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALFAP----------LSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQ----AN 367
Cdd:COG4608 7 LLEVRDLKKHFPVRGGLFGRtvgvvkavdgVSFDIRRGETLGLVGESGCGKSTLGRLLLRleeptsgeiLFDGQditgLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 368 GELLRP-NVKISYVRQN-YE--NNRGTLQD-FAE----------ANQLDYSAFLnnLRKLGMERNVFQNQIEEMSMGQRK 432
Cdd:COG4608 87 GRELRPlRRRMQMVFQDpYAslNPRMTVGDiIAEplrihglaskAERRERVAEL--LELVGLRPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 433 KVELAKSLAQEAELYIWDEPLNYLDVFNQKQ----LEDllLQKQ--PTMLIVEHD 481
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQvlnlLED--LQDElgLTYLFISHD 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
310-451 |
8.04e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 310 QLLKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQAnGELLRPNVKISyvRQNYENNR- 388
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-GEILLDGKPVT--AEQPEDYRk 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 389 ---GTLQDF-----------AEANQLDYSAFLNNL---RKLGMERNVFQNQieEMSMGQRKKVELAKSLAQEAELYIWDE 451
Cdd:PRK10522 398 lfsAVFTDFhlfdqllgpegKPANPALVEKWLERLkmaHKLELEDGRISNL--KLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-190 |
8.14e-06 |
|
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: 47.02 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 23 DANLTIDSSWKLGLVGRNGRGKTTLLQLLLGK-------------------------------YAYQGEIQFPLRPVY-- 69
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEelptsgtirvngqdvsdlrgraipylrrkigVVFQDFRLLPDRNVYen 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 70 --FPATISEQD----QLTYYALLEVADFElwELEREMnliqldpqvlwqPYQtLSGGEQTKVLLALLFTQENFFPLIDEP 143
Cdd:cd03292 99 vaFALEVTGVPpreiRKRVPAALELVGLS--HKHRAL------------PAE-LSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 144 TNHLDLQGRQHVANYFQ--HKDGFIVV--SHDRQFLNQVTDHTLAIEKSQL 190
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKkiNKAGTTVVvaTHAKELVDTTRHRVIALERGKL 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
331-483 |
8.66e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.79 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLG---TFAGQA--NGELLR----PNVKISYVRQNY---------ENNRGTL- 391
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlekPTEGQIfiDGEDVThrsiQQRDICMVFQSYalfphmslgENVGYGLk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 392 ----------QDFAEANQL-DYSAFlnnlrklgmeRNVFQNQIeemSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFN 460
Cdd:PRK11432 105 mlgvpkeerkQRVKEALELvDLAGF----------EDRYVDQI---SGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180
....*....|....*....|....*..
gi 2255859273 461 QKQLEDLL--LQKQ--PTMLIVEHDQT 483
Cdd:PRK11432 172 RRSMREKIreLQQQfnITSLYVTHDQS 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-183 |
8.84e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.03 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 1 MST-IKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIQFP--LRPVYFPATISE 76
Cdd:PRK09544 1 MTSlVSLENVSVSFGQRRVL--SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIKRNgkLRIGYVPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 77 QDQLTyyalLEVADFelweleremnlIQLDPQV-----------------LWQPYQTLSGGEQTKVLLALLFTQENFFPL 139
Cdd:PRK09544 79 DTTLP----LTVNRF-----------LRLRPGTkkedilpalkrvqaghlIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 140 IDEPTNHLDLQGRqhVANY-----FQHKDGFIV--VSHDRQFLNQVTDHTL 183
Cdd:PRK09544 144 LDEPTQGVDVNGQ--VALYdlidqLRRELDCAVlmVSHDLHLVMAKTDEVL 192
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
331-488 |
9.07e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 46.98 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLG------TfAGQA--NGELL-------R---------------PNVKISY- 379
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkyevT-SGSIllDGEDIlelspdeRaragiflafqypveiPGVSVSNf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 380 VRQNYENNRGTLQDFAEANQLdysaFLNNLRKLGM-----ERNVfqNqiEEMSMGQRKKVELAKSLAQEAELYIWDEPLN 454
Cdd:COG0396 98 LRTALNARRGEELSAREFLKL----LKEKMKELGLdedflDRYV--N--EGFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2255859273 455 YLDV---------FNQkqledlLLQKQPTMLIVEHDQTFLKNI 488
Cdd:COG0396 170 GLDIdalrivaegVNK------LRSPDRGILIITHYQRILDYI 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
308-481 |
1.18e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 308 HTQLLKMENLSL---HYTEQEALFAPLSFEVQRGTIVALTGPNGIGKS----SVLH--------YLLGT--FAGQ----A 366
Cdd:PRK15134 2 TQPLLAIENLSVafrQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRllpsppvvYPSGDirFHGEsllhA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 367 NGELLR-------------PNVKI----SYVRQNYEN---NRGTLQDFAEA---NQLDYSAFLNNLRKLgmerNVFQNQi 423
Cdd:PRK15134 82 SEQTLRgvrgnkiamifqePMVSLnplhTLEKQLYEVlslHRGMRREAARGeilNCLDRVGIRQAAKRL----TDYPHQ- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 424 eeMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQPTM--LIVEHD 481
Cdd:PRK15134 157 --LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMglLFITHN 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
290-483 |
1.35e-05 |
|
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: 46.31 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 290 LKDLEDVDRLTMSYHPSRHTQLLKmenlslhyteqealfaPLSFEVQRGTIVALTGPNGIGKSSVLHyLLGTFAGQANGE 369
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRPDTLVLQ----------------DVSFTLHPGEVTALVGPSGSGKSTVVA-LLENFYQPQGGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 370 LL---RP---------NVKISYVRQNYENNRGTLQD-------------FAEANQLDYSAFLNNLRKLGMERNVFQNQiE 424
Cdd:cd03248 71 VLldgKPisqyehkylHSKVSLVGQEPVLFARSLQDniayglqscsfecVKEAAQKAHAHSFISELASGYDTEVGEKG-S 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 425 EMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL---LQKQPTMLIVEHDQT 483
Cdd:cd03248 150 QLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALydwPERRTVLVIAHRLST 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-148 |
1.53e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 47.14 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEI--------QFP--LRPV---- 68
Cdd:PRK11607 20 LEIRNLTKSFDGQHAV--DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQImldgvdlsHVPpyQRPInmmf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 69 ----YFPATISE--------QDQLtyyALLEVADfelwELEREMNLIQLDPQVLWQPYQtLSGGEQTKVLLALLFTQENF 136
Cdd:PRK11607 98 qsyaLFPHMTVEqniafglkQDKL---PKAEIAS----RVNEMLGLVHMQEFAKRKPHQ-LSGGQRQRVALARSLAKRPK 169
|
170
....*....|..
gi 2255859273 137 FPLIDEPTNHLD 148
Cdd:PRK11607 170 LLLLDEPMGALD 181
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-206 |
1.78e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.54 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLF---EDANLTIDSSWKLGLVGRNGRGKTTLLQL------------LLGKYAYQGEI------- 61
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliisetgqtIVGDYAIPANLkkikevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 62 ----------QFPL---------RPVYF-PATISEQDQLTYYALLEVADfeLWELEREMnliqldpqVLWQPYQtLSGGE 121
Cdd:PRK13645 87 rlrkeiglvfQFPEyqlfqetieKDIAFgPVNLGENKQEAYKKVPELLK--LVQLPEDY--------VKRSPFE-LSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 122 QTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYF-----QHKDGFIVVSHDRQFLNQVTDHTLAIEKSQLVLYQGN 196
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
250
....*....|
gi 2255859273 197 FATYEEQKEL 206
Cdd:PRK13645 236 FEIFSNQELL 245
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
411-488 |
2.08e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 46.62 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 411 KLGMERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTM---LI-VEHDQTFLK 486
Cdd:PRK15079 147 KVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglsLIfIAHDLAVVK 226
|
..
gi 2255859273 487 NI 488
Cdd:PRK15079 227 HI 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-174 |
2.25e-05 |
|
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: 45.56 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLF--EDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG--KyAYQGEI------------------ 61
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldR-PTSGEVrvdgtdisklsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 62 ----------QFPLRP-------VYFPATIS----EQDQLTYYALLEVADfelweLEREMNliqldpqvlwQPYQTLSGG 120
Cdd:cd03255 80 rrrhigfvfqSFNLLPdltalenVELPLLLAgvpkKERRERAEELLERVG-----LGDRLN----------HYPSELSGG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 121 EQTKVLLALLFTQEnffPLI---DEPTNHLDLQGRQHVANYFQ---HKDG--FIVVSHDRQF 174
Cdd:cd03255 145 QQQRVAIARALAND---PKIilaDEPTGNLDSETGKEVMELLRelnKEAGttIVVVTHDPEL 203
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
312-478 |
2.32e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.06 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLH--------YLLGTFAGQA--NGE--------LLRP 373
Cdd:PRK14247 4 IEIRDLKVSFGQVEVL-DGVNLEIPDNTITALMGPSGSGKSTLLRvfnrlielYPEARVSGEVylDGQdifkmdviELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 374 NVKISYVRQNYENNRGTLQDFAEANQLDysAFLNNLRKL------GMERNVFQNQIEE--------MSMGQRKKVELAKS 439
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLN--RLVKSKKELqervrwALEKAQLWDEVKDrldapagkLSGGQQQRLCIARA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 2255859273 440 LAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIV 478
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIV 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-191 |
2.43e-05 |
|
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: 45.20 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQFPLRPVYFPATISE------ 76
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDSGEILIDGRDVTGVPPERRnigmvf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 77 QDqltyYAL---LEVAD---FELWEL--------EREMNLIQ---LDPQVLWQPYQtLSGGEQTKVLLA--------LLf 131
Cdd:cd03259 79 QD----YALfphLTVAEniaFGLKLRgvpkaeirARVRELLElvgLEGLLNRYPHE-LSGGQQQRVALAralarepsLL- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 132 tqenffpLIDEPTNHLDLQGRQ----HVANYF-QHKDGFIVVSHDRQFLNQVTDHTLAIEKSQLV 191
Cdd:cd03259 153 -------LLDEPLSALDAKLREelreELKELQrELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
116-180 |
2.44e-05 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 46.72 E-value: 2.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 116 TLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQH-----KDGFIVVSHDRQFLNQVTD 180
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKareemEQTFIIVSHDMDFVLDVCD 496
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
311-481 |
2.93e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALFAP---LSFEVQRGTIVALTGPNGIGKS-SVLHYL-LGTFAGQANGELLRPN----VKISyvr 381
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAvdrISYSVKQGEVVGIVGESGSGKSvSSLAIMgLIDYPGRVMAEKLEFNgqdlQRIS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 382 qnyENNRGTL--QDFAEANQlDYSAFLNNLRKLG---ME----------RNVFQNQIE-------------------EMS 427
Cdd:PRK11022 80 ---EKERRNLvgAEVAMIFQ-DPMTSLNPCYTVGfqiMEaikvhqggnkKTRRQRAIDllnqvgipdpasrldvyphQLS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859273 428 MGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQPTM--LIVEHD 481
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLleLQQKENMalVLITHD 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
312-480 |
3.01e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 46.70 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG---------TFAGQ----ANGELLRPNvkIS 378
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfydptsgriLIDGVdirdLTLESLRRQ--IG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQN--------YEN--------NRGTLQDFAEANQLDysAFLNNLRK-----LGmERNVfqnqieEMSMGQRKKVELA 437
Cdd:COG1132 418 VVPQDtflfsgtiRENirygrpdaTDEEVEEAAKAAQAH--EFIEALPDgydtvVG-ERGV------NLSGGQRQRIAIA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2255859273 438 KSLAQEAELYIWDEPLNYLDVFN----QKQLEDLLlqKQPTMLIVEH 480
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETealiQEALERLM--KGRTTIVIAH 533
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
311-457 |
3.23e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.94 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQeALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtfagqangeLLRPNV-KISYVRQNYENNRG 389
Cdd:PRK13540 1 MLDVIELDFDYHDQ-PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG---------LLNPEKgEILFERQSIKKDLC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 390 TLQdfaeaNQLDYSAFLNNLR-KLGMERNVFQN--------QIEE-----------------MSMGQRKKVELAKSLAQE 443
Cdd:PRK13540 71 TYQ-----KQLCFVGHRSGINpYLTLRENCLYDihfspgavGITElcrlfslehlidypcglLSSGQKRQVALLRLWMSK 145
|
170
....*....|....
gi 2255859273 444 AELYIWDEPLNYLD 457
Cdd:PRK13540 146 AKLWLLDEPLVALD 159
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
345-488 |
3.42e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 345 GPNGIGKSSVLHYLLGT---FAGQAngeLLRPNVKISY------------VRQNYENN----RGTLQDFAEANQLdYSAF 405
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVdkeFEGEA---RPAPGIKVGYlpqepqldpektVRENVEEGvaevKAALDRFNEIYAA-YAEP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 406 LNNLRKLGMERNVFQNQIE-----------EMSM-----------------GQRKKVELAKSLAQEAELYIWDEPLNYLD 457
Cdd:PRK11819 116 DADFDALAAEQGELQEIIDaadawdldsqlEIAMdalrcppwdakvtklsgGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
170 180 190
....*....|....*....|....*....|.
gi 2255859273 458 VFNQKQLEDLLLQKQPTMLIVEHDQTFLKNI 488
Cdd:PRK11819 196 AESVAWLEQFLHDYPGTVVAVTHDRYFLDNV 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
409-497 |
3.55e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 45.35 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 409 LRKLGMERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLD---VFNQKQLEDLLLQKQPTMLIVEHDQTFL 485
Cdd:PRK10619 136 LAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFA 215
|
90
....*....|..
gi 2255859273 486 KNIGAQQIALKK 497
Cdd:PRK10619 216 RHVSSHVIFLHQ 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
296-488 |
3.69e-05 |
|
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: 44.83 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 296 VDRLTMSYH-PSRHTQLLKMENLSLHYTEQEALFA--PLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTFAGqangeLLR 372
Cdd:cd03220 3 LENVSKSYPtYKGGSSSLKKLGILGRKGEVGEFWAlkDVSFEVPRGERIGLIGRNGAGKST----LLRLLAG-----IYP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 373 PN---VKIsyvrqnyennRGTLqdfaeANQLDYSAFLN-------NLRKLGMERNVFQNQIEEM---------------- 426
Cdd:cd03220 74 PDsgtVTV----------RGRV-----SSLLGLGGGFNpeltgreNIYLNGRLLGLSRKEIDEKideiiefselgdfidl 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 427 -----SMGQRKKVELAKSLAQEAELYIWDEPLNYLDV-FNQKQLEDL--LLQKQPTMLIVEHDQTFLKNI 488
Cdd:cd03220 139 pvktySSGMKARLAFAIATALEPDILLIDEVLAVGDAaFQEKCQRRLreLLKQGKTVILVSHDPSSIKRL 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-61 |
4.04e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 46.31 E-value: 4.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 8 HLTFGFDKQVELLfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEI 61
Cdd:COG1132 344 NVSFSYPGDRPVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdPTSGRI 397
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-155 |
4.16e-05 |
|
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: 44.79 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEI--------QFPLR-------- 66
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSIlidgvdisKIGLHdlrsrisi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 67 ----PVYFPATISEQ-DQLTYYallevADFELWE-LERemnlIQLDPQVLWQPYQ----------TLSGGEQTKVLLALL 130
Cdd:cd03244 83 ipqdPVLFSGTIRSNlDPFGEY-----SDEELWQaLER----VGLKEFVESLPGGldtvveeggeNLSVGQRQLLCLARA 153
|
170 180
....*....|....*....|....*
gi 2255859273 131 FTQENFFPLIDEPTNHLDLQGRQHV 155
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALI 178
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
331-458 |
4.23e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSVLHYLLGT---FAGQA--NGELLRPN-----VK--ISYVRQNYENNrGTLQDFAEAN 398
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVdkrAGGEIrlNGKDISPRspldaVKkgMAYITESRRDN-GFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 399 QLDYSAFLNNLRKLG--------MERNVFQNQ--------------IEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYL 456
Cdd:PRK09700 361 NMAISRSLKDGGYKGamglfhevDEQRTAENQrellalkchsvnqnITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGI 440
|
..
gi 2255859273 457 DV 458
Cdd:PRK09700 441 DV 442
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-192 |
4.58e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 45.42 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 1 MStIKITHLTFGFDKQVEllFE-----DANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEI------------- 61
Cdd:PRK13637 1 MS-IKIENLTHIYMEGTP--FEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLkPTSGKIiidgvditdkkvk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 62 ------------QFPLRPVyFPATIsEQDQLTYYALLEVADFELWE-LEREMNLIQLDPQVL--WQPYQtLSGGEQTKVL 126
Cdd:PRK13637 78 lsdirkkvglvfQYPEYQL-FEETI-EKDIAFGPINLGLSEEEIENrVKRAMNIVGLDYEDYkdKSPFE-LSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 127 LALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQ--HKD---GFIVVSHDRQFLNQVTDHTLAIEKSQLVL 192
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKelHKEynmTIILVSHSMEDVAKLADRIIVMNKGKCEL 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-178 |
4.70e-05 |
|
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: 44.44 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKqVELLfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAY---QGEIQFPLRPVYFpATISEQDQ- 79
Cdd:cd03217 1 LEIKDLHVSVGG-KEIL-KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevtEGEILFKGEDITD-LPPEERARl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 80 ---LTYYALLEVADFELWELEREMNliqldpqvlwqpyQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVA 156
Cdd:cd03217 78 gifLAFQYPPEIPGVKNADFLRYVN-------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180
....*....|....*....|....*.
gi 2255859273 157 NYFQH----KDGFIVVSHDRQFLNQV 178
Cdd:cd03217 145 EVINKlreeGKSVLIITHYQRLLDYI 170
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
332-452 |
4.84e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.79 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 332 SFEVQRGTIVALTGPNGIGKS---SVL--HYllgtfagQA-------NGELLR---PNVKISY----------------V 380
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKStlmKILygLY-------QPdsgeiliDGKPVRirsPRDAIALgigmvhqhfmlvpnltV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 381 RQN----YENNRGTLQDFAEANQLdysaflnnLRKLgMERNVFQ----NQIEEMSMGQRKKVELAKSLAQEAELYIWDEP 452
Cdd:COG3845 98 AENivlgLEPTKGGRLDRKAARAR--------IREL-SERYGLDvdpdAKVEDLSVGEQQRVEILKALYRGARILILDEP 168
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
183-240 |
4.92e-05 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 41.79 E-value: 4.92e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 183 LAIEKSQLVLYQGNFATYEEQKELRDEFELAQNRKIKKEVSRLK------RTAAEKAEWSRSRE 240
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEefidrfRAKASKAKQAQSRI 64
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
5.12e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.08 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLF---EDANLTIDSSWKLGLVGRNGRGKTTLLQ----LLLGKyayQGEIQFPL----------- 65
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkalDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnaLLLPD---TGTIEWIFkdeknkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 66 ---------------RPVYFPATISEQD----QLTYYALLE---------------VADFELWELEREM-NLIQLDPQVL 110
Cdd:PRK13651 80 kekvleklviqktrfKKIKKIKEIRRRVgvvfQFAEYQLFEqtiekdiifgpvsmgVSKEEAKKRAAKYiELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 111 WQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQ--HKDG--FIVVSHDRQFLNQVTDHTLAIE 186
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDnlNKQGktIILVTHDLDNVLEWTKRTIFFK 239
|
250 260
....*....|....*....|....*....
gi 2255859273 187 KSQLVlYQGNfaTYEeqkELRDEFELAQN 215
Cdd:PRK13651 240 DGKII-KDGD--TYD---ILSDNKFLIEN 262
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
298-497 |
5.13e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 298 RLTMSYHPSRHTQLLKMENLSLHYTE-QEALFAPL---SFEVQRGTIVALTGPNGIGKSS-VLHY--LLGTFAGQANGEL 370
Cdd:PRK13631 8 KKLKVPNPLSDDIILRVKNLYCVFDEkQENELVALnniSYTFEKNKIYFIIGNSGSGKSTlVTHFngLIKSKYGTIQVGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 371 LRPNVKISYVRQNYENNRGTLQDFAEANQL--------DYSAFLNNLRK--------LG--------------------- 413
Cdd:PRK13631 88 IYIGDKKNNHELITNPYSKKIKNFKELRRRvsmvfqfpEYQLFKDTIEKdimfgpvaLGvkkseakklakfylnkmgldd 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 414 --MERNVFqnqieEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLL---QKQPTMLIVEHDQTFLKNI 488
Cdd:PRK13631 168 syLERSPF-----GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILdakANNKTVFVITHTMEHVLEV 242
|
....*....
gi 2255859273 489 GAQQIALKK 497
Cdd:PRK13631 243 ADEVIVMDK 251
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
304-481 |
5.72e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.77 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 304 HPSRHTQ-LLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVL------HYLLGTFAGQA-----NGELL 371
Cdd:PRK14243 2 STLNGTEtVLRTENLNVYYGSFLAV-KNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVEGkvtfhGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 372 RPNVKISYVRQN---------------YENnrgtlqdFAEANQLD-YSAFLNNLRKLGMERNVFQNQIEE--------MS 427
Cdd:PRK14243 81 APDVDPVEVRRRigmvfqkpnpfpksiYDN-------IAYGARINgYKGDMDELVERSLRQAALWDEVKDklkqsglsLS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2255859273 428 MGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQPTMLIVEHD 481
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMheLKEQYTIIIVTHN 209
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-177 |
6.05e-05 |
|
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: 43.85 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 23 DANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQGEIQFPlrPVYFPATISEQDQLTyyALLEVAdfelwelereMNL 102
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFL--PKFSRNKLIFIDQLQ--FLIDVG----------LGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 103 IQLDpqvlwQPYQTLSGGEQTKVLLAlLFTQENFFP---LIDEPTNHLDLQGRQHVANYF----QHKDGFIVVSHDRQFL 175
Cdd:cd03238 79 LTLG-----QKLSTLSGGELQRVKLA-SELFSEPPGtlfILDEPSTGLHQQDINQLLEVIkgliDLGNTVILIEHNLDVL 152
|
..
gi 2255859273 176 NQ 177
Cdd:cd03238 153 SS 154
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
342-470 |
6.09e-05 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 43.84 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 342 ALTGPNGIGKSSVLHYLLGTFAGQANGelLRPNVKisyVRQNYENNRgtlqdfAEANQLDYSAFLNNLRKLgmernVFQN 421
Cdd:cd03239 26 AIVGPNGSGKSNIVDAICFVLGGKAAK--LRRGSL---LFLAGGGVK------AGINSASVEITFDKSYFL-----VLQG 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 422 QIEEM-SMGQRKKVELAKSLA----QEAELYIWDEPLNYLDVFNQKQLEDLLLQ 470
Cdd:cd03239 90 KVEQIlSGGEKSLSALALIFAlqeiKPSPFYVLDEIDAALDPTNRRRVSDMIKE 143
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-186 |
6.62e-05 |
|
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: 44.00 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDK---QVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGK-YAYQGEIQFPLRPVYFP-------A 72
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGElEKLSGSVSVPGSIAYVSqepwiqnG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 73 TI-------SEQDQLTYYALLEV----ADFELWEL-------EREMNliqldpqvlwqpyqtLSGGEQTKVLLALLFTQE 134
Cdd:cd03250 81 TIrenilfgKPFDEERYEKVIKAcalePDLEILPDgdlteigEKGIN---------------LSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 135 NFFPLIDEPTNHLDlqgrQHVANY-FQH------KDG--FIVVSHDRQFLNQVtDHTLAIE 186
Cdd:cd03250 146 ADIYLLDDPLSAVD----AHVGRHiFENcilgllLNNktRILVTHQLQLLPHA-DQIVVLD 201
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
340-489 |
6.66e-05 |
|
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: 44.14 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 340 IVALTGPNGIGKSSVLHYLL----GTFAGQANG-----ELLRPNVKISYVRQNYENNRGTL----QDFaeaNQLDYSAFL 406
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELPPNSKGgahdpKLIREGEVRAQVKLAFENANGKKytitRSL---AILENVIFC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 407 N--NLRKLGMErnvfqnQIEEMSMGQRKKVE------LAKSLAQEAELYIWDEPLNYLDVFN-QKQLEDLL----LQKQP 473
Cdd:cd03240 101 HqgESNWPLLD------MRGRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLDEENiEESLAEIIeerkSQKNF 174
|
170
....*....|....*.
gi 2255859273 474 TMLIVEHDQTFLKNIG 489
Cdd:cd03240 175 QLIVITHDEELVDAAD 190
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
311-481 |
7.02e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 44.61 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQaNGELLRPNVKISYVRqnyennRGT 390
Cdd:PRK13638 1 MLATSDLWFRYQDEPVL-KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ-KGAVLWQGKPLDYSK------RGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 391 L---QDFAEA-----NQLDYS------AFlnNLRKLG-----MERNV-----------FQNQ-IEEMSMGQRKKVELAKS 439
Cdd:PRK13638 73 LalrQQVATVfqdpeQQIFYTdidsdiAF--SLRNLGvpeaeITRRVdealtlvdaqhFRHQpIQCLSHGQKKRVAIAGA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2255859273 440 LAQEAELYIWDEPLNYLDVFNQKQLEDL---LLQKQPTMLIVEHD 481
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIirrIVAQGNHVIISSHD 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-148 |
7.05e-05 |
|
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: 45.67 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 6 ITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQGEIQF--------------------PL 65
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIdgvswnsvtlqtwrkafgviPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 66 RPVYFPATIseQDQLTYYAllEVADFELWELEREMNLIQLDPQ-------VLWQPYQTLSGGEQTKVLLALLFTQENFFP 138
Cdd:TIGR01271 1300 KVFIFSGTF--RKNLDPYE--QWSDEEIWKVAEEVGLKSVIEQfpdkldfVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
170
....*....|
gi 2255859273 139 LIDEPTNHLD 148
Cdd:TIGR01271 1376 LLDEPSAHLD 1385
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
311-360 |
7.28e-05 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 44.34 E-value: 7.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTeQEALFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLG 360
Cdd:COG4559 1 MLEAENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG 49
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
321-481 |
7.30e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 44.69 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 321 YTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtfagqangeLLRP---NVKI-SYV----RQNYENNRGTLq 392
Cdd:COG4586 32 YREVEAV-DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG---------ILVPtsgEVRVlGYVpfkrRKEFARRIGVV- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 393 dFAEANQL--DYSAF--LNNLRKL-GMERNVFQNQIEEM-----------------SMGQRKKVELAKSLAQEAELYIWD 450
Cdd:COG4586 101 -FGQRSQLwwDLPAIdsFRLLKAIyRIPDAEYKKRLDELvelldlgelldtpvrqlSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190
....*....|....*....|....*....|....*
gi 2255859273 451 EPLNYLDVFNQKQLEDLLLQ----KQPTMLIVEHD 481
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEynreRGTTILLTSHD 214
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
331-482 |
7.38e-05 |
|
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: 44.17 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 331 LSFEVQRGTIVALTGPNGIGKSSV----------LHYL--LGTFAGQANGELLRPNVK--------ISyVRQNY--ENNR 388
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVesLSAYARQFLGQMDKPDVDsieglspaIA-IDQKTtsRNPR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 389 GTLQDFAEANqlDY----------SAFLNNLRKLGMERNVFQNQIEEMSMGQRKKVELAKSLAQEAE--LYIWDEP---L 453
Cdd:cd03270 93 STVGTVTEIY--DYlrllfarvgiRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPsigL 170
|
170 180 190
....*....|....*....|....*....|.
gi 2255859273 454 NYLDvfNQKQLEDL--LLQKQPTMLIVEHDQ 482
Cdd:cd03270 171 HPRD--NDRLIETLkrLRDLGNTVLVVEHDE 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
337-485 |
8.50e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 337 RGTIVALTGPNGIGKSSVLHYLLgtfagqanGELLRPNVKISYVrqnyennrgTLQDFAEANQLDYSAFLNNLRKLgmer 416
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA--------RELGPPGGGVIYI---------DGEDILEEVLDQLLLIIVGGKKA---- 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 417 nvfqnqieemSMGQRKKVELAKSLAQE--AELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQTFL 485
Cdd:smart00382 60 ----------SGSGELRLRLALALARKlkPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
338-488 |
9.52e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 338 GTIVALTGPNGIGKSSVLHYLLGTFAGQANGELLRPNVKISYVRQN------------------YENNRGTLQDFAEANQ 399
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQEtpalpqpaleyvidgdreYRQLEAQLHDANERND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 400 LDYSAFLNN-----------------LRKLGMERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQK 462
Cdd:PRK10636 107 GHAIATIHGkldaidawtirsraaslLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVI 186
|
170 180
....*....|....*....|....*.
gi 2255859273 463 QLEDLLLQKQPTMLIVEHDQTFLKNI 488
Cdd:PRK10636 187 WLEKWLKSYQGTLILISHDRDFLDPI 212
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
112-174 |
1.07e-04 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 43.72 E-value: 1.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 112 QPYQTLSGGEQTKVLLALLFTQENFFP----LIDEPTNHLDLQGRQHVANYFQHKDG----FIVVSHDRQF 174
Cdd:cd03275 151 RDMDNLSGGEKTMAALALLFAIHSYQPapffVLDEVDAALDNTNVGKVASYIREQAGpnfqFIVISLKEEF 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-192 |
1.15e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.96 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 20 LFeDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEI---------------------------QFPLRPVYfp 71
Cdd:PRK13649 23 LF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVpTQGSVrvddtlitstsknkdikqirkkvglvfQFPESQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 72 atisEQDQLTYYAL----LEVADFELWELERE-MNLIQLDPQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNH 146
Cdd:PRK13649 100 ----EETVLKDVAFgpqnFGVSQEEAEALAREkLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2255859273 147 LDLQGRQHVANYFQ--HKDGF--IVVSHDRQFLNQVTDHTLAIEKSQLVL 192
Cdd:PRK13649 176 LDPKGRKELMTLFKklHQSGMtiVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-172 |
1.23e-04 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 44.32 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 1 MSTIKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQF---------P-LRPVy 69
Cdd:COG3842 3 MPALELENVSKRYGDVTAL--DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPDSGRILLdgrdvtglpPeKRNV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 70 fpATISeQDqltyYAL---LEVAD---FEL--WELERE---------MNLIQLDPQVLWQPYQtLSGGEQTKVLLA---- 128
Cdd:COG3842 80 --GMVF-QD----YALfphLTVAEnvaFGLrmRGVPKAeirarvaelLELVGLEGLADRYPHQ-LSGGQQQRVALArala 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 129 -----LLFtqenffpliDEPTNHLDLQGRQHVANYF---QHKDG--FIVVSHDR 172
Cdd:COG3842 152 peprvLLL---------DEPLSALDAKLREEMREELrrlQRELGitFIYVTHDQ 196
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-148 |
1.26e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 43.53 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQ-GEIQFPLRPVYFP----------- 71
Cdd:PRK11248 2 LQISHLYADYGGKPAL--EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEGPgaergvvfqne 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 72 ATISEQDQLTYYAL-LEVADFELWELE---REM----NLIQLDPQVLWQpyqtLSGGEQTKVLLALLFTQENFFPLIDEP 143
Cdd:PRK11248 80 GLLPWRNVQDNVAFgLQLAGVEKMQRLeiaHQMlkkvGLEGAEKRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEP 155
|
....*
gi 2255859273 144 TNHLD 148
Cdd:PRK11248 156 FGALD 160
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-192 |
1.70e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 43.47 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 23 DANLTIDSSWKLGLVGRNGRGKTTLLQLL------------LGKYAYQGE----------------IQFPLRPVyFPATI 74
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLngllqptsgtvtIGERVITAGkknkklkplrkkvgivFQFPEHQL-FEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 75 sEQDQLTYYALLEVADFELWELEREM-NLIQLDPQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQ 153
Cdd:PRK13634 104 -EKDICFGPMNFGVSEEDAKQKAREMiELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2255859273 154 HVANYFQ--HKDG---FIVVSHDRQFLNQVTDHTLAIEKSQLVL 192
Cdd:PRK13634 183 EMMEMFYklHKEKgltTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-206 |
1.76e-04 |
|
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: 44.55 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 17 VELLFEDANLTIDSSWKLGLVGRNGRGKTTL-LQLLLGKYAYQGEI--------QFPLRPVYFPATISEQDQLTYYALLE 87
Cdd:TIGR00957 1298 LDLVLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAEGEIiidglniaKIGLHDLRFKITIIPQDPVLFSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 88 V--------ADFELW---ELEREMNLIQLDPQVL----WQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGR 152
Cdd:TIGR00957 1378 MnldpfsqySDEEVWwalELAHLKTFVSALPDKLdhecAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2255859273 153 QHVANYF--QHKDGFIVVSHDRqfLNQVTDHTLAIeksqlVLYQGNFATYEEQKEL 206
Cdd:TIGR00957 1458 NLIQSTIrtQFEDCTVLTIAHR--LNTIMDYTRVI-----VLDKGEVAEFGAPSNL 1506
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-195 |
1.81e-04 |
|
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: 43.19 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 23 DANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQF------PLRP----------------VYFPATISE--- 76
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrPTSGSVLFdgeditGLPPheiarlgigrtfqiprLFPELTVLEnvm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 77 ---QDQLTYYALLEVADFELWEL-EREMNLIQ---LDPqVLWQPYQTLSGGEQTKVLLALLFTQEnffP---LIDEPTNH 146
Cdd:cd03219 98 vaaQARTGSGLLLARARREEREArERAEELLErvgLAD-LADRPAGELSYGQQRRLEIARALATD---PkllLLDEPAAG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 147 LDLQGRQHVANYF----QHKDGFIVVSHDRQFLNQVTDHTlaieksqLVLYQG 195
Cdd:cd03219 174 LNPEETEELAELIrelrERGITVLLVEHDMDVVMSLADRV-------TVLDQG 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
312-452 |
1.89e-04 |
|
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: 42.92 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYLLGtFAGQANGELL-------------RPNVKIS 378
Cdd:cd03218 1 LRAENLSKRYGKRKVVNG-VSLSVKQGEIVGLLGPNGAGKTTTFYMIVG-LVKPDSGKILldgqditklpmhkRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 379 YVRQN---------YENNRGTL--QDFAEANQLDYSAFLnnLRKLGMERnVFQNQIEEMSMGQRKKVELAKSLAQEAELY 447
Cdd:cd03218 79 YLPQEasifrkltvEENILAVLeiRGLSKKEREEKLEEL--LEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFL 155
|
....*
gi 2255859273 448 IWDEP 452
Cdd:cd03218 156 LLDEP 160
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-61 |
1.89e-04 |
|
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: 42.98 E-value: 1.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2255859273 2 STIKITHLTFGFDKQVELLfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQ-GEI 61
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQkGQI 60
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
338-457 |
1.99e-04 |
|
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: 42.23 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 338 GTIVALTGPNGIGKSSVLHYLLG-TFAGQANGELL---RPNVK-----ISYVRQNYennrgTLQDFA---EAnqLDYSAf 405
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGrKTAGVITGEILingRPLDKnfqrsTGYVEQQD-----VHSPNLtvrEA--LRFSA- 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 406 lnNLRKLGMErnvfqnqieemsmgQRKKVELAKSLAQEAELYIWDEPLNYLD 457
Cdd:cd03232 105 --LLRGLSVE--------------QRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
288-373 |
2.97e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 43.26 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 288 GLLKDLEDVDRLTMSYHPSRHTQ--LLKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTFAG- 364
Cdd:COG4178 337 GFEEALEAADALPEAASRIETSEdgALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKST----LLRAIAGl 412
|
90
....*....|.
gi 2255859273 365 --QANGELLRP 373
Cdd:COG4178 413 wpYGSGRIARP 423
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
315-364 |
3.32e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 3.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2255859273 315 ENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTFAG 364
Cdd:NF033858 5 EGVSHRYGKTVALDD-VSLDIPAGCMVGLIGPDGVGKSS----LLSLIAG 49
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-191 |
3.37e-04 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 41.95 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 1 MST-IKITHLTFGF---DKQVELLfEDANLTIDSSWKLGLVGRNGRGKTTLLQLL--L-----GKYAYQG-EI------- 61
Cdd:COG1136 1 MSPlLELRNLTKSYgtgEGEVTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILggLdrptsGEVLIDGqDIsslsere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 62 -------------QFP-LRP-------VYFPATIS----EQDQLTYYALLEvaDFELWELEREMnliqldpqvlwqPYQt 116
Cdd:COG1136 80 larlrrrhigfvfQFFnLLPeltalenVALPLLLAgvsrKERRERARELLE--RVGLGDRLDHR------------PSQ- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 117 LSGGEQ------------TKVLLAllftqenffpliDEPTNHLDLQGRQHVANYFQ---HKDG--FIVVSHDRQFLNQvT 179
Cdd:COG1136 145 LSGGQQqrvaiaralvnrPKLILA------------DEPTGNLDSKTGEEVLELLRelnRELGttIVMVTHDPELAAR-A 211
|
250
....*....|..
gi 2255859273 180 DHTLAIEKSQLV 191
Cdd:COG1136 212 DRVIRLRDGRIV 223
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-193 |
3.51e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 42.38 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 23 DANLTIDSSWKLGLVGRNGRGKTTLLQLL-------LGKYAYQGEIQFPL------RP-------VYFPATI---SEQDQ 79
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIagileptSGRVEVNGRVSALLelgagfHPeltgrenIYLNGRLlglSRKEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 80 LTYYAllEVADF-ELWEleremnliQLDpqvlwQPYQTLSGGEQTKVLLALLFTQEnffP---LIDEPTNHLDLqgrqhv 155
Cdd:COG1134 124 DEKFD--EIVEFaELGD--------FID-----QPVKTYSSGMRARLAFAVATAVD---PdilLVDEVLAVGDA------ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2255859273 156 anYFQHK----------DG--FIVVSHDRQFLNQVTDHTLAIEKSQLVLY 193
Cdd:COG1134 180 --AFQKKclarirelreSGrtVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-148 |
3.63e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.86 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 13 FDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQ-GEIQFplrpvyFPATISE-----QDQLT----- 81
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILF------ERQSIKKdlctyQKQLCfvghr 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859273 82 -----YYALLEVADFEL------WELEREMNLIQLDpQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLD 148
Cdd:PRK13540 83 sginpYLTLRENCLYDIhfspgaVGITELCRLFSLE-HLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
314-493 |
3.69e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 42.04 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 314 MENLSLHYTEQEALFApLSFEVQRGTIVALTGPNGIGKSSVLHYL-------LGTFA------------GQANGELLRPN 374
Cdd:PRK11264 6 VKNLVKKFHGQTVLHG-IDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRvgditidtarslSQQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 375 VKISYVRQNY---------EN-------NRGTLQDFAEA--NQLdysaflnnLRKLGME--RNVFQNQieeMSMGQRKKV 434
Cdd:PRK11264 85 QHVGFVFQNFnlfphrtvlENiiegpviVKGEPKEEATAraREL--------LAKVGLAgkETSYPRR---LSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 435 ELAKSLAQEAELYIWDEPLNYLD------VFNQKQledLLLQKQPTMLIVEHDQTFLKNIGAQQI 493
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDpelvgeVLNTIR---QLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
427-488 |
3.83e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 3.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 427 SMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPTMLIVEHDQTFLKNI 488
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
305-497 |
4.08e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.77 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 305 PSRHTQLLKMENLSLHYTEQEALFA----------PLSFEVQRGTIVALTGPNGIGKSSVLHYLLG--------TFAGQA 366
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFPIRKGILKrtvdhnvvvkNISFTLRPGETLGLVGESGSGKSTTGLALLRlinsqgeiWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 367 NGELLRPNV-----KISYVRQNYE---NNR-GTLQDFAEANQLDYSAF---------LNNLRKLGMERNVFQNQIEEMSM 428
Cdd:PRK15134 349 LHNLNRRQLlpvrhRIQVVFQDPNsslNPRlNVLQIIEEGLRVHQPTLsaaqreqqvIAVMEEVGLDPETRHRYPAEFSG 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 429 GQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQK--QPTMLIVEHDQTFLKNIGAQQIALKK 497
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLksLQQkhQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-107 |
4.28e-04 |
|
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: 41.83 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAY-QGEIqfplrpvyfpaTISEQDqlty 82
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRI-----------LIDGHD---- 65
|
90 100
....*....|....*....|....*
gi 2255859273 83 yalleVADFELWELEREMNLIQLDP 107
Cdd:cd03251 66 -----VRDYTLASLRRQIGLVSQDV 85
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-62 |
4.42e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 42.29 E-value: 4.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEIQ 62
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLkPQSGEIK 67
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
409-481 |
4.95e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.07 E-value: 4.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 409 LRKLGMERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQ----PTMLIVEHD 481
Cdd:PRK13646 129 LMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD 205
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
312-355 |
7.79e-04 |
|
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: 40.21 E-value: 7.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2255859273 312 LKMENLSLHYTEQEALFAPLSFEVQRGTIVALTGPNGIGKSSVL 355
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF 44
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-149 |
7.88e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 41.13 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 8 HLTFGFDKQVelLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLL-----------------LGKYAYQG---EIQFPLRP 67
Cdd:PRK10253 12 QLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLsrlmtpahghvwldgehIQHYASKEvarRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 68 VYFPATISEQDQLTYYALLEVADFELWELERE------MNLIQLDpQVLWQPYQTLSGGEQTKVLLALLFTQENFFPLID 141
Cdd:PRK10253 90 ATTPGDITVQELVARGRYPHQPLFTRWRKEDEeavtkaMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
....*...
gi 2255859273 142 EPTNHLDL 149
Cdd:PRK10253 169 EPTTWLDI 176
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-204 |
8.43e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.02 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 14 DKQVELLfEDANLTIDSSWKLGLVGRNGRGKTTLLQLL-------LGKYAYQG--------EIQFPLRPVYFPATISEQD 78
Cdd:PRK10535 18 EEQVEVL-KGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGqdvatldaDALAQLRREHFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 79 QLTY------------YALLEVADfelwELEREMNLIQ---LDPQVLWQPYQtLSGGEQTKVLLALLFTQENFFPLIDEP 143
Cdd:PRK10535 97 LLSHltaaqnvevpavYAGLERKQ----RLLRAQELLQrlgLEDRVEYQPSQ-LSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 144 TNHLDLQGRQHVANYF----QHKDGFIVVSHDRQFLNQvTDHTLAIEKSQLVLYQGNFATYEEQK 204
Cdd:PRK10535 172 TGALDSHSGEEVMAILhqlrDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQEKVNVAG 235
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
111-177 |
9.23e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 9.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 111 WQPYQTLSGGEQTKVLLALLFTQENFFP----LIDEPTNHLDLQGRQHVANYF-QHKDG--FIVVSHDRQFLNQ 177
Cdd:pfam02463 1072 VKNLDLLSGGEKTLVALALIFAIQKYKPapfyLLDEIDAALDDQNVSRVANLLkELSKNaqFIVISLREEMLEK 1145
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
96-169 |
9.41e-04 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 40.74 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 96 LEREMNLIQLDPQVLWQPYQTLSGGEQTKVLLALLFTQENFFP----LIDEPTNHLDLQGRQHVANYFQHKDG---FIVV 168
Cdd:cd03274 107 LQGEVEQIAQMPKKSWKNISNLSGGEKTLSSLALVFALHHYKPtplyVMDEIDAALDFRNVSIVANYIKERTKnaqFIVI 186
|
.
gi 2255859273 169 S 169
Cdd:cd03274 187 S 187
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-210 |
1.06e-03 |
|
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: 40.56 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQ-GEIQFPLRPVyFPATISEQDQLTY 82
Cdd:cd03261 1 IELRGLTKSFGGRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDI-SGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 83 Y--------AL---LEVAD---FELWE---LEREM---------NLIQLDPQVLWQPYQtLSGGEQTKVLLA-------- 128
Cdd:cd03261 78 RmgmlfqsgALfdsLTVFEnvaFPLREhtrLSEEEireivleklEAVGLRGAEDLYPAE-LSGGMKKRVALAralaldpe 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 129 LLFtqenffplIDEPTNHLD-------------LQGRQHVAnyfqhkdgFIVVSHDRQFLNQVTDHTlaieksqLVLYQG 195
Cdd:cd03261 157 LLL--------YDEPTAGLDpiasgviddlirsLKKELGLT--------SIMVTHDLDTAFAIADRI-------AVLYDG 213
|
250
....*....|....*...
gi 2255859273 196 N---FATYEEQKELRDEF 210
Cdd:cd03261 214 KivaEGTPEELRASDDPL 231
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-148 |
1.17e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 40.99 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAYQGEIQF-------------------- 63
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIdgvswnsvplqkwrkafgvi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 64 PLRPVYFPATIseQDQLTYYAllEVADFELWELEREMNLI--------QLDPQVLWQPYqTLSGGEQTKVLLALLFTQEN 135
Cdd:cd03289 83 PQKVFIFSGTF--RKNLDPYG--KWSDEEIWKVAEEVGLKsvieqfpgQLDFVLVDGGC-VLSHGHKQLMCLARSVLSKA 157
|
170
....*....|...
gi 2255859273 136 FFPLIDEPTNHLD 148
Cdd:cd03289 158 KILLLDEPSAHLD 170
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
309-481 |
1.29e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 40.87 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 309 TQLLKMENLSLHY-TEQEA-LFAPLSFEVQRGTIVALTGPNGIGKSSVLHYLLGTFAGQA-----NGELLRP-NV----- 375
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESgqiiiDGDLLTEeNVwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 376 KISYVRQNYENNrgtlqdFAEANQLDYSAFlnNLRKLGMERNVFQNQIEE-----------------MSMGQRKKVELAK 438
Cdd:PRK13650 82 KIGMVFQNPDNQ------FVGATVEDDVAF--GLENKGIPHEEMKERVNEalelvgmqdfkereparLSGGQKQRVAIAG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2255859273 439 SLAQEAELYIWDEPLNYLDVFNQKQL----EDLLLQKQPTMLIVEHD 481
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELiktiKGIRDDYQMTVISITHD 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
113-488 |
1.60e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 113 PYQtLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDL----QGRQHVANYFQHKD-GFIVVSHDRQFLNQVTDHTLaiek 187
Cdd:PRK10261 166 PHQ-LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSmGVIFITHDMGVVAEIADRVL---- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 188 sqlVLYQGNFAtyeEQKELRDEFELAQNRKIKKEVSRLKRTAAEKaewsrsretekygkpsekgsGGIFDTGFIGARAAR 267
Cdd:PRK10261 241 ---VMYQGEAV---ETGSVEQIFHAPQHPYTRALLAAVPQLGAMK--------------------GLDYPRRFPLISLEH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 268 TMKRSKTIEQrmyDQIEVKEGLLKDLEDVDRLtmsyhPSRhTQLLKMENLSLHYTEQealfapLSFEVQRGTIVALTGPN 347
Cdd:PRK10261 295 PAKQEPPIEQ---DTVVDGEPILQVRNLVTRF-----PLR-SGLLNRVTREVHAVEK------VSFDLWPGETLSLVGES 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 348 GIGKSSVLHYLLG---------TFAGQANGELlrPNVKISYVRQNYE------------------------NNRGTLQDF 394
Cdd:PRK10261 360 GSGKSTTGRALLRlvesqggeiIFNGQRIDTL--SPGKLQALRRDIQfifqdpyasldprqtvgdsimeplRVHGLLPGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 395 AEANQLdysAFLnnLRKLGMERNVFQNQIEEMSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLLLQKQPT 474
Cdd:PRK10261 438 AAAARV---AWL--LERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRD 512
|
410
....*....|....*...
gi 2255859273 475 M----LIVEHDQTFLKNI 488
Cdd:PRK10261 513 FgiayLFISHDMAVVERI 530
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-191 |
1.72e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 40.03 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 20 LFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYA-YQGEIQFPLRPVYFPATISEQD-------------QLTYYAL 85
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDGKVLYFGKDIFQIDaiklrkevgmvfqQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 86 LEVADFELWELE-------REMNLIQ---LDPQVLWQ--------PYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHL 147
Cdd:PRK14246 105 LSIYDNIAYPLKshgikekREIKKIVeecLRKVGLWKevydrlnsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2255859273 148 DLQGRQHVANY---FQHKDGFIVVSHDRQFLNQVTDHTLAIEKSQLV 191
Cdd:PRK14246 185 DIVNSQAIEKLiteLKNEIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
115-170 |
2.06e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 39.21 E-value: 2.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2255859273 115 QTLSGGEQTKVLLALLFTQENFFP----LIDEPTNHLDLQGRQHVANY----FQHKDGFIVVSH 170
Cdd:cd03239 93 QILSGGEKSLSALALIFALQEIKPspfyVLDEIDAALDPTNRRRVSDMikemAKHTSQFIVITL 156
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
311-481 |
2.32e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 40.44 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 311 LLKMENLSLHYTEQEALFAP----------LSFEVQRGTIVALTGPNGIGKSSVLHYLLG--------TFAGQA----NG 368
Cdd:COG4172 275 LLEARDLKVWFPIKRGLFRRtvghvkavdgVSLTLRRGETLGLVGESGSGKSTLGLALLRlipsegeiRFDGQDldglSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 369 ELLRP---NVKIsyVRQN-YennrGTL-------QDFAE-----ANQLDYSAFLNN----LRKLGMERNVFQNQIEEMSM 428
Cdd:COG4172 355 RALRPlrrRMQV--VFQDpF----GSLsprmtvgQIIAEglrvhGPGLSAAERRARvaeaLEEVGLDPAARHRYPHEFSG 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2255859273 429 GQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQK--QPTMLIVEHD 481
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLrdLQRehGLAYLFISHD 485
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
117-187 |
2.39e-03 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 39.69 E-value: 2.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2255859273 117 LSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYFQH--KDG--FIVVSHDRQFLNQVTDHTLAIEK 187
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDlaEEGmtMVIVTHEIGFAEKVASRLIFIDK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-171 |
2.61e-03 |
|
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: 39.38 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 4 IKITHLTFGFDKQVELL--FEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQF---PLRPVYFPATISEQ 77
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGlERPTSGEVLVdgePVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 78 DqltyYALLE----------------VADFELWELEREM-NLIQLDPQVLWQPYQtLSGGEQTKVLLALLFTQEnffP-- 138
Cdd:cd03293 81 Q----DALLPwltvldnvalglelqgVPKAEARERAEELlELVGLSGFENAYPHQ-LSGGMRQRVALARALAVD---Pdv 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 2255859273 139 -LIDEPTNHLDLQGRQHVANYFQ---HKDGFIV--VSHD 171
Cdd:cd03293 153 lLLDEPFSALDALTREQLQEELLdiwRETGKTVllVTHD 191
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
113-173 |
2.84e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 39.38 E-value: 2.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2255859273 113 PYQtLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGRQHVANYF-----QHKDGFIVVSHDRQ 173
Cdd:PRK10584 144 PAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnrEHGTTLILVTHDLQ 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
296-355 |
2.96e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 39.29 E-value: 2.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 296 VDRLTMSYH-PSRHTQLLKMENLSLHYTEQEALFA--PLSFEVQRGTIVALTGPNGIGKSSVL 355
Cdd:COG1134 7 VENVSKSYRlYHEPSRSLKELLLRRRRTRREEFWAlkDVSFEVERGESVGIIGRNGAGKSTLL 69
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
312-480 |
3.56e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 39.05 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 312 LKMENLSLHYTEQEALfAPLSFEVQRGTIVALTGPNGIGKSSvlhyLLGTF--------AGQANGE-------LLRPNVK 376
Cdd:PRK14267 5 IETVNLRVYYGSNHVI-KGVDLKIPQNGVFALMGPSGCGKST----LLRTFnrllelneEARVEGEvrlfgrnIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 377 ISYVRQ------NYENnrgtlqDFAEANQLDYSAF---LNNLRKLGME------------------RNVFQNQIEEMSMG 429
Cdd:PRK14267 80 PIEVRRevgmvfQYPN------PFPHLTIYDNVAIgvkLNGLVKSKKEldervewalkkaalwdevKDRLNDYPSNLSGG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 430 QRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQPTMLIVEH 480
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfeLKKEYTIVLVTH 206
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
116-188 |
3.60e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 116 TLSGGEQTKVLLALLFTQENF------FPLIDEPTNHLDLQGRQHVANYFQHK-------DGFIVVSHDRQFLNqVTDHT 182
Cdd:PRK01156 801 SLSGGEKTAVAFALRVAVAQFlnndksLLIMDEPTAFLDEDRRTNLKDIIEYSlkdssdiPQVIMISHHRELLS-VADVA 879
|
....*.
gi 2255859273 183 LAIEKS 188
Cdd:PRK01156 880 YEVKKS 885
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
426-472 |
3.97e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 3.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2255859273 426 MSMGQRKKVELAKSLAQEAELYIWDEPLNYLDVFNQKQLEDLL--LQKQ 472
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLasLHQS 184
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-53 |
4.19e-03 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 39.29 E-value: 4.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2255859273 1 MSTIKITHLTFGFDKQVELlfEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG 53
Cdd:COG3839 1 MASLELENVSKSYGGVEAL--KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG 51
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-148 |
4.36e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 38.94 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 3 TIKITHLT--FGfDKQVellFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLG-KYAYQGEIQF---PLRPV------YF 70
Cdd:COG4152 1 MLELKGLTkrFG-DKTA---VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGiLAPDSGEVLWdgePLDPEdrrrigYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 71 PatisE----------QDQLTYYALL---------EVAD--FELWELEREMNliqldpqvlwQPYQTLSGGEQTKVLL-- 127
Cdd:COG4152 77 P----EerglypkmkvGEQLVYLARLkglskaeakRRADewLERLGLGDRAN----------KKVEELSKGNQQKVQLia 142
|
170 180
....*....|....*....|....
gi 2255859273 128 ALLFTqenffP--LI-DEPTNHLD 148
Cdd:COG4152 143 ALLHD-----PelLIlDEPFSGLD 161
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-70 |
5.29e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.33 E-value: 5.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2255859273 22 EDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKYAY-QGEIQFPLRPVYF 70
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKdSGSILFQGKEIDF 64
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-55 |
5.47e-03 |
|
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: 38.62 E-value: 5.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY 55
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY 52
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
35-73 |
7.68e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 38.74 E-value: 7.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2255859273 35 GLVGRNGRGKTTLLQLLLGKYAYQ-GEIQFPLRPVYFPAT 73
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDaGSILIDGQEMRFAST 73
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-61 |
8.19e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 38.85 E-value: 8.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2255859273 4 IKITHLTFGFDKQVELLFEDANLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY-AYQGEI 61
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYdIDEGEI 400
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-79 |
9.30e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.37 E-value: 9.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2255859273 25 NLTIDSSWKLGLVGRNGRGKTTLLQLLLGKY---AYQGEIQFPLRPVYFpATISEQDQ 79
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgTYEGEIIFEGEELQA-SNIRDTER 81
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
112-198 |
9.67e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 38.49 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2255859273 112 QPYQTLSGGEQTKVLLALLFTQENFFPLIDEPTNHLDLQGR------------QHVAnyfqhkdgFIVVSHDRQFLNQVT 179
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARndiyqlirsiaaQNVA--------VLFISSDLEEIEQMA 470
|
90
....*....|....*....
gi 2255859273 180 DHTlaieksqLVLYQGNFA 198
Cdd:PRK15439 471 DRV-------LVMHQGEIS 482
|
|
| |
