|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-532 |
1.72e-115 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 351.67 E-value: 1.72e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGL--GVMRQfigslrgagesSPGGDgrDSR 90
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLriGYLPQ-----------EPPLD--DDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TVQDLLLSVAPvRVKEAAERLNGAELAMMEREDEktQMRYAQAITDYTDAGGYDIE-----VLwdtctmAALGAPYDNVk 165
Cdd:COG0488 77 TVLDTVLDGDA-ELRALEAELEELEAKLAEPDED--LERLAELQEEFEALGGWEAEaraeeIL------SGLGFPEEDL- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 166 YRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESG 244
Cdd:COG0488 147 DRPVSELSGGWRRRVALaRALLSEPD-LLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 245 NVWIHGGGFATYSEARKDRNERLDELRRRWDEEHAKLKRLVVMLRQKAtyndSMAApyhAAQTRLRRFEEAGPPELAPKD 324
Cdd:COG0488 226 KLTLYPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKA----RKAK---QAQSRIKALEKLEREEPPRRD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 325 QLISMRLRGG-RTAKRAVICENLELSG----LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARV 399
Cdd:COG0488 299 KTVEIRFPPPeRLGKKVLELEGLSKSYgdktLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 400 VPGHFAQTHArpEL-LGRTPCEiVMTEHARLKNE--AMKALARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLL 476
Cdd:COG0488 379 KIGYFDQHQE--ELdPDKTVLD-ELRDGAPGGTEqeVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 477 LDEPTDNLDLASAEALQAGLDAFDGTVLAVTHDRWFAADF-DRYMVFgTDGRVYESP 532
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVaTRILEF-EDGGVREYP 511
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-518 |
7.04e-58 |
|
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: 202.09 E-value: 7.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 5 RLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVmrqfiGSLrgagESSPGG 84
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKV-----GYL----PQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 85 DgrDSRTVQD-LLLSVAPVrvKEAAERLNGAELAMMEREDEKTQMRYAQA-ITDYTDA-GGYDIEVLWDTcTMAALGAPY 161
Cdd:TIGR03719 80 D--PTKTVREnVEEGVAEI--KDALDRFNEISAKYAEPDADFDKLAAEQAeLQEIIDAaDAWDLDSQLEI-AMDALRCPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 162 DNVkyrDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVT 240
Cdd:TIGR03719 155 WDA---DVTKLSGGERRRVALcRLLLSKPD-MLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 241 VESGNVWIHGGGFATYSEARkdrNERLdELRRRWDEEHAK-LKRLVVMLRQ--KATYNDSMAapyhaaqtRLRRFEEAGP 317
Cdd:TIGR03719 231 LDRGRGIPWEGNYSSWLEQK---QKRL-EQEEKEESARQKtLKRELEWVRQspKGRQAKSKA--------RLARYEELLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 318 PELAPKDQLISMRLRGGRTAKRAVIcenlELSGLMKPFDLEIWY---------GERVAVLGSNGSGKSHFLRLIAGEEVR 388
Cdd:TIGR03719 299 QEFQKRNETAEIYIPPGPRLGDKVI----EAENLTKAFGDKLLIddlsfklppGGIVGVIGPNGAGKSTLFRMITGQEQP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 389 HTGVARLGARVVPGHFAQThaRPELLG-RTPCEIVM--TEHARLKNEAMKA---LARYELAGGVAEQRFETLSGGQQARL 462
Cdd:TIGR03719 375 DSGTIEIGETVKLAYVDQS--RDALDPnKTVWEEISggLDIIKLGKREIPSrayVGRFNFKGSDQQKKVGQLSGGERNRV 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2796936914 463 QILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFDGTVLAVTHDRWFaadFDR 518
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWF---LDR 505
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-512 |
9.71e-50 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 179.93 E-value: 9.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVmrqfiGSLrgagES 80
Cdd:PRK11819 7 YTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKV-----GYL----PQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 SPGGDgrDSRTV-QDLLLSVAPvrVKEAAERLN--GAELAMMEREDEKTQMRYA--QAITDYTDAGGYD--IEVlwdtcT 153
Cdd:PRK11819 78 EPQLD--PEKTVrENVEEGVAE--VKAALDRFNeiYAAYAEPDADFDALAAEQGelQEIIDAADAWDLDsqLEI-----A 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 154 MAALGAPYDNVkyrDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLA 232
Cdd:PRK11819 149 MDALRCPPWDA---KVTKLSGGERRRVALcRLLLEKPD-MLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 233 NAVDRIVTVESGnvwiHG----GGFATYSEArkdRNERLdELRRRWDEEHAK-LKRLVVMLRQ--KATYNDSMAapyhaa 305
Cdd:PRK11819 225 NVAGWILELDRG----RGipweGNYSSWLEQ---KAKRL-AQEEKQEAARQKaLKRELEWVRQspKARQAKSKA------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 306 qtRLRRFEE--AGPPELAPKDQLISM----RLrGGRtakraVIcenlELSGLMKPFdleiwyGER--------------- 364
Cdd:PRK11819 291 --RLARYEEllSEEYQKRNETNEIFIppgpRL-GDK-----VI----EAENLSKSF------GDRlliddlsfslppggi 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 365 VAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHAR--PEllgRTPCEIVM--TEHARLKNEAMKA---L 437
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDAldPN---KTVWEEISggLDIIKVGNREIPSrayV 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 438 ARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFDGTVLAVTHDRWF 512
Cdd:PRK11819 430 GRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWF 504
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-512 |
3.16e-40 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 154.34 E-value: 3.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQfigslrgagESSPggdgrdSRTVQD 94
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARL---------QQDP------PRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 95 LLLSVAPVRVKEAAERLNG---AELAMMEREDEK--TQMRYAQAITDYTDAGGYD---IEVLwdtctmAALGAPYDnvky 166
Cdd:PRK11147 82 TVYDFVAEGIEEQAEYLKRyhdISHLVETDPSEKnlNELAKLQEQLDHHNLWQLEnriNEVL------AQLGLDPD---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 167 RDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGN 245
Cdd:PRK11147 152 AALSSLSGGWLRKAALgRALVSNPD-VLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 246 VWIHGGGFATYSEArKDRNERLDEL------RRRWDEEhaklkrlvVMLRQ--KA--TYNDSMAAPYHAA-QTRLRRFEE 314
Cdd:PRK11147 231 LVSYPGNYDQYLLE-KEEALRVEELqnaefdRKLAQEE--------VWIRQgiKArrTRNEGRVRALKALrRERSERREV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 315 AGPPELAPKDqlismrlrGGRTAKRAVICENL--ELSG--LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHT 390
Cdd:PRK11147 302 MGTAKMQVEE--------ASRSGKIVFEMENVnyQIDGkqLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 391 GVARLGARVVPGHFAQThaRPELlgrTPCEIVMTEHARLKNEAMkalaryelAGGVAE------QRF-----------ET 453
Cdd:PRK11147 374 GRIHCGTKLEVAYFDQH--RAEL---DPEKTVMDNLAEGKQEVM--------VNGRPRhvlgylQDFlfhpkramtpvKA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2796936914 454 LSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFDGTVLAVTHDRWF 512
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-509 |
1.36e-38 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 150.40 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAgdLQPIEGSVTHAGGLGVMRQFIGslrgagesspggdgrDSRTV 92
Cdd:PLN03073 189 GRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGIPKNCQILHVEQEVVG---------------DDTTA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 QDLLLSVAPVRVKEAAERLN-GAELAMMEREDEKTQMRYAQAITDYTDAGGYDIEVLW------DTCTMAALGAPY---- 161
Cdd:PLN03073 252 LQCVLNTDIERTQLLEEEAQlVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYkrleliDAYTAEARAASIlagl 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 162 ---DNVKYRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDR 237
Cdd:PLN03073 332 sftPEMQVKATKTFSGGWRMRIALaRALFIEPD-LLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTD 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 238 IVTVESGNVWIHGGGFATYseaRKDRNERLDELRRRWdEEHAKLKRLVVMLRQKATYNDSMAApyhAAQTRLRRFEEAG- 316
Cdd:PLN03073 411 ILHLHGQKLVTYKGDYDTF---ERTREEQLKNQQKAF-ESNERSRSHMQAFIDKFRYNAKRAS---LVQSRIKALDRLGh 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 317 ---------------PPELAPKDQLISMRLRGGRTAKRAVICENLELSglmkpFDLEiwygERVAVLGSNGSGKSHFLRL 381
Cdd:PLN03073 484 vdavvndpdykfefpTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFG-----IDLD----SRIAMVGPNGIGKSTILKL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 382 IAGEEVRHTGVARLGARVVPGHFAQTHARPELLGRTPCEIVMTEHARLKNEAMKA-LARYELAGGVAEQRFETLSGGQQA 460
Cdd:PLN03073 555 ISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAhLGSFGVTGNLALQPMYTLSGGQKS 634
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2796936914 461 RLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFDGTVLAVTHD 509
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHD 683
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-528 |
1.01e-37 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 147.24 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG--GLGVMRQFIGSL-RGAGESSPGGDgRDSR 90
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQETPALpQPALEYVIDGD-REYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TVQDLLlsvapvrvKEAAERLNGAELAMMEredekTQMRYAQAITDYTDAGGYdievlwdtctMAALGAPYDNVKyRDLT 170
Cdd:PRK10636 93 QLEAQL--------HDANERNDGHAIATIH-----GKLDAIDAWTIRSRAASL----------LHGLGFSNEQLE-RPVS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 171 TLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGNVWIHG 250
Cdd:PRK10636 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 251 GGFATYSEARKDRNERLDELRRRWDEEHAKLKRLVVMLRQKATYNDSmaapyhaAQTR---LRRFEEAGP---------- 317
Cdd:PRK10636 229 GNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQ-------AQSRikmLERMELIAPahvdnpfhfs 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 318 ---PELAPKDQLISMRLRGGRTAKraVICENLELSglMKPfdleiwyGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVAR 394
Cdd:PRK10636 302 fraPESLPNPLLKMEKVSAGYGDR--IILDSIKLN--LVP-------GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 395 LGARVVPGHFAQTHArpELLgrTPCEIVMTEHARLKNEAMKALARYELAG------GVAEQRfETLSGGQQARLQILLLE 468
Cdd:PRK10636 371 LAKGIKLGYFAQHQL--EFL--RADESPLQHLARLAPQELEQKLRDYLGGfgfqgdKVTEET-RRFSGGEKARLVLALIV 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796936914 469 MSGATLLLLDEPTDNLDLASAEALQAGLDAFDGTVLAVTHDRWF--AADFDRYMVFgtDGRV 528
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLlrSTTDDLYLVH--DGKV 505
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-244 |
1.32e-37 |
|
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: 135.27 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVmrqfigslrgagesspggdgrdsrt 91
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKI------------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 vqdlllsvapvrvkeaaerlngaelammeredektqmryaqaitdytdagGYdievlwdtctmaalgapydnvkyrdLTT 171
Cdd:cd03221 66 --------------------------------------------------GY-------------------------FEQ 70
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESG 244
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
341-512 |
7.04e-37 |
|
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: 133.34 E-value: 7.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 341 VICENLELSG----LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQtharpellgr 416
Cdd:cd03221 1 IELENLSKTYggklLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 tpceivmteharlkneamkalaryelaggvaeqrfetLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGL 496
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170
....*....|....*.
gi 2796936914 497 DAFDGTVLAVTHDRWF 512
Cdd:cd03221 114 KEYPGTVILVSHDRYF 129
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-512 |
1.35e-36 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 142.72 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG--LGVMRQ--FigslrgAGEsspggdgrDS 89
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNerLGKLRQdqF------AFE--------EF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 90 RTVQDLLLSVAPV-RVKEAAERLNGaeLAMMEREDektQMRYAQAITDYTDAGGY-------------DIEVLWDTCTMA 155
Cdd:PRK15064 80 TVLDTVIMGHTELwEVKQERDRIYA--LPEMSEED---GMKVADLEVKFAEMDGYtaearagelllgvGIPEEQHYGLMS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 156 ALgAPydNVKYRDLttlsggeqkrLAlEALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLaNAV 235
Cdd:PRK15064 155 EV-AP--GWKLRVL----------LA-QALFSNPD-ILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL-NSV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 236 -DRIVTVESGNVWIHGGGFATYSEARKDRNERLDELRRRWDEEHAKLKRLVVmlRQKAtyNDSMAapyHAAQTRLRRFEE 314
Cdd:PRK15064 219 cTHMADLDYGELRVYPGNYDEYMTAATQARERLLADNAKKKAQIAELQSFVS--RFSA--NASKA---KQATSRAKQIDK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 315 AGPPELAPKD-QLISMRLRGGRTAKR-AVICENL----ELSGLMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVR 388
Cdd:PRK15064 292 IKLEEVKPSSrQNPFIRFEQDKKLHRnALEVENLtkgfDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 389 HTGVARLGARVVPGHFAQTHARPELLGRTPCEIvMTEHARLK-NEAM--KALARYELAGGVAEQRFETLSGGQQARLQIL 465
Cdd:PRK15064 372 DSGTVKWSENANIGYYAQDHAYDFENDLTLFDW-MSQWRQEGdDEQAvrGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFG 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2796936914 466 LLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFDGTVLAVTHDRWF 512
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREF 497
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-256 |
1.75e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 133.65 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGL--GVMRQFIGSLRgagesspggdgrDS 89
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVkiGYFDQHQEELD------------PD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 90 RTVQDLLLSVAPvrvkeaaerlngaelammeredektqmryaqaitdytdaGGYDIEVlwdtctMAALGA---PYDNVkY 166
Cdd:COG0488 394 KTVLDELRDGAP---------------------------------------GGTEQEV------RGYLGRflfSGDDA-F 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 167 RDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:COG0488 428 KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGV 507
|
250
....*....|
gi 2796936914 247 WIHGGGFATY 256
Cdd:COG0488 508 REYPGGYDDY 517
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-250 |
8.46e-30 |
|
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: 117.27 E-value: 8.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHvLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG------GLGVMRQfIGSLr 75
Cdd:COG4555 3 EVENLSK-KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkePREARRQ-IGVL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 76 gagessPGGDGRDSR-TVQDLLLSVA---PVRVKEAAERlngaelamMEREDEKTQMRyaqaitDYTDaggydievlwdt 151
Cdd:COG4555 80 ------PDERGLYDRlTVRENIRYFAelyGLFDEELKKR--------IEELIELLGLE------EFLD------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 152 ctmaalgapydnvkyRDLTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQ---ALRETSKTVLLVSHD 227
Cdd:COG4555 128 ---------------RRVGELSTGMKKKVALaRALVHDP-KVLLLDEPTNGLDVMARRLLREilrALKKEGKTVLFSSHI 191
|
250 260
....*....|....*....|...
gi 2796936914 228 RQLLANAVDRIVTVESGNVWIHG 250
Cdd:COG4555 192 MQEVEALCDRVVILHKGKVVAQG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-250 |
4.00e-28 |
|
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: 112.04 E-value: 4.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThAGGLGVMRQFIGSLRgagess 81
Cdd:COG1122 2 ELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL-VDGKDITKKNLRELR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 82 pggdgRD-------------SRTVQD--------LLLSVAPV--RVKEAAERLNGAELAmmERedektqmryaqaitdyt 138
Cdd:COG1122 75 -----RKvglvfqnpddqlfAPTVEEdvafgpenLGLPREEIreRVEEALELVGLEHLA--DR----------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 139 daggydievlwdtctmaalgAPYDnvkyrdlttLSGGEQKRLALEALL-RGPDqTLLLDEPDNYLDVPGKIWLEQALRE- 216
Cdd:COG1122 131 --------------------PPHE---------LSGGQKQRVAIAGVLaMEPE-VLVLDEPTAGLDPRGRRELLELLKRl 180
|
250 260 270
....*....|....*....|....*....|....*.
gi 2796936914 217 --TSKTVLLVSHDRQLLANAVDRIVTVESGNVWIHG 250
Cdd:COG1122 181 nkEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-244 |
5.58e-28 |
|
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: 111.02 E-value: 5.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDG-RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG------GLGVMRQFIGSL 74
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 75 rgagesspggdgrdsrtVQD-----LLLSVApvrvKEAAerlNGAELAMMEREDEKtqmryaQAITDYTDAGGydIEVLW 149
Cdd:cd03225 81 -----------------FQNpddqfFGPTVE----EEVA---FGLENLGLPEEEIE------ERVEEALELVG--LEGLR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 150 DtctmaalgapydnvkyRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETS---KTVLLVS 225
Cdd:cd03225 129 D----------------RSPFTLSGGQKQRVAIaGVLAMDPD-ILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVT 191
|
250
....*....|....*....
gi 2796936914 226 HDRQLLANAVDRIVTVESG 244
Cdd:cd03225 192 HDLDLLLELADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-531 |
8.93e-28 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 116.93 E-value: 8.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDGR-PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQP---IEGSVTHAGglgvmrqfigslRGA 77
Cdd:COG1123 6 EVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDG------------RDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 78 GESSPGGDGRDSRTV-QDLLLSVAPVRV-KEAAErlnGAELAMMEREDEKTQMryaqaitdytdaggydIEVLwdtcTMA 155
Cdd:COG1123 74 LELSEALRGRRIGMVfQDPMTQLNPVTVgDQIAE---ALENLGLSRAEARARV----------------LELL----EAV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 156 ALGAPYDnvkyRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKI----WLEQALRETSKTVLLVSHDRQLL 231
Cdd:COG1123 131 GLERRLD----RYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAeildLLRELQRERGTTVLLITHDLGVV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 232 ANAVDRIVTVESGNVWIHGGGFATYSEARKdrnerldelrrrwdeehaklkrlvvmlrqkatyndsmaapyHAAQTRLRR 311
Cdd:COG1123 207 AEIADRVVVMDDGRIVEDGPPEEILAAPQA-----------------------------------------LAAVPRLGA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 312 FEEAGPPELAPKDQLISMR------LRGGRTAKRAVicenlelsglmKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGE 385
Cdd:COG1123 246 ARGRAAPAAAAAEPLLEVRnlskryPVRGKGGVRAV-----------DDVSLTLRRGETLGLVGESGSGKSTLARLLLGL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 386 EVRHTGVARLGARVVPGHFAQthARPELLGR----------------TPCEIVM--------TEHARLKNEAMKALARYE 441
Cdd:COG1123 315 LRPTSGSILFDGKDLTKLSRR--SLRELRRRvqmvfqdpysslnprmTVGDIIAeplrlhglLSRAERRERVAELLERVG 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 442 LAGGVAEQRFETLSGGQQARLQI---LLLEmsgATLLLLDEPTDNLDLASA-------EALQaglDAFDGTVLAVTHDRW 511
Cdd:COG1123 393 LPPDLADRYPHELSGGQRQRVAIaraLALE---PKLLILDEPTSALDVSVQaqilnllRDLQ---RELGLTYLFISHDLA 466
|
570 580
....*....|....*....|.
gi 2796936914 512 FAADF-DRYMVFGtDGRVYES 531
Cdd:COG1123 467 VVRYIaDRVAVMY-DGRIVED 486
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-239 |
4.14e-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: 108.77 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-GLGVMRQFIGSLRGAGESSPGgdgrdsr 90
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkPLEKERKRIGYVPQRRSIDRD------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 tvqdlllsvAPVRVKeaaerlngaELAMMERedektqMRYAQAITDYTDAGGYDIEVLWDTCTMAALgapydnvKYRDLT 170
Cdd:cd03235 83 ---------FPISVR---------DVVLMGL------YGHKGLFRRLSKADKAKVDEALERVGLSEL-------ADRQIG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796936914 171 TLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGK---IWLEQALRETSKTVLLVSHDRQLLANAVDRIV 239
Cdd:cd03235 132 ELSGGQQQRVLLaRALVQDPD-LLLLDEPFAGVDPKTQediYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-250 |
1.67e-25 |
|
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: 105.51 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThaggLgvmrqfigslrgagesspggDGRD--S 89
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVL----L--------------------DGRDlaS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 90 RTVQDL--LLSVAPVRVkEAAERLNGAELAMMERedektqMRYAQAITDYTDAggyDIEVLWDtcTMAALGApyDNVKYR 167
Cdd:COG1120 68 LSRRELarRIAYVPQEP-PAPFGLTVRELVALGR------YPHLGLFGRPSAE---DREAVEE--ALERTGL--EHLADR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 168 DLTTLSGGEQKR--LALeALLRGPDqTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVSHDRQLLANAVDRIVTV 241
Cdd:COG1120 134 PVDELSGGERQRvlIAR-ALAQEPP-LLLLDEPTSHLDLAHQLEVLELLRrlarERGRTVVMVLHDLNLAARYADRLVLL 211
|
....*....
gi 2796936914 242 ESGNVWIHG 250
Cdd:COG1120 212 KDGRIVAQG 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-250 |
3.52e-25 |
|
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: 102.13 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrqfigslrgagesspggdgrdsrt 91
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG----------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 vQDLllsvapvrvkeaaERLNGAELAmmeredekTQMRY-AQAitdytdaggydievlwdtctMAALGApyDNVKYRDLT 170
Cdd:cd03214 61 -KDL-------------ASLSPKELA--------RKIAYvPQA--------------------LELLGL--AHLADRPFN 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 171 TLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVSHDRQLLANAVDRIVTVESGN 245
Cdd:cd03214 97 ELSGGERQRVLLaRALAQEPP-ILLLDEPTSHLDIAHQIELLELLRrlarERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
....*
gi 2796936914 246 VWIHG 250
Cdd:cd03214 176 IVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-239 |
8.91e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 103.25 E-value: 8.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG-LGVMRQFIGSLrgagessPggdgrdsr 90
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpPRRARRRIGYV-------P-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 tvQDLLLSVA-PVRVKE--AAERLNGAELAMMEREDEKTQMRYAqaitdytdaggydievlwdtctMAALGApyDNVKYR 167
Cdd:COG1121 82 --QRAEVDWDfPITVRDvvLMGRYGRRGLFRRPSRADREAVDEA----------------------LERVGL--EDLADR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796936914 168 DLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLE---QALRETSKTVLLVSHDRQLLANAVDRIV 239
Cdd:COG1121 136 PIGELSGGQQQRVLLaRALAQDPD-LLLLDEPFAGVDAATEEALYellRELRREGKTILVVTHDLGAVREYFDRVL 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-244 |
2.57e-24 |
|
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: 99.24 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDgRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHagglgvmrqfigslrgagess 81
Cdd:cd00267 1 EIENLSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 82 pggDGRDsrtvqdlllsVAPVRVKEAAERLngaelammeredektqmryaqaitdytdagGYdievlwdtctmaalgapy 161
Cdd:cd00267 59 ---DGKD----------IAKLPLEELRRRI------------------------------GY------------------ 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 162 dnvkyrdLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSK---TVLLVSHDRQLLANAVDR 237
Cdd:cd00267 78 -------VPQLSGGQRQRVALaRALLLNPD-LLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADR 149
|
....*..
gi 2796936914 238 IVTVESG 244
Cdd:cd00267 150 VIVLKDG 156
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-234 |
1.38e-21 |
|
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: 92.93 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLThVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrqfigslrgages 80
Cdd:COG4133 3 LEAENLS-CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 spGGDGRDSRTVQDLLLSVAP-VRVKEAaerLNGAElammeredektQMRYAQAItdytDAGGYDIEVLWDtcTMAALG- 158
Cdd:COG4133 64 --EPIRDAREDYRRRLAYLGHaDGLKPE---LTVRE-----------NLRFWAAL----YGLRADREAIDE--ALEAVGl 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796936914 159 APYDNVKYRdltTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK---TVLLVSHDRQLLANA 234
Cdd:COG4133 122 AGLADLPVR---QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQPLELAAA 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-246 |
2.98e-21 |
|
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: 90.92 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrqfigslrgagesspggdgrdsrtv 92
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEI---------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 qdlllsvapvrvkeaaeRLNGAElamMEREDEKTQMRyaqaItdytdagGYDIEVlwdtctmaalGAPYDNVKYRDLTTL 172
Cdd:cd03230 58 -----------------KVLGKD---IKKEPEEVKRR----I-------GYLPEE----------PSLYENLTVRENLKL 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 173 SGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRE---TSKTVLLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:cd03230 97 SGGMKQRLALaQALLHDPE-LLILDEPTSGLDPESRREFWELLRElkkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
353-518 |
7.40e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 91.03 E-value: 7.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQT--------HARPELLGRTPCE---- 420
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrrqvayvPQEPALWGGTVRDnlpf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 421 IVMTEHARLKNEAMKA-LARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEA----LQAG 495
Cdd:COG4619 97 PFQLRERKFDRERALElLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRveelLREY 176
|
170 180
....*....|....*....|....
gi 2796936914 496 LDAFDGTVLAVTHDR-WFAADFDR 518
Cdd:COG4619 177 LAEEGRAVLWVSHDPeQIERVADR 200
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-244 |
8.50e-21 |
|
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: 89.36 E-value: 8.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrqfigslrgagesspggdgrdsr 90
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 tvqdlllsvapvrvkeaaeRLNGAELAMMEREDektqmrYAQAItdytdagGY---DIeVLWDTcTMAalgapyDNVkyr 167
Cdd:cd03228 60 -------------------LIDGVDLRDLDLES------LRKNI-------AYvpqDP-FLFSG-TIR------ENI--- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 168 dlttLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETS--KTVLLVSHDRQLLANAvDRIVTVESG 244
Cdd:cd03228 97 ----LSGGQRQRIAIaRALLRDPP-ILILDEATSALDPETEALILEALRALAkgKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-239 |
1.32e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 90.89 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-----GLGVMRQFIGSLrgagessPGGDG 86
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvarDPAEVRRRIGYV-------PQEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 87 -RDSRTVQDLLLSVApvrvkeaaeRLNGAelammereDEKTQMRYAQAITDYTDaggydievLWDtctmaalgapydnVK 165
Cdd:COG1131 84 lYPDLTVRENLRFFA---------RLYGL--------PRKEARERIDELLELFG--------LTD-------------AA 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 166 YRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETS---KTVLLVSHDRQLLANAVDRIV 239
Cdd:COG1131 126 DRKVGTLSGGMKQRLGLaLALLHDPE-LLILDEPTSGLDPEARRELWELLRELAaegKTVLLSTHYLEEAERLCDRVA 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-246 |
1.51e-20 |
|
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: 88.81 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDG-RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrqfigslrgages 80
Cdd:cd03246 2 EVENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 spggdgrdsrtvqdlllsvapvrvkeaaeRLNGAELAMMEREDektqmrYAQAItdytdagGY---DIEVLWDTCTmaal 157
Cdd:cd03246 60 -----------------------------RLDGADISQWDPNE------LGDHV-------GYlpqDDELFSGSIA---- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 158 gapyDNVkyrdlttLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRETSK---TVLLVSHDRQLLAn 233
Cdd:cd03246 94 ----ENI-------LSGGQRQRLGLaRALYGNP-RILVLDEPNSHLDVEGERALNQAIAALKAagaTRIVIAHRPETLA- 160
|
250
....*....|...
gi 2796936914 234 AVDRIVTVESGNV 246
Cdd:cd03246 161 SADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
356-527 |
3.65e-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: 89.06 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHAR--------PE--LLGRTP------- 418
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRkvglvfqnPDdqFFGPTVeeevafg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 419 CEIVMTEHARLKNEAMKALARYELAgGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDA 498
Cdd:cd03225 101 LENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK 179
|
170 180 190
....*....|....*....|....*....|...
gi 2796936914 499 F--DG-TVLAVTHDRWFAADF-DRYMVFGtDGR 527
Cdd:cd03225 180 LkaEGkTIIIVTHDLDLLLELaDRVIVLE-DGK 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
332-509 |
5.19e-20 |
|
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: 88.30 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 332 RGGRTakravICENLelsglmkpfDLEIWYGERVAVLGSNGSGKSHFLRLIAGE------EVRHTGVARlgARVVPGHFA 405
Cdd:COG4133 12 RGERL-----LFSGL---------SFTLAAGEALALTGPNGSGKTTLLRILAGLlppsagEVLWNGEPI--RDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 406 QTHARPELLG----RTPCEIVMTeHARLKN------EAMKALARYELAGgVAEQRFETLSGGQQARLQILLLEMSGATLL 475
Cdd:COG4133 76 RLAYLGHADGlkpeLTVRENLRF-WAALYGlradreAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 2796936914 476 LLDEPTDNLDLASAEALQAGLDAF---DGTVLAVTHD 509
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQ 190
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-200 |
1.34e-19 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 85.39 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVT-------------HAGGLGVMRQFIGSLRgagESSPG 83
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderksLRKEIGYVFQDPQLFP---RLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 84 GDGRDSRTVQDLLLSVAPVRVKEAAERLNGAELAmmeredektqmryaqaitdytdaggydievlwdtctmaalgapyDN 163
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLA--------------------------------------------DR 113
|
170 180 190
....*....|....*....|....*....|....*...
gi 2796936914 164 VKYRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDN 200
Cdd:pfam00005 114 PVGERPGTLSGGQRQRVAIaRALLTKPK-LLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-246 |
1.58e-19 |
|
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: 91.74 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-------------GLGVMRQ----FIGS 73
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQnpylFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 74 LR-----GAGESSpggdgrdsrtvqdlllsvaPVRVKEAAERLNGAELAMmeredektqmryaqaitdyTDAGGYDievl 148
Cdd:COG4988 427 IRenlrlGRPDAS-------------------DEELEAALEAAGLDEFVA-------------------ALPDGLD---- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 149 wdtcTMAALGApydnvkyrdlTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETS--KTVLLVS 225
Cdd:COG4988 465 ----TPLGEGG----------RGLSGGQAQRLALaRALLRDAP-LLLLDEPTAHLDAETEAEILQALRRLAkgRTVILIT 529
|
250 260
....*....|....*....|.
gi 2796936914 226 HDRQLLANAvDRIVTVESGNV 246
Cdd:COG4988 530 HRLALLAQA-DRILVLDDGRI 549
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2-244 |
3.19e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 86.16 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrqFIGslrgaGESS 81
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI-----------LLN-----GKPI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 82 PGGDGRDS-----RTVQDLLLSVApVRvkeaAERLNGAELAmmeredektqmryaqaitdytDAGGYDIEVLWDTCTMAA 156
Cdd:cd03226 65 KAKERRKSigyvmQDVDYQLFTDS-VR----EELLLGLKEL---------------------DAGNEQAETVLKDLDLYA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 LgapydnvKYRDLTTLSGGEQKRLALE-ALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRE---TSKTVLLVSHDRQLLA 232
Cdd:cd03226 119 L-------KERHPLSLSGGQKQRLAIAaALLSGKD-LLIFDEPTSGLDYKNMERVGELIRElaaQGKAVIVITHDYEFLA 190
|
250
....*....|..
gi 2796936914 233 NAVDRIVTVESG 244
Cdd:cd03226 191 KVCDRVLLLANG 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-535 |
5.78e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 90.25 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 26 EGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGL-GVMRQFIGS-LRGAGESSPGGDGRDSRTVQ--DLLlsvaP 101
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWdEVLKRFRGTeLQNYFKKLYNGEIKVVHKPQyvDLI----P 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 102 VRVKEAAERLngaelamMEREDEKTQMRyaqaitDYTDAggYDIEVLWDtctmaalgapydnvkyRDLTTLSGGEQKRLA 181
Cdd:PRK13409 174 KVFKGKVREL-------LKKVDERGKLD------EVVER--LGLENILD----------------RDISELSGGELQRVA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 182 LEA-LLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETS--KTVLLVSHDRQLLANAVDRIVTVesgnvwiHG--GGFATY 256
Cdd:PRK13409 223 IAAaLLRDAD-FYFFDEPTSYLDIRQRLNVARLIRELAegKYVLVVEHDLAVLDYLADNVHIA-------YGepGAYGVV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 257 SEARKDR---NERLD-ELRrrwdEEHaklkrlvVMLRQKATyndsmaapyhaaqtrlrRFEEAGPPELAPKDQLIsmrlr 332
Cdd:PRK13409 295 SKPKGVRvgiNEYLKgYLP----EEN-------MRIRPEPI-----------------EFEERPPRDESERETLV----- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 333 ggrtakravicenlELSGLMKP---FDL-----EIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVV--PG 402
Cdd:PRK13409 342 --------------EYPDLTKKlgdFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISykPQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 403 H-FAQTHARPELLGRTPCEIVMTEHarLKNEAMKALARYELaggvAEQRFETLSGGQQARLQI---LLLEmsgATLLLLD 478
Cdd:PRK13409 408 YiKPDYDGTVEDLLRSITDDLGSSY--YKSEIIKPLQLERL----LDKNVKDLSGGELQRVAIaacLSRD---ADLYLLD 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 479 EPTDNLD----LASAEALQAGLDAFDGTVLAVTHDRWFaADF--DRYMVF-GTDGRVYESPEPV 535
Cdd:PRK13409 479 EPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYM-IDYisDRLMVFeGEPGKHGHASGPM 541
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
353-529 |
5.98e-19 |
|
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: 86.64 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLG------------ARVVpGHFAQTHARPE-------- 412
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlaslsrrelARRI-AYVPQEPPAPFgltvrelv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 413 LLGRTP-CEIVMTEHARLKNEAMKALARYELAgGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASA-- 489
Cdd:COG1120 97 ALGRYPhLGLFGRPSAEDREAVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQle 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2796936914 490 --EALQAGLDAFDGTVLAVTHDRWFAADF-DRyMVFGTDGRVY 529
Cdd:COG1120 176 vlELLRRLARERGRTVVMVLHDLNLAARYaDR-LVLLKDGRIV 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-246 |
6.51e-19 |
|
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: 90.28 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG------GLGVMRQFIGSLrgagesspgg 84
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqiDPASLRRQIGVV---------- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 85 dGRD----SRTVQD-LLLSVAPV---RVKEAAERLNGAELAMmeredeKTQMRYAQAITDytdaGGydievlwdtctmaa 156
Cdd:COG2274 555 -LQDvflfSGTIREnITLGDPDAtdeEIIEAARLAGLHDFIE------ALPMGYDTVVGE----GG-------------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 lgapydnvkyrdlTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRE--TSKTVLLVSHDRQLLAN 233
Cdd:COG2274 610 -------------SNLSGGQRQRLAIaRALLRNP-RILILDEATSALDAETEAIILENLRRllKGRTVIIIAHRLSTIRL 675
|
250
....*....|...
gi 2796936914 234 AvDRIVTVESGNV 246
Cdd:COG2274 676 A-DRIIVLDKGRI 687
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-239 |
1.02e-18 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 84.83 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGR---PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfigsLRGA 77
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVL--------------VDGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 78 GESSPGGDG-----RDS----RTVQD---LLLSVAPVRVKEAAERLNGAeLAMMEREDektqmrYAQAitdYtdaggydi 145
Cdd:cd03293 67 PVTGPGPDRgyvfqQDAllpwLTVLDnvaLGLELQGVPKAEARERAEEL-LELVGLSG------FENA---Y-------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 146 evlwdtctmaalgaPYDnvkyrdlttLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKI----WLEQALRETSKT 220
Cdd:cd03293 129 --------------PHQ---------LSGGMRQRVALaRALAVDPD-VLLLDEPFSALDALTREqlqeELLDIWRETGKT 184
|
250 260
....*....|....*....|..
gi 2796936914 221 VLLVSHDrqlLANAV---DRIV 239
Cdd:cd03293 185 VLLVTHD---IDEAVflaDRVV 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-527 |
2.66e-18 |
|
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: 88.30 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 26 EGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGL-GVMRQFIGSLrgagesspggdgrdsrtVQDLL-------L 97
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWdEVLKRFRGTE-----------------LQDYFkklangeI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 98 SVA--PVRVKEAAERLNGAELAMMEREDEKTQMRYAqaitdytdAGGYDIEVLWDtctmaalgapydnvkyRDLTTLSGG 175
Cdd:COG1245 161 KVAhkPQYVDLIPKVFKGTVRELLEKVDERGKLDEL--------AEKLGLENILD----------------RDISELSGG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 176 EQKRLALEA-LLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETS---KTVLLVSHDRQLLanavDRIvtveSGNVWI-HG 250
Cdd:COG1245 217 ELQRVAIAAaLLRDAD-FYFFDEPSSYLDIYQRLNVARLIRELAeegKYVLVVEHDLAIL----DYL----ADYVHIlYG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 251 --GGFATYSEARKDR---NERLD-ELRrrwdEEHaklkrlvVMLRQKATyndsmaapyhaaqtrlrRFEEAGPPelapkd 324
Cdd:COG1245 288 epGVYGVVSKPKSVRvgiNQYLDgYLP----EEN-------VRIRDEPI-----------------EFEVHAPR------ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 325 qlismrlrggRTAKRAVICENLELSGLMKPFDL-----EIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARV 399
Cdd:COG1245 334 ----------REKEEETLVEYPDLTKSYGGFSLeveggEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 400 ------VPGHFAQTHArpELLGRTPCEIVMTehARLKNEAMKALARYELaggvAEQRFETLSGGQQARLQI---LLLEms 470
Cdd:COG1245 404 sykpqyISPDYDGTVE--EFLRSANTDDFGS--SYYKTEIIKPLGLEKL----LDKNVKDLSGGELQRVAIaacLSRD-- 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 471 gATLLLLDEPTDNLD----LASAEALQAGLDAFDGTVLAVTHDRWFaADF--DRYMVF-GTDGR 527
Cdd:COG1245 474 -ADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYL-IDYisDRLMVFeGEPGV 535
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-239 |
4.72e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.99 E-value: 4.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLP---DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfigsLRGAG 78
Cdd:COG1116 9 ELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVL--------------VDGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 79 ESSPGGD-G----RDS----RTVQD---LLLSVAPVRVKEAAERLNGAeLAMMEredektqmryaqaITDYTDAggYdie 146
Cdd:COG1116 75 VTGPGPDrGvvfqEPAllpwLTVLDnvaLGLELRGVPKAERRERAREL-LELVG-------------LAGFEDA--Y--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 147 vlwdtctmaalgaPYdnvkyrdltTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKI----WLEQALRETSKTV 221
Cdd:COG1116 136 -------------PH---------QLSGGMRQRVAIaRALANDPE-VLLMDEPFGALDALTRErlqdELLRLWQETGKTV 192
|
250 260
....*....|....*....|.
gi 2796936914 222 LLVSHDrqlLANAV---DRIV 239
Cdd:COG1116 193 LFVTHD---VDEAVflaDRVV 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-246 |
5.09e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.18 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG----------------GLGVMRQfigsl 74
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQ----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 75 rgagesspggDGR--DSRTVQD---LLLSVAPVRVKEAAERLNGAeLAMMEREDEKTQMryaqaitdytdaggydievlw 149
Cdd:COG2884 87 ----------DFRllPDRTVYEnvaLPLRVTGKSRKEIRRRVREV-LDLVGLSDKAKAL--------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 150 dtctmaalgaPYdnvkyrdltTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDvP---GKIW-LEQALRETSKTVLLV 224
Cdd:COG2884 135 ----------PH---------ELSGGEQQRVAIaRALVNRPE-LLLADEPTGNLD-PetsWEIMeLLEEINRRGTTVLIA 193
|
250 260
....*....|....*....|..
gi 2796936914 225 SHDRQLLANAVDRIVTVESGNV 246
Cdd:COG2884 194 THDLELVDRMPKRVLELEDGRL 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-250 |
6.36e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 83.63 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLpDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG-------------LGVM 67
Cdd:COG4559 2 LEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRplaawspwelarrRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 68 RQfigslrgageSSpggdgrdsrtvqdlllSVA-PVRVKEAAE--RLNGAElammEREDEKTQMRYAQAITDytdaggyd 144
Cdd:COG4559 81 PQ----------HS----------------SLAfPFTVEEVVAlgRAPHGS----SAAQDRQIVREALALVG-------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 145 ievlwdtctMAALGApydnvkyRDLTTLSGGEQKR--LA-----LEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRET 217
Cdd:COG4559 123 ---------LAHLAG-------RSYQTLSGGEQQRvqLArvlaqLWEPVDGGPRWLFLDEPTSALDLAHQHAVLRLARQL 186
|
250 260 270
....*....|....*....|....*....|....*.
gi 2796936914 218 SK---TVLLVSHDRQLLANAVDRIVTVESGNVWIHG 250
Cdd:COG4559 187 ARrggGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
13-246 |
7.54e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.28 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG-------------LGVMRQfigslrgage 79
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelarrRAVLPQ---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 80 SSpggdgrdsrtvqdlllSVA-PVRVKEAAeRLNGAELAMMEREDEktqmRYAQAITDYTDAGGYdievlwdtctmaalg 158
Cdd:PRK13548 84 HS----------------SLSfPFTVEEVV-AMGRAPHGLSRAEDD----ALVAAALAQVDLAHL--------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 159 apydnvKYRDLTTLSGGEQKRLALEALL------RGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDR 228
Cdd:PRK13548 128 ------AGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHerglAVIVVLHDL 201
|
250
....*....|....*...
gi 2796936914 229 QLLANAVDRIVTVESGNV 246
Cdd:PRK13548 202 NLAARYADRIVLLHQGRL 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-235 |
7.59e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 86.93 E-value: 7.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV------------THAGGLGVMRQFIGSLrGAGE 79
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevayfdQHRAELDPEKTVMDNL-AEGK 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 80 SSPGGDGRDsRTV----QDLLLSvaPVRvkeaaerlngaelAMmeredektqmryaqaitdytdaggydievlwdtctma 155
Cdd:PRK11147 409 QEVMVNGRP-RHVlgylQDFLFH--PKR-------------AM------------------------------------- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 156 algAPydnVKyrdltTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAV 235
Cdd:PRK11147 436 ---TP---VK-----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTV 504
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-241 |
8.09e-18 |
|
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: 86.57 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 3 VSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrqfigslRGAGESSP 82
Cdd:TIGR02857 324 FSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI----------------AVNGVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 83 GGDgRDSRTVQDLLLSVAPVRV-KEAAErlngaELAMMEREDEKTQMRYAqaitdYTDAGGYDIEvlwdtctmAALGAPY 161
Cdd:TIGR02857 388 DAD-ADSWRDQIAWVPQHPFLFaGTIAE-----NIRLARPDASDAEIREA-----LERAGLDEFV--------AALPQGL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 162 DNVKYRDLTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRETS--KTVLLVSHDRQLLANAvDRI 238
Cdd:TIGR02857 449 DTPIGEGGAGLSGGQAQRLALaRAFLRDA-PLLLLDEPTAHLDAETEAEVLEALRALAqgRTVLLVTHRLALAALA-DRI 526
|
...
gi 2796936914 239 VTV 241
Cdd:TIGR02857 527 VVL 529
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
356-528 |
1.14e-17 |
|
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: 82.00 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAG-------------EEVRHTGVARLGARVV-----PGH--FAQTHAR----- 410
Cdd:COG1122 21 SLSIEKGEFVAIIGPNGSGKSTLLRLLNGllkptsgevlvdgKDITKKNLRELRRKVGlvfqnPDDqlFAPTVEEdvafg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 411 PELLGRTPCEIvmteHARlkneAMKALARYELAgGVAEQRFETLSGGQQARLQIL-LLEMsGATLLLLDEPTDNLDLASA 489
Cdd:COG1122 101 PENLGLPREEI----RER----VEEALELVGLE-HLADRPPHELSGGQKQRVAIAgVLAM-EPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2796936914 490 EALQ---AGLDAFDGTVLAVTHDRWFAAD-FDRYMVFGtDGRV 528
Cdd:COG1122 171 RELLellKRLNKEGKTVIIVTHDLDLVAElADRVIVLD-DGRI 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-246 |
1.39e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.89 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrqfigslRGAGESSPGGDGRDSRTV 92
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG------------DDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 -QDLLLSVApVRVKEAAErlngaelamMEREDEKTqmRYAQAitdyTDAGGYDIEVLWDTCTMAALGApydnvkyRDLTT 171
Cdd:PRK09536 83 pQDTSLSFE-FDVRQVVE---------MGRTPHRS--RFDTW----TETDRAAVERAMERTGVAQFAD-------RPVTS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIW---LEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRtleLVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
356-509 |
1.43e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 82.44 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGE------EVRHTG--VARLGARV--VPghfaQthaRPELLGRTP---CEIV 422
Cdd:COG1121 26 SLTIPPGEFVAIVGPNGAGKSTLLKAILGLlpptsgTVRLFGkpPRRARRRIgyVP----Q---RAEVDWDFPitvRDVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 423 MTE-----------HARLKNEAMKALARYELAGgVAEQRFETLSGGQQARL---QILlleMSGATLLLLDEPTDNLDLAS 488
Cdd:COG1121 99 LMGrygrrglfrrpSRADREAVDEALERVGLED-LADRPIGELSGGQQQRVllaRAL---AQDPDLLLLDEPFAGVDAAT 174
|
170 180
....*....|....*....|....
gi 2796936914 489 AEALQA---GLDAFDGTVLAVTHD 509
Cdd:COG1121 175 EEALYEllrELRREGKTILVVTHD 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
351-527 |
1.52e-17 |
|
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: 79.98 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 351 LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpghfaqtHARPELLGRTPCEIVMteharlk 430
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-------AKLPLEELRRRIGYVP------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 431 neamkalaryelaggvaeQrfetLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF---DGTVLAVT 507
Cdd:cd00267 80 ------------------Q----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVT 137
|
170 180
....*....|....*....|
gi 2796936914 508 HDRWFAADFDRYMVFGTDGR 527
Cdd:cd00267 138 HDPELAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-244 |
1.93e-17 |
|
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: 80.31 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPdGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfigslrgages 80
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 spggdgrdsrtvqdlllsvapvrvkeaaerLNGAELAMMEREDEKTQMRYAQAITDYTdaggydievLWDTCTMaalgap 160
Cdd:cd03229 59 ------------------------------IDGEDLTDLEDELPPLRRRIGMVFQDFA---------LFPHLTV------ 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 161 YDNVKYRdlttLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVSHDRQLLANAV 235
Cdd:cd03229 94 LENIALG----LSGGQQQRVALaRALAMDPD-VLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLA 168
|
....*....
gi 2796936914 236 DRIVTVESG 244
Cdd:cd03229 169 DRVVVLRDG 177
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-250 |
2.62e-17 |
|
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: 81.67 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHA-----GGLGV--MRQFIG----SLrgaGES 80
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLfgerrGGEDVweLRKRIGlvspAL---QLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 SPGGDgrdsrTVQDLLLSvapvrvkeaaerlngaelammeredektqmryaqaitdytdaGGYDIEVLWDTCT------- 153
Cdd:COG1119 91 FPRDE-----TVLDVVLS------------------------------------------GFFDSIGLYREPTdeqrera 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 154 ---MAALGApyDNVKYRDLTTLSGGEQKR-LALEALLRGPdQTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVS 225
Cdd:COG1119 124 relLELLGL--AHLADRPFGTLSQGEQRRvLIARALVKDP-ELLILDEPTAGLDLGARELLLALLDklaaEGAPTLVLVT 200
|
250 260
....*....|....*....|....*
gi 2796936914 226 HDRQLLANAVDRIVTVESGNVWIHG 250
Cdd:COG1119 201 HHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
353-481 |
2.62e-17 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 78.84 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEE-------------VRHTGVARLGARVV-----PGHFAQTHARPELL 414
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLsptegtilldgqdLTDDERKSLRKEIGyvfqdPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796936914 415 GRTPCEIVMTEH--ARLKnEAMKALARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPT 481
Cdd:pfam00005 82 LGLLLKGLSKREkdARAE-EALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-247 |
6.52e-17 |
|
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: 79.86 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDG-RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVtHAGGLGVMRQFIGSLRGAGe 79
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-YINGYSIRTDRKAARQSLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 80 SSPGGDGRDSR-TVQDLLLSVApvrvkeaaeRLNGAELAMMEREDEktQMRYAQAITDYTDaggydievlwdtctmaalg 158
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFYA---------RLKGLPKSEIKEEVE--LLLRVLGLTDKAN------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 159 apydnvkyRDLTTLSGGEQKRLALE-ALLRGPdQTLLLDEPDNYLDVPGK--IW-LEQALREtSKTVLLVSHDRQLLANA 234
Cdd:cd03263 129 --------KRARTLSGGMKRKLSLAiALIGGP-SVLLLDEPTSGLDPASRraIWdLILEVRK-GRSIILTTHSMDEAEAL 198
|
250
....*....|...
gi 2796936914 235 VDRIVTVESGNVW 247
Cdd:cd03263 199 CDRIAIMSDGKLR 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
302-531 |
7.75e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 83.66 E-value: 7.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 302 YHAAQTRLRRFEEAGPPELAPKDQLIsmrlrggRTAKRAVICENLELS------GLMKPFDLEIWYGERVAVLGSNGSGK 375
Cdd:COG4987 302 VRAAARRLNELLDAPPAVTEPAEPAP-------APGGPSLELEDVSFRypgagrPVLDGLSLTLPPGERVAIVGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 376 SHFLRLIAGEEVRHTGVARLGarvvpGHFAQTHARPELLGRTpceIVMTEHARLKN-----------------EAMKALA 438
Cdd:COG4987 375 STLLALLLRFLDPQSGSITLG-----GVDLRDLDEDDLRRRI---AVVPQRPHLFDttlrenlrlarpdatdeELWAALE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 439 RYELAGGVAEQRF----------ETLSGGQQARLQI--LLLemSGATLLLLDEPTDNLDLASAEALQAGLDAF--DGTVL 504
Cdd:COG4987 447 RVGLGDWLAALPDgldtwlgeggRRLSGGERRRLALarALL--RDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVL 524
|
250 260
....*....|....*....|....*..
gi 2796936914 505 AVTHDRWFAADFDRyMVFGTDGRVYES 531
Cdd:COG4987 525 LITHRLAGLERMDR-ILVLEDGRIVEQ 550
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-247 |
1.70e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGdLQPI-EGSVTHAGGLGVMrqF--------I 71
Cdd:COG4178 363 LALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIARPAGARVL--FlpqrpylpL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 72 GSLRGAgESSPGGDGRDSRTvqdlllsvapvRVKEAAERLNGAELAmmEREDEktqmryaqaitdytdaggydiEVLWDt 151
Cdd:COG4178 440 GTLREA-LLYPATAEAFSDA-----------ELREALEAVGLGHLA--ERLDE---------------------EADWD- 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 152 ctmaalgapydnvkyrdlTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSHdR 228
Cdd:COG4178 484 ------------------QVLSLGEQQRLAFaRLLLHKPD-WLFLDEATSALDEENEAALYQLLREELPgtTVISVGH-R 543
|
250
....*....|....*....
gi 2796936914 229 QLLANAVDRIVTVESGNVW 247
Cdd:COG4178 544 STLAAFHDRVLELTGDGSW 562
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-246 |
2.17e-16 |
|
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: 78.30 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDGR---PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG---------------- 62
Cdd:cd03255 2 ELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisklsekelaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 63 -GLGVMRQF---IGSLrgagesspggdgrdsrTVQD---LLLSVAPVRVKEAAERLngaeLAMMER---EDEKTqmRYAQ 132
Cdd:cd03255 82 rHIGFVFQSfnlLPDL----------------TALEnveLPLLLAGVPKKERRERA----EELLERvglGDRLN--HYPS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 133 aitdytdaggydievlwdtctmaalgapydnvkyrdltTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLD-VPGKIWL 210
Cdd:cd03255 140 --------------------------------------ELSGGQQQRVAIaRALANDPK-IILADEPTGNLDsETGKEVM 180
|
250 260 270
....*....|....*....|....*....|....*....
gi 2796936914 211 E--QAL-RETSKTVLLVSHDRQlLANAVDRIVTVESGNV 246
Cdd:cd03255 181 EllRELnKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
356-509 |
3.41e-16 |
|
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: 77.57 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARL--------GARV--VPGHFAQTHARPeLLGRtpcEIVMT- 424
Cdd:cd03235 19 SFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplekeRKRIgyVPQRRSIDRDFP-ISVR---DVVLMg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 425 --EHARL--------KNEAMKALARYELaGGVAEQRFETLSGGQQARL---QILlleMSGATLLLLDEPTDNLDLASAEA 491
Cdd:cd03235 95 lyGHKGLfrrlskadKAKVDEALERVGL-SELADRQIGELSGGQQQRVllaRAL---VQDPDLLLLDEPFAGVDPKTQED 170
|
170 180
....*....|....*....|.
gi 2796936914 492 LQAGLD--AFDG-TVLAVTHD 509
Cdd:cd03235 171 IYELLRelRREGmTILVVTHD 191
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
356-529 |
3.58e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.27 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVV----PGHFAQTHA----RPEL-----------LGR 416
Cdd:PRK13548 22 SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwsPAELARRRAvlpqHSSLsfpftveevvaMGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPCEIVMTEHARLkneAMKALARYELAGgVAEQRFETLSGGQQARLQI------LLLEMSGATLLLLDEPTDNLDL---- 486
Cdd:PRK13548 102 APHGLSRAEDDAL---VAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLarvlaqLWEPDGPPRWLLLDEPTSALDLahqh 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2796936914 487 -----ASAEALQAGldafdGTVLAVTHDRWFAADF-DRYMVFgTDGRVY 529
Cdd:PRK13548 178 hvlrlARQLAHERG-----LAVIVVLHDLNLAARYaDRIVLL-HQGRLV 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
346-528 |
4.02e-16 |
|
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: 77.53 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF-------------DLEIWYGERVAVLGSNGSGKSHFLRLIA-------------GEEVRHTGVARLGA-R 398
Cdd:cd03255 1 IELKNLSKTYggggekvqalkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGgldrptsgevrvdGTDISKLSEKELAAfR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 399 -----VVpghFAQTHARPELLGR----TPCEIVMTEHARLKNEAMKALARYELaGGVAEQRFETLSGGQQARLQILLLEM 469
Cdd:cd03255 81 rrhigFV---FQSFNLLPDLTALenveLPLLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 470 SGATLLLLDEPTDNLDLASAEA----LQAGLDAFDGTVLAVTHDRWFAADFDR--YMVfgtDGRV 528
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEvmelLRELNKEAGTTIVVVTHDPELAEYADRiiELR---DGKI 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-244 |
4.35e-16 |
|
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: 77.26 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfigslrgagesspggdgrdsrtv 92
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT--------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 qdlLLSVAPVRVKEAAERLnGAEL-------AMMEREDektqMRYAQAITDYTDAggyDIEVLWDTCTMAAlgAPYDNVK 165
Cdd:cd03268 59 ---FDGKSYQKNIEALRRI-GALIeapgfypNLTAREN----LRLLARLLGIRKK---RIDEVLDVVGLKD--SAKKKVK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 166 yrdltTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQ---ALRETSKTVLLVSHDRQLLANAVDRIVTV 241
Cdd:cd03268 126 -----GFSLGMKQRLGIaLALLGNPD-LLILDEPTNGLDPDGIKELRElilSLRDQGITVLISSHLLSEIQKVADRIGII 199
|
...
gi 2796936914 242 ESG 244
Cdd:cd03268 200 NKG 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-256 |
5.60e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 81.06 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrqfigSLRGAGESSPGGDGRDsr 90
Cdd:PLN03073 519 PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA----------KVRMAVFSQHHVDGLD-- 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 tvqdllLSVAPVrvkeaaerlngaeLAMMEREDEKTQMRYAQAITDYTDAGgydievlwdtctmaalgapydNVKYRDLT 170
Cdd:PLN03073 587 ------LSSNPL-------------LYMMRCFPGVPEQKLRAHLGSFGVTG---------------------NLALQPMY 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 171 TLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGNVWIHG 250
Cdd:PLN03073 627 TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFH 706
|
....*.
gi 2796936914 251 GGFATY 256
Cdd:PLN03073 707 GTFHDY 712
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
12-246 |
6.64e-16 |
|
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: 76.79 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVT-----------HAGGLGVMRQFIGSLrgages 80
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtgvppERRNIGMVFQDYALF------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 spggdgrDSRTVQDLLLSvapvrvkeaaerlnGAELAMMEREDEKTQMRyaqaitdytdaggydiEVLWdtctMAALgap 160
Cdd:cd03259 85 -------PHLTVAENIAF--------------GLKLRGVPKAEIRARVR----------------ELLE----LVGL--- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 161 yDNVKYRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQAL----RETSKTVLLVSHDRQLLANAV 235
Cdd:cd03259 121 -EGLLNRYPHELSGGQQQRVALaRALAREPS-LLLLDEPLSALDAKLREELREELkelqRELGITTIYVTHDQEEALALA 198
|
250
....*....|.
gi 2796936914 236 DRIVTVESGNV 246
Cdd:cd03259 199 DRIAVMNEGRI 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-246 |
9.16e-16 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 80.55 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGL------GVMRQFIGSL 74
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 75 rgagessPGGDGRDSRTVQDLLLSVAPVRVKEAaERLNGAELAMMEREDEKTQMryaqaitdytdagGYDIEVLWDTctm 154
Cdd:TIGR01193 554 -------PQEPYIFSGSILENLLLGAKENVSQD-EIWAACEIAEIKDDIENMPL-------------GYQTELSEEG--- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 155 aalgapydnvkyrdlTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDV--PGKIwLEQALRETSKTVLLVSHdRQLLA 232
Cdd:TIGR01193 610 ---------------SSISGGQKQRIALARALLTDSKVLILDESTSNLDTitEKKI-VNNLLNLQDKTIIFVAH-RLSVA 672
|
250
....*....|....
gi 2796936914 233 NAVDRIVTVESGNV 246
Cdd:TIGR01193 673 KQSDKIIVLDHGKI 686
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-244 |
1.13e-15 |
|
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: 76.09 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-------------GLGVMRQ----FIGS 73
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQdvtlFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 74 LRgagesspggdgrdsrtvQDLLLSVAPVrvkEAAERLNGAELAmmeredektqmryaqAITDYTD--AGGYDIEVlwdt 151
Cdd:cd03245 94 LR-----------------DNITLGAPLA---DDERILRAAELA---------------GVTDFVNkhPNGLDLQI---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 152 ctmaalGAPYDNvkyrdlttLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRET--SKTVLLVSHdR 228
Cdd:cd03245 135 ------GERGRG--------LSGGQRQAVALaRALLNDP-PILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITH-R 198
|
250
....*....|....*.
gi 2796936914 229 QLLANAVDRIVTVESG 244
Cdd:cd03245 199 PSLLDLVDRIIVMDSG 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
353-508 |
1.40e-15 |
|
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: 76.66 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGE----------------------EVRHtgvaRLGarVVPGHFAQTHAR 410
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpptygndvrlfgerrggedvwELRK----RIG--LVSPALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 411 PEllgrTPCEIVMT---------EH--ARLKNEAMKALARYELAGgVAEQRFETLSGGQQARLQI---LlleMSGATLLL 476
Cdd:COG1119 94 DE----TVLDVVLSgffdsiglyREptDEQRERARELLELLGLAH-LADRPFGTLSQGEQRRVLIaraL---VKDPELLI 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 2796936914 477 LDEPTDNLDLASAEALQAGLDAFDG----TVLAVTH 508
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-246 |
1.48e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 79.44 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfIgslrgagesspggDGRDSR 90
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL-----------I-------------DGVDIR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TV--QDLLLSVAPV-------------------------RVKEAAERLNGAELAM-MEredektqmryaqaitdytdaGG 142
Cdd:COG1132 406 DLtlESLRRQIGVVpqdtflfsgtirenirygrpdatdeEVEEAAKAAQAHEFIEaLP--------------------DG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 143 YDievlwdtcTMaaLGapydnvkyRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRE--TSK 219
Cdd:COG1132 466 YD--------TV--VG--------ERGVNLSGGQRQRIAIaRALLKDPP-ILILDEATSALDTETEALIQEALERlmKGR 526
|
250 260
....*....|....*....|....*..
gi 2796936914 220 TVLLVSHDRQLLANAvDRIVTVESGNV 246
Cdd:COG1132 527 TTIVIAHRLSTIRNA-DRILVLDDGRI 552
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-244 |
2.48e-15 |
|
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: 74.81 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQ--FIgslrgagesspggdgrDSRTV 92
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQepWI----------------QNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 QDlllsvapvrvkeaaerlN---GAELammereDEKtqmRYAQAItdytdaggydievlwDTCtmaALGAPYDNVKYRDL 169
Cdd:cd03250 83 RE-----------------NilfGKPF------DEE---RYEKVI---------------KAC---ALEPDLEILPDGDL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 170 T-------TLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLD--VPGKIWlEQALRE---TSKTVLLVSHDRQLLANAvD 236
Cdd:cd03250 119 TeigekgiNLSGGQKQRISLaRAVYSDAD-IYLLDDPLSAVDahVGRHIF-ENCILGlllNNKTRILVTHQLQLLPHA-D 195
|
....*...
gi 2796936914 237 RIVTVESG 244
Cdd:cd03250 196 QIVVLDNG 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-246 |
2.87e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.82 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLrgagesspgGDGRDSRTVQ 93
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD------KPISML---------SSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 94 DL---LLSVAPVRVKEAAE-----------RLNGAELAMMEREDEKTQmryaqaITDYTDaggydievlwdtctmaalga 159
Cdd:PRK11231 80 LLpqhHLTPEGITVRELVAygrspwlslwgRLSAEDNARVNQAMEQTR------INHLAD-------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 160 pydnvkyRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETS---KTVLLVSHDRQLLANAVD 236
Cdd:PRK11231 134 -------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtqgKTVVTVLHDLNQASRYCD 206
|
250
....*....|
gi 2796936914 237 RIVTVESGNV 246
Cdd:PRK11231 207 HLVVLANGHV 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
17-244 |
3.24e-15 |
|
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: 75.46 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG------------GLGVMRQF-------------- 70
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglpphriaRLGIARTFqnprlfpeltvlen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 71 --IGSLRGAGESSPGGDGRDSRTVQDLllsvapVRVKEAAERLngaeLAMMEredektqmryaqaITDYTDaggydievl 148
Cdd:COG0411 100 vlVAAHARLGRGLLAALLRLPRARREE------REARERAEEL----LERVG-------------LADRAD--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 149 wdtcTMAAlgapydnvkyrdltTLSGGEQKRLAL-EALLRGPdQTLLLDEP---------DNYLDVpgkiwLEQALRETS 218
Cdd:COG0411 148 ----EPAG--------------NLSYGQQRRLEIaRALATEP-KLLLLDEPaaglnpeetEELAEL-----IRRLRDERG 203
|
250 260
....*....|....*....|....*.
gi 2796936914 219 KTVLLVSHDRQLLANAVDRIVTVESG 244
Cdd:COG0411 204 ITILLIEHDMDLVMGLADRIVVLDFG 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-246 |
3.38e-15 |
|
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: 74.71 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAgGLGVMRQFIGSLRGAGeSSPGGDGRDSR-TVQDL 95
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-GFDVVKEPAEARRRLG-FVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 96 LLSVApvrvkeaaeRLNGaelamMERedektqmryaQAITDytdaggyDIEVLWDTCTMaalgAPYDNVKYRDLTTlsgG 175
Cdd:cd03266 99 LEYFA---------GLYG-----LKG----------DELTA-------RLEELADRLGM----EELLDRRVGGFST---G 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 176 EQKRLAL-EALLRGPdQTLLLDEPDNYLDVPG-KIWLE--QALRETSKTVLLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:cd03266 141 MRQKVAIaRALVHDP-PVLLLDEPTTGLDVMAtRALREfiRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
353-529 |
4.11e-15 |
|
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: 73.62 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGarvvpGHFAQTHARPELlgrtpceivmtehARLKNE 432
Cdd:cd03214 16 DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD-----GKDLASLSPKEL-------------ARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 433 AMKALARYELAGgVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASA----EALQAGLDAFDGTVLAVTH 508
Cdd:cd03214 78 VPQALELLGLAH-LADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQiellELLRRLARERGKTVVMVLH 156
|
170 180
....*....|....*....|..
gi 2796936914 509 DRWFAADF-DRYMVFGtDGRVY 529
Cdd:cd03214 157 DLNLAARYaDRVILLK-DGRIV 177
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-267 |
4.85e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.85 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfIGSlrgagesspggdgrdsrT 91
Cdd:PRK11819 335 GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-----------IGE-----------------T 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 VQdlLLSVAPVRvkeaaERLNgaelammereDEKTQMryaQAIT---DYTDAGGYDIEvlwdtcTMAALGApyDNVKYRD 168
Cdd:PRK11819 387 VK--LAYVDQSR-----DALD----------PNKTVW---EEISgglDIIKVGNREIP------SRAYVGR--FNFKGGD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 169 ----LTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLanavDRIVT---- 240
Cdd:PRK11819 439 qqkkVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFL----DRIAThila 514
|
250 260
....*....|....*....|....*....
gi 2796936914 241 --VESGNVWIHGggfaTYSEARKDRNERL 267
Cdd:PRK11819 515 feGDSQVEWFEG----NFQEYEEDKKRRL 539
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
356-530 |
6.02e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 74.31 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGE------EVRHTG--VARLGARvvpghfAQTHARPELLG------------ 415
Cdd:COG1136 28 SLSIEAGEFVAIVGPSGSGKSTLLNILGGLdrptsgEVLIDGqdISSLSER------ELARLRRRHIGfvfqffnllpel 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 416 ------RTPCEIVMTEHARLKNEAMKALARYELaGGVAEQRFETLSGGQQARLQI---LlleMSGATLLLLDEPTDNLDL 486
Cdd:COG1136 102 talenvALPLLLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIaraL---VNRPKLILADEPTGNLDS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2796936914 487 ASAEALqagLDAFDG-------TVLAVTHDRWFAADFDRyMVFGTDGRVYE 530
Cdd:COG1136 178 KTGEEV---LELLRElnrelgtTIVMVTHDPELAARADR-VIRLRDGRIVS 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-250 |
7.37e-15 |
|
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: 73.38 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDGRpLLNDVSFRIGEGTkAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGV-----MRQFIGSLrg 76
Cdd:cd03264 2 QLENLTKRYGKKR-ALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkqpqkLRRRIGYL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 77 agessPggdgrdsrtvQDLLLSvAPVRVKEAAERLngAELAMMEREDEKTQMRYAQAITDYTDaggydievlwdtctmaa 156
Cdd:cd03264 78 -----P----------QEFGVY-PNFTVREFLDYI--AWLKGIPSKEVKARVDEVLELVNLGD----------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 lgapydnVKYRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRE--TSKTVLLVSHDRQLLANA 234
Cdd:cd03264 123 -------RAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSElgEDRIVILSTHIVEDVESL 195
|
250
....*....|....*.
gi 2796936914 235 VDRIVTVESGNVWIHG 250
Cdd:cd03264 196 CNQVAVLNKGKLVFEG 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
15-246 |
8.83e-15 |
|
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: 73.91 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-----------GLGVMRQFIGSLRgagesspg 83
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHYALFR-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 84 gdgrdSRTVQDlllSVA-PVRVKEAAERLNGAELAmmEREDEktqmryaqaitdytdaggydievLWDTCTMAALGAPYD 162
Cdd:cd03296 88 -----HMTVFD---NVAfGLRVKPRSERPPEAEIR--AKVHE-----------------------LLKLVQLDWLADRYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 163 NvkyrdltTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDvpGKI------WLEQALRETSKTVLLVSHDRQLLANAVD 236
Cdd:cd03296 135 A-------QLSGGQRQRVALARALAVEPKVLLLDEPFGALD--AKVrkelrrWLRRLHDELHVTTVFVTHDQEEALEVAD 205
|
250
....*....|
gi 2796936914 237 RIVTVESGNV 246
Cdd:cd03296 206 RVVVMNKGRI 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-262 |
1.06e-14 |
|
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: 73.63 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG------------GLGVMRQF--IGSLRGAgessp 82
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeditglppheiaRLGIGRTFqiPRLFPEL----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 83 ggdgrdsrTVQDLLLsVApvrvkeAAERLNGAELAMMEREDEKTQMRYAQAITDYTDaggydievLWDtctmaalgapyd 162
Cdd:cd03219 91 --------TVLENVM-VA------AQARTGSGLLLARARREEREARERAEELLERVG--------LAD------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 163 nvkYRDLT--TLSGGEQKRLAL-EALLRGPDqTLLLDEPD---NYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVD 236
Cdd:cd03219 136 ---LADRPagELSYGQQRRLEIaRALATDPK-LLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLAD 211
|
250 260
....*....|....*....|....*.
gi 2796936914 237 RIVTVESGNVWIHGggfaTYSEARKD 262
Cdd:cd03219 212 RVTVLDQGRVIAEG----TPDEVRNN 233
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-256 |
1.28e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 76.47 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV--THAGGLGVMRQfigslrgagesspggdgrDS 89
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQ------------------DH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 90 RTvqdlllsvapvrvkeaaerlngaelammEREDEKTQMRYaqaITDYTDAGGYDIEVlwdtctMAALGA---PYDNVKy 166
Cdd:PRK15064 392 AY----------------------------DFENDLTLFDW---MSQWRQEGDDEQAV------RGTLGRllfSQDDIK- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 167 RDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:PRK15064 434 KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
250
....*....|
gi 2796936914 247 WIHGGGFATY 256
Cdd:PRK15064 514 VDFSGTYEEY 523
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
355-528 |
1.86e-14 |
|
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: 72.53 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLG----------ARVVPGHFAQTHARPEL-------LGRT 417
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaappaDRPVSMLFQENNLFAHLtveqnvgLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 418 PcEIVMTEHARlknEAMKALARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLA---SAEALQA 494
Cdd:cd03298 97 P-GLKLTAEDR---QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAlraEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 2796936914 495 GLDAFDG-TVLAVTHDRWFAADFDRYMVFGTDGRV 528
Cdd:cd03298 173 DLHAETKmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
362-508 |
2.06e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.21 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAG------EEVRHTGvarlGARVVPGHFAQTHarpeLLG-RTPCEIVMTEH------AR 428
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGllppaaGTIKLDG----GDIDDPDVAEACH----YLGhRNAMKPALTVAenlefwAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 429 LKN----EAMKALARYELAGgVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLAS----AEALQAGLDAfD 500
Cdd:PRK13539 100 FLGgeelDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAvalfAELIRAHLAQ-G 177
|
....*...
gi 2796936914 501 GTVLAVTH 508
Cdd:PRK13539 178 GIVIAATH 185
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-246 |
2.53e-14 |
|
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: 72.54 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDGR---PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG-LGVMRQFIGSLRga 77
Cdd:cd03257 3 EVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdLLKLSRRLRKIR-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 78 gesspggdGRDSRTV-QDLLLSVAPV-RVKEA-AERLngaELAMMEREDEKTQMRYAQAitdytdaggydievlwdtctM 154
Cdd:cd03257 81 --------RKEIQMVfQDPMSSLNPRmTIGEQiAEPL---RIHGKLSKKEARKEAVLLL--------------------L 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 155 AALGAPyDNVKYRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVSHDRQ 229
Cdd:cd03257 130 VGVGLP-EEVLNRYPHELSGGQRQRVAIaRALALNPK-LLIADEPTSALDVSVQAQILDLLKklqeELGLTLLFITHDLG 207
|
250
....*....|....*..
gi 2796936914 230 LLANAVDRIVTVESGNV 246
Cdd:cd03257 208 VVAKIADRVAVMYAGKI 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
288-518 |
2.55e-14 |
|
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: 75.40 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 288 LRQKAT-YNDSMAApyHAAQTRLRRFEEAGPPELAPKDQLismrlrgGRTAKRAVICENLELS-----GLMKPFDLEIWY 361
Cdd:TIGR02857 277 LRQLGAqYHARADG--VAAAEALFAVLDAAPRPLAGKAPV-------TAAPASSLEFSGVSVAypgrrPALRPVSFTVPP 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPG--------HFAQTHARPELLGRTpceivMTEHARL-KNE 432
Cdd:TIGR02857 348 GERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADadadswrdQIAWVPQHPFLFAGT-----IAENIRLaRPD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 433 A-----MKALARYELAGGVAE--QRFET--------LSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLD 497
Cdd:TIGR02857 423 AsdaeiREALERAGLDEFVAAlpQGLDTpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALR 502
|
250 260
....*....|....*....|...
gi 2796936914 498 AFDG--TVLAVTHDRWFAADFDR 518
Cdd:TIGR02857 503 ALAQgrTVLLVTHRLALAALADR 525
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-246 |
3.01e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.35 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 16 LLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGdlqpiegsvthagglgVMRQFIGSLRGAGESSPGGDGRDSR----- 90
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG----------------LEHQTSGHIRFHGTDVSRLHARDRKvgfvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 ---------TVQDLL---LSVAPVRvkeaaERLNGAELammereDEKtqmryaqaitdytdaggydIEVLWDTCTMAALG 158
Cdd:PRK10851 81 qhyalfrhmTVFDNIafgLTVLPRR-----ERPNAAAI------KAK-------------------VTQLLEMVQLAHLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 159 APYDnvkyrdlTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKI----WLEQALRETSKTVLLVSHDRQLLANA 234
Cdd:PRK10851 131 DRYP-------AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKelrrWLRQLHEELKFTSVFVTHDQEEAMEV 203
|
250
....*....|..
gi 2796936914 235 VDRIVTVESGNV 246
Cdd:PRK10851 204 ADRVVVMSQGNI 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
17-250 |
3.46e-14 |
|
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: 71.54 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVtHAGGLGV---MRQFIGSL---RGAgesspggdgRDSR 90
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV-LFDGKPLdiaARNRIGYLpeeRGL---------YPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TVQDLLLSVApvrvkeaaeRLNGaelamMEREDEKTQMRY---AQAITDYtdaggydievlwdtctmaalgapydnvKYR 167
Cdd:cd03269 86 KVIDQLVYLA---------QLKG-----LKKEEARRRIDEwleRLELSEY---------------------------ANK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 168 DLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLD-VPGKIWLE--QALRETSKTVLLVSHDRQLLANAVDRIVTVES 243
Cdd:cd03269 125 RVEELSKGNQQKVQFiAAVIHDPE-LLILDEPFSGLDpVNVELLKDviRELARAGKTVILSTHQMELVEELCDRVLLLNK 203
|
....*..
gi 2796936914 244 GNVWIHG 250
Cdd:cd03269 204 GRAVLYG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-244 |
3.51e-14 |
|
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: 71.83 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLThVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGdlqpiegsvthagglgvMRQFIGSLRGAGES 80
Cdd:cd03260 1 IELRDLN-VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNR-----------------LNDLIPGAPDEGEV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 SPGGDGRDSRTVQDLLL--SVAPVRVKEAAERLNGAElammeredektQMRYAQAITDYTDAGGYDIEVLWdTCTMAALg 158
Cdd:cd03260 63 LLDGKDIYDLDVDVLELrrRVGMVFQKPNPFPGSIYD-----------NVAYGLRLHGIKLKEELDERVEE-ALRKAAL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 159 apYDNVKYR-DLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSHDRQLLANA 234
Cdd:cd03260 130 --WDEVKDRlHALGLSGGQQQRLCLaRALANEPE-VLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARV 206
|
250
....*....|
gi 2796936914 235 VDRIVTVESG 244
Cdd:cd03260 207 ADRTAFLLNG 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
353-509 |
4.54e-14 |
|
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: 71.81 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGArvVPGHFAQTHARPEL----------LGRTPCEIV 422
Cdd:COG4555 18 KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG--EDVRKEPREARRQIgvlpderglyDRLTVRENI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 423 mTEHARLKNEAMKALAR--YELA-----GGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAG 495
Cdd:COG4555 96 -RYFAELYGLFDEELKKriEELIellglEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREI 174
|
170
....*....|....*..
gi 2796936914 496 LDAF---DGTVLAVTHD 509
Cdd:COG4555 175 LRALkkeGKTVLFSSHI 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
352-527 |
4.82e-14 |
|
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: 70.29 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 352 MKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpghfaQTHARPELLGRTPCEIVMTEHARLKN 431
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL-----TDLEDELPPLRRRIGMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 432 EAmkalaryelaggVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGL----DAFDGTVLAVT 507
Cdd:cd03229 91 LT------------VLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLkslqAQLGITVVLVT 158
|
170 180
....*....|....*....|.
gi 2796936914 508 HDRWFAADF-DRYMVFGtDGR 527
Cdd:cd03229 159 HDLDEAARLaDRVVVLR-DGK 178
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-244 |
5.07e-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: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQF-----IGSLRGAGESS----PGGD 85
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKkflrrIGVVFGQKTQLwwdlPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 86 GrdsrtvqdLLLSVAPVRVKEAAERLNGAELA-MMEREDE-KTQMRyaqaitdytdaggydievlwdtctmaalgapydn 163
Cdd:cd03267 115 S--------FYLLAAIYDLPPARFKKRLDELSeLLDLEELlDTPVR---------------------------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 164 vkyrdltTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKI----WLEQALRETSKTVLLVSHDRQLLANAVDRI 238
Cdd:cd03267 153 -------QLSLGQRMRAEIaAALLHEPE-ILFLDEPTIGLDVVAQEnirnFLKEYNRERGTTVLLTSHYMKDIEALARRV 224
|
....*.
gi 2796936914 239 VTVESG 244
Cdd:cd03267 225 LVIDKG 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-246 |
6.01e-14 |
|
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: 71.35 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDgRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQ--FIGSLRGAGESSPGgdgRD 88
Cdd:cd03248 25 PD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhkYLHSKVSLVGQEPV---LF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 89 SRTVQDL----LLSVAPVRVKEAAERLNgAELAMMEREDektqmryaqaitdytdagGYDIEVlwdtctmAALGApydnv 164
Cdd:cd03248 101 ARSLQDNiaygLQSCSFECVKEAAQKAH-AHSFISELAS------------------GYDTEV-------GEKGS----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 165 kyrdltTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRE--TSKTVLLVSHDRQLLANAvDRIVTV 241
Cdd:cd03248 150 ------QLSGGQKQRVAIaRALIRNP-QVLILDEATSALDAESEQQVQQALYDwpERRTVLVIAHRLSTVERA-DQILVL 221
|
....*
gi 2796936914 242 ESGNV 246
Cdd:cd03248 222 DGGRI 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-246 |
7.50e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 71.11 E-value: 7.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfIgslrgagesspggDGRDSR 90
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIL-----------I-------------DGQDIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TV-------------QDLLL--------------SVAPVRVKEAAERlngaelAMMEREdektqmryaqaITDYTDagGY 143
Cdd:cd03253 67 EVtldslrraigvvpQDTVLfndtigynirygrpDATDEEVIEAAKA------AQIHDK-----------IMRFPD--GY 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 144 DievlwdtcTMaalgapydnVKYRDLtTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRE--TSKT 220
Cdd:cd03253 128 D--------TI---------VGERGL-KLSGGEKQRVAIaRAILKNPP-ILLLDEATSALDTHTEREIQAALRDvsKGRT 188
|
250 260
....*....|....*....|....*.
gi 2796936914 221 VLLVSHDRQLLANAvDRIVTVESGNV 246
Cdd:cd03253 189 TIVIAHRLSTIVNA-DKIIVLKDGRI 213
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-271 |
8.77e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 74.05 E-value: 8.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG--LGVMRQFIGSLRGAGESSpggdgrdsrt 91
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGikLGYFAQHQLEFLRADESP---------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 VQDLllsvapvrvkeaaerlngAELAMMEREdektqmryaQAITDYTdaGGYdievlwdtctmaalGAPYDNVKyrDLTT 171
Cdd:PRK10636 395 LQHL------------------ARLAPQELE---------QKLRDYL--GGF--------------GFQGDKVT--EETR 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 172 -LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGNVWIHG 250
Cdd:PRK10636 430 rFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFD 509
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2796936914 251 GGFATY-------------------------SEARKDRNERLDELR 271
Cdd:PRK10636 510 GDLEDYqqwlsdvqkqenqtdeapkennansAQARKDQKRREAELR 555
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-250 |
1.03e-13 |
|
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: 69.26 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfigslrgagesspggdgrdsrtvqd 94
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT----------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 95 lllsvapvrvkeaaerLNGAELAMMEREDEKTQMRYAQAITdytdaggydievLWDTCTMAALGAPydnvkyrdlttLSG 174
Cdd:cd03247 61 ----------------LDGVPVSDLEKALSSLISVLNQRPY------------LFDTTLRNNLGRR-----------FSG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 175 GEQKRLALEALLRGPDQTLLLDEPDNYLDvpgKIwLEQALRET------SKTVLLVSHDRQLLANaVDRIVTVESGNVWI 248
Cdd:cd03247 102 GERQRLALARILLQDAPIVLLDEPTVGLD---PI-TERQLLSLifevlkDKTLIWITHHLTGIEH-MDKILFLENGKIIM 176
|
..
gi 2796936914 249 HG 250
Cdd:cd03247 177 QG 178
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
353-527 |
1.37e-13 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 68.95 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGE------EVRHTGV--ARLGARVVPGHFAQTHARPELLGRTpceIvmt 424
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLydptsgEILIDGVdlRDLDLESLRKNIAYVPQDPFLFSGT---I--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 425 eharlkneamkalaryelaggvaeqRFETLSGGQQARLQI---LLlemSGATLLLLDEPTDNLDLASAEALQAGLDAFDG 501
Cdd:cd03228 93 -------------------------RENILSGGQRQRIAIaraLL---RDPPILILDEATSALDPETEALILEALRALAK 144
|
170 180
....*....|....*....|....*...
gi 2796936914 502 --TVLAVTHDRWFAADFDRyMVFGTDGR 527
Cdd:cd03228 145 gkTVIVIAHRLSTIRDADR-IIVLDDGR 171
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-277 |
1.54e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 73.28 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 24 IGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQFIgslrgagesSPGGDGrdsrTVQDLLLSVAPVR 103
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYI---------SPDYDG----TVEEFLRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 104 VK------EAAERLNgaelammeredektqmryaqaitdytdaggydIEVLWDtctmaalgapydnvkyRDLTTLSGGEQ 177
Cdd:COG1245 430 FGssyyktEIIKPLG--------------------------------LEKLLD----------------KNVKDLSGGEL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 178 KRLALEA-LLRGPDqTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVSHDRQLLANAVDRIVtVESGNVWIHGGG 252
Cdd:COG1245 462 QRVAIAAcLSRDAD-LYLLDEPSAHLDVEQRLAVAKAIRrfaeNRGKTAMVVDHDIYLIDYISDRLM-VFEGEPGVHGHA 539
|
250 260
....*....|....*....|....*....
gi 2796936914 253 FATYSeARKDRNERLDEL----RRrwDEE 277
Cdd:COG1245 540 SGPMD-MREGMNRFLKELgitfRR--DEE 565
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
327-509 |
1.85e-13 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 70.09 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 327 ISMRLRGGRTAkravicenleLSGLmkpfDLEIWYGERVAVLGSNGSGKSHFLRLIAGE------EVRHTG--VARLGAR 398
Cdd:COG3638 8 LSKRYPGGTPA----------LDDV----SLEIERGEFVALIGPSGAGKSTLLRCLNGLveptsgEILVDGqdVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 399 VVPGHFAQT---HARPELLGRTPceiVMTE--HARL-----------------KNEAMKALARYELAGgVAEQRFETLSG 456
Cdd:COG3638 74 ALRRLRRRIgmiFQQFNLVPRLS---VLTNvlAGRLgrtstwrsllglfppedRERALEALERVGLAD-KAYQRADQLSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796936914 457 GQQARLQI--LLleMSGATLLLLDEPTDNLDLASAEALqagLDAF------DG-TVLAVTHD 509
Cdd:COG3638 150 GQQQRVAIarAL--VQEPKLILADEPVASLDPKTARQV---MDLLrriareDGiTVVVNLHQ 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-246 |
1.90e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 69.69 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDG---RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG---------GLGVMR 68
Cdd:COG1136 5 LELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 69 --------QF---IGSLrgagesspggdgrdsrTVQD-----LLLS-----VAPVRVKEAAERLNgaelaMMEREDEKTq 127
Cdd:COG1136 85 rrhigfvfQFfnlLPEL----------------TALEnvalpLLLAgvsrkERRERARELLERVG-----LGDRLDHRP- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 128 mryaqaitdytdaggydievlwdtctmaalgapydnvkyrdlTTLSGGEQKRLAL-EALLRGPDqtLLL-DEPDNYLD-V 204
Cdd:COG1136 143 ------------------------------------------SQLSGGQQQRVAIaRALVNRPK--LILaDEPTGNLDsK 178
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2796936914 205 PGKIWLE--QAL-RETSKTVLLVSHDRQlLANAVDRIVTVESGNV 246
Cdd:COG1136 179 TGEEVLEllRELnRELGTTIVMVTHDPE-LAARADRVIRLRDGRI 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-242 |
2.00e-13 |
|
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: 70.13 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 24 IGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG-LGVMRQFIgslrgagesSPGGDGrdsrTVQDLLLSvapv 102
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQYI---------KADYEG----TVRDLLSS---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 103 rvkeaaerlngaelammeredeKTQMRYAQAitdytdaggydievLWDTCTMAALGapYDNVKYRDLTTLSGGEQKRLAL 182
Cdd:cd03237 85 ----------------------ITKDFYTHP--------------YFKTEIAKPLQ--IEQILDREVPELSGGELQRVAI 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 183 EALLRGPDQTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVSHDRQLLANAVDRIVTVE 242
Cdd:cd03237 127 AACLSKDADIYLLDEPSAYLDVEQRLMASKVIRrfaeNNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-251 |
2.46e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMR--QFIGSLRGAG 78
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEneKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 79 ESSPgGDGRDSRTVQDlllSVA--PVRVkeaaeRLNGAELamMEREDEKTQmryAQAITDYTDAggydievlwdtctmaa 156
Cdd:PRK13647 85 FQDP-DDQVFSSTVWD---DVAfgPVNM-----GLDKDEV--ERRVEEALK---AVRMWDFRDK---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 lgAPYDnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETS---KTVLLVSHDRQLLAN 233
Cdd:PRK13647 135 --PPYH---------LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnqgKTVIVATHDVDLAAE 203
|
250
....*....|....*...
gi 2796936914 234 AVDRIVTVESGNVWIHGG 251
Cdd:PRK13647 204 WADQVIVLKEGRVLAEGD 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-251 |
2.84e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 69.73 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG----LGVMRQFIGSLrgagesspggdgrdsrTV 92
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsalLELGAGFHPEL----------------TG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 QDLLlsvapvrvkeaaeRLNGAELAMMERE-DEKTqmryaQAITDYTDAGGYdievlwdtctmaaLGAPydnVKyrdltT 171
Cdd:COG1134 106 RENI-------------YLNGRLLGLSRKEiDEKF-----DEIVEFAELGDF-------------IDQP---VK-----T 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 172 LSGGEQKRLA------LEallrgPDqTLLLDEpdnyldvpgkiWLE--------------QALRETSKTVLLVSHDRQLL 231
Cdd:COG1134 147 YSSGMRARLAfavataVD-----PD-ILLVDE-----------VLAvgdaafqkkclariRELRESGRTVIFVSHSMGAV 209
|
250 260
....*....|....*....|
gi 2796936914 232 ANAVDRIvtvesgnVWIHGG 251
Cdd:COG1134 210 RRLCDRA-------IWLEKG 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
346-510 |
2.97e-13 |
|
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: 69.09 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMK---------PFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpghfaqTHARPEllgR 416
Cdd:cd03259 1 LELKGLSKtygsvraldDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV------TGVPPE---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPCEIVMTEHA------------------RLKNEAMKALARYELA----GGVAEQRFETLSGGQQARLQILLLEMSGATL 474
Cdd:cd03259 72 RNIGMVFQDYAlfphltvaeniafglklrGVPKAEIRARVRELLElvglEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2796936914 475 LLLDEPTDNLDLASAEALQAGL----DAFDGTVLAVTHDR 510
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELkelqRELGITTIYVTHDQ 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
356-518 |
3.68e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.03 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHARPELLGRTPCEIVM------------ 423
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVAmgrwarrglwrr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 424 -TEHARLknEAMKALARYELAgGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFDG- 501
Cdd:NF040873 92 lTRDDRA--AVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAr 168
|
170
....*....|....*....
gi 2796936914 502 --TVLAVTHDRWFAADFDR 518
Cdd:NF040873 169 gaTVVVVTHDLELVRRADP 187
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-250 |
5.28e-13 |
|
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: 68.23 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG--------------GLG-VM--RQFIGSLrgage 79
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglppheraraGIGyVPegRRIFPEL----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 80 sspggdgrdsrTVQDLLLSVAPVRVKEAAERLNGAELAMMEREDEktqmRYAQAitdytdAGgydievlwdtctmaalga 159
Cdd:cd03224 91 -----------TVEENLLLGAYARRRAKRKARLERVYELFPRLKE----RRKQL------AG------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 160 pydnvkyrdltTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYL------DVPGKIwleQALRETSKTVLLVSHDRQLLA 232
Cdd:cd03224 132 -----------TLSGGEQQMLAIaRALMSRPK-LLLLDEPSEGLapkiveEIFEAI---RELRDEGVTILLVEQNARFAL 196
|
250
....*....|....*...
gi 2796936914 233 NAVDRIVTVESGNVWIHG 250
Cdd:cd03224 197 EIADRAYVLERGRVVLEG 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-277 |
7.08e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 33 VGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQFIgslrgagesSPGGDGrdsrTVQDLLLSVAP------VRVkE 106
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYI---------KPDYDG----TVEDLLRSITDdlgssyYKS-E 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 107 AAERLNgaelammeredektqmryaqaitdytdaggydIEVLWDtctmaalgapydnvkyRDLTTLSGGEQKRLALEA-L 185
Cdd:PRK13409 437 IIKPLQ--------------------------------LERLLD----------------KNVKDLSGGELQRVAIAAcL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 186 LRGPDqTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVSHDRQLLANAVDRIVtVESGNVWIHGGGFATYSeARK 261
Cdd:PRK13409 469 SRDAD-LYLLDEPSAHLDVEQRLAVAKAIRriaeEREATALVVDHDIYMIDYISDRLM-VFEGEPGKHGHASGPMD-MRE 545
|
250 260
....*....|....*....|
gi 2796936914 262 DRNERLDEL----RRrwDEE 277
Cdd:PRK13409 546 GMNRFLKELgitfRR--DEE 563
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-226 |
8.28e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 67.38 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGlgvmrqfigslrgagessPGGDGRDSRT 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT------------------PLAEQRDEPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 VQDLLLSVAPvRVKeaaerlngAELAMMEredektQMRYAQAITDYTDaggydiEVLWDTCTMAALgapyDNVKYRDLTT 171
Cdd:TIGR01189 73 ENILYLGHLP-GLK--------PELSALE------NLHFWAAIHGGAQ------RTIEDALAAVGL----TGFEDLPAAQ 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRE---TSKTVLLVSH 226
Cdd:TIGR01189 128 LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhlaRGGIVLLTTH 185
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-246 |
8.97e-13 |
|
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: 67.98 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLgvmrqfIGSLRGAGEss 81
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTD------INKLKGKAL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 82 pggdgRDSRT-----VQDLLLSvapvrvkeaaERLNGAELAMMEREDEKTQMRyaqaitdyTDAGGY---DIEVlwdtcT 153
Cdd:cd03256 74 -----RQLRRqigmiFQQFNLI----------ERLSVLENVLSGRLGRRSTWR--------SLFGLFpkeEKQR-----A 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 154 MAALgapyDNVKYRDL-----TTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVP-GKI---WLEQALRETSKTVLL 223
Cdd:cd03256 126 LAAL----ERVGLLDKayqraDQLSGGQQQRVAIaRALMQQPK-LILADEPVASLDPAsSRQvmdLLKRINREEGITVIV 200
|
250 260
....*....|....*....|...
gi 2796936914 224 VSHDRQLLANAVDRIVTVESGNV 246
Cdd:cd03256 201 SLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-246 |
9.54e-13 |
|
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: 67.32 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 19 DVSFRIGEGTkAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVmrqfigslrgagesspggdgrDSRtvQDLLLS 98
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLF---------------------DSR--KKINLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 99 VAPVRV----KEAA--ERLNGAE-LAMMEREDEKTQMRY-AQAITDYTDaggydievlwdtctmaalgapYDNVKYRDLT 170
Cdd:cd03297 72 PQQRKIglvfQQYAlfPHLNVREnLAFGLKRKRNREDRIsVDELLDLLG---------------------LDHLLNRYPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 171 TLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLANAVDRIVTVESGN 245
Cdd:cd03297 131 QLSGGEKQRVALaRALAAQPE-LLLLDEPFSALDRALRLQLLPELKQIKKnlniPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
.
gi 2796936914 246 V 246
Cdd:cd03297 210 L 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
12-246 |
1.13e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 69.41 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHagglgvmrqfigslrgagesspggDGRD--- 88
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL------------------------NGRDlft 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 89 SRTVQD----------LL-------------LSVAPVRVKEAAERLNGaELAMMERED-EKtqmRY-AQaitdytdaggy 143
Cdd:COG1118 69 NLPPRErrvgfvfqhyALfphmtvaeniafgLRVRPPSKAEIRARVEE-LLELVQLEGlAD---RYpSQ----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 144 dievlwdtctmaalgapydnvkyrdlttLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVpgKI------WLEQALRE 216
Cdd:COG1118 134 ----------------------------LSGGQRQRVALaRALAVEPE-VLLLDEPFGALDA--KVrkelrrWLRRLHDE 182
|
250 260 270
....*....|....*....|....*....|.
gi 2796936914 217 TSKTVLLVSHDrQLLANAV-DRIVTVESGNV 246
Cdd:COG1118 183 LGGTTVFVTHD-QEEALELaDRVVVMNQGRI 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-227 |
1.37e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.80 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPdGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfigsLRGAGES 80
Cdd:PRK11248 2 LQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSIT--------------LDGKPVE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 SPGGDgrdsRTV---QDLLLSVAPVRVKEAAerlnGAELAMMEREDEKTQmryAQAITDYTDAGGYDIEVLWDtctmaal 157
Cdd:PRK11248 67 GPGAE----RGVvfqNEGLLPWRNVQDNVAF----GLQLAGVEKMQRLEI---AHQMLKKVGLEGAEKRYIWQ------- 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 158 gapydnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQAL----RETSKTVLLVSHD 227
Cdd:PRK11248 129 --------------LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
337-508 |
1.48e-12 |
|
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: 66.61 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 337 AKRAVICENLELSgLMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHARPELLGR 416
Cdd:TIGR01189 2 AARNLACSRGERM-LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPC---EIVMTE--------HARLKNEAMKALARYELAGgvAEQR-FETLSGGQQARLQILLLEMSGATLLLLDEPTDNL 484
Cdd:TIGR01189 81 LPGlkpELSALEnlhfwaaiHGGAQRTIEDALAAVGLTG--FEDLpAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*..
gi 2796936914 485 DLASAEALQAGLDAF---DGTVLAVTH 508
Cdd:TIGR01189 159 DKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
356-515 |
1.49e-12 |
|
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: 66.90 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPG----------------HFAQTHARPELLgrtpc 419
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAkerrksigyvmqdvdyQLFTDSVREELL----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 420 eIVMTEHARLKNEAMKALARYELAGgVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQA---GL 496
Cdd:cd03226 95 -LGLKELDAGNEQAETVLKDLDLYA-LKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGElirEL 172
|
170
....*....|....*....
gi 2796936914 497 DAFDGTVLAVTHDRWFAAD 515
Cdd:cd03226 173 AAQGKAVIVITHDYEFLAK 191
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-250 |
1.89e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.54 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 8 HVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQpiegsvthagglgvmrqfiGSLRGAGESSPGG--- 84
Cdd:PRK13547 8 HVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT-------------------GGGAPRGARVTGDvtl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 85 DGRDSRTVQDLLLSVAPVRVKEAAER---LNGAELAMMERedeKTQMRYAQAITDytdaggYDIEVLWdtCTMAALGApy 161
Cdd:PRK13547 69 NGEPLAAIDAPRLARLRAVLPQAAQPafaFSAREIVLLGR---YPHARRAGALTH------RDGEIAW--QALALAGA-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 162 DNVKYRDLTTLSGGEQKRL----ALEALLRGPDQT-----LLLDEPDNYLDVPGKIWLEQALRETSKT----VLLVSHDR 228
Cdd:PRK13547 136 TALVGRDVTTLSGGELARVqfarVLAQLWPPHDAAqppryLLLDEPTAALDLAHQHRLLDTVRRLARDwnlgVLAIVHDP 215
|
250 260
....*....|....*....|..
gi 2796936914 229 QLLANAVDRIVTVESGNVWIHG 250
Cdd:PRK13547 216 NLAARHADRIAMLADGAIVAHG 237
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
356-507 |
2.09e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.35 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLR----LIAGEEVRHTGVARLG---------------ARVVPGH-FAQTHARPEL-- 413
Cdd:PRK09984 24 DLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGrtvqregrlardirkSRANTGYiFQQFNLVNRLsv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 414 --------LGRTP----CEIVMTEHArlKNEAMKALARYELAGgVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPT 481
Cdd:PRK09984 104 lenvligaLGSTPfwrtCFSWFTREQ--KQRALQALTRVGMVH-FAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180
....*....|....*....|....*....
gi 2796936914 482 DNLDLASAEALQAGL---DAFDGTVLAVT 507
Cdd:PRK09984 181 ASLDPESARIVMDTLrdiNQNDGITVVVT 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
353-509 |
2.28e-12 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 66.63 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHAR----PELLG----RTPCEIVMT 424
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRigyvPQEPAlypdLTVRENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 425 eHARL--------KNEAMKALARYELAgGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGL 496
Cdd:COG1131 97 -FARLyglprkeaRERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELL 174
|
170
....*....|....*.
gi 2796936914 497 DAF---DGTVLAVTHD 509
Cdd:COG1131 175 RELaaeGKTVLLSTHY 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
355-509 |
2.43e-12 |
|
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: 66.34 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQT---HARPELLG-RT-------PCEIVM 423
Cdd:cd03293 23 ISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRgyvFQQDALLPwLTvldnvalGLELQG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 424 TEHARLKNEAMKALARYELAGgvAEQRF-ETLSGGQQARLQI---LLLEMSgatLLLLDEPTDNLDLASAEALQAGL--- 496
Cdd:cd03293 103 VPKAEARERAEELLELVGLSG--FENAYpHQLSGGMRQRVALaraLAVDPD---VLLLDEPFSALDALTREQLQEELldi 177
|
170
....*....|....
gi 2796936914 497 -DAFDGTVLAVTHD 509
Cdd:cd03293 178 wRETGKTVLLVTHD 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-246 |
2.86e-12 |
|
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: 66.24 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPLlNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAgGLGVMRQFIGSLRGAGES 80
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVA-GHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 SpggdgrDSRTVQDLLLSVAPVRVKEAAERLNGAELAmmEREDEktqmryaqaITDYTDaggydievLWDtctmaalgap 160
Cdd:cd03265 79 F------QDLSVDDELTGWENLYIHARLYGVPGAERR--ERIDE---------LLDFVG--------LLE---------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 161 ydnVKYRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGK--IW--LEQALRETSKTVLLVSHDRQLLANAV 235
Cdd:cd03265 124 ---AADRLVKTYSGGMRRRLEIaRSLVHRPE-VLFLDEPTIGLDPQTRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLC 199
|
250
....*....|.
gi 2796936914 236 DRIVTVESGNV 246
Cdd:cd03265 200 DRVAIIDHGRI 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-250 |
2.89e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 67.38 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPL----LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrqFIgslrg 76
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI-----------II----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 77 agesspggDGRDsrtVQDLLLSVAPVRvKEAAERLNGAELAMMER---------------EDEKTQMRYAQAitdytdag 141
Cdd:PRK13637 67 --------DGVD---ITDKKVKLSDIR-KKVGLVFQYPEYQLFEEtiekdiafgpinlglSEEEIENRVKRA-------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 142 gydievlwdtctMAALGAPYDNVKYRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGK---IWLEQALRETS 218
Cdd:PRK13637 127 ------------MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRdeiLNKIKELHKEY 194
|
250 260 270
....*....|....*....|....*....|...
gi 2796936914 219 K-TVLLVSHDRQLLANAVDRIVTVESGNVWIHG 250
Cdd:PRK13637 195 NmTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-273 |
3.03e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.44 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGL--GVMRQFIGSL---RGagesspggdGRDSRT 91
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPldPEDRRRIGYLpeeRG---------LYPKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 VQDLLLSVApvrvkeaaeRLNGaelamMEREDEKTQMRYaqaitdytdaggydievlWdtctMAALG-APYDNVKyrdLT 170
Cdd:COG4152 88 VGEQLVYLA---------RLKG-----LSKAEAKRRADE------------------W----LERLGlGDRANKK---VE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 171 TLSGGEQKRLAL-EALLRGPDqtLL-LDEPDNYLDVPGKIWLEQALRE---TSKTVLLVSHDrqlLANA---VDRIVTVE 242
Cdd:COG4152 129 ELSKGNQQKVQLiAALLHDPE--LLiLDEPFSGLDPVNVELLKDVIRElaaKGTTVIFSSHQ---MELVeelCDRIVIIN 203
|
250 260 270
....*....|....*....|....*....|.
gi 2796936914 243 SGNVWIHGggfatysearkdrneRLDELRRR 273
Cdd:COG4152 204 KGRKVLSG---------------SVDEIRRQ 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
356-528 |
3.27e-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: 66.44 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAG-------------EEV------------RHTG--------VARLGA--RVV 400
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGlveptsgsvlidgTDInklkgkalrqlrRQIGmifqqfnlIERLSVleNVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 401 PGHFAQTHARPELLGR-TPCEivmteharlKNEAMKALARYELAGgVAEQRFETLSGGQQARLQILLLEMSGATLLLLDE 479
Cdd:cd03256 101 SGRLGRRSTWRSLFGLfPKEE---------KQRALAALERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 480 PTDNLDLASAEALQAGL----DAFDGTVLAVTHDRWFAADF-DRyMVFGTDGRV 528
Cdd:cd03256 171 PVASLDPASSRQVMDLLkrinREEGITVIVSLHQVDLAREYaDR-IVGLKDGRI 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-259 |
3.29e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.10 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLqPIEGSVTHAG------GLGVMRQFIGSLrGAGESSPGG 84
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielrelDPESWRKHLSWV-GQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 85 dgrdsrTVQDLLLsvapvrvkeaaerlngaeLAMMEREDEKTQMRYAQA-ITDYTD--AGGYDIEVlwdtcTMAALGapy 161
Cdd:PRK11174 438 ------TLRDNVL------------------LGNPDASDEQLQQALENAwVSEFLPllPQGLDTPI-----GDQAAG--- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 162 dnvkyrdlttLSGGEQKRLAL-EALLRgPDQTLLLDEPDNYLDVPGKIWLEQALRETS--KTVLLVSHDRQLLANaVDRI 238
Cdd:PRK11174 486 ----------LSVGQAQRLALaRALLQ-PCQLLLLDEPTASLDAHSEQLVMQALNAASrrQTTLMVTHQLEDLAQ-WDQI 553
|
250 260
....*....|....*....|.
gi 2796936914 239 VTVESGNVwIHGGGFATYSEA 259
Cdd:PRK11174 554 WVMQDGQI-VQQGDYAELSQA 573
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-231 |
4.46e-12 |
|
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: 66.24 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 26 EGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGL-GVMRQFIGS-LRGAGESSPGGDGRDSRTVQ--DLLlsvaP 101
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWdEILDEFRGSeLQNYFTKLLEGDVKVIVKPQyvDLI----P 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 102 VRVKeaaerlnGAELAMMEREDEKTQMRYAqaitdytdaggydIEVLwdtctmaalgaPYDNVKYRDLTTLSGGEQKRLA 181
Cdd:cd03236 101 KAVK-------GKVGELLKKKDERGKLDEL-------------VDQL-----------ELRHVLDRNIDQLSGGELQRVA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2796936914 182 LEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETS---KTVLLVSHDRQLL 231
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAeddNYVLVVEHDLAVL 202
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
356-533 |
4.68e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.46 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTG--------VARLGARVVPGH-------FaQTHarpELL-GRT-- 417
Cdd:COG2884 22 SLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGqvlvngqdLSRLKRREIPYLrrrigvvF-QDF---RLLpDRTvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 418 -----PCEIVMTEHARLKNEAMKALARYELaGGVAEQRFETLSGGQQARLQIlllemsgA-------TLLLLDEPTDNLD 485
Cdd:COG2884 98 envalPLRVTGKSRKEIRRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAI-------AralvnrpELLLADEPTGNLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 486 LASAEALqagLDAFDG------TVLAVTHDRWFAADFDRYMVFGTDGRVYESPE 533
Cdd:COG2884 170 PETSWEI---MELLEEinrrgtTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
14-239 |
6.43e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.91 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGL--GVMRQFIGSlrgagesspggDGRDSRT 91
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYL-----------DTTLPLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 VQDLLLSVAPVRVKE---AAERLNGAELammeredektqmryaqaitdytdaggydievlwdtctmaaLGAPydnvkyrd 168
Cdd:PRK09544 86 VNRFLRLRPGTKKEDilpALKRVQAGHL----------------------------------------IDAP-------- 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796936914 169 LTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWL----EQALRETSKTVLLVSHDRQLLANAVDRIV 239
Cdd:PRK09544 118 MQKLSGGETQRVLLaRALLNRP-QLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-250 |
7.87e-12 |
|
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: 65.33 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG------GLGVMRQFIGSLRgagesspgg 84
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdyTLASLRRQIGLVS--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 85 dgrdsrtvQDLLLSVAPVRVKEAAERLNgaelAMMEREDEKTQMRYAQAITDYTDAGgydievlwdtctmaalgapYDNV 164
Cdd:cd03251 83 --------QDVFLFNDTVAENIAYGRPG----ATREEVEEAARAANAHEFIMELPEG-------------------YDTV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 165 KYRDLTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSHDRQLLANAvDRIVTV 241
Cdd:cd03251 132 IGERGVKLSGGQRQRIAIaRALLKDP-PILILDEATSALDTESERLVQAALERLMKnrTTFVIAHRLSTIENA-DRIVVL 209
|
....*....
gi 2796936914 242 ESGNVWIHG 250
Cdd:cd03251 210 EDGKIVERG 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
356-531 |
8.44e-12 |
|
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: 64.89 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAG-----EEVRHTGVARLGARVVPGhfaqTHARPELLGRT-------PCEIVM 423
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYD----LDVDVLELRRRvgmvfqkPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 424 T---------------EHARLKNEAMKALARYELAGGVAEQRFET-LSGGQQARLQI---LLLEMSgatLLLLDEPTDNL 484
Cdd:cd03260 96 SiydnvayglrlhgikLKEELDERVEEALRKAALWDEVKDRLHALgLSGGQQQRLCLaraLANEPE---VLLLDEPTSAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2796936914 485 DLASAEALQAGLDAF--DGTVLAVTHDRWFAADFDRYMVFGTDGRVYES 531
Cdd:cd03260 173 DPISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-246 |
8.44e-12 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 66.67 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 19 DVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmRQFIGSlrGAGESSPGGDGRDSRTVQDLLL- 97
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-----RTLFDS--RKGIFLPPEKRRIGYVFQEARLf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 98 ---SVapvrvkeaaerlngaelammeredeKTQMRYAqaitdYTDAGGYDIEVLWDTCT-MAALGAPYDnvkyRDLTTLS 173
Cdd:TIGR02142 88 phlSV-------------------------RGNLRYG-----MKRARPSERRISFERVIeLLGIGHLLG----RLPGRLS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 174 GGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKI----WLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:TIGR02142 134 GGEKQRVAIgRALLSSPR-LLLMDEPLAALDDPRKYeilpYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-246 |
9.06e-12 |
|
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: 64.86 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGlgvmrqfIGSLRGAGES-SPGGDGRDSrtvqdl 95
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-------VSSLLGLGGGfNPELTGREN------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 96 llsvapvrvkeaaERLNGAELAMMEREDEKtqmrYAQAITDYTDAGGYdievlwdtctmaaLGAPydnVKyrdltTLSGG 175
Cdd:cd03220 105 -------------IYLNGRLLGLSRKEIDE----KIDEIIEFSELGDF-------------IDLP---VK-----TYSSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 176 EQKRLALE-ALLRGPDqTLLLDEpdnyldvpgkiWLE--------------QALRETSKTVLLVSHDRQLLANAVDRIVT 240
Cdd:cd03220 147 MKARLAFAiATALEPD-ILLIDE-----------VLAvgdaafqekcqrrlRELLKQGKTVILVSHDPSSIKRLCDRALV 214
|
....*.
gi 2796936914 241 VESGNV 246
Cdd:cd03220 215 LEKGKI 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-246 |
9.06e-12 |
|
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: 67.24 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrqfiGSLRGAGESSPGGDGRDSR 90
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG---------KDLTKLSRRSLRELRRRVQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TV-QDLLLSVAP-VRVKEA-AE--RLNGaelaMMEREDEKTQMRYAqaitdytdaggydievlwdtctMAALGAPYDnVK 165
Cdd:COG1123 346 MVfQDPYSSLNPrMTVGDIiAEplRLHG----LLSRAERRERVAEL----------------------LERVGLPPD-LA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 166 YRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKI----WLEQALRETSKTVLLVSHDRQLLANAVDRIV- 239
Cdd:COG1123 399 DRYPHELSGGQRQRVAIaRALALEPK-LLILDEPTSALDVSVQAqilnLLRDLQRELGLTYLFISHDLAVVRYIADRVAv 477
|
250
....*....|..
gi 2796936914 240 -----TVESGNV 246
Cdd:COG1123 478 mydgrIVEDGPT 489
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
346-509 |
9.76e-12 |
|
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: 65.45 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGE------EVRHTG----------VARLG-AR- 398
Cdd:COG0411 5 LEVRGLTKRFgglvavddvSLEVERGEIVGLIGPNGAGKTTLFNLITGFyrptsgRILFDGrditglpphrIARLGiARt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 399 ----------------VVPGHFAQTHARPELLGRTPceIVMTEHARLKNEAMKALARYELAGgVAEQRFETLSGGQQARL 462
Cdd:COG0411 85 fqnprlfpeltvlenvLVAAHARLGRGLLAALLRLP--RARREEREARERAEELLERVGLAD-RADEPAGNLSYGQQRRL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2796936914 463 QILLLEMSGATLLLLDEPTDNLDLASAEALQAGL----DAFDGTVLAVTHD 509
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIrrlrDERGITILLIEHD 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-63 |
1.01e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.12 E-value: 1.01e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG 63
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG 64
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-267 |
1.13e-11 |
|
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: 64.83 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG---------GLGVMRQFIGSL--RGAges 80
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaELYRLRRRMGMLfqSGA--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 spggdGRDSRTVQDlllSVA-PVRvkeaaERLNGAElammEREDEKTQMryaqaitdytdaggydievlwdtcTMAALGA 159
Cdd:cd03261 88 -----LFDSLTVFE---NVAfPLR-----EHTRLSE----EEIREIVLE------------------------KLEAVGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 160 PYDNVKYRDltTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLANA 234
Cdd:cd03261 127 RGAEDLYPA--ELSGGMKKRVALaRALALDP-ELLLYDEPTAGLDPIASGVIDDLIRSLKKelglTSIMVTHDLDTAFAI 203
|
250 260 270
....*....|....*....|....*....|...
gi 2796936914 235 VDRIVTVESGNVWIHGggfaTYSEARKDRNERL 267
Cdd:cd03261 204 ADRIAVLYDGKIVAEG----TPEELRASDDPLV 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
355-531 |
1.15e-11 |
|
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: 67.55 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTG--------VARLGARVVPGHFAQTHARPELLGRTPCE-IVMTE 425
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGrilidgidLRQIDPASLRRQIGVVLQDVFLFSGTIREnITLGD 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 426 HARLKNEAMKALARYELAGGVAE--QRFET--------LSGGQQARLQI---LLLEmsgATLLLLDEPTDNLDLASAEAL 492
Cdd:COG2274 574 PDATDEEIIEAARLAGLHDFIEAlpMGYDTvvgeggsnLSGGQRQRLAIaraLLRN---PRILILDEATSALDAETEAII 650
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2796936914 493 QAGLDAFDG--TVLAVTHDRWFAADFDRYMVFgTDGRVYES 531
Cdd:COG2274 651 LENLRRLLKgrTVIIIAHRLSTIRLADRIIVL-DKGRIVED 690
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
355-529 |
1.52e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 64.39 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTG--------VARL--GARVVPGHFAQTHARPEL-------LGRT 417
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGrilwngqdLTALppAERPVSMLFQENNLFPHLtvaqnigLGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 418 P-CEIVMTEHARLkneaMKALARYELAGgvAEQRF-ETLSGGQQARLQILLLEMSGATLLLLDEPTDNLD---------L 486
Cdd:COG3840 98 PgLKLTAEQRAQV----EQALERVGLAG--LLDRLpGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrqemldL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2796936914 487 ASAEALQAGLdafdgTVLAVTHDRWFAADFDRYMVFGTDGRVY 529
Cdd:COG3840 172 VDELCRERGL-----TVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-246 |
1.74e-11 |
|
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: 64.24 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 4 SRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-------------GLGVMRQF 70
Cdd:cd03295 4 ENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 71 IGSLrgagessPggdgrdSRTVQD------LLLSVAPVRVKEAAERLngaeLAMMEREDEKTQMRYaqaitdytdaggyd 144
Cdd:cd03295 84 IGLF-------P------HMTVEEnialvpKLLKWPKEKIRERADEL----LALVGLDPAEFADRY-------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 145 ievlwdtctmaalgaPYDnvkyrdlttLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQAL----RETSK 219
Cdd:cd03295 133 ---------------PHE---------LSGGQQQRVGVaRALAADPP-LLLMDEPFGALDPITRDQLQEEFkrlqQELGK 187
|
250 260
....*....|....*....|....*..
gi 2796936914 220 TVLLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:cd03295 188 TIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-250 |
1.78e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 64.33 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLpDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG-------------LGVM 67
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdvattpsrelakrLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 68 RQ---FIgslrgagesspggdgrdSR-TVQDLllsVAPVRVKEAAERLNGAELAMMEredektqmryaQAItDYTDAGGY 143
Cdd:COG4604 81 RQenhIN-----------------SRlTVREL---VAFGRFPYSKGRLTAEDREIID-----------EAI-AYLDLEDL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 144 dievlwdtctmaalgapydnvKYRDLTTLSGGeQKRLALEALLRGPD-QTLLLDEPDNYLDVPGKIWLEQALR----ETS 218
Cdd:COG4604 129 ---------------------ADRYLDELSGG-QRQRAFIAMVLAQDtDYVLLDEPLNNLDMKHSVQMMKLLRrladELG 186
|
250 260 270
....*....|....*....|....*....|..
gi 2796936914 219 KTVLLVSHDRQLLANAVDRIVTVESGNVWIHG 250
Cdd:COG4604 187 KTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-250 |
1.87e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 64.62 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-------GLGVMRQFIGS 73
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 74 LRGAGESSPGGdgrdsRTVQDLL------LSVAPVRVKEAAERlngaelAMMEREDEKtqmryaqaitdytdaggydiev 147
Cdd:PRK13644 82 VFQNPETQFVG-----RTVEEDLafgpenLCLPPIEIRKRVDR------ALAEIGLEK---------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 148 lwdtctmaalgapydnVKYRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDV-PGKIWLE--QALRETSKTVLLV 224
Cdd:PRK13644 129 ----------------YRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPdSGIAVLEriKKLHEKGKTIVYI 192
|
250 260
....*....|....*....|....*.
gi 2796936914 225 SHDRQLLANAvDRIVTVESGNVWIHG 250
Cdd:PRK13644 193 THNLEELHDA-DRIIVMDRGKIVLEG 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-246 |
2.10e-11 |
|
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: 63.78 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-------------GLGVMRQ----FIGSLR 75
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQdtflFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 76 gagesspggD----GRDSRTVQDlllsvapvrVKEAAERLNGAELaMMEREDektqmryaqaitdytdagGYDievlwdt 151
Cdd:cd03254 95 ---------EnirlGRPNATDEE---------VIEAAKEAGAHDF-IMKLPN------------------GYD------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 152 cTMAALGApydnvkyrdlTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSHDR 228
Cdd:cd03254 131 -TVLGENG----------GNLSQGERQLLAIaRAMLRDPK-ILILDEATSNIDTETEKLIQEALEKLMKgrTSIIIAHRL 198
|
250
....*....|....*...
gi 2796936914 229 QLLANAvDRIVTVESGNV 246
Cdd:cd03254 199 STIKNA-DKILVLDDGKI 215
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
12-238 |
2.22e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVtHAGGLGVMRQ---------FIGSLRGagessp 82
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-LWQGEPIRRQrdeyhqdllYLGHQPG------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 83 ggdgrdsrtVQDLLlsvapvrvkEAAERLngaelammeredektqmRYAQAItdytdAGGYDIEVLWDtcTMAALG-APY 161
Cdd:PRK13538 85 ---------IKTEL---------TALENL-----------------RFYQRL-----HGPGDDEALWE--ALAQVGlAGF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 162 DNVKYRdltTLSGGEQKRLALeALLRGPDQTL-LLDEPDNYLDVPGKIWLEQALRETSK---TVLLVSH-DRQLLANAVD 236
Cdd:PRK13538 123 EDVPVR---QLSAGQQRRVAL-ARLWLTRAPLwILDEPFTAIDKQGVARLEALLAQHAEqggMVILTTHqDLPVASDKVR 198
|
..
gi 2796936914 237 RI 238
Cdd:PRK13538 199 KL 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
346-509 |
2.45e-11 |
|
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: 63.61 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGE------EVRHTG----------VARLG---- 396
Cdd:cd03219 1 LEVRGLTKRFgglvalddvSFSVRPGEIHGLIGPNGAGKTTLFNLISGFlrptsgSVLFDGeditglppheIARLGigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 397 ---ARVVP----------GHFAQTHARPELLGRtpceivMTEHARLKNEAMKALARYELAGgVAEQRFETLSGGQQARLQ 463
Cdd:cd03219 81 fqiPRLFPeltvlenvmvAAQARTGSGLLLARA------RREEREARERAEELLERVGLAD-LADRPAGELSYGQQRRLE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2796936914 464 ILLLEMSGATLLLLDEPTDNLDLASAEALQA---GLDAFDGTVLAVTHD 509
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAElirELRERGITVLLVEHD 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-518 |
2.83e-11 |
|
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: 65.98 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAG--DLQPIEGSVTHAGGLGVMRQFIGSLRGAGESSPGGDGRDS 89
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALCEKCGYVERPSKVGEPCPVCGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 90 RTVQDLLLSVAPVRvkeaaERLNGAELAMMER-----EDEKTQMRYAQAITDYTDAGGYDIEVLWDTCTMAALGAPYDNV 164
Cdd:TIGR03269 91 PEEVDFWNLSDKLR-----RRIRKRIAIMLQRtfalyGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 165 KyRDlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLANAVDRIVT 240
Cdd:TIGR03269 166 A-RD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasgiSMVLTSHWPEVIEDLSDKAIW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 241 VESGNVWIHGGGfatysearkdrnerldelrrrwDEEHAKLKRLVVMLRQKAtyndsmaapyhaaqtrlrrfeeagppEL 320
Cdd:TIGR03269 242 LENGEIKEEGTP----------------------DEVVAVFMEGVSEVEKEC--------------------------EV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 321 APKDQLISMRlrggRTAKRAVICENlelsGLMKPFD---LEIWYGERVAVLGSNGSGKSHFLRLIAGeeVRHTGVARLGA 397
Cdd:TIGR03269 274 EVGEPIIKVR----NVSKRYISVDR----GVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAG--VLEPTSGEVNV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 398 RVVPGHFAQTHARPELLGRTPCEIVM--------TEHARLKN--EA-----------MKALARYELAG-------GVAEQ 449
Cdd:TIGR03269 344 RVGDEWVDMTKPGPDGRGRAKRYIGIlhqeydlyPHRTVLDNltEAiglelpdelarMKAVITLKMVGfdeekaeEILDK 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 450 RFETLSGGQQARL---QILLLEmsgATLLLLDEPTDNLD----LASAEALQAGLDAFDGTVLAVTHDRWFAADF-DR 518
Cdd:TIGR03269 424 YPDELSEGERHRValaQVLIKE---PRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDMDFVLDVcDR 497
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-246 |
4.05e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 63.12 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrqfigSLRGAGESSPGGDGRDSRTV-QDL 95
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI--------------LLNGKDITNLPPEKRDISYVpQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 96 LLsVAPVRVKEaaerlNGAELAMMEREDEKTQMRYAQAItdytdAGGYDIEVLWDtctmaalgapydnvkyRDLTTLSGG 175
Cdd:cd03299 81 AL-FPHMTVYK-----NIAYGLKKRKVDKKEIERKVLEI-----AEMLGIDHLLN----------------RKPETLSGG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796936914 176 EQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:cd03299 134 EQQRVAIaRALVVNP-KILLLDEPFSALDVRTKEKLREELKKIRKefgvTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1-247 |
4.29e-11 |
|
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: 61.40 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGdLQPI-EGSVTHAGGLGVMrqFI-------- 71
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRIGMPEGEDLL--FLpqrpylpl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 72 GSLRgagesspggdgrdsrtvqdlllsvapvrvkeaaerlngaelammeredekTQMRYAqaitdytdaggydievlWDt 151
Cdd:cd03223 78 GTLR--------------------------------------------------EQLIYP-----------------WD- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 152 ctmaalgapydnvkyrdlTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHdRQL 230
Cdd:cd03223 90 ------------------DVLSGGEQQRLAFaRLLLHKPK-FVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPS 149
|
250
....*....|....*..
gi 2796936914 231 LANAVDRIVTVESGNVW 247
Cdd:cd03223 150 LWKFHDRVLDLDGEGGW 166
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-226 |
4.55e-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: 62.13 E-value: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfigslrgageSSPGGDGRDSRT 91
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL--------------------LNGGPLDFQRDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 VQDLLLSVApvrvkeaaeRLNGAELAMMEREDektqMRYAQAItdytdaggYDIEVLWDTCTMAALGApydnVKYRDLTT 171
Cdd:cd03231 71 IARGLLYLG---------HAPGIKTTLSVLEN----LRFWHAD--------HSDEQVEEALARVGLNG----FEDRPVAQ 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALR---ETSKTVLLVSH 226
Cdd:cd03231 126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAghcARGGMVVLTTH 183
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-62 |
4.61e-11 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 61.29 E-value: 4.61e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG 62
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG 61
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-246 |
4.76e-11 |
|
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: 62.43 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 7 THVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLRGAG----ESSP 82
Cdd:cd03292 7 TKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG------QDVSDLRGRAipylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 83 GGDGRDSRTVQDL--------LLSVAPVRVKEAAERLNgaelAMMEREDEKTQMRyaqaitdytdaggydievlwdtcTM 154
Cdd:cd03292 81 GVVFQDFRLLPDRnvyenvafALEVTGVPPREIRKRVP----AALELVGLSHKHR-----------------------AL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 155 AAlgapydnvkyrdltTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDvPGKIW----LEQALRETSKTVLLVSHDRQ 229
Cdd:cd03292 134 PA--------------ELSGGEQQRVAIaRAIVNSP-TILIADEPTGNLD-PDTTWeimnLLKKINKAGTTVVVATHAKE 197
|
250
....*....|....*..
gi 2796936914 230 LLANAVDRIVTVESGNV 246
Cdd:cd03292 198 LVDTTRHRVIALERGKL 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
356-535 |
4.86e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.80 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLR-------------LIAGEEVRHTGVA----RLGARVVpghFAQTHARPELlgrTP 418
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGLKVNDPKVDerliRQEAGMV---FQQFYLFPHL---TA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 419 CEIVM--TEHAR-LKNEAMKALARYELAG-GVAEQRFE---TLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLA-SAE 490
Cdd:PRK09493 95 LENVMfgPLRVRgASKEEAEKQARELLAKvGLAERAHHypsELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElRHE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2796936914 491 ALQAGLD-AFDG-TVLAVTHDRWFAADFDRYMVFGTDGRVYESPEPV 535
Cdd:PRK09493 175 VLKVMQDlAEEGmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQ 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
352-490 |
5.24e-11 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 63.09 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 352 MKPFDLEIWYGERVAVLGSNGSGKSHFLR-------------LIAGEEV------------RHTG--------VARLGA- 397
Cdd:TIGR02315 18 LKNINLNINPGEFVAIIGPSGAGKSTLLRcinrlvepssgsiLLEGTDItklrgkklrklrRRIGmifqhynlIERLTVl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 398 -RVVPGHFAQTHARPELLGRTPCEIvmteharlKNEAMKALARYELAGgVAEQRFETLSGGQQARLQILLLEMSGATLLL 476
Cdd:TIGR02315 98 eNVLHGRLGYKPTWRSLLGRFSEED--------KERALSALERVGLAD-KAYQRADQLSGGQQQRVAIARALAQQPDLIL 168
|
170
....*....|....
gi 2796936914 477 LDEPTDNLDLASAE 490
Cdd:TIGR02315 169 ADEPIASLDPKTSK 182
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-522 |
6.20e-11 |
|
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: 62.81 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 358 EIWYGERVAVLGSNGSGKSHFLRLIAGE---EVRHTGVARLGARVVPGHFA---QTHARPELLGRTPceiVMTEHARLKN 431
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVlkpDEGDIEIELDTVSYKPQYIKadyEGTVRDLLSSITK---DFYTHPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 432 EAMKALaRYElagGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLD----LASAEALQAGLDAFDGTVLAVT 507
Cdd:cd03237 98 EIAKPL-QIE---QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVE 173
|
170
....*....|....*..
gi 2796936914 508 HDRWFaADF--DRYMVF 522
Cdd:cd03237 174 HDIIM-IDYlaDRLIVF 189
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
351-510 |
6.75e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 64.01 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 351 LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpghFAQTHAR-------------------- 410
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL---FTNLPPRerrvgfvfqhyalfphmtva 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 411 ------PELLGRTPCEIvmteharlKNEAMKALARYELAGgvAEQRFET-LSGGQQARL---QILLLEmsgATLLLLDEP 480
Cdd:COG1118 94 eniafgLRVRPPSKAEI--------RARVEELLELVQLEG--LADRYPSqLSGGQRQRValaRALAVE---PEVLLLDEP 160
|
170 180 190
....*....|....*....|....*....|....
gi 2796936914 481 TDNLDLASAEALQAGL----DAFDGTVLAVTHDR 510
Cdd:COG1118 161 FGALDAKVRKELRRWLrrlhDELGGTTVFVTHDQ 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
330-534 |
6.96e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.08 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 330 RLRGGRTA---KRAVICENLELSglmkpfdleIWYGERVAVLGSNGSGKSHFLRLIA-------------GEEVRHTGVA 393
Cdd:PRK10253 7 RLRGEQLTlgyGKYTVAENLTVE---------IPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahghvwldGEHIQHYASK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 394 RLGARVvpGHFAQTHARP------ELL--GRTPCEIVMTehaRLKNEAMKALARYELAGGV---AEQRFETLSGGQQARL 462
Cdd:PRK10253 78 EVARRI--GLLAQNATTPgditvqELVarGRYPHQPLFT---RWRKEDEEAVTKAMQATGIthlADQSVDTLSGGQRQRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796936914 463 QILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFDG----TVLAVTHDRWFAADFDRYMVFGTDGRVYESPEP 534
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-258 |
6.96e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.70 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG------------GLGVMRQFigslrgages 80
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQF---------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 spggDGRDSR-TVQDLLLsvapvrvkeaaerLNGAELAMMEREDEktqmryaqaitdytdaggydiEVLWDTCTMAALGA 159
Cdd:PRK13536 123 ----DNLDLEfTVRENLL-------------VFGRYFGMSTREIE---------------------AVIPSLLEFARLES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 160 PYDNvkyrDLTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGK--IWLE-QALRETSKTVLLVSHDRQLLANAV 235
Cdd:PRK13536 165 KADA----RVSDLSGGMKRRLTLaRALINDP-QLLILDEPTTGLDPHARhlIWERlRSLLARGKTILLTTHFMEEAERLC 239
|
250 260
....*....|....*....|...
gi 2796936914 236 DRIVTVESGNVWIHGGGFATYSE 258
Cdd:PRK13536 240 DRLCVLEAGRKIAEGRPHALIDE 262
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-246 |
7.02e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVtHAGGLGVM----RQFIGSLR---GAGESSPGGDGRDS 89
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV-TVGDIVVSstskQKEIKPVRkkvGVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 90 RTVQDLLLSVAPVRV-KEAAERLNGAELAMMEREDEktqmryaqaitdytdaggydievLWDTctmaalgAPYDnvkyrd 168
Cdd:PRK13643 101 TVLKDVAFGPQNFGIpKEKAEKIAAEKLEMVGLADE-----------------------FWEK-------SPFE------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 169 lttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIW---LEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGN 245
Cdd:PRK13643 145 ---LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEmmqLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGH 221
|
.
gi 2796936914 246 V 246
Cdd:PRK13643 222 I 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-251 |
7.03e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.33 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG--------GLGVMRQFIG 72
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 73 SLRgageSSPGGDGRDSRTVQDllLSVAPVRVKeaaerlngaelamMEREDEKTQMRYAQAITdytdaggyDIEVLWDTC 152
Cdd:PRK13636 86 MVF----QDPDNQLFSASVYQD--VSFGAVNLK-------------LPEDEVRKRVDNALKRT--------GIEHLKDKP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 153 TMAalgapydnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDR 228
Cdd:PRK13636 139 THC----------------LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelglTIIIATHDI 202
|
250 260
....*....|....*....|...
gi 2796936914 229 QLLANAVDRIVTVESGNVWIHGG 251
Cdd:PRK13636 203 DIVPLYCDNVFVMKEGRVILQGN 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
12-246 |
8.63e-11 |
|
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: 62.25 E-value: 8.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG----GLGVMRqfigslrgagesspggdgR 87
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkditNLPPHK------------------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 88 DSRTV-QDLLL--------SVA-PVRVKeaaeRLNGAELammeredektQMRYAQAItDYTDAGGYdievlwdtctmaal 157
Cdd:cd03300 73 PVNTVfQNYALfphltvfeNIAfGLRLK----KLPKAEI----------KERVAEAL-DLVQLEGY-------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 158 gapydnvKYRDLTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLA 232
Cdd:cd03300 124 -------ANRKPSQLSGGQQQRVAIaRALVNEP-KVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEAL 195
|
250
....*....|....
gi 2796936914 233 NAVDRIVTVESGNV 246
Cdd:cd03300 196 TMSDRIAVMNKGKI 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
352-534 |
1.03e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.36 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 352 MKPFDLEIWYGERVAVLGSNGSGKSHFLRLI-------AGE-EVRHTGVARLG----ARVVPGHFAQTHARPELLG---- 415
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTyRVAGQDVATLDadalAQLRREHFGFIFQRYHLLShlta 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 416 ----RTPCEIVMTEHARLKNEAMKALARYELAGGVaEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEA 491
Cdd:PRK10535 104 aqnvEVPAVYAGLERKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2796936914 492 LQAGLDAFDG---TVLAVTHDRWFAADFDRYMVFgTDGRVYESPEP 534
Cdd:PRK10535 183 VMAILHQLRDrghTVIIVTHDPQVAAQAERVIEI-RDGEIVRNPPA 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
352-528 |
1.20e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 61.39 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 352 MKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHARPELLG-----------RTPCE 420
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGmvfqqfnlfphLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 421 IVM----TEHARLKNEAmKALARYELAG-GVAEQRFE---TLSGGQQARLQILLLEMSGATLLLLDEPTDNLD--LAsAE 490
Cdd:cd03262 96 NITlapiKVKGMSKAEA-EERALELLEKvGLADKADAypaQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpeLV-GE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2796936914 491 ALQAGLD-AFDG-TVLAVTHDRWFAADF-DRyMVFGTDGRV 528
Cdd:cd03262 174 VLDVMKDlAEEGmTMVVVTHEMGFAREVaDR-VIFMDDGRI 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
346-509 |
1.60e-10 |
|
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: 60.10 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARlgarvVPGH--FAQTHARPELL 414
Cdd:cd03230 1 IEVRNLSKRYgkktalddiSLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-----VLGKdiKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 415 GrtpceiVMTEHARLkNEAMKAlarYELAggvaeqrfeTLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQ- 493
Cdd:cd03230 76 G------YLPEEPSL-YENLTV---RENL---------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWe 136
|
170
....*....|....*...
gi 2796936914 494 --AGLDAFDGTVLAVTHD 509
Cdd:cd03230 137 llRELKKEGKTILLSSHI 154
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
355-509 |
1.69e-10 |
|
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: 60.77 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLEIWY---GERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARV---------VPGH-------FAQTHARPELLG 415
Cdd:cd03297 13 FTLKIDFdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinLPPQqrkiglvFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 416 RTPCEIVMTEHAR--LKNEAMKALARYELaGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQ 493
Cdd:cd03297 93 RENLAFGLKRKRNreDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180
....*....|....*....|
gi 2796936914 494 AGLDA----FDGTVLAVTHD 509
Cdd:cd03297 172 PELKQikknLNIPVIFVTHD 191
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-274 |
1.72e-10 |
|
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: 61.15 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG--------------GLG-VM--RQFIGSLrgage 79
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditglpphriarlGIGyVPegRRIFPSL----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 80 sspggdgrdsrTVQD-LLLSVAPVRVKEAAErlngAELAMM--------ERedeKTQMryaqaitdytdAGgydievlwd 150
Cdd:COG0410 94 -----------TVEEnLLLGAYARRDRAEVR----ADLERVyelfprlkER---RRQR-----------AG--------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 151 tctmaalgapydnvkyrdltTLSGGEQKRLAL-EALLRGPDqTLLLDEP---------DNYLDVpgkIwleQALRETSKT 220
Cdd:COG0410 136 --------------------TLSGGEQQMLAIgRALMSRPK-LLLLDEPslglaplivEEIFEI---I---RRLNREGVT 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 221 VLLVSHD-RQLLANAvDRIVTVESGNVWIHGGGfatySEARKDrnerlDELRRRW 274
Cdd:COG0410 189 ILLVEQNaRFALEIA-DRAYVLERGRIVLEGTA----AELLAD-----PEVREAY 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
346-510 |
2.21e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 62.42 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpghfaqTHARPEllgR 416
Cdd:COG3842 6 LELENVSKRYgdvtalddvSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV------TGLPPE---K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPCEIV---------MT---------EHARLKNEAMKALARYELA----GGVAEQRFETLSGGQQARLQI---LLLEMSg 471
Cdd:COG3842 77 RNVGMVfqdyalfphLTvaenvafglRMRGVPKAEIRARVAELLElvglEGLADRYPHQLSGGQQQRVALaraLAPEPR- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2796936914 472 atLLLLDEPTDNLDLASAEALQAGL----DAFDGTVLAVTHDR 510
Cdd:COG3842 156 --VLLLDEPLSALDAKLREEMREELrrlqRELGITFIYVTHDQ 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
362-508 |
2.30e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.20 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHARPELLGR--------TPCEIVMTEHARLKNEA 433
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHapgikttlSVLENLRFWHADHSDEQ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796936914 434 M-KALARYELaGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQ---AGLDAFDGTVLAVTH 508
Cdd:cd03231 106 VeEALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAeamAGHCARGGMVVLTTH 183
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
362-535 |
2.33e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.18 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIA------GEEVRHTG--VARLGARVVPGHFA---QTHARPEllGRTPCEIVM------- 423
Cdd:PRK11231 28 GKITALIGPNGCGKSTLLKCFArlltpqSGTVFLGDkpISMLSSRQLARRLAllpQHHLTPE--GITVRELVAygrspwl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 424 -------TEHARLKNEAMKALARYELAggvaEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLA-SAE--ALQ 493
Cdd:PRK11231 106 slwgrlsAEDNARVNQAMEQTRINHLA----DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhQVElmRLM 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2796936914 494 AGLDAFDGTVLAVTHDRWFAADFDRYMVFGTDGRVYE--SPEPV 535
Cdd:PRK11231 182 RELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAqgTPEEV 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-306 |
3.11e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.97 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 6 LTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG------GLGVMRQFIGSLRGAGE 79
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkeNIREVRKFVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 80 sspggDGRDSRTV-QDllLSVAPVrvkeaaeRLNGAELAMMEREDEKTQMryaQAITDYTDAggydievlwdtctmaalg 158
Cdd:PRK13652 89 -----DQIFSPTVeQD--IAFGPI-------NLGLDEETVAHRVSSALHM---LGLEELRDR------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 159 APYDnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLANA 234
Cdd:PRK13652 134 VPHH---------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEM 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796936914 235 VDRIVTVESGNVWIHGGGFATYSEarkdrnerlDELRRRWDEEHAKLKRLVVMLRQKATyNDSMAAPYHAAQ 306
Cdd:PRK13652 205 ADYIYVMDKGRIVAYGTVEEIFLQ---------PDLLARVHLDLPSLPKLIRSLQAQGI-AIDMAYTYQEAE 266
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-239 |
3.46e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 61.65 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSL----RGAGesspggdgr 87
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG------RDVTGLppekRNVG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 88 dsrTV-QDLLL----SVA-----PVRVK-----EAAERLNGAeLAMMEredektqmryaqaitdytdaggydievlwdtc 152
Cdd:COG3842 81 ---MVfQDYALfphlTVAenvafGLRMRgvpkaEIRARVAEL-LELVG-------------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 153 tMAALGApydnvkyRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGK----IWLEQALRETSKTVLLVSHD 227
Cdd:COG3842 125 -LEGLAD-------RYPHQLSGGQQQRVALaRALAPEPR-VLLLDEPLSALDAKLReemrEELRRLQRELGITFIYVTHD 195
|
250
....*....|...
gi 2796936914 228 rQLLANAV-DRIV 239
Cdd:COG3842 196 -QEEALALaDRIA 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-250 |
3.48e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 60.15 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 21 SFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLrgagesSPGgdgrdSRTV----QD-- 94
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG------QDLTAL------PPA-----ERPVsmlfQEnn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 95 LL--LSVA--------P---------VRVKEAAERLNgaelammeredektqmryaqaITDYTDaggydievlwdtctma 155
Cdd:COG3840 82 LFphLTVAqniglglrPglkltaeqrAQVEQALERVG---------------------LAGLLD---------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 156 algapydnvkyRDLTTLSGGEQKRLAL-EALLRG-PdqTLLLDEPDNYLDvPGK-----IWLEQALRETSKTVLLVSHDR 228
Cdd:COG3840 125 -----------RLPGQLSGGQRQRVALaRCLVRKrP--ILLLDEPFSALD-PALrqemlDLVDELCRERGLTVLMVTHDP 190
|
250 260
....*....|....*....|..
gi 2796936914 229 QLLANAVDRIVTVESGNVWIHG 250
Cdd:COG3840 191 EDAARIADRVLLVADGRIAADG 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
355-488 |
3.85e-10 |
|
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: 59.83 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVArlgarVVPGHFAQTH---ARPEL----------LGRTPCEI 421
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA-----YINGYSIRTDrkaARQSLgycpqfdalfDELTVREH 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 422 VMTeHARLK-------NEAMKALARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLAS 488
Cdd:cd03263 96 LRF-YARLKglpkseiKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
346-509 |
4.01e-10 |
|
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: 60.21 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGarvvpGHFAQTHARPELLG- 415
Cdd:cd03261 1 IELRGLTKSFggrtvlkgvDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-----GEDISGLSEAELYRl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 416 RTPCEIV---------MT----------EHARLKNEAMKALARYELA----GGVAEQRFETLSGGQQARLQI---LLLEM 469
Cdd:cd03261 76 RRRMGMLfqsgalfdsLTvfenvafplrEHTRLSEEEIREIVLEKLEavglRGAEDLYPAELSGGMKKRVALaraLALDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2796936914 470 SgatLLLLDEPTDNLDLASAEALQAGL----DAFDGTVLAVTHD 509
Cdd:cd03261 156 E---LLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHD 196
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-227 |
4.23e-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: 61.99 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 3 VSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfigsLRGAGESSP 82
Cdd:TIGR02868 337 LRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT--------------LDGVPVSSL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 83 GGDGRDSRTV---QDLLLSVAPVR--VKEAAERLNGAEL-AMMERedektqmryaqaitdytdAGGYDievlWdtctMAA 156
Cdd:TIGR02868 403 DQDEVRRRVSvcaQDAHLFDTTVRenLRLARPDATDEELwAALER------------------VGLAD----W----LRA 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796936914 157 LGAPYDNVKYRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALR--ETSKTVLLVSHD 227
Cdd:TIGR02868 457 LPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLaaLSGRTVVLITHH 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-246 |
5.93e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.09 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG--------GLGVMRQFIGSLrgagessp 82
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRKTVGIV-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 83 ggdgrdSRTVQDLLLsvAPvRVKE--AAERLNgaeLAMMEREDEKTQMRYAQAItdytDAGGYDIEvlwdtctmaalgAP 160
Cdd:PRK13639 84 ------FQNPDDQLF--AP-TVEEdvAFGPLN---LGLSKEEVEKRVKEALKAV----GMEGFENK------------PP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 161 YDnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK---TVLLVSHDRQLLANAVDR 237
Cdd:PRK13639 136 HH---------LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHDVDLVPVYADK 206
|
....*....
gi 2796936914 238 IVTVESGNV 246
Cdd:PRK13639 207 VYVMSDGKI 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-292 |
7.55e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.49 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG--------------GLgVMRQfigslrgagessp 82
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrrkefarriGV-VFGQ------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 83 ggdgrdsRTvQ---DLllsvaPVRvkeaaE--RLNGAelamMEREDEKtqmRYAQAITDYTDAggYDIEVLWDTCTmaal 157
Cdd:COG4586 104 -------RS-QlwwDL-----PAI-----DsfRLLKA----IYRIPDA---EYKKRLDELVEL--LDLGELLDTPV---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 158 gapydnvkyRdltTLSGGEQKR--LALeALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLL 231
Cdd:COG4586 153 ---------R---QLSLGQRMRceLAA-ALLHRP-KILFLDEPTIGLDVVSKEAIREFLKEYNRergtTILLTSHDMDDI 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796936914 232 ANAVDRIVTVESGNVwIHGGGfatysearkdrnerLDELRRRWdeehAKLKRLVVMLRQKA 292
Cdd:COG4586 219 EALCDRVIVIDHGRI-IYDGS--------------LEELKERF----GPYKTIVLELAEPV 260
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
17-280 |
7.72e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.64 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQFIGSLrgagesspGGDGRDSRTVQDLL 96
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRL--------ARDIRKSRANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 97 LSVAPVrvkeaAERLNGAELAMMeredektqmryaqaitdytdaGGYDIEVLWDTC--------TMAALGA----PYDNV 164
Cdd:PRK09984 92 FQQFNL-----VNRLSVLENVLI---------------------GALGSTPFWRTCfswftreqKQRALQAltrvGMVHF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 165 KYRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLANAVDRIVT 240
Cdd:PRK09984 146 AHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVA 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2796936914 241 VESGNVWIHGGgfatyseARKDRNERLDELRRRWD--EEHAK 280
Cdd:PRK09984 226 LRQGHVFYDGS-------SQQFDNERFDHLYRSINrvEENAK 260
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
346-508 |
9.98e-10 |
|
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: 58.45 E-value: 9.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARlgarvVPGHFAQTHAR------ 410
Cdd:cd03269 1 LEVENVTKRFgrvtalddiSFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL-----FDGKPLDIAARnrigyl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 411 PELLGRTPCEIVMTE---HARLKN----EAMKA----LARYELaGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDE 479
Cdd:cd03269 76 PEERGLYPKMKVIDQlvyLAQLKGlkkeEARRRidewLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|..
gi 2796936914 480 PTDNLDLASAEALQAGLDAFDG---TVLAVTH 508
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARagkTVILSTH 186
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
356-534 |
1.17e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.24 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHAR-----PE--------------LLGR 416
Cdd:PRK09536 23 DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRrvasvPQdtslsfefdvrqvvEMGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPCEIVMTEHARLKNEAM-KALARYELAgGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAE---AL 492
Cdd:PRK09536 103 TPHRSRFDTWTETDRAAVeRAMERTGVA-QFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVrtlEL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2796936914 493 QAGLDAFDGTVLAVTHDRWFAADFDRYMVFGTDGRVYESPEP 534
Cdd:PRK09536 182 VRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
346-532 |
1.21e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 60.35 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPFD---------LEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpghfaqTHARPEllgR 416
Cdd:PRK09452 15 VELRGISKSFDgkevisnldLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI------THVPAE---N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPCEIV---------MT--------------EHARLKNEAMKALARYELAGgVAEQRFETLSGGQQARLQILLLEMSGAT 473
Cdd:PRK09452 86 RHVNTVfqsyalfphMTvfenvafglrmqktPAAEITPRVMEALRMVQLEE-FAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796936914 474 LLLLDEPTDNLDLASAEALQAGLDAFDG----TVLAVTHDRWFAADF-DRYMVF--------GTDGRVYESP 532
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMsDRIVVMrdgrieqdGTPREIYEEP 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
12-246 |
1.38e-09 |
|
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: 58.04 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGsvthagglgvmRQFIGslrgagesspggdGRDsrt 91
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG-----------RIYIG-------------GRD--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 VQDLllsvapvrvkEAAER--------------LNGAE-------LAMMEREDEKTQMRYAQAItdytdaggYDIEVLWD 150
Cdd:cd03301 64 VTDL----------PPKDRdiamvfqnyalyphMTVYDniafglkLRKVPKDEIDERVREVAEL--------LQIEHLLD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 151 tctmaalgapydnvkyRDLTTLSGGEQKRLAL-EALLRGPdQTLLLDEP----DNYLDVPGKIWLEQALRETSKTVLLVS 225
Cdd:cd03301 126 ----------------RKPKQLSGGQRQRVALgRAIVREP-KVFLMDEPlsnlDAKLRVQMRAELKRLQQRLGTTTIYVT 188
|
250 260
....*....|....*....|..
gi 2796936914 226 HDrQLLANAV-DRIVTVESGNV 246
Cdd:cd03301 189 HD-QVEAMTMaDRIAVMNDGQI 209
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
356-509 |
1.45e-09 |
|
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: 60.45 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAG------EEVRHTGVARLGA-----RVVPGHFAQthaRPELLGRTpceivMT 424
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGlldplqGEVTLDGVPVSSLdqdevRRRVSVCAQ---DAHLFDTT-----VR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 425 EHARLKN------EAMKALARYELAGGVAE----------QRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLAS 488
Cdd:TIGR02868 427 ENLRLARpdatdeELWAALERVGLADWLRAlpdgldtvlgEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
170 180
....*....|....*....|...
gi 2796936914 489 AEALQAGL-DAFDG-TVLAVTHD 509
Cdd:TIGR02868 507 ADELLEDLlAALSGrTVVLITHH 529
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-246 |
1.84e-09 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 59.34 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 19 DVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV-----------------THAGGLGVMRQfigslrgagess 81
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevlqdsargiflpPHRRRIGYVFQ------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 82 pggdgrDSR-----TVQD-LLLSVAPVRVKEAAERLNGAelammeredektqmryaqaitdytdaggydIEVLwdtctma 155
Cdd:COG4148 85 ------EARlfphlSVRGnLLYGRKRAPRAERRISFDEV------------------------------VELL------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 156 ALGAPYDnvkyRDLTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGK--I--WLEQALRETSKTVLLVSHDR-- 228
Cdd:COG4148 122 GIGHLLD----RRPATLSGGERQRVAIgRALLSSP-RLLLMDEPLAALDLARKaeIlpYLERLRDELDIPILYVSHSLde 196
|
250
....*....|....*....
gi 2796936914 229 -QLLAnavDRIVTVESGNV 246
Cdd:COG4148 197 vARLA---DHVVLLEQGRV 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
7-265 |
1.88e-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: 58.71 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 7 THVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQFIGSLRGagesspggdg 86
Cdd:cd03291 43 SNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPG---------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 87 rdsrTVQDLLL---SVAPVRVKEAAErlngaelAMMEREDektqmryaqaITDYTDAggydievlwDTCTMAALGapydn 163
Cdd:cd03291 113 ----TIKENIIfgvSYDEYRYKSVVK-------ACQLEED----------ITKFPEK---------DNTVLGEGG----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 164 vkyrdlTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDvpgkIWLEQALRET-------SKTVLLVSHDRQLLANAv 235
Cdd:cd03291 158 ------ITLSGGQRARISLaRAVYKDAD-LYLLDSPFGYLD----VFTEKEIFEScvcklmaNKTRILVTSKMEHLKKA- 225
|
250 260 270
....*....|....*....|....*....|
gi 2796936914 236 DRIVTVESGNVWIHGggfaTYSEARKDRNE 265
Cdd:cd03291 226 DKILILHEGSSYFYG----TFSELQSLRPD 251
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
353-528 |
2.18e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 57.83 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTG-VARLG-----------ARVVPGH----FAQTHARPELlgr 416
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGtVRLAGqdlfaldedarARLRARHvgfvFQSFQLLPTL--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPCEIVMT-----EHARLKNEAMKALARYELAggvaeQRFE----TLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLA 487
Cdd:COG4181 106 TALENVMLplelaGRRDARARARALLERVGLG-----HRLDhypaQLSGGEQQRVALARAFATEPAILFADEPTGNLDAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2796936914 488 SAEALQA---GLDAFDGTVLA-VTHDRWFAADFDRYMVFGtDGRV 528
Cdd:COG4181 181 TGEQIIDllfELNRERGTTLVlVTHDPALAARCDRVLRLR-AGRL 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
344-534 |
2.29e-09 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 57.73 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 344 ENLELSG---LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARL-GARVvpghfaqTHARPELLGRTpc 419
Cdd:cd03299 4 ENLSKDWkefKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDI-------TNLPPEKRDIS-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 420 eIVMTEHARL------KNEA----MKALARYELAGGVAE------------QRFETLSGGQQARLQI---LLLEMSgatL 474
Cdd:cd03299 75 -YVPQNYALFphmtvyKNIAyglkKRKVDKKEIERKVLEiaemlgidhllnRKPETLSGGEQQRVAIaraLVVNPK---I 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 475 LLLDEPTDNLDLASAEALQAGL----DAFDGTVLAVTHD----RWFAadfDRYMVFgTDGRVYESPEP 534
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELkkirKEFGVTVLHVTHDfeeaWALA---DKVAIM-LNGKLIQVGKP 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
355-485 |
2.36e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FD--LEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTG---VA---------------RLGARVVPGHFAQTHARPEL- 413
Cdd:PRK11124 19 FDitLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlnIAgnhfdfsktpsdkaiRELRRNVGMVFQQYNLWPHLt 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 414 ----LGRTPCEIVMTEHARLKNEAMKALARYELAGGVaeQRFET-LSGGQQARLQILLLEMSGATLLLLDEPTDNLD 485
Cdd:PRK11124 99 vqqnLIEAPCRVLGLSKDQALARAEKLLERLRLKPYA--DRFPLhLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
356-532 |
2.38e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARlgARVVPGHFAQTHARPELLGRtpceivmtehARLKNEAMK 435
Cdd:COG2401 50 NLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC--VDVPDNQFGREASLIDAIGR----------KGDFKDAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 436 ALARYELAGGVA-EQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGL----DAFDGTVLAVTHDR 510
Cdd:COG2401 118 LLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLqklaRRAGITLVVATHHY 197
|
170 180
....*....|....*....|....
gi 2796936914 511 WFAADF--DRYMVFGTDGRVYESP 532
Cdd:COG2401 198 DVIDDLqpDLLIFVGYGGVPEEKR 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
346-508 |
2.53e-09 |
|
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: 56.28 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHfaqtharpellgr 416
Cdd:cd03216 1 LELRGITKRFggvkaldgvSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPceivmteharlkNEAMKAlaryelagGVA--EQrfetLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQA 494
Cdd:cd03216 68 SP------------RDARRA--------GIAmvYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170
....*....|....*..
gi 2796936914 495 GLDAF--DG-TVLAVTH 508
Cdd:cd03216 124 VIRRLraQGvAVIFISH 140
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
345-542 |
2.81e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.94 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 345 NLELSGLMKPFD---------LEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTG--------VARLGAR-----VVPG 402
Cdd:PRK10851 2 SIEIANIKKSFGrtqvlndisLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGhirfhgtdVSRLHARdrkvgFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 403 HFA----QTHARPELLGRTpceiVMTEHAR-----LKNEAMKALARYELAgGVAEQRFETLSGGQQARLQI---LLLEms 470
Cdd:PRK10851 82 HYAlfrhMTVFDNIAFGLT----VLPRRERpnaaaIKAKVTQLLEMVQLA-HLADRYPAQLSGGQKQRVALaraLAVE-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 471 gATLLLLDEPTDNLDLASAEALQAGL----DAFDGTVLAVTHDRWFAADF-DRYMVFGtDGRVYE--SPEPVWDE--TRV 541
Cdd:PRK10851 155 -PQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVaDRVVVMS-QGNIEQagTPDQVWREpaTRF 232
|
.
gi 2796936914 542 V 542
Cdd:PRK10851 233 V 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
357-510 |
3.14e-09 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 57.03 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 357 LEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTG--------VARLGARVVP------GHFAQTHARpeLLGRT----- 417
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtirvngqdVSDLRGRAIPylrrkiGVVFQDFRL--LPDRNvyenv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 418 --PCEIVMTEHARLKNEAMKALARYELAGGVAEQRFEtLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEA---L 492
Cdd:cd03292 100 afALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEimnL 178
|
170
....*....|....*...
gi 2796936914 493 QAGLDAFDGTVLAVTHDR 510
Cdd:cd03292 179 LKKINKAGTTVVVATHAK 196
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-246 |
3.26e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.10 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-------------GLGVM-----RQFIGSlr 75
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvrrQVGMVfqnpdNQFVGA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 76 gagesspggdgrdsrTVQDlllSVApvrvkeaaerlNGAELAMMEREDEKTQMRYAQA---ITDYTDaggydievlwdtc 152
Cdd:PRK13635 98 ---------------TVQD---DVA-----------FGLENIGVPREEMVERVDQALRqvgMEDFLN------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 153 tmaalgapydnvkyRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVSHDR 228
Cdd:PRK13635 136 --------------REPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRqlkeQKGITVLSITHDL 201
|
250
....*....|....*...
gi 2796936914 229 QLLANAvDRIVTVESGNV 246
Cdd:PRK13635 202 DEAAQA-DRVIVMNKGEI 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
356-497 |
3.42e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTG--------VARLGARVVPGHFAQTHAR---------PELLGRTP 418
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfshITRLSFEQLQKLVSDEWQRnntdmlspgEDDTGRTT 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796936914 419 CEIVMTEHArlKNEAMKALARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLD 497
Cdd:PRK10938 103 AEIIQDEVK--DPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLA 179
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
327-530 |
3.53e-09 |
|
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: 57.13 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 327 ISMRLRGGRTAKRAVicenlelsglmKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHfaq 406
Cdd:cd03257 7 LSVSFPTGGGSVKAL-----------DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 407 THARPELLGRT-------------PCEIV-------MTEHARLKNEAMKALARYELAGGV--AEQRFE----TLSGGQQA 460
Cdd:cd03257 73 SRRLRKIRRKEiqmvfqdpmsslnPRMTIgeqiaepLRIHGKLSKKEARKEAVLLLLVGVglPEEVLNryphELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 461 RLQI---LLLEMSgatLLLLDEPTDNLDLAS-AEALQ--AGL-DAFDGTVLAVTHDRWFAADF-DRYMVFgTDGRVYE 530
Cdd:cd03257 153 RVAIaraLALNPK---LLIADEPTSALDVSVqAQILDllKKLqEELGLTLLFITHDLGVVAKIaDRVAVM-YAGKIVE 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
356-509 |
3.92e-09 |
|
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: 56.99 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEeVRHTGvarlGARVVPGH----------------FAQTHARPELLGRTPC 419
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTL-LKPTS----GRATVAGHdvvreprevrrrigivFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 420 EIvmteHARL--------KNEAMKALARYELaGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASA-- 489
Cdd:cd03265 95 YI----HARLygvpgaerRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRah 169
|
170 180
....*....|....*....|..
gi 2796936914 490 --EALQAGLDAFDGTVLAVTHD 509
Cdd:cd03265 170 vwEYIEKLKEEFGMTILLTTHY 191
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
356-530 |
4.64e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRL-------------IAGEEVR-----HTGVARLGARVVPGHFAQTHARPEL---- 413
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSSLLRVlnlletpdsgqlnIAGHQFDfsqkpSEKAIRLLRQKVGMVFQQYNLWPHLtvme 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 414 -LGRTPCEIVMTEHARLKNEAMKALARYELAGgvAEQRFET-LSGGQQARLQILLLEMSGATLLLLDEPTDNLD------ 485
Cdd:COG4161 102 nLIEAPCKVLGLSKEQAREKAMKLLARLRLTD--KADRFPLhLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaq 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2796936914 486 LAS--AEALQAGLdafdgTVLAVTHDRWFAADFDRYMVFGTDGRVYE 530
Cdd:COG4161 180 VVEiiRELSQTGI-----TQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
355-531 |
4.88e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLeiWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARvvPGHFAQTHARPE----LLGRTPCEIVmTEHAR-- 428
Cdd:PRK11701 27 FDL--YPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR--DGQLRDLYALSEaerrRLLRTEWGFV-HQHPRdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 429 -------------------------LKNEAMKALARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDN 483
Cdd:PRK11701 102 lrmqvsaggnigerlmavgarhygdIRATAGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGG 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 484 LDLasaeALQAGL--------DAFDGTVLAVTHD----RWFAadfDRYMVFgTDGRVYES 531
Cdd:PRK11701 182 LDV----SVQARLldllrglvRELGLAVVIVTHDlavaRLLA---HRLLVM-KQGRVVES 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
351-528 |
4.88e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.53 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 351 LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGE---EVRHTGVARLG---------ARVVPGHFAQTHA------RPE 412
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgGGAPRGARVTGdvtlngeplAAIDAPRLARLRAvlpqaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 413 ---------LLGRTPceivmteHARLKNE--------AMKALARYElAGGVAEQRFETLSGGQQARLQILLL-------- 467
Cdd:PRK13547 96 fafsareivLLGRYP-------HARRAGAlthrdgeiAWQALALAG-ATALVGRDVTTLSGGELARVQFARVlaqlwpph 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796936914 468 -EMSGATLLLLDEPTDNLDLASAEALQAGLDA----FDGTVLAVTHDRWFAADFDRYMVFGTDGRV 528
Cdd:PRK13547 168 dAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRlardWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-246 |
5.24e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.66 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV-----------THAG--GLGVMRQFIGSLRGAGESSPg 83
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGpdGRGRAKRYIGILHQEYDLYP- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 84 gdgrdSRTVQDLLLSVAPVRV-KEAAERLNGAELAMMEREDEKtqmryAQAITDytdaggydievlwdtctmaalgapyd 162
Cdd:TIGR03269 379 -----HRTVLDNLTEAIGLELpDELARMKAVITLKMVGFDEEK-----AEEILD-------------------------- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 163 nvKYRDltTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLE----QALRETSKTVLLVSHDRQLLANAVDR 237
Cdd:TIGR03269 423 --KYPD--ELSEGERHRVALaQVLIKEP-RIVILDEPTGTMDPITKVDVThsilKAREEMEQTFIIVSHDMDFVLDVCDR 497
|
....*....
gi 2796936914 238 IVTVESGNV 246
Cdd:TIGR03269 498 AALMRDGKI 506
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
351-509 |
5.53e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 56.34 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 351 LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAG---EEVRHTGVARLGARVVPGhfAQTHAR----------------- 410
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlsPAFSASGEVLLNGRRLTA--LPAEQRrigilfqddllfphlsv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 411 --------PELLGRtpceivmteHARlKNEAMKALARYELAGgVAEQRFETLSGGQQAR---LQILLLEMSgatLLLLDE 479
Cdd:COG4136 94 genlafalPPTIGR---------AQR-RARVEQALEEAGLAG-FADRDPATLSGGQRARvalLRALLAEPR---ALLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 2796936914 480 PTDNLDLA-SAEALQ---AGLDAFDGTVLAVTHD 509
Cdd:COG4136 160 PFSKLDAAlRAQFREfvfEQIRQRGIPALLVTHD 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
353-508 |
6.15e-09 |
|
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: 56.00 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEvrhtgvarlGARVVPGHFAqtharpeLLGRTPCEIVMTEHARLK-N 431
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHP---------KYEVTEGEIL-------FKGEDITDLPPEERARLGiF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 432 EAMKALARYElagGVAEQRF-----ETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF---DGTV 503
Cdd:cd03217 81 LAFQYPPEIP---GVKNADFlryvnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreeGKSV 157
|
....*
gi 2796936914 504 LAVTH 508
Cdd:cd03217 158 LIITH 162
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-269 |
6.73e-09 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 56.53 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG---------GLGVMRQFIGSL--RGAges 80
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekELYELRRRIGMLfqGGAl-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 spggdgrDSRTVQDlllSVA-PVRvkeaaERLNGAELAMMEREDEKtqmryaqaitdytdaggydievlwdtctMAALGA 159
Cdd:COG1127 94 ------fDSLTVFE---NVAfPLR-----EHTDLSEAEIRELVLEK----------------------------LELVGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 160 PYDNVKY-RDLttlSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLAN 233
Cdd:COG1127 132 PGAADKMpSEL---SGGMRKRVALaRALALDPE-ILLYDEPTAGLDPITSAVIDELIRELRDelglTSVVVTHDLDSAFA 207
|
250 260 270
....*....|....*....|....*....|....*.
gi 2796936914 234 AVDRIVTVESGNVWIHGggfaTYSEARKDRNERLDE 269
Cdd:COG1127 208 IADRVAVLADGKIIAEG----TPEELLASDDPWVRQ 239
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
356-528 |
6.78e-09 |
|
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: 55.30 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpghfaqTHARPELLGRTpCEIVMTEhARLkneamk 435
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI------SQWDPNELGDH-VGYLPQD-DEL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 436 alaryeLAGGVAEQrfeTLSGGQQARLqILLLEMSGA-TLLLLDEPTDNLDLASAEALQ---AGLDAFDGTVLAVTHDRW 511
Cdd:cd03246 88 ------FSGSIAEN---ILSGGQRQRL-GLARALYGNpRILVLDEPNSHLDVEGERALNqaiAALKAAGATRIVIAHRPE 157
|
170
....*....|....*..
gi 2796936914 512 FAADFDRYMVFgTDGRV 528
Cdd:cd03246 158 TLASADRILVL-EDGRV 173
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
356-530 |
7.47e-09 |
|
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: 56.00 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHARPELLGRTPCEIVMTEHARLKNEAMK 435
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 436 ALAR-YELA--GGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF---DGTVLAVTHD 509
Cdd:cd03220 122 KIDEiIEFSelGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHD 201
|
170 180
....*....|....*....|..
gi 2796936914 510 RWFAADF-DRYMVFgTDGRVYE 530
Cdd:cd03220 202 PSSIKRLcDRALVL-EKGKIRF 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-251 |
8.18e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.73 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDG-RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVM------------ 67
Cdd:PRK13640 6 VEFKHVSFTYPDSkKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITltaktvwdirek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 68 ---------RQFIGSlrgagesspggdgrdsrTVQDlllSVApvrvkeaaerlNGAELAMMEREDEKTQMRYAQA---IT 135
Cdd:PRK13640 86 vgivfqnpdNQFVGA-----------------TVGD---DVA-----------FGLENRAVPRPEMIKIVRDVLAdvgML 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 136 DYTDAggydievlwdtctmaalgapydnvkyrDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALR 215
Cdd:PRK13640 135 DYIDS---------------------------EPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIR 187
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2796936914 216 ETSK----TVLLVSHDRQlLANAVDRIVTVESGNVWIHGG 251
Cdd:PRK13640 188 KLKKknnlTVISITHDID-EANMADQVLVLDDGKLLAQGS 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
347-508 |
8.43e-09 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 55.63 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 347 ELSGLMKPfdleiwyGERVAVLGSNGSGKSHFLRLIAGeevRHTGVARLGARVVPGhfaqthaRPELLGRTPCEI--VMT 424
Cdd:cd03213 27 NVSGKAKP-------GELTAIMGPSGAGKSTLLNALAG---RRTGLGVSGEVLING-------RPLDKRSFRKIIgyVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 425 E---HARLK-NEAMKALAryELAGgvaeqrfetLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLD--A 498
Cdd:cd03213 90 DdilHPTLTvRETLMFAA--KLRG---------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRrlA 158
|
170
....*....|.
gi 2796936914 499 FDG-TVLAVTH 508
Cdd:cd03213 159 DTGrTIICSIH 169
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-244 |
8.55e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 56.29 E-value: 8.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDGR-PL--LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLrgaG 78
Cdd:COG4181 10 ELRGLTKTVGTGAgELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG------QDLFAL---D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 79 EsspggDGR---DSRTV----QDLLL--------SVA-P---VRVKEAAERlngAElAMMERedektqmryaqaitdytd 139
Cdd:COG4181 81 E-----DARarlRARHVgfvfQSFQLlptltaleNVMlPlelAGRRDARAR---AR-ALLER------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 140 aggydievlwdtctmAALGA-----PydnvkyrdlTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVP-GK--IWL 210
Cdd:COG4181 134 ---------------VGLGHrldhyP---------AQLSGGEQQRVALaRAFATEPA-ILFADEPTGNLDAAtGEqiIDL 188
|
250 260 270
....*....|....*....|....*....|....*
gi 2796936914 211 EQALRETSKTVL-LVSHDRQlLANAVDRIVTVESG 244
Cdd:COG4181 189 LFELNRERGTTLvLVTHDPA-LAARCDRVLRLRAG 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-250 |
8.84e-09 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 55.25 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQP--IEGSVthagglgvmrqFIgslrgagesspggDGRD 88
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEV-----------LI-------------NGRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 89 SRtvqdlllsvapvrvkeaaERLNGAELAMMEREDektqmryaQAITDYTdaggydievLWDTCTMAALgapydnvkyrd 168
Cdd:cd03213 75 LD------------------KRSFRKIIGYVPQDD--------ILHPTLT---------VRETLMFAAK----------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 169 LTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDvPGK----IWLEQALRETSKTVLLVSHD-RQLLANAVDRIVTVE 242
Cdd:cd03213 109 LRGLSGGERKRVSIaLELVSNP-SLLFLDEPTSGLD-SSSalqvMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLS 186
|
....*...
gi 2796936914 243 SGNVWIHG 250
Cdd:cd03213 187 QGRVIYFG 194
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
352-531 |
9.66e-09 |
|
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: 55.01 E-value: 9.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 352 MKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGvarlgarvvpghfaqtharpellgrtpcEIVMTEHARLKN 431
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQG----------------------------EITLDGVPVSDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 432 EamKALARYElagGVAEQR---FET---------LSGGQQARLQILLLEMSGATLLLLDEPTDNLD-LASAEALQAGLDA 498
Cdd:cd03247 70 E--KALSSLI---SVLNQRpylFDTtlrnnlgrrFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQLLSLIFEV 144
|
170 180 190
....*....|....*....|....*....|....
gi 2796936914 499 F-DGTVLAVTHDRWFAADFDRyMVFGTDGRVYES 531
Cdd:cd03247 145 LkDKTLIWITHHLTGIEHMDK-ILFLENGKIIMQ 177
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
352-536 |
9.71e-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: 56.09 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 352 MKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARV---VPGH-------FaQTHAR-PELlgrT--- 417
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHkrpvntvF-QNYALfPHL---Tvfe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 418 ----PCEIVMTEHARLKNEAMKALARYELaGGVAEQRFETLSGGQQARLQI---LLLEmsgATLLLLDEPTDNLDLASAE 490
Cdd:cd03300 92 niafGLRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIaraLVNE---PKVLLLDEPLGALDLKLRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2796936914 491 ALQAGLDAFDG----TVLAVTHDRWFAADF-DRYMVF--------GTDGRVYESPEPVW 536
Cdd:cd03300 168 DMQLELKRLQKelgiTFVFVTHDQEEALTMsDRIAVMnkgkiqqiGTPEEIYEEPANRF 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-227 |
9.82e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.41 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfigsLRGAGESSPGGDgrdsRTV- 92
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT--------------LDGVPVTGPGAD----RGVv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 --QDLLLSVAPVRVKEAAerlnGAELAMMEREDEKTQMRYAQAITDYTDAGGYDIevlWDtctmaalgapydnvkyrdlt 170
Cdd:COG4525 82 fqKDALLPWLNVLDNVAF----GLRLRGVPKAERRARAEELLALVGLADFARRRI---WQ-------------------- 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796936914 171 tLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPG---------KIWleqalRETSKTVLLVSHD 227
Cdd:COG4525 135 -LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTreqmqelllDVW-----QRTGKGVFLITHS 194
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
17-241 |
1.03e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.04 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrqFIgslrgagesspggDGRD--SRTVQ- 93
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-----------FI-------------DGEDvtHRSIQq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 94 -DLLL---SVAPVRVKEAAERLnGAELAMMEREDEKTQMRYAQAItDYTDAGGYDievlwDtctmaalgapydnvKYRDl 169
Cdd:PRK11432 78 rDICMvfqSYALFPHMSLGENV-GYGLKMLGVPKEERKQRVKEAL-ELVDLAGFE-----D--------------RYVD- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 170 tTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPgkiwLEQALRETSK--------TVLLVSHDrQLLANAVDRIVT 240
Cdd:PRK11432 136 -QISGGQQQRVALaRALILKP-KVLLFDEPLSNLDAN----LRRSMREKIRelqqqfniTSLYVTHD-QSEAFAVSDTVI 208
|
.
gi 2796936914 241 V 241
Cdd:PRK11432 209 V 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-246 |
1.10e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.81 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDgRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglGVMRQF----IGSLRGAGESSPGGDG 86
Cdd:TIGR00958 492 PD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG--VPLVQYdhhyLHRQVALVGQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 87 RDSRTVQDLLLSVAPVRVKEAAERLNGAELAMMEREDektqmryaqaitdytdagGYDIEVlwdtctmAALGapydnvky 166
Cdd:TIGR00958 569 GSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPN------------------GYDTEV-------GEKG-------- 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 167 rdlTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAvDRIVTVESGN 245
Cdd:TIGR00958 616 ---SQLSGGQKQRIAIaRALVRKP-RVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERA-DQILVLKKGS 690
|
.
gi 2796936914 246 V 246
Cdd:TIGR00958 691 V 691
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-263 |
1.15e-08 |
|
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: 58.00 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQFIGSLrgagessPGgdgrdsrTV 92
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIM-------PG-------TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 QD-LLLSVApvrvkeaaerlngaelammerEDEktqMRYAQAItdytdaggydievlwDTCTMA---ALGAPYDNVKYRD 168
Cdd:TIGR01271 504 KDnIIFGLS---------------------YDE---YRYTSVI---------------KACQLEediALFPEKDKTVLGE 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 169 -LTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDV-PGKIWLEQALRE--TSKTVLLVSHDRQLLANAvDRIVTVESG 244
Cdd:TIGR01271 545 gGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVvTEKEIFESCLCKlmSNKTRILVTSKLEHLKKA-DKILLLHEG 623
|
250
....*....|....*....
gi 2796936914 245 NVWIHGggfaTYSEARKDR 263
Cdd:TIGR01271 624 VCYFYG----TFSELQAKR 638
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-58 |
1.23e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 55.89 E-value: 1.23e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV 58
Cdd:COG4674 21 DGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSV 67
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-246 |
1.44e-08 |
|
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: 55.57 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG------GLGVMRQFIGSLrgagesspgg 84
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlalaDPAWLRRQVGVV---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 85 dgrdsrtVQDLLLSVAPVRvkeaaERLNGAELAM-MEREDEKTQMryaqaitdytdAGGYDIevlwdtctMAALGAPYDN 163
Cdd:cd03252 82 -------LQENVLFNRSIR-----DNIALADPGMsMERVIEAAKL-----------AGAHDF--------ISELPEGYDT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 164 VKYRDLTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSHDRQLLANAvDRIVT 240
Cdd:cd03252 131 IVGEQGAGLSGGQRQRIAIaRALIHNP-RILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAHRLSTVKNA-DRIIV 208
|
....*.
gi 2796936914 241 VESGNV 246
Cdd:cd03252 209 MEKGRI 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
346-508 |
1.56e-08 |
|
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: 54.92 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAG------EEVR---------HTGVARLGARV-V 400
Cdd:cd03268 1 LKTNDLTKTYgkkrvlddiSLHVKKGEIYGFLGPNGAGKTTTMKIILGlikpdsGEITfdgksyqknIEALRRIGALIeA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 401 PGHFaqtharPELLGRTPCEIVMTEHARLKNEAMKALARYELaGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEP 480
Cdd:cd03268 81 PGFY------PNLTARENLRLLARLLGIRKKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190
....*....|....*....|....*....|.
gi 2796936914 481 TDNLDLASAEALQA---GLDAFDGTVLAVTH 508
Cdd:cd03268 154 TNGLDPDGIKELRElilSLRDQGITVLISSH 184
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
356-481 |
1.60e-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: 55.13 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGhfAQTHAR--------PEllGR------TPCE- 420
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG--LPPHERaragigyvPE--GRrifpelTVEEn 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 421 IVMTEHARLKNEAMKALAR-YELAGGVAE---QRFETLSGGQQARLQILLLEMSGATLLLLDEPT 481
Cdd:cd03224 96 LLLGAYARRRAKRKARLERvYELFPRLKErrkQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-247 |
1.64e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSvthagglgvmrqfigslrGAGESSPGGDGRDsRTVQ 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA------------------GCVDVPDNQFGRE-ASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 94 DLLLSVAPvrVKEAAERLNGAELAmmeredektqmryaqaitdytDAggydieVLWDtctmaalgAPYDNvkyrdlttLS 173
Cdd:COG2401 104 DAIGRKGD--FKDAVELLNAVGLS---------------------DA------VLWL--------RRFKE--------LS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 174 GGEQKRLALEALLRGPDQTLLLDEPDNYLDVP-----GKIWLEqALRETSKTVLLVSHdRQLLANAV--DRIVTVESGNV 246
Cdd:COG2401 139 TGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrvARNLQK-LARRAGITLVVATH-HYDVIDDLqpDLLIFVGYGGV 216
|
.
gi 2796936914 247 W 247
Cdd:COG2401 217 P 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-253 |
1.65e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.28 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG--LGVMRQfigSLRgagesspggdgRD 88
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdiRTVTRA---SLR-----------RN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 89 SRTV-QDLLL---SVA-----------PVRVKEAAERlnGAELAMMEREDektqmryaqaitdytdaGGYDIevlwdtct 153
Cdd:PRK13657 411 IAVVfQDAGLfnrSIEdnirvgrpdatDEEMRAAAER--AQAHDFIERKP-----------------DGYDT-------- 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 154 maalgapydNVKYRDLTtLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSHDRQL 230
Cdd:PRK13657 464 ---------VVGERGRQ-LSGGERQRLAIaRALLKDP-PILILDEATSALDVETEAKVKAALDELMKgrTTFIIAHRLST 532
|
250 260
....*....|....*....|...
gi 2796936914 231 LANAvDRIVTVESGNVwIHGGGF 253
Cdd:PRK13657 533 VRNA-DRILVFDNGRV-VESGSF 553
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
357-528 |
1.84e-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: 54.90 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 357 LEIWYGERVAVLGSNGSGKSHFLRLIAGE------EVRHTGV--ARLGARVVPGHFAQTHARPELLGRTPCE-IVMTEHA 427
Cdd:cd03245 25 LTIRAGEKVAIIGRVGSGKSTLLKLLAGLykptsgSVLLDGTdiRQLDPADLRRNIGYVPQDVTLFYGTLRDnITLGAPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 428 RLKNEAMKALaryELAG----------GVAEQ---RFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQA 494
Cdd:cd03245 105 ADDERILRAA---ELAGvtdfvnkhpnGLDLQigeRGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKE 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 2796936914 495 GLDAF--DGTVLAVTHDRWFAADFDRYMVFgTDGRV 528
Cdd:cd03245 182 RLRQLlgDKTLIIITHRPSLLDLVDRIIVM-DSGRI 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
346-533 |
1.93e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.53 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLG------ARVVPGHFAQTHAR 410
Cdd:PRK11264 4 IEVKNLVKKFhgqtvlhgiDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 411 PELLG-----------RTPCEIVMTEHARLKNE--------AMKALARYELAGgvAEQRF-ETLSGGQQARLQIL-LLEM 469
Cdd:PRK11264 84 RQHVGfvfqnfnlfphRTVLENIIEGPVIVKGEpkeeatarARELLAKVGLAG--KETSYpRRLSGGQQQRVAIArALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 470 SgATLLLLDEPTDNLDLA-SAEALQA--GLDAFDGTVLAVTHDRWFAADFDRYMVFGTDGRVYESPE 533
Cdd:PRK11264 162 R-PEVILFDEPTSALDPElVGEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-231 |
1.96e-08 |
|
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: 54.46 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 8 HVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAG--DLQPIEGSVTHAGglgvmrqfigslrgagesspggd 85
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKG----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 86 grdsrtvQDLLlsvapvrvkeaaerlngaELAMMERedektqmryaqaitdytdaggydievlwdtctmAALG------- 158
Cdd:cd03217 64 -------EDIT------------------DLPPEER---------------------------------ARLGiflafqy 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 159 -APYDNVKYRDL-----TTLSGGEQKRLA-LEALLRGPDqTLLLDEPDNYLDVPG-KIWLEQ--ALRETSKTVLLVSHDR 228
Cdd:cd03217 86 pPEIPGVKNADFlryvnEGFSGGEKKRNEiLQLLLLEPD-LAILDEPDSGLDIDAlRLVAEVinKLREEGKSVLIITHYQ 164
|
...
gi 2796936914 229 QLL 231
Cdd:cd03217 165 RLL 167
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2-226 |
2.27e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.98 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 2 QVSRLTHVLPDGRP---LLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQP---IEGSVT---HAGGLGVMRQ--- 69
Cdd:TIGR00955 23 LVSRLRGCFCRERPrkhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLlngMPIDAKEMRAisa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 70 -------FIGSLrgagesspggdgrdsrTVQDLLLSVAPVRvkeaaerlngaelamMEREDEKTQMRyaQAITdytdagg 142
Cdd:TIGR00955 103 yvqqddlFIPTL----------------TVREHLMFQAHLR---------------MPRRVTKKEKR--ERVD------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 143 ydiEVLWDT----CTMAALGAPyDNVKyrdltTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRET 217
Cdd:TIGR00955 143 ---EVLQALglrkCANTRIGVP-GRVK-----GLSGGERKRLAFaSELLTDP-PLLFCDEPTSGLDSFMAYSVVQVLKGL 212
|
250
....*....|..
gi 2796936914 218 S---KTVLLVSH 226
Cdd:TIGR00955 213 AqkgKTIICTIH 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
13-59 |
2.44e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.04 E-value: 2.44e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVT 59
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIF 61
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-250 |
2.89e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 19 DVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV-------THAGGLGVMRQfIGsLRGAGESSPGgdgrdSRT 91
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiQHYASKEVARR-IG-LLAQNATTPG-----DIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 VQDLLlsvapVRVKEAAERLngaeLAMMEREDEKTQMRYAQAiTDYTDAGGYDIEvlwdtctmaalgapydnvkyrdltT 171
Cdd:PRK10253 98 VQELV-----ARGRYPHQPL----FTRWRKEDEEAVTKAMQA-TGITHLADQSVD------------------------T 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQAL----RETSKTVLLVSHDRQLLANAVDRIVTVESGNVW 247
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLselnREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
...
gi 2796936914 248 IHG 250
Cdd:PRK10253 224 AQG 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-237 |
3.07e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.78 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLtHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLI--AGDLQPiegSVTHAGGLgvmrqfigSLRGAG 78
Cdd:PRK14239 6 LQVSDL-SVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNP---EVTITGSI--------VYNGHN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 79 ESSPGGDGRDSRTvqdlllsvapvrvkeaaerlngaELAMMEREDEKTQMR-YAQAITDYTDAGGYDIEVLWDTCTMAAL 157
Cdd:PRK14239 74 IYSPRTDTVDLRK-----------------------EIGMVFQQPNPFPMSiYENVVYGLRLKGIKDKQVLDEAVEKSLK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 158 GAP-YDNVKYR---DLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLD--VPGKIwlEQALRETSK--TVLLVSHDRQ 229
Cdd:PRK14239 131 GASiWDEVKDRlhdSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDpiSAGKI--EETLLGLKDdyTMLLVTRSMQ 208
|
....*...
gi 2796936914 230 LLANAVDR 237
Cdd:PRK14239 209 QASRISDR 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
356-508 |
3.73e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 53.65 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAG-------------EEVRHTGVARLGARVVPGHfaQTHARPELlgrTPCE-- 420
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGlarpdagevlwqgEPIRRQRDEYHQDLLYLGH--QPGIKTEL---TALEnl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 421 -IVMTEHARLKNEAM-KALARYELAGgvaeqrFE-----TLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQ 493
Cdd:PRK13538 96 rFYQRLHGPGDDEALwEALAQVGLAG------FEdvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLE 169
|
170
....*....|....*...
gi 2796936914 494 AGLDAF---DGTVLAVTH 508
Cdd:PRK13538 170 ALLAQHaeqGGMVILTTH 187
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-244 |
3.74e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 54.26 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLgvmrqfigslrgagESSPGGDGRDSRTV 92
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKN--------------ESEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 QDlllsvapvrVKEAAER---LNGAELAMMEREDEKTQMRYaQAITDYTDAGGyDIEVL--WDTCTMAALGapydnvkyr 167
Cdd:cd03290 79 YS---------VAYAAQKpwlLNATVEENITFGSPFNKQRY-KAVTDACSLQP-DIDLLpfGDQTEIGERG--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 168 dlTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQA-----LRETSKTVLLVSHDRQLLANAvDRIVTVE 242
Cdd:cd03290 139 --INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYLPHA-DWIIAMK 215
|
..
gi 2796936914 243 SG 244
Cdd:cd03290 216 DG 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-250 |
3.79e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.99 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-------------GLGVMRQ----FIGS 73
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAISVVSQrvhlFSAT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 74 LRgagesspggdgrdsrtvQDLLLSVAPVRVKEAAERLNGAELAMMEREDEktqmryaqaitdytdagGYDievLWdtct 153
Cdd:PRK11160 430 LR-----------------DNLLLAAPNASDEALIEVLQQVGLEKLLEDDK-----------------GLN---AW---- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 154 MAALGAPydnvkyrdlttLSGGEQKRLAL-EALLR-GPdqTLLLDEPDNYLDVPGKIWLEQALRETS--KTVLLVSHDRQ 229
Cdd:PRK11160 469 LGEGGRQ-----------LSGGEQRRLGIaRALLHdAP--LLLLDEPTEGLDAETERQILELLAEHAqnKTVLMITHRLT 535
|
250 260
....*....|....*....|.
gi 2796936914 230 LLANaVDRIVTVESGNVWIHG 250
Cdd:PRK11160 536 GLEQ-FDRICVMDNGQIIEQG 555
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
17-246 |
3.98e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 55.46 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-----------GLGVMRQF------------IGS 73
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdlppkdrNIAMVFQSyalyphmtvyenIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 74 -LRGAGESspgGDGRDSrtvqdlllsvapvRVKEAAERLNgaelammeredektqmryaqaITDYTDaggydievlwdtc 152
Cdd:COG3839 99 pLKLRKVP---KAEIDR-------------RVREAAELLG---------------------LEDLLD------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 153 tmaalgapydnvkyRDLTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQAL----RETSKTVLLVSHD 227
Cdd:COG3839 129 --------------RKPKQLSGGQRQRVALgRALVREPK-VFLLDEPLSNLDAKLRVEMRAEIkrlhRRLGTTTIYVTHD 193
|
250 260
....*....|....*....|...
gi 2796936914 228 rQL----LAnavDRIVTVESGNV 246
Cdd:COG3839 194 -QVeamtLA---DRIAVMNDGRI 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-481 |
4.00e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.79 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAgglGVMRQFigslrgageSSPggdgRDSR-----T 91
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD---GEPVRF---------RSP----RDAQaagiaI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 V-QDLLLsvapvrvkeaAERLNGAELAMMERE-------DEKTQMRYAQAItdytdaggydievlwdtctMAALGAPYDN 163
Cdd:COG1129 84 IhQELNL----------VPNLSVAENIFLGREprrggliDWRAMRRRAREL-------------------LARLGLDIDP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 164 vkYRDLTTLSGGEQKRLAL-EALLRGPdQTLLLDEP---------DNYLDVpgkiwLEQaLRETSKTVLLVSHdrqllan 233
Cdd:COG1129 135 --DTPVGDLSVAQQQLVEIaRALSRDA-RVLILDEPtaslterevERLFRI-----IRR-LKAQGVAIIYISH------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 234 avdrivtvesgnvwihgggfatysearkdrneRLDELRRRWDeehaklkRLVVMlrqkatyndsmaapyhaaqtrlR--R 311
Cdd:COG1129 199 --------------------------------RLDEVFEIAD-------RVTVL----------------------RdgR 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 312 FEEAGPPELAPKDQLISM----RLRGGRTAKRAVI------CENLELSGLMKPFDLEIWYGERVAVLGSNGSGKSHFLRL 381
Cdd:COG1129 218 LVGTGPVAELTEDELVRLmvgrELEDLFPKRAAAPgevvleVEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARA 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 382 IAGEEVRHTGVARL-GARVVPGHFAQTHAR-----PE-------LLGRTPCE-IVMTEHARL-----------KNEAMKA 436
Cdd:COG1129 298 LFGADPADSGEIRLdGKPVRIRSPRDAIRAgiayvPEdrkgeglVLDLSIREnITLASLDRLsrgglldrrreRALAEEY 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2796936914 437 LARYELAGGVAEQRFETLSGG-QQ----ARLqiLLLEMSgatLLLLDEPT 481
Cdd:COG1129 378 IKRLRIKTPSPEQPVGNLSGGnQQkvvlAKW--LATDPK---VLILDEPT 422
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
346-510 |
4.51e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.11 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAG-------------EEVRHTGVARLGARVVpgh 403
Cdd:PRK11432 7 VVLKNITKRFgsntvidnlNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlekptegqifidgEDVTHRSIQQRDICMV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 404 FaQTHAR-PEL------------LGRTPCEIVmtehARLKneamKALARYELAGgvAEQRF-ETLSGGQQARLQI---LL 466
Cdd:PRK11432 84 F-QSYALfPHMslgenvgyglkmLGVPKEERK----QRVK----EALELVDLAG--FEDRYvDQISGGQQQRVALaraLI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2796936914 467 LEmsgATLLLLDEPTDNLDL----ASAEALQAGLDAFDGTVLAVTHDR 510
Cdd:PRK11432 153 LK---PKVLLFDEPLSNLDAnlrrSMREKIRELQQQFNITSLYVTHDQ 197
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
358-518 |
4.62e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.05 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 358 EIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARvvPGHFAQTHARPELLGRTPCEIVMTEH-----ARLKNE 432
Cdd:PRK11629 31 SIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ--PMSKLSSAAKAELRNQKLGFIYQFHHllpdfTALENV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 433 AMKAL------------ARYELAGGVAEQRFE----TLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEA---LQ 493
Cdd:PRK11629 109 AMPLLigkkkpaeinsrALEMLAAVGLEHRANhrpsELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSifqLL 188
|
170 180
....*....|....*....|....*.
gi 2796936914 494 AGLDAFDGTV-LAVTHDRWFAADFDR 518
Cdd:PRK11629 189 GELNRLQGTAfLVVTHDLQLAKRMSR 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-246 |
5.04e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 54.08 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDgRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGG-------------LGVMRQ----FIGS 73
Cdd:cd03249 14 PD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQepvlFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 74 LRgagesspggD----GRDSRTVQDlllsvapvrVKEAAERLNGAELammeredektqmryaqaITDYTDagGYDIEVlw 149
Cdd:cd03249 93 IA---------EniryGKPDATDEE---------VEEAAKKANIHDF-----------------IMSLPD--GYDTLV-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 150 dtctmaalGAPYdnvkyrdlTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSH 226
Cdd:cd03249 134 --------GERG--------SQLSGGQKQRIAIaRALLRNPK-ILLLDEATSALDAESEKLVQEALDRAMKgrTTIVIAH 196
|
250 260
....*....|....*....|
gi 2796936914 227 DRQLLANAvDRIVTVESGNV 246
Cdd:cd03249 197 RLSTIRNA-DLIAVLQNGQV 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
14-47 |
5.09e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 55.60 E-value: 5.09e-08
10 20 30
....*....|....*....|....*....|....
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLI 47
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-250 |
5.16e-08 |
|
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: 53.70 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV-------THA-----GGLGvmrqfIGSLrgAGES 80
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqdiTKLpmhkrARLG-----IGYL--PQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 SPGGDgrdsRTVQDLLLSVAPVRVKEAAERLNGAELAMMEREDEKTQMRYAQaitdytdaggydievlwdtctmaalgap 160
Cdd:cd03218 85 SIFRK----LTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKAS---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 161 ydnvkyrdltTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDvPGKIWLEQA----LRETSKTVLLVSHD-RQLLAnA 234
Cdd:cd03218 133 ----------SLSGGERRRVEIaRALATNPK-FLLLDEPFAGVD-PIAVQDIQKiikiLKDRGIGVLITDHNvRETLS-I 199
|
250
....*....|....*.
gi 2796936914 235 VDRIVTVESGNVWIHG 250
Cdd:cd03218 200 TDRAYIIYEGKVLAEG 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-263 |
5.39e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.12 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 3 VSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThAGGLGVMRQFIGSLRGAGESSP 82
Cdd:PRK15056 9 VNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIS-ILGQPTRQALQKNLVAYVPQSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 83 GGDGRDSRTVQDLLlsvapvrvkeaaerlngaelaMMEREDEKTQMRYAQAitdytdaggYDIEvlwdtCTMAALgAPYD 162
Cdd:PRK15056 88 EVDWSFPVLVEDVV---------------------MMGRYGHMGWLRRAKK---------RDRQ-----IVTAAL-ARVD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 163 NVKY--RDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGK---IWLEQALRETSKTVLLVSHDRQLLANAVDR 237
Cdd:PRK15056 132 MVEFrhRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEariISLLRELRDEGKTMLVSTHNLGSVTEFCDY 211
|
250 260
....*....|....*....|....*.
gi 2796936914 238 IVTVEsGNVWIHGGGFATYSEARKDR 263
Cdd:PRK15056 212 TVMVK-GTVLASGPTETTFTAENLEL 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
352-509 |
5.98e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.91 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 352 MKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGArvVPGHFAQTHARpellgrtpceiVMTEHARL-- 429
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT--APLAEAREDTR-----------LMFQDARLlp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 430 ----------------KNEAMKALAryelAGGVAEQRFE---TLSGGQQARLQILLLEMSGATLLLLDEPTDNLD-LASA 489
Cdd:PRK11247 95 wkkvidnvglglkgqwRDAALQALA----AVGLADRANEwpaALSGGQKQRVALARALIHRPGLLLLDEPLGALDaLTRI 170
|
170 180
....*....|....*....|....*...
gi 2796936914 490 EA--------LQAGLdafdgTVLAVTHD 509
Cdd:PRK11247 171 EMqdlieslwQQHGF-----TVLLVTHD 193
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
5-227 |
6.06e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 5 RLTHVLPDGRplLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGdLQPIEGSVTHAGglgvmrqfigslrgagesspgg 84
Cdd:PRK03695 2 QLNDVAVSTR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAG---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 85 dgrdsrtvQDLLLsvapvrvkeaaerLNGAELAMM-----EREDEKTQMRYAQAITDYTDAGG--YDIE-VLWDTCTMAA 156
Cdd:PRK03695 57 --------QPLEA-------------WSAAELARHraylsQQQTPPFAMPVFQYLTLHQPDKTrtEAVAsALNEVAEALG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 LgapyDNVKYRDLTTLSGGEQKRLALEA--LLRGPD-----QTLLLDEPDNYLDVPGKIWLEQALRETSK---TVLLVSH 226
Cdd:PRK03695 116 L----DDKLGRSVNQLSGGEWQRVRLAAvvLQVWPDinpagQLLLLDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSH 191
|
.
gi 2796936914 227 D 227
Cdd:PRK03695 192 D 192
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-244 |
6.30e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 53.59 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGS--VTHAGG------------LGVMRQFIG-------- 72
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGwvdlaqaspreiLALRRRTIGyvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 73 ------------SLRGAGESSpggdgrdsrtvqdlllSVAPVRVKEAAERLNgaelammeredektqmryaqaitdytda 140
Cdd:COG4778 105 iprvsaldvvaePLLERGVDR----------------EEARARARELLARLN---------------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 141 ggydI-EVLWDTctmaalgAPydnvkyrdlTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGK---IWLEQALR 215
Cdd:COG4778 141 ----LpERLWDL-------PP---------ATFSGGEQQRVNIaRGFIADPP-LLLLDEPTASLDAANRavvVELIEEAK 199
|
250 260
....*....|....*....|....*....
gi 2796936914 216 ETSKTVLLVSHDRQLLANAVDRIVTVESG 244
Cdd:COG4778 200 ARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-62 |
6.45e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.94 E-value: 6.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG 62
Cdd:COG1101 16 VNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG 67
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
17-246 |
6.99e-08 |
|
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: 53.27 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGE-----------GTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThAGGLGVMrqfigslrgageSSPGGD 85
Cdd:cd03298 3 LDKIRFSYGEqpmhfdltfaqGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVL-INGVDVT------------AAPPAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 86 GRDSRTVQDL-LLSVAPVRVKEAAERLNGAELammeREDEKTQMRYAqaitdytdaggydievlwdtctMAALGapYDNV 164
Cdd:cd03298 70 RPVSMLFQENnLFAHLTVEQNVGLGLSPGLKL----TAEDRQAIEVA----------------------LARVG--LAGL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 165 KYRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDvPGKIWLEQAL-----RETSKTVLLVSHDRQLLANAVDRIV 239
Cdd:cd03298 122 EKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD-PALRAEMLDLvldlhAETKMTVLMVTHQPEDAKRLAQRVV 200
|
....*..
gi 2796936914 240 TVESGNV 246
Cdd:cd03298 201 FLDNGRI 207
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
157-251 |
7.58e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 55.61 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 LGAPYDNVKyRDLTTLSGGEQKRLALEALLRGP--DQTLLLDEPDNYL---DVPGKIWLEQALRETSKTVLLVSHDRQLL 231
Cdd:PRK00635 463 LGLPYLTPE-RALATLSGGEQERTALAKHLGAEliGITYILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVEHDEQMI 541
|
90 100
....*....|....*....|
gi 2796936914 232 ANAvDRIVTVESGnVWIHGG 251
Cdd:PRK00635 542 SLA-DRIIDIGPG-AGIFGG 559
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-263 |
8.27e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLR----------GAGESS 81
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG------EDISTLKpeiyrqqvsyCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 82 PGGDgrdsrTVQDLLLSVAPVRVKEAAERLNGAELAMMEREDEKTQmryaQAITDytdaggydievlwdtctmaalgapy 161
Cdd:PRK10247 92 LFGD-----TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILT----KNIAE------------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 162 dnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKI----WLEQALRETSKTVLLVSHDRQLLANAvDR 237
Cdd:PRK10247 138 ----------LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHnvneIIHRYVREQNIAVLWVTHDKDEINHA-DK 206
|
250 260
....*....|....*....|....*.
gi 2796936914 238 IVTVESgnvwiHGGgfaTYSEARKDR 263
Cdd:PRK10247 207 VITLQP-----HAG---EMQEARYEL 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
344-509 |
8.59e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.31 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 344 ENLELSGLMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGeEVRHTGVARLGARVVPG--HFAQTHARPELLGRTPCEI 421
Cdd:COG4138 4 NDVAVAGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDwsAAELARHRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 422 VMTEH-------ARLKNEAMKALARYELAggvaeQRFE----------TLSGGQQAR-------LQILLLEMSGATLLLL 477
Cdd:COG4138 83 AMPVFqylalhqPAGASSEAVEQLLAQLA-----EALGledklsrpltQLSGGEWQRvrlaavlLQVWPTINPEGQLLLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 2796936914 478 DEPTDNLDLASAEALQAGLDAF---DGTVLAVTHD 509
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHD 192
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
160-293 |
9.14e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 160 PYDNVKyRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKI----WLEQALRETSKTVLLVSHDRQLLANAV 235
Cdd:PRK13645 140 PEDYVK-RSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEYKKRIIMVTHNMDQVLRIA 218
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 236 DRIVTVESGNVWIHGGGFATYSEArkdrnerldELRRRWDEEHAKLKRLVVMLRQKAT 293
Cdd:PRK13645 219 DEVIVMHEGKVISIGSPFEIFSNQ---------ELLTKIEIDPPKLYQLMYKLKNKGI 267
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-246 |
1.00e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.46 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-------------GLGVM-----RQFIG 72
Cdd:PRK13632 19 NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeirkKIGIIfqnpdNQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 73 SlrgagesspggdgrdsrTVQDlllSVApvrvkeaaerlNGAELAMMEREDEKTqmryaqAITDYTDAGGydIEVLWDtc 152
Cdd:PRK13632 99 A-----------------TVED---DIA-----------FGLENKKVPPKKMKD------IIDDLAKKVG--MEDYLD-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 153 tmaalgapydnvkyRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRE----TSKTVLLVSHDR 228
Cdd:PRK13632 138 --------------KEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrktRKKTLISITHDM 203
|
250
....*....|....*...
gi 2796936914 229 QLLANAvDRIVTVESGNV 246
Cdd:PRK13632 204 DEAILA-DKVIVFSEGKL 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
5-227 |
1.16e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.92 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 5 RLTHVLPDGRplLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGdLQPIEGSVTHAGglgvmrqfigslrgagesspgg 84
Cdd:COG4138 2 QLNDVAVAGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNG---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 85 dgrdsrtvQDLllsvapvrvkeaaERLNGAELAMM-----EREDEKTQMRYAQAITDYTDAGG---YDIEVLWDTCTMAA 156
Cdd:COG4138 57 --------RPL-------------SDWSAAELARHraylsQQQSPPFAMPVFQYLALHQPAGAsseAVEQLLAQLAEALG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 LGAPYDnvkyRDLTTLSGGEQKRLALEA-LLR-----GPD-QTLLLDEPDNYLDVPGKIWLEQALRETSK---TVLLVSH 226
Cdd:COG4138 116 LEDKLS----RPLTQLSGGEWQRVRLAAvLLQvwptiNPEgQLLLLDEPMNSLDVAQQAALDRLLRELCQqgiTVVMSSH 191
|
.
gi 2796936914 227 D 227
Cdd:COG4138 192 D 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
353-508 |
1.25e-07 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 52.93 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIA-------------GEEVRHTGVARLGAR--VV---PGHFAQTHARPELL 414
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsgeilldGVDIRDLNLRWLRSQigLVsqePVLFDGTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 415 GRTPCEIVMTEHARLKNEA----MKALARYE-LAGGVAEQrfetLSGGQQARLQI---LLLEmsgATLLLLDEPTDNLDL 486
Cdd:cd03249 100 GKPDATDEEVEEAAKKANIhdfiMSLPDGYDtLVGERGSQ----LSGGQKQRIAIaraLLRN---PKILLLDEATSALDA 172
|
170 180
....*....|....*....|....
gi 2796936914 487 ASAEALQAGLDAF--DGTVLAVTH 508
Cdd:cd03249 173 ESEKLVQEALDRAmkGRTTIVIAH 196
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-246 |
1.28e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQFIGSLRGAGESSPGGDGR-DSRTVQDl 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQfVGATVED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 96 llsvapvRVKEAAERLNGAELAMMEREDEktqmryaqaitdytdaggydievlwdtctmAALGAPYDNVKYRDLTTLSGG 175
Cdd:PRK13642 102 -------DVAFGMENQGIPREEMIKRVDE------------------------------ALLAVNMLDFKTREPARLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 176 EQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLANAvDRIVTVESGNV 246
Cdd:PRK13642 145 QKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyqlTVLSITHDLDEAASS-DRILVMKAGEI 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
362-512 |
1.34e-07 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 52.44 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLI-------AGE-EVRHTG----VARLGARVVpghfaqTHARPELLG----------RTPC 419
Cdd:COG4778 37 GECVALTGPSGAGKSTLLKCIygnylpdSGSiLVRHDGgwvdLAQASPREI------LALRRRTIGyvsqflrvipRVSA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 420 -EIVM-------TEHARLKNEAMKALARYelagGVAEQRFE----TLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLA 487
Cdd:COG4778 111 lDVVAepllergVDREEARARARELLARL----NLPERLWDlppaTFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAA 186
|
170 180 190
....*....|....*....|....*....|...
gi 2796936914 488 S--------AEALQAGLdafdgTVLAVTHDRWF 512
Cdd:COG4778 187 NravvveliEEAKARGT-----AIIGIFHDEEV 214
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
351-535 |
1.75e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.48 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 351 LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHAR---------PELLGRTPCEI 421
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkvaylpqqlPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 422 VMTE----HARLKNEAMKALARYELA------GGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLA-SAE 490
Cdd:PRK10575 106 VAIGrypwHGALGRFGAADREKVEEAislvglKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhQVD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2796936914 491 AL--------QAGLdafdgTVLAVTHDRWFAADFDRYMVFGTDGRVYESPEPV 535
Cdd:PRK10575 186 VLalvhrlsqERGL-----TVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-228 |
1.75e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrQFIGSlrgagesspgGDGRDSRTVQ 93
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI----------LFERQ----------SIKKDLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 94 DLLLSVApvrvkeaaeRLNGAELAMMEREDEKTQMryaqaitdYTDAGGYDIEVLwdtCTMAALGapydnvKYRDLTT-- 171
Cdd:PRK13540 74 KQLCFVG---------HRSGINPYLTLRENCLYDI--------HFSPGAVGITEL---CRLFSLE------HLIDYPCgl 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLD------VPGKIwleQALRETSKTVLLVSHDR 228
Cdd:PRK13540 128 LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDelslltIITKI---QEHRAKGGAVLLTSHQD 187
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
17-254 |
1.90e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.19 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQFIGSLRGAGESSPGGDGRDSR-TVQDl 95
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRmTVEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 96 llsvapvrvkeaaerlngaELAMMEREDEKTQmrYAQAITDYTDaggydievlwdtctmaaLGAPYDNVKYRDLTTLSGG 175
Cdd:PRK11614 100 -------------------NLAMGGFFAERDQ--FQERIKWVYE-----------------LFPRLHERRIQRAGTMSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 176 EQKRLALEALLRGPDQTLLLDEPDnyLDVPGKIWLE-----QALRETSKTVLLVSHDRQLLANAVDRIVTVESGNVWIHG 250
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLDEPS--LGLAPIIIQQifdtiEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLED 219
|
....
gi 2796936914 251 GGFA 254
Cdd:PRK11614 220 TGDA 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-246 |
2.26e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.47 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPL----LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHaGGLGVM--------- 67
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-DDITIThktkdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 68 --RQFIGSLRGAGESSPGGDGrdsrtvqdlllsvapvrvkeaaerlngaelamMEREDEKTQMRYAQAITDYTDaggYDI 145
Cdd:PRK13646 82 pvRKRIGMVFQFPESQLFEDT--------------------------------VEREIIFGPKNFKMNLDEVKN---YAH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 146 EVLWDtctmaaLGAPyDNVKYRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALR----ETSKTV 221
Cdd:PRK13646 127 RLLMD------LGFS-RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslqtDENKTI 199
|
250 260
....*....|....*....|....*
gi 2796936914 222 LLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:PRK13646 200 ILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
362-528 |
2.29e-07 |
|
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: 53.72 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGE-------------EVRHTGVARLGARVvpGHFAQTharPELLGRTPCEIVMTEHAR 428
Cdd:TIGR03375 491 GEKVAIIGRIGSGKSTLLKLLLGLyqptegsvlldgvDIRQIDPADLRRNI--GYVPQD---PRLFYGTLRDNIALGAPY 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 429 LKNEAMKALARyelAGGVAE--------------QRFETLSGGQQ-----ARLqiLLLEMSgatLLLLDEPTDNLDLASA 489
Cdd:TIGR03375 566 ADDEEILRAAE---LAGVTEfvrrhpdgldmqigERGRSLSGGQRqavalARA--LLRDPP---ILLLDEPTSAMDNRSE 637
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2796936914 490 EALQAGLDAF--DGTVLAVTHDRWFAADFDRYMVFgTDGRV 528
Cdd:TIGR03375 638 ERFKDRLKRWlaGKTLVLVTHRTSLLDLVDRIIVM-DNGRI 677
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
353-509 |
2.38e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.17 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFA------QTHArpeLLgrtPCEIVMTEH 426
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAdrgvvfQKDA---LL---PWLNVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 427 A---RLKN---EAMKALARYELA----GGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAG- 495
Cdd:COG4525 98 AfglRLRGvpkAERRARAEELLAlvglADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELl 177
|
170
....*....|....*..
gi 2796936914 496 LDAFDGT---VLAVTHD 509
Cdd:COG4525 178 LDVWQRTgkgVFLITHS 194
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-250 |
2.41e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.33 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgvmrqfIGSlrgaGESSPGGDGRDSRtvqdll 96
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-----------IGE----RVITAGKKNKKLK------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 97 lsvaPVRVK--------------EAAERlngaELAM------MEREDEKTQMRYAQAITdytdagGYDIEVLWDTctmaa 156
Cdd:PRK13634 82 ----PLRKKvgivfqfpehqlfeETVEK----DICFgpmnfgVSEEDAKQKAREMIELV------GLPEELLARS----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 lgaPYDnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWL----EQALRETSKTVLLVSHDRQLLA 232
Cdd:PRK13634 143 ---PFE---------LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMmemfYKLHKEKGLTTVLVTHSMEDAA 210
|
250
....*....|....*...
gi 2796936914 233 NAVDRIVTVESGNVWIHG 250
Cdd:PRK13634 211 RYADQIVVMHKGTVFLQG 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-246 |
2.51e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.43 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGV------MRQFIGSLRGAGESSPGGdgr 87
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeenvwdIRHKIGMVFQNPDNQFVG--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 88 dsRTVQDlllSVApvrvkeaaerlNGAELAMMEREDEKTQMRYAQAITDYTDaggydievlwdtctmaalgapydnVKYR 167
Cdd:PRK13650 97 --ATVED---DVA-----------FGLENKGIPHEEMKERVNEALELVGMQD------------------------FKER 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 168 DLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLANAvDRIVTVES 243
Cdd:PRK13650 137 EPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyqmTVISITHDLDEVALS-DRVLVMKN 215
|
...
gi 2796936914 244 GNV 246
Cdd:PRK13650 216 GQV 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
362-529 |
3.19e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.41 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVRHTG--------VARLGARVVP------GHFAQTHARpeLLGRT-------PCE 420
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGkiwfsghdITRLKNREVPflrrqiGMIFQDHHL--LMDRTvydnvaiPLI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 421 IVMTEHARLKNEAMKALARYELAGGVAEQRFEtLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFD 500
Cdd:PRK10908 106 IAGASGDDIRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFN 184
|
170 180 190
....*....|....*....|....*....|..
gi 2796936914 501 G---TVLAVTHDRWFAADFDRYMVFGTDGRVY 529
Cdd:PRK10908 185 RvgvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-250 |
3.60e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG--------GLGVMRQFIGSLRGAGESSPGGDG 86
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpldyskrGLLALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 87 RDSrtvqDLLLSVAPVRVKEAaerlngaELAmmEREDEktqmryaqAITdYTDAGGYdievlwdtctmaalgapydnvKY 166
Cdd:PRK13638 95 IDS----DIAFSLRNLGVPEA-------EIT--RRVDE--------ALT-LVDAQHF---------------------RH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 167 RDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALR---ETSKTVLLVSHDRQLLANAVDRIVTVES 243
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRrivAQGNHVIISSHDIDLIYEISDAVYVLRQ 211
|
....*..
gi 2796936914 244 GNVWIHG 250
Cdd:PRK13638 212 GQILTHG 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
362-509 |
3.68e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 51.62 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHARPELLGRTPCEIVM-----------TEHARLK 430
Cdd:PRK11248 27 GELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQdnvafglqlagVEKMQRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 431 NEAMKALARYELAGgvAEQRF-ETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQA-GLDAFDGT---VLA 505
Cdd:PRK11248 107 EIAHQMLKKVGLEG--AEKRYiWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTlLLKLWQETgkqVLL 184
|
....
gi 2796936914 506 VTHD 509
Cdd:PRK11248 185 ITHD 188
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
356-532 |
3.68e-07 |
|
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: 51.19 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpghfAQTHARPELLG-----------RTPCEIV-- 422
Cdd:cd03296 22 SLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----TDVPVQERNVGfvfqhyalfrhMTVFDNVaf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 423 ---MTEHARLKNEAMKALARYELAGGVA----EQRF-ETLSGGQQARLQI---LLLEMSgatLLLLDEPTDNLDLASAEA 491
Cdd:cd03296 98 glrVKPRSERPPEAEIRAKVHELLKLVQldwlADRYpAQLSGGQRQRVALaraLAVEPK---VLLLDEPFGALDAKVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 492 LQAGL----DAFDGTVLAVTHDRWFAADF-DRYMV--------FGTDGRVYESP 532
Cdd:cd03296 175 LRRWLrrlhDELHVTTVFVTHDQEEALEVaDRVVVmnkgrieqVGTPDEVYDHP 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-269 |
3.96e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.75 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLRGagesspggdgrdSRTVQDLL 96
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG------YHITPETG------------NKNLKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 97 LSVAPVrvkeaaerLNGAELAMMEREDEKTQMrYAQAITDYTDAGGYDIEVLWdtctMAALGAPyDNVKYRDLTTLSGGE 176
Cdd:PRK13641 85 KKVSLV--------FQFPEAQLFENTVLKDVE-FGPKNFGFSEDEAKEKALKW----LKKVGLS-EDLISKSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 177 QKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK---TVLLVSHDRQLLANAVDRIVTVESGNVWIHGGGF 253
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPK 230
|
250
....*....|....*.
gi 2796936914 254 ATYSEARKDRNERLDE 269
Cdd:PRK13641 231 EIFSDKEWLKKHYLDE 246
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-244 |
4.13e-07 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 50.93 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrqfigSLRGAGESSPGGDgrdsRTV--QD 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV--------------ILEGKQITEPGPD----RMVvfQN 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 95 L-LLSVAPVR--VKEAAERLNgAELAMMEREdektqmryaqaitdytdaggydiEVLWDTCTMAALGAPYDnvkyRDLTT 171
Cdd:TIGR01184 63 YsLLPWLTVRenIALAVDRVL-PDLSKSERR-----------------------AIVEEHIALVGLTEAAD----KRPGQ 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQAL----RETSKTVLLVSHDRQLLANAVDRIVTVESG 244
Cdd:TIGR01184 115 LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-246 |
4.20e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGsvthagglgvmrqfigslrgagesspggdgrdsrtv 92
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG------------------------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 qDLLLSVAPvrvkeaaerLNGAelammeREDekTQMRYAQA----ITDYTDAGGYDIEVLWDTCTMAALGApydnVKYRD 168
Cdd:PRK11247 68 -ELLAGTAP---------LAEA------RED--TRLMFQDArllpWKKVIDNVGLGLKGQWRDAALQALAA----VGLAD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 169 LTT-----LSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQAL----RETSKTVLLVSHDrqlLANAV--- 235
Cdd:PRK11247 126 RANewpaaLSGGQKQRVALaRALIHRP-GLLLLDEPLGALDALTRIEMQDLIeslwQQHGFTVLLVTHD---VSEAVama 201
|
250
....*....|.
gi 2796936914 236 DRIVTVESGNV 246
Cdd:PRK11247 202 DRVLLIEEGKI 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-250 |
4.20e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.43 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVT-HAGGLGVMRQFIGSLRGAGESSPGGDGRDSRT 91
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiDDEDISLLPLHARARRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 VQDLLLSVAPVRvkeaaerlngAELAMMEREDEKTQMRYAQAITDYTDAGGydievlwdtctmaalgapydnvkyrdlTT 171
Cdd:PRK10895 95 VYDNLMAVLQIR----------DDLSAEQREDRANELMEEFHIEHLRDSMG---------------------------QS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLE---QALRETSKTVLLVSHDRQLLANAVDRIVTVESGNVWI 248
Cdd:PRK10895 138 LSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKriiEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
..
gi 2796936914 249 HG 250
Cdd:PRK10895 218 HG 219
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
172-242 |
4.70e-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: 4.70e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVSHDRQLLANAVDRIVTVE 242
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlseEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
18-244 |
5.21e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.14 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 18 NDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVT----HAGGL--------GVMRQFiGSLRGAgesspggd 85
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqHIEGLpghqiarmGVVRTF-QHVRLF-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 86 gRDSRTVQDLLlsVAPVRvkeaaeRLNGAELAMMeredEKTQmRYAQAITDYTDAGGYDIEVLWDTctmaalgaPYDNvk 165
Cdd:PRK11300 93 -REMTVIENLL--VAQHQ------QLKTGLFSGL----LKTP-AFRRAESEALDRAATWLERVGLL--------EHAN-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 166 yRDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQAL----RETSKTVLLVSHDRQLLANAVDRIVTV 241
Cdd:PRK11300 149 -RQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
...
gi 2796936914 242 ESG 244
Cdd:PRK11300 228 NQG 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
346-492 |
5.50e-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: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARL-GARVVPGHFAQTHAR----- 410
Cdd:COG1129 5 LEMRGISKSFggvkaldgvSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSPRDAQAAgiaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 411 -------PEL-------LGRTPCEIVMTEHARLKNEAMKALARYELAGGVaEQRFETLSGGQQARLQI---LLLEmsgAT 473
Cdd:COG1129 85 hqelnlvPNLsvaenifLGREPRRGGLIDWRAMRRRARELLARLGLDIDP-DTPVGDLSVAQQQLVEIaraLSRD---AR 160
|
170
....*....|....*....
gi 2796936914 474 LLLLDEPTDNLDLASAEAL 492
Cdd:COG1129 161 VLILDEPTASLTEREVERL 179
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
353-509 |
6.23e-07 |
|
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: 50.33 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVV----PGH------FAQTHARP----------- 411
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtdlpPKDrdiamvFQNYALYPhmtvydniafg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 412 -ELLGRTPCEIvmteharlkNEAMKALARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLD----- 485
Cdd:cd03301 97 lKLRKVPKDEI---------DERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrv 167
|
170 180
....*....|....*....|....*.
gi 2796936914 486 --LASAEALQAGLDAfdgTVLAVTHD 509
Cdd:cd03301 168 qmRAELKRLQQRLGT---TTIYVTHD 190
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
346-510 |
6.47e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.76 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPFD---------LEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGvarlgaRVVPGHFAQTHARPEllgR 416
Cdd:PRK11607 20 LEIRNLTKSFDgqhavddvsLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAG------QIMLDGVDLSHVPPY---Q 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPCEIVMTEHARL------KNEAM----KALARYELAGGVAE-------QRF-----ETLSGGQQARLQILLLEMSGATL 474
Cdd:PRK11607 91 RPINMMFQSYALFphmtveQNIAFglkqDKLPKAEIASRVNEmlglvhmQEFakrkpHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2796936914 475 LLLDEPTDNLDLASAEALQAG----LDAFDGTVLAVTHDR 510
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEvvdiLERVGVTCVMVTHDQ 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
12-246 |
6.52e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 51.49 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLrgagessPgGDGRDSRT 91
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG------QDITHV-------P-AENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 92 V-QDLLL--------SVA------PVRVKEAAERLNGAeLAMMEREDektqmrYAQaitdytdaggydievlwdtctmaa 156
Cdd:PRK09452 91 VfQSYALfphmtvfeNVAfglrmqKTPAAEITPRVMEA-LRMVQLEE------FAQ------------------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 lgapydnvkyRDLTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLD----VPGKIWLEQALRETSKTVLLVSHDRQLL 231
Cdd:PRK09452 140 ----------RKPHQLSGGQQQRVAIaRAVVNKP-KVLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTHDQEEA 208
|
250
....*....|....*
gi 2796936914 232 ANAVDRIVTVESGNV 246
Cdd:PRK09452 209 LTMSDRIVVMRDGRI 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-246 |
6.53e-07 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 50.66 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 6 LTHVLPDGR---PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLRGAGEssp 82
Cdd:cd03258 7 VSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG------TDLTLLSGKEL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 83 ggdgR----------------DSRTVQD---LLLSVAPVRVKEAAERLNgaEL----AMMEREDektqmRYaqaitdytd 139
Cdd:cd03258 78 ----RkarrrigmifqhfnllSSRTVFEnvaLPLEIAGVPKAEIEERVL--ELlelvGLEDKAD-----AY--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 140 aggydievlwdtctmaalgaPydnvkyrdlTTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETS 218
Cdd:cd03258 138 --------------------P---------AQLSGGQKQRVGIaRALANNPK-VLLCDEATSALDPETTQSILALLRDIN 187
|
250 260 270
....*....|....*....|....*....|..
gi 2796936914 219 K----TVLLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:cd03258 188 RelglTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-250 |
6.85e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 50.78 E-value: 6.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIagDLQPIEGSvthagglgvmrqfiGSLRGAGESSPGGDGRDSRTVQDLL 96
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVL--NLLETPDS--------------GQLNIAGHQFDFSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 97 ---------------LSV------APVRV----KEAAerlngaelamMEREDEK-TQMRyaqaITDYTDAggydievlWd 150
Cdd:COG4161 82 qkvgmvfqqynlwphLTVmenlieAPCKVlglsKEQA----------REKAMKLlARLR----LTDKADR--------F- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 151 tctmaalgaPydnvkyrdlTTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDvPG------KIWLEqaLRETSKTVLL 223
Cdd:COG4161 139 ---------P---------LHLSGGQQQRVAIaRALMMEP-QVLLFDEPTAALD-PEitaqvvEIIRE--LSQTGITQVI 196
|
250 260
....*....|....*....|....*..
gi 2796936914 224 VSHDRQLLANAVDRIVTVESGNVWIHG 250
Cdd:COG4161 197 VTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-250 |
7.64e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 50.40 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmRQFIGSlrgageSSPG-GDGRDSR----- 90
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAG-----NHFDFS------KTPSdKAIRELRrnvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 -----------TVQDLLLSvAPVRV----KEAAerlngaelamMEREDEK-TQMRyaqaITDYTDAggYDIEvlwdtctm 154
Cdd:PRK11124 87 vfqqynlwphlTVQQNLIE-APCRVlglsKDQA----------LARAEKLlERLR----LKPYADR--FPLH-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 155 aalgapydnvkyrdlttLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDvPG------KIWLEqaLRETSKTVLLVSHD 227
Cdd:PRK11124 142 -----------------LSGGQQQRVAIaRALMMEP-QVLLFDEPTAALD-PEitaqivSIIRE--LAETGITQVIVTHE 200
|
250 260
....*....|....*....|...
gi 2796936914 228 RQLLANAVDRIVTVESGNVWIHG 250
Cdd:PRK11124 201 VEVARKTASRVVYMENGHIVEQG 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
304-528 |
9.01e-07 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 51.58 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 304 AAQTRLRRFEEAGPPELAPkdqlisMRL---RGGRTAKRAVICENLELSGLMKPFDLEIWYGERVAVLGSNGSGKSHFLR 380
Cdd:TIGR01842 289 QAYKRLNELLANYPSRDPA------MPLpepEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLAR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 381 LIAGEEVRHTGVARL----------------------GARVVPGHFAQTHARpellgrtpceivMTEHArlknEAMKALA 438
Cdd:TIGR01842 363 LIVGIWPPTSGSVRLdgadlkqwdretfgkhigylpqDVELFPGTVAENIAR------------FGENA----DPEKIIE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 439 RYELAGgVAE--QRF------------ETLSGGQQARLQiLLLEMSGA-TLLLLDEPTDNLD----LASAEALQAgLDAF 499
Cdd:TIGR01842 427 AAKLAG-VHEliLRLpdgydtvigpggATLSGGQRQRIA-LARALYGDpKLVVLDEPNSNLDeegeQALANAIKA-LKAR 503
|
250 260
....*....|....*....|....*....
gi 2796936914 500 DGTVLAVTHDRWFAADFDRYMVFgTDGRV 528
Cdd:TIGR01842 504 GITVVVITHRPSLLGCVDKILVL-QDGRI 531
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
11-246 |
1.04e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 49.72 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLrgagessPGGDGRDSR 90
Cdd:cd03369 18 PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG------IDISTI-------PLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TV--QDLLLSVAPVRVKeaaerlngaelamMEREDEktqmryaqaitdYTDAggyDIevlwdtctMAALgapydNVKYRD 168
Cdd:cd03369 85 TIipQDPTLFSGTIRSN-------------LDPFDE------------YSDE---EI--------YGAL-----RVSEGG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 169 LtTLSGGEQKRLAL-EALLRGPdQTLLLDEPDNYLDVPGKIWLEQALRE--TSKTVLLVSHDRQLLANaVDRIVTVESGN 245
Cdd:cd03369 124 L-NLSQGQRQLLCLaRALLKRP-RVLVLDEATASIDYATDALIQKTIREefTNSTILTIAHRLRTIID-YDKILVMDAGE 200
|
.
gi 2796936914 246 V 246
Cdd:cd03369 201 V 201
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-62 |
1.08e-06 |
|
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: 49.16 E-value: 1.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAG--DLQPIEGSVTHAG 62
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILING 70
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
346-509 |
1.15e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.08 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF--------------DLEIWYGERVAVLGSNGSGKSHFLRLIAGE--------EVRHTGVARLgarvvpgh 403
Cdd:COG1101 2 LELKNLSKTFnpgtvnekraldglNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSlppdsgsiLIDGKDVTKL-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 404 faQTHARPELLGRtpceiV-----------MT------------EHARLK---NEAMKALARYELAG---GVaEQRFET- 453
Cdd:COG1101 74 --PEYKRAKYIGR-----VfqdpmmgtapsMTieenlalayrrgKRRGLRrglTKKRRELFRELLATlglGL-ENRLDTk 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796936914 454 ---LSGGQ-QArLQILLLEMSGATLLLLDEPTDNLDLASAEAL---------QAGLdafdgTVLAVTHD 509
Cdd:COG1101 146 vglLSGGQrQA-LSLLMATLTKPKLLLLDEHTAALDPKTAALVleltekiveENNL-----TTLMVTHN 208
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-250 |
1.40e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.13 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV------THAGGLGVMRQFIGSLRGAGESSPGGDgrdsr 90
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRKHIGIVFQNPDNQFVGS----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TVQdllLSVApvrvkeaaerlNGAELAMMERedEKTQMRYAQAITDytdaggydievlwdtctmaalgapYDNVKYRDL- 169
Cdd:PRK13648 100 IVK---YDVA-----------FGLENHAVPY--DEMHRRVSEALKQ------------------------VDMLERADYe 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 170 -TTLSGGEQKRLALEALLR-GPDqTLLLDEPDNYLDVPGK---IWLEQALRETSK-TVLLVSHDrqlLANAV--DRIVTV 241
Cdd:PRK13648 140 pNALSGGQKQRVAIAGVLAlNPS-VIILDEATSMLDPDARqnlLDLVRKVKSEHNiTIISITHD---LSEAMeaDHVIVM 215
|
....*....
gi 2796936914 242 ESGNVWIHG 250
Cdd:PRK13648 216 NKGTVYKEG 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
352-528 |
1.68e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.73 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 352 MKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGH--------------------FAQTHAR- 410
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEnekwvrskvglvfqdpddqvFSSTVWDd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 411 ----PELLGRTPCEIvmtehARLKNEAMKALARYELAggvaEQRFETLSGGQQARLQIL-LLEMSgATLLLLDEPTDNLD 485
Cdd:PRK13647 101 vafgPVNMGLDKDEV-----ERRVEEALKAVRMWDFR----DKPPYHLSYGQKKRVAIAgVLAMD-PDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2796936914 486 LASAEALQAGLDAFDG---TVLAVTHDRWFAADFDRYMVFGTDGRV 528
Cdd:PRK13647 171 PRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-257 |
1.81e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.70 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQ--VSRLTHVLPDGRPL----LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrQFIGSl 74
Cdd:PRK13651 1 MQikVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI----------EWIFK- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 75 rgaGESSPGGDGRDSRTVQDLLLSVAPVR----VKEAAERL----NGAELAMMEREDEK-----------TQMRYAQAIT 135
Cdd:PRK13651 70 ---DEKNKKKTKEKEKVLEKLVIQKTRFKkikkIKEIRRRVgvvfQFAEYQLFEQTIEKdiifgpvsmgvSKEEAKKRAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 136 DYTDAGGYDIEVLWDTctmaalgaPYDnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKI-WLE--Q 212
Cdd:PRK13651 147 KYIELVGLDESYLQRS--------PFE---------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeILEifD 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2796936914 213 ALRETSKTVLLVSHDrqlLANAVD---RIVTVESGNVwIHGGGfaTYS 257
Cdd:PRK13651 210 NLNKQGKTIILVTHD---LDNVLEwtkRTIFFKDGKI-IKDGD--TYD 251
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
351-531 |
1.84e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.31 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 351 LMKPFDLEIWYGERVAVLGSNGSGKShfLRLIAGEEVRHTGVARLGARVVPGhfAQTHARPELLGRTPCEIV-------- 422
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLD--GKPVAPCALRGRKIATIMqnprsafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 423 ----MTEHARlknEAMKALARYEL---------AGGVAEQR-------FEtLSGGQQARLQILLLEMSGATLLLLDEPTD 482
Cdd:PRK10418 94 plhtMHTHAR---ETCLALGKPADdatltaaleAVGLENAArvlklypFE-MSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2796936914 483 NLDL-ASAEALQ--AGLDAFDGT-VLAVTHDRWFAADFDRYMVFGTDGRVYES 531
Cdd:PRK10418 170 DLDVvAQARILDllESIVQKRALgMLLVTHDMGVVARLADDVAVMSHGRIVEQ 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-246 |
1.90e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 50.79 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAG--DLQpiEGSVTHagglgvmrqfigslrgagesspggDGRDSR-- 90
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfyDID--EGEILL------------------------DGHDLRdy 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TVQDLLLSVAPVRVK------EAAERLNGAELAMMERED--EKTQMRYAQAITDYTDAGgydievlwdtctmaalgapYD 162
Cdd:PRK11176 411 TLASLRNQVALVSQNvhlfndTIANNIAYARTEQYSREQieEAARMAYAMDFINKMDNG-------------------LD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 163 NVKYRDLTTLSGGEQKRLAL-EALLR-GPdqTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSHDRQLLANAvDRI 238
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIaRALLRdSP--ILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEKA-DEI 548
|
....*...
gi 2796936914 239 VTVESGNV 246
Cdd:PRK11176 549 LVVEDGEI 556
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-62 |
1.98e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 1.98e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG 62
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG 65
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-58 |
2.03e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.22 E-value: 2.03e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV 58
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI 76
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
302-508 |
2.12e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.58 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 302 YHAAQTRLRRFEEAgppeLAPKDQLISMRLRGGRTAKRAVICENLELSG-----LMKPFDLEIWYGERVAVLGSNGSGKS 376
Cdd:COG4178 328 WRATVDRLAGFEEA----LEAADALPEAASRIETSEDGALALEDLTLRTpdgrpLLEDLSLSLKPGERLLITGPSGSGKS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 377 HFLRLIAGEEVRHTGVARL--GARV--VPghfaQthaRPEL-LGR---------TPCEIvmtEHARLKnEAMKALARYEL 442
Cdd:COG4178 404 TLLRAIAGLWPYGSGRIARpaGARVlfLP----Q---RPYLpLGTlreallypaTAEAF---SDAELR-EALEAVGLGHL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796936914 443 AGGVAEQR--FETLSGGQQARLQI--LLLemSGATLLLLDEPTDNLDLASAEALQAGLDA--FDGTVLAVTH 508
Cdd:COG4178 473 AERLDEEAdwDQVLSLGEQQRLAFarLLL--HKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH 542
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
356-543 |
2.18e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 49.73 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHARP-----ELLGRTPcEIVMTEHARLK 430
Cdd:PRK13643 26 DLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPvrkkvGVVFQFP-ESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 431 N-------------EAMKALARYELAGGVAEQRFET----LSGGQQARLQILLLEMSGATLLLLDEPTDNLD-LASAEAL 492
Cdd:PRK13643 105 DvafgpqnfgipkeKAEKIAAEKLEMVGLADEFWEKspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpKARIEMM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 493 Q--AGLDAFDGTVLAVTHDRWFAADFDRYMVFGTDGRVYE--SPEPVWDETRVVR 543
Cdd:PRK13643 185 QlfESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIScgTPSDVFQEVDFLK 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-266 |
2.29e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.14 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 16 LLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAG--DLQP---IEGSVtHAGGLGVMRQFIGSLRgagesspggdgrdsR 90
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEV-YLDGQDIFKMDVIELR--------------R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TVQDLLLSVAPVRVKEAAERLN-GAELAMMEREDEKTQMRYAQAITDYTdaggydievLWDTcTMAALGAPydnvkyrdL 169
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVAlGLKLNRLVKSKKELQERVRWALEKAQ---------LWDE-VKDRLDAP--------A 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 170 TTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSHDRQLLANAVDRIVTVESGNVW 247
Cdd:PRK14247 145 GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
250
....*....|....*....
gi 2796936914 248 IHGGGFATYSEARKDRNER 266
Cdd:PRK14247 225 EWGPTREVFTNPRHELTEK 243
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
356-518 |
2.30e-06 |
|
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: 48.62 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGeEVRHTGvarlGARVVPGHFA---QTharPELLGRTPCE-IVMTE---HAR 428
Cdd:cd03250 25 NLEVPKGELVAIVGPVGSGKSSLLSALLG-ELEKLS----GSVSVPGSIAyvsQE---PWIQNGTIREnILFGKpfdEER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 429 LKnEAMKALARYE----LAGG----VAEqRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEAL--QA--GL 496
Cdd:cd03250 97 YE-KVIKACALEPdleiLPDGdlteIGE-KGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfeNCilGL 174
|
170 180
....*....|....*....|..
gi 2796936914 497 DAFDGTVLAVTHDRWFAADFDR 518
Cdd:cd03250 175 LLNNKTRILVTHQLQLLPHADQ 196
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
353-531 |
2.57e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 48.93 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFL----RL---------IAGEEVRHTGVARLgARVVP-----GHFAqthAR---P 411
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLsmisRLlppdsgevlVDGLDVATTPSREL-AKRLAilrqeNHIN---SRltvR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 412 ELL--GRTPceivmteHA--RLKNE--AM--KALARYELaGGVAEQRFETLSGGQQARLQIlllEMsgaTL------LLL 477
Cdd:COG4604 94 ELVafGRFP-------YSkgRLTAEdrEIidEAIAYLDL-EDLADRYLDELSGGQRQRAFI---AM---VLaqdtdyVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 478 DEPTDNLDLASAEALQAGL----DAFDGTVLAVTHDRWFAADFDRYMVFGTDGRVYES 531
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLrrlaDELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
356-509 |
2.58e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 49.30 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAG-EEVRHTGVARLGARVVPGHFAQTHA-RPEL-------LG-----RTPCEI 421
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGlESPSQGNVSWRGEPLAKLNRAQRKAfRRDIqmvfqdsISavnprKTVREI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 422 V---MTEHARLKNEAMKALAR-----YELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDL---ASAE 490
Cdd:PRK10419 112 IrepLRHLLSLDKAERLARASemlraVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqAGVI 191
|
170 180
....*....|....*....|
gi 2796936914 491 ALQAGLDAFDGTV-LAVTHD 509
Cdd:PRK10419 192 RLLKKLQQQFGTAcLFITHD 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-59 |
2.68e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 49.69 E-value: 2.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGdLQ-PIEGSVT 59
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LErPTSGSVL 63
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-250 |
2.68e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.40 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG-----GLGVMRQFIGslrgageSSPGGD 85
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietNLDAVRQSLG-------MCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 86 GR-DSRTVQDLLLSVAPVRVKEAAErlngAELAmMEREDEKTQMRYAQaitdytdaggydievlwdtctmaalgapydNV 164
Cdd:TIGR01257 1013 ILfHHLTVAEHILFYAQLKGRSWEE----AQLE-MEAMLEDTGLHHKR------------------------------NE 1057
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 165 KYRDlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGK--IWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVE 242
Cdd:TIGR01257 1058 EAQD---LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRrsIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
....*...
gi 2796936914 243 SGNVWIHG 250
Cdd:TIGR01257 1135 QGRLYCSG 1142
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
13-59 |
2.83e-06 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 48.81 E-value: 2.83e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVT 59
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIL 59
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-58 |
2.85e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 2.85e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV 58
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEI 62
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-58 |
3.03e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.99 E-value: 3.03e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV 58
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
171-246 |
3.19e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 171 TLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGK----IWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGN 245
Cdd:PRK11144 128 SLSGGEKQRVAIgRALLTAPE-LLLMDEPLASLDLPRKrellPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
.
gi 2796936914 246 V 246
Cdd:PRK11144 207 V 207
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-251 |
3.32e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.63 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLRGAGESspggdgrdsRTV 92
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA------QPLESWSSKAFA---------RKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 QDLllsvaPVRVKeAAERLNGAELAMMEREDEKTQM-RYAQAitdytdaggyDIEVLWDTCTMAALgAPYDNvkyRDLTT 171
Cdd:PRK10575 88 AYL-----PQQLP-AAEGMTVRELVAIGRYPWHGALgRFGAA----------DREKVEEAISLVGL-KPLAH---RLVDS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKI----WLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGNVW 247
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVdvlaLVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
....
gi 2796936914 248 IHGG 251
Cdd:PRK10575 228 AQGT 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
355-508 |
3.35e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.78 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLEIWYGERVAVLGSNGSGKSHFLRLIA-------------GEEVRHTGVARLGARV--VPGH---FAQT------HAR 410
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsgrilidGVDIRDLTLESLRRQIgvVPQDtflFSGTirenirYGR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 411 PEllgRTPCEIVmteharlknEAMKALARYE----LAGG---VAEQRFETLSGGQQARLQI---LLLEmsgATLLLLDEP 480
Cdd:COG1132 439 PD---ATDEEVE---------EAAKAAQAHEfieaLPDGydtVVGERGVNLSGGQRQRIAIaraLLKD---PPILILDEA 503
|
170 180 190
....*....|....*....|....*....|
gi 2796936914 481 TDNLDLASAEALQAGLDAF--DGTVLAVTH 508
Cdd:COG1132 504 TSALDTETEALIQEALERLmkGRTTIVIAH 533
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
351-534 |
3.38e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.81 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 351 LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLI-------------AGEEVR---------------HTGVARLGARVVPG 402
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsegsivvNGQTINlvrdkdgqlkvadknQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 403 HF-AQTHARP-ELLGRTPCEIVMTEHARLKNEAMKALARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEP 480
Cdd:PRK10619 100 HFnLWSHMTVlENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 481 TDNLD---LASAEALQAGLDAFDGTVLAVTHDRWFAADFDRYMVFGTDGRVYESPEP 534
Cdd:PRK10619 180 TSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-62 |
3.67e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 48.03 E-value: 3.67e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 2 QVSRLTHVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQP---IEGSVTHAG 62
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNG 71
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
367-538 |
4.04e-06 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 49.03 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 367 VLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpghfaqTHARPELLG--------------------RTPCEIVMTEH 426
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV------TNVPPHLRHinmvfqsyalfphmtveenvAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 427 ARLKNEAMKALARYELaGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFDG----T 502
Cdd:TIGR01187 75 AEIKPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEqlgiT 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 2796936914 503 VLAVTHDRWFAADFDRYMVFGTDGRVYE--SPEPVWDE 538
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQigTPEEIYEE 191
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-250 |
4.20e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.59 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgVMRQFIGSlrgageSSPGGDGRDSR 90
Cdd:PRK13649 17 PFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVR------VDDTLITS------TSKNKDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 TVQDLLLSVAPVRV-------------------KEAAERLNGAELAMMEREDEktqmryaqaitdytdaggydievLWDT 151
Cdd:PRK13649 85 KKVGLVFQFPESQLfeetvlkdvafgpqnfgvsQEEAEALAREKLALVGISES-----------------------LFEK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 152 ctmaalgAPYDnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGK---IWLEQALRETSKTVLLVSHDR 228
Cdd:PRK13649 142 -------NPFE---------LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRkelMTLFKKLHQSGMTIVLVTHLM 205
|
250 260
....*....|....*....|..
gi 2796936914 229 QLLANAVDRIVTVESGNVWIHG 250
Cdd:PRK13649 206 DDVANYADFVYVLEKGKLVLSG 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-203 |
4.56e-06 |
|
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: 48.04 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 16 LLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQP---IEGSVTHAG---GLGVMRQFIGSLRGAGESSPGgdgrds 89
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGqprKPDQFQKCVAYVRQDDILLPG------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 90 RTVQDLLLSVAPVRVKeaaERLNGAELAMMereDEKTQMRYAqAITDytdaggydievlwdtctmaaLGAPYdnvkyrdL 169
Cdd:cd03234 96 LTVRETLTYTAILRLP---RKSSDAIRKKR---VEDVLLRDL-ALTR--------------------IGGNL-------V 141
|
170 180 190
....*....|....*....|....*....|....*
gi 2796936914 170 TTLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLD 203
Cdd:cd03234 142 KGISGGERRRVSIaVQLLWDPK-VLILDEPTSGLD 175
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
345-509 |
4.76e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.01 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 345 NLELSGLMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAG---------------EEVRHTGVARLGA------RVVPG- 402
Cdd:PRK03695 5 DVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGllpgsgsiqfagqplEAWSAAELARHRAylsqqqTPPFAm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 403 ---HFAQTHaRPELLGRTPCEIVMTEHARLKNEAMKaLARyelaggvaeqRFETLSGG--QQARLQILLLEMS-----GA 472
Cdd:PRK03695 85 pvfQYLTLH-QPDKTRTEAVASALNEVAEALGLDDK-LGR----------SVNQLSGGewQRVRLAAVVLQVWpdinpAG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2796936914 473 TLLLLDEPTDNLDLASAEALQAGLDAF---DGTVLAVTHD 509
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHD 192
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
354-486 |
5.27e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 354 PFDLEIWYGERVAVLGSNGSGKSHFLRLIAGeeVRHTGVARLGarvVPGHFAQTHARPEL---LGRTP-----------C 419
Cdd:PRK13543 29 PLDFHVDAGEALLVQGDNGAGKTTLLRVLAG--LLHVESGQIQ---IDGKTATRGDRSRFmayLGHLPglkadlstlenL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 420 EIVMTEHA-RLKNEAMKALARYELAGgVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDL 486
Cdd:PRK13543 104 HFLCGLHGrRAKQMPGSALAIVGLAG-YEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-67 |
5.73e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 5.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVM 67
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI 90
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
362-529 |
5.83e-06 |
|
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: 46.21 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVRHTGvarlgarvvpghfaqtharpellgrtPCEIVMTEHARlkneamkALARYE 441
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGG--------------------------GVIYIDGEDIL-------EEVLDQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 442 LAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF---------DGTVLAVTHDRWF 512
Cdd:smart00382 49 LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRlllllksekNLTVILTTNDEKD 128
|
170
....*....|....*..
gi 2796936914 513 AadFDRYMVFGTDGRVY 529
Cdd:smart00382 129 L--GPALLRRRFDRRIV 143
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
355-530 |
6.79e-06 |
|
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: 47.61 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLEIWYGERVAVLGSNGSGKSHFLRLIA-------------GEEVRHTGVARLGARVvpGHFAQ-------------TH 408
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPrfydvdsgrilidGHDVRDYTLASLRRQI--GLVSQdvflfndtvaeniAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 409 ARPellGRTPCEIVmtEHARLKNeAMKALARYELA-GGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLA 487
Cdd:cd03251 99 GRP---GATREEVE--EAARAAN-AHEFIMELPEGyDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2796936914 488 SAEALQAGLDAF--DGTVLAVTHDRWFAADFDRYMVFgTDGRVYE 530
Cdd:cd03251 173 SERLVQAALERLmkNRTTFVIAHRLSTIENADRIVVL-EDGKIVE 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
369-519 |
6.99e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.87 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 369 GSNGSGKSHFLRLIAG-------------EEVRHTGVARLGARVVPGHfaQTHARPELLGRTPCeiVMTEHARLKNEAMK 435
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGllnpekgeilferQSIKKDLCTYQKQLCFVGH--RSGINPYLTLRENC--LYDIHFSPGAVGIT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 436 ALARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF---DGTVLAVTHDRWF 512
Cdd:PRK13540 110 ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHrakGGAVLLTSHQDLP 189
|
....*....
gi 2796936914 513 --AADFDRY 519
Cdd:PRK13540 190 lnKADYEEY 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-98 |
7.06e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDlqpiegsvtHAGGLGVMRQFIGSLRGAGE-------------S 80
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD---------HPQGYSNDLTLFGRRRGSGEtiwdikkhigyvsS 343
|
90
....*....|....*...
gi 2796936914 81 SPGGDGRDSRTVQDLLLS 98
Cdd:PRK10938 344 SLHLDYRVSTSVRNVILS 361
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
170-266 |
7.19e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.73 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 170 TTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSHDRQLLANAVDRIVTVESGNVW 247
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
90
....*....|....*....
gi 2796936914 248 IHGGGFATYSEARKDRNER 266
Cdd:PRK14246 232 EWGSSNEIFTSPKNELTEK 250
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
362-508 |
1.05e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.18 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKS-------HFLR------LIAGEEVR-------HTGVARLGARVVPGHFAQTHARPELLGRTPCEI 421
Cdd:TIGR00958 507 GEVVALVGPSGSGKStvaallqNLYQptggqvLLDGVPLVqydhhylHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEE 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 422 VMteharlkNEAMKALAR---YELAGGVAEQRFET---LSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAG 495
Cdd:TIGR00958 587 IM-------AAAKAANAHdfiMEFPNGYDTEVGEKgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES 659
|
170
....*....|...
gi 2796936914 496 LDAFDGTVLAVTH 508
Cdd:TIGR00958 660 RSRASRTVLLIAH 672
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-246 |
1.14e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.72 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 18 NDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGdLQPIEgsvthAGGLgvmrqFIGSLRgAGESSPGGdgrdsRTVQDLLL 97
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG-LEDIT-----SGDL-----FIGEKR-MNDVPPAE-----RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 98 SVAPVRVKEAAERLN-GAELAMMEREDekTQMRYAQAitdytdaggydIEVLwdtctmaALGAPYDnvkyRDLTTLSGGE 176
Cdd:PRK11000 83 SYALYPHLSVAENMSfGLKLAGAKKEE--INQRVNQV-----------AEVL-------QLAHLLD----RKPKALSGGQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 177 QKRLAL-EALLRGPDqTLLLDEP----DNYLDVPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESGNV 246
Cdd:PRK11000 139 RQRVAIgRTLVAEPS-VFLLDEPlsnlDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-244 |
1.18e-05 |
|
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: 46.37 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThAGGLGVmrqfigslrgagesspGGDGRDSRTV---- 92
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTII-IDGLKL----------------TDDKKNINELrqkv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 ----QDLLL----------SVAPVRVKeaaerlngaelAMMEREDEKTQMRYAQ--AITDYTDAggYDIEvlwdtctmaa 156
Cdd:cd03262 79 gmvfQQFNLfphltvleniTLAPIKVK-----------GMSKAEAEERALELLEkvGLADKADA--YPAQ---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 lgapydnvkyrdlttLSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLD---VPGKIWLEQALRETSKTVLLVSHDRQLLA 232
Cdd:cd03262 136 ---------------LSGGQQQRVAIaRALAMNPK-VMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAR 199
|
250
....*....|..
gi 2796936914 233 NAVDRIVTVESG 244
Cdd:cd03262 200 EVADRVIFMDDG 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
353-487 |
1.24e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.72 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLG-ARV--VP------GHFAQTHA-RPEL-------LG 415
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGeKRMndVPpaergvGMVFQSYAlYPHLsvaenmsFG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796936914 416 RTPCEIVMTEHARLKNEAMKALaryELAgGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLA 487
Cdd:PRK11000 100 LKLAGAKKEEINQRVNQVAEVL---QLA-HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
356-510 |
1.30e-05 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 46.47 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHfaQTHARPEL--------------LGRTPCE- 420
Cdd:TIGR02673 22 SLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRL--RGRQLPLLrrrigvvfqdfrllPDRTVYEn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 421 IVMTEHARLKNEA-----MKALARYElagGVAEQRF---ETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEAL 492
Cdd:TIGR02673 100 VALPLEVRGKKEReiqrrVGAALRQV---GLEHKADafpEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERI 176
|
170 180
....*....|....*....|.
gi 2796936914 493 QAGLDAFDG---TVLAVTHDR 510
Cdd:TIGR02673 177 LDLLKRLNKrgtTVIVATHDL 197
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
353-509 |
1.61e-05 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 46.99 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAG-EEVRHtGVARLGARVVpghfaqTHARPE------------------- 412
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPTS-GEILIGGRDV------TDLPPKdrniamvfqsyalyphmtv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 413 ---------LLGRTPCEIvmteHARLKnEAMKALaryELaGGVAEQRFETLSGGQQARLQI---LLLEmsgATLLLLDEP 480
Cdd:COG3839 93 yeniafplkLRKVPKAEI----DRRVR-EAAELL---GL-EDLLDRKPKQLSGGQRQRVALgraLVRE---PKVFLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 2796936914 481 TDNLDLAS-----AE--ALQAGLDAfdgTVLAVTHD 509
Cdd:COG3839 161 LSNLDAKLrvemrAEikRLHRRLGT---TTIYVTHD 193
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-251 |
2.16e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 46.02 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLRgagesspggdgrdSRTV 92
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG------HDITRLK-------------NREV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 qdlllsvaPVRVKEAAERLNGAELAMMEREDEKTQMRYAQAitdytDAGGYDIEvlwdtctmAALGAPYDNVKYRDLT-- 170
Cdd:PRK10908 75 --------PFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIA-----GASGDDIR--------RRVSAALDKVGLLDKAkn 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 171 ---TLSGGEQKRLALEALLRGPDQTLLLDEPDNYLD---VPGKIWLEQALRETSKTVLLVSHDRQLLANAVDRIVTVESG 244
Cdd:PRK10908 134 fpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
....*..
gi 2796936914 245 NvwIHGG 251
Cdd:PRK10908 214 H--LHGG 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
356-481 |
2.16e-05 |
|
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: 46.13 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGhfAQTHAR--------PEllGR------TPCE- 420
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG--LPPHRIarlgigyvPE--GRrifpslTVEEn 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796936914 421 IVMTEHARLKNEAMKA-LAR-YEL-----------AGgvaeqrfeTLSGGQQarlQIL-----LleMSGATLLLLDEPT 481
Cdd:COG0410 99 LLLGAYARRDRAEVRAdLERvYELfprlkerrrqrAG--------TLSGGEQ---QMLaigraL--MSRPKLLLLDEPS 164
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
355-531 |
2.20e-05 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 47.02 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLEIWYGERVAVLGSNGSGKSHFLRLIA-------------GEEVRHTGVARLGArvvpgHFAQtharpellgrtpcei 421
Cdd:TIGR02203 351 ISLVIEPGETVALVGRSGSGKSTLVNLIPrfyepdsgqilldGHDLADYTLASLRR-----QVAL--------------- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 422 vMTEHARLKNEAMKALARYELAGGVAEQRFET----------------------------LSGGQQARLQILLLEMSGAT 473
Cdd:TIGR02203 411 -VSQDVVLFNDTIANNIAYGRTEQADRAEIERalaaayaqdfvdklplgldtpigengvlLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 474 LLLLDEPTDNLDLASAEALQAGLDAF--DGTVLAVTHDRWFAADFDRYMVFgTDGRVYES 531
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVM-DDGRIVER 548
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-545 |
2.21e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.06 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 351 LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAG-----EEVRHTGVARL-GARVVPGHFAQTHARPELLGRTPCEI--- 421
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLdGQDIFKMDVIELRRRVQMVFQIPNPIpnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 422 --------------VMTEHARLKNEAMKALARYELAGGVaEQRFET----LSGGQQARLQILLLEMSGATLLLLDEPTDN 483
Cdd:PRK14247 98 sifenvalglklnrLVKSKKELQERVRWALEKAQLWDEV-KDRLDApagkLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 484 LD---LASAEALQAGLDAfDGTVLAVTHDRWFAADFDRYMVFGTDGRVYEspepvWDETRVV--RPR 545
Cdd:PRK14247 177 LDpenTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVE-----WGPTREVftNPR 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-530 |
2.33e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 366 AVLGSNGSGKSHFLRLI--AGEEV---RHTGVARLGARVVPGH--FAQTHARPELLGRTPCEIVMT--EHARLKNEAMKA 436
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLnrMNDKVsgyRYSGDVLLGGRSIFNYrdVLEFRRRVGMLFQRPNPFPMSimDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 437 LARYELAGgVAEQRFET-----------------LSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF 499
Cdd:PRK14271 131 VPRKEFRG-VAQARLTEvglwdavkdrlsdspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL 209
|
170 180 190
....*....|....*....|....*....|....
gi 2796936914 500 DG--TVLAVTHDRWFAADF-DRYMVFgTDGRVYE 530
Cdd:PRK14271 210 ADrlTVIIVTHNLAQAARIsDRAALF-FDGRLVE 242
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-206 |
2.36e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.61 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 12 DGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV---THAGGLGVMRQFIGSLrgageSSPGGDGRD 88
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidGKTATRGDRSRFMAYL-----GHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 89 SRTVQDL--LLSVAPVRvkeaAERLNGAELAMMeredektqmryaqAITDYTDAggydievlwdtctmaalgapydnvky 166
Cdd:PRK13543 97 LSTLENLhfLCGLHGRR----AKQMPGSALAIV-------------GLAGYEDT-------------------------- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2796936914 167 rDLTTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPG 206
Cdd:PRK13543 134 -LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
354-515 |
2.36e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.10 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 354 PFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGH------------FAQTHARPELLGRtpcei 421
Cdd:COG4615 350 PIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADnreayrqlfsavFSDFHLFDRLLGL----- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 422 vmtEHARLKNEAMKALARYELAGGVAEQ--RFET--LSGGQQARLQIL--LLEmsGATLLLLDE---------------- 479
Cdd:COG4615 425 ---DGEADPARARELLERLELDHKVSVEdgRFSTtdLSQGQRKRLALLvaLLE--DRPILVFDEwaadqdpefrrvfyte 499
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2796936914 480 --PtdnldlasaeALQA-GLdafdgTVLAVTHD-RWF-AAD 515
Cdd:COG4615 500 llP----------ELKArGK-----TVIAISHDdRYFdLAD 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
165-245 |
2.44e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 165 KYRDLTTLSGGEQK------RLALEALLRGPDQTLLLDEPDNYLDVPGKIWL----EQALRETSKtVLLVSHDRQlLANA 234
Cdd:PRK03918 782 KERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLvdimERYLRKIPQ-VIIVSHDEE-LKDA 859
|
90
....*....|.
gi 2796936914 235 VDRIVTVESGN 245
Cdd:PRK03918 860 ADYVIRVSLEG 870
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-62 |
2.54e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.73 E-value: 2.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2796936914 21 SFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG 62
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG 60
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
16-244 |
3.08e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 45.95 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 16 LLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEgsvthagglgvmrqfiGSLRGAGESSPGGDGRDSRTVqdl 95
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA----------------GSISLCGEPVPSRARHARQRV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 96 llSVAPvrvkeaaeRLNGAELAMMEREDEKTQMRY----AQAITdytdaggydiEVLWDTCTMAALGAPYDnVKYRDltt 171
Cdd:PRK13537 83 --GVVP--------QFDNLDPDFTVRENLLVFGRYfglsAAAAR----------ALVPPLLEFAKLENKAD-AKVGE--- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 172 LSGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGK--IWLE-QALRETSKTVLLVSHDRQLLANAVDRIVTVESG 244
Cdd:PRK13537 139 LSGGMKRRLTLaRALVNDPD-VLVLDEPTTGLDPQARhlMWERlRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
356-384 |
3.12e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.46 E-value: 3.12e-05
10 20
....*....|....*....|....*....
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAG 384
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAG 74
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
356-528 |
3.25e-05 |
|
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: 45.40 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVvPGHfaqthARPELLGRTpcEIVMTEHARL-----K 430
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-PWK-----RRKKFLRRI--GVVFGQKTQLwwdlpV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 431 NEAMKALAR-YELAGGVAEQRFE-----------------TLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEAL 492
Cdd:cd03267 113 IDSFYLLAAiYDLPPARFKKRLDelselldleelldtpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2796936914 493 QAGLDAF----DGTVLAVTHD-RWFAADFDRYMVFGTdGRV 528
Cdd:cd03267 193 RNFLKEYnrerGTTVLLTSHYmKDIEALARRVLVIDK-GRL 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
355-384 |
3.43e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.34 E-value: 3.43e-05
10 20 30
....*....|....*....|....*....|
gi 2796936914 355 FDLEIWYGERVAVLGSNGSGKSHFLRLIAG 384
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAG 47
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
341-508 |
3.48e-05 |
|
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: 44.45 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 341 VICENLELSG-----LMKPFDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGvarlgarvvpghfaqtharpellg 415
Cdd:cd03223 1 IELENLSLATpdgrvLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 416 rtpcEIVMTEHARLkneAMKALARYELAGGVAEQRF----ETLSGGQQARLQI--LLLemSGATLLLLDEPTDNLDLASA 489
Cdd:cd03223 57 ----RIGMPEGEDL---LFLPQRPYLPLGTLREQLIypwdDVLSGGEQQRLAFarLLL--HKPKFVFLDEATSALDEESE 127
|
170
....*....|....*....
gi 2796936914 490 EALQAGLDAFDGTVLAVTH 508
Cdd:cd03223 128 DRLYQLLKELGITVISVGH 146
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
454-508 |
4.30e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.17 E-value: 4.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 454 LSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF--DGTVLAVTH 508
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAH 537
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
357-509 |
4.52e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.10 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 357 LEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHARPELLGRTPCEIVMTEHARLKNEAMKA 436
Cdd:PRK09544 25 LELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 437 LARYElAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLD----AFDGTVLAVTHD 509
Cdd:PRK09544 105 LKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDqlrrELDCAVLMVSHD 180
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
9-230 |
4.62e-05 |
|
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: 46.28 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 9 VLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGdLQPIEGsvthagglgvmrqfigslrgagesspggdGRD 88
Cdd:TIGR00954 460 VTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYG-----------------------------GRL 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 89 SRTVQDLLLSVaPVRvkeaaerlngaelAMMEREDEKTQMRYAQAITDYTDAGGYDievlwdtctmAALGAPYDNVKYRD 168
Cdd:TIGR00954 510 TKPAKGKLFYV-PQR-------------PYMTLGTLRDQIIYPDSSEDMKRRGLSD----------KDLEQILDNVQLTH 565
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 169 LTT--------------LSGGEQKRLALEALLRGPDQTLLLDEPDNYL--DVPGKIWleQALRETSKTVLLVSHDRQL 230
Cdd:TIGR00954 566 ILEreggwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVsvDVEGYMY--RLCREFGITLFSVSHRKSL 641
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-58 |
4.87e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 4.87e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV 58
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-202 |
4.88e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 45.37 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLThvLPDGRPLLN-DVSFRIGEGTKAaLVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQ---------- 69
Cdd:COG3950 1 MRIKSLT--IENFRGFEDlEIDFDNPPRLTV-LVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRngefgdsakl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 70 --FIGSLRGAGESSPGGDGRDSRTVQDLLLSV-----APVRVKEAAERLNGAELAMMEREDEKTQMRYA---QAITDYTD 139
Cdd:COG3950 78 ilYYGTSRLLLDGPLKKLERLKEEYFSRLDGYdslldEDSNLREFLEWLREYLEDLENKLSDELDEKLEavrEALNKLLP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 140 aGGYDIEVLWDTCTMAALGAPYDNVkyrDLTTLSGGEQKRLAL---------------EALLRGPdQTLLLDEPDNYL 202
Cdd:COG3950 158 -DFKDIRIDRDPGRLVILDKNGEEL---PLNQLSDGERSLLALvgdlarrlaelnpalENPLEGE-GIVLIDEIDLHL 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-237 |
5.82e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.09 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLiagdlqpiegsvthaggLGVMRQFIGSLRGAGESSPGGdgRDSRTV 92
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRT-----------------LNRMNDKVSGYRYSGDVLLGG--RSIFNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 QDLLLSVApvRVKEAAERLNGAELAMME------REDEKTQMRYAQAITD--YTDAGgydievLWDTCTMAALGAPYdnv 164
Cdd:PRK14271 94 RDVLEFRR--RVGMLFQRPNPFPMSIMDnvlagvRAHKLVPRKEFRGVAQarLTEVG------LWDAVKDRLSDSPF--- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 165 kyrdltTLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK--TVLLVSHDRQLLANAVDR 237
Cdd:PRK14271 163 ------RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDR 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-251 |
6.00e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 44.70 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIaGDLQPIEGSVTHAGGLGVmrqfigslrgageSSPGGDGRDSR---- 90
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSGDLIVDGLKV-------------NDPKVDERLIRqeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 91 -TVQDLLL--------SVA--PVRV----KEAAERLNGAELA---MMERedektqmryaqaitdytdAGGYDIEvlwdtc 152
Cdd:PRK09493 81 mVFQQFYLfphltaleNVMfgPLRVrgasKEEAEKQARELLAkvgLAER------------------AHHYPSE------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 153 tmaalgapydnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGK---IWLEQALRETSKTVLLVSHDRQ 229
Cdd:PRK09493 137 -------------------LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRhevLKVMQDLAEEGMTMVIVTHEIG 197
|
250 260
....*....|....*....|..
gi 2796936914 230 LLANAVDRIVTVESGNVWIHGG 251
Cdd:PRK09493 198 FAEKVASRLIFIDKGRIAEDGD 219
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-68 |
6.40e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.92 E-value: 6.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796936914 1 MQVSRLTHvLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMR 68
Cdd:PRK11701 7 LSVRGLTK-LYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR 73
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-244 |
6.59e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 44.68 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrQFIGSLRGAGEsspGGDGRDSRTV-QDL 95
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRG------EPLAKLNRAQR---KAFRRDIQMVfQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 96 LLSVAPvrvKEAAERLNGAELAMMEREDEKTQMRYAQAItdyTDAGGYDIEVLwdtctmaalgapydnvkYRDLTTLSGG 175
Cdd:PRK10419 99 ISAVNP---RKTVREIIREPLRHLLSLDKAERLARASEM---LRAVDLDDSVL-----------------DKRPPQLSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 176 EQKRLAL-EALLRGPdQTLLLDEPDNYLDV---PGKIWLEQALRETSKTV-LLVSHDRQLLANAVDRIVTVESG 244
Cdd:PRK10419 156 QLQRVCLaRALAVEP-KLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNG 228
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
166-251 |
7.32e-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: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 166 YRDLTTLSGGEQKRLAL----EALLRGpdQTLLLDEPDNYL---DVPGKIWLEQALRETSKTVLLVSHDRQLLANAvDRI 238
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLatqiGSGLTG--VLYVLDEPSIGLhprDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAA-DHV 208
|
90
....*....|...
gi 2796936914 239 VTVESGnVWIHGG 251
Cdd:cd03270 209 IDIGPG-AGVHGG 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
355-531 |
7.80e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.59 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 355 FDLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGAR---------------VVPG--H-----------FAQ 406
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaisVVSQrvHlfsatlrdnllLAA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 407 THARPELLgrtpceIVMTEHARLKN--EAMKALARYELAGGvaeqrfETLSGGQQARLQILLLEMSGATLLLLDEPTDNL 484
Cdd:PRK11160 439 PNASDEAL------IEVLQQVGLEKllEDDKGLNAWLGEGG------RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2796936914 485 DLASAEALQAGLDAF--DGTVLAVTHDRWFAADFDRYMVFGtDGRVYES 531
Cdd:PRK11160 507 DAETERQILELLAEHaqNKTVLMITHRLTGLEQFDRICVMD-NGQIIEQ 554
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-69 |
7.80e-05 |
|
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: 45.71 E-value: 7.80e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGGLGVMRQ 69
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQ 706
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
169-241 |
8.14e-05 |
|
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: 43.12 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 169 LTTLSGGEQKRLALEALLR----GPDQTLLLDEPDNYLD-VPGKIwLEQALRETSK---TVLLVSHDRQLLANAvDRIVT 240
Cdd:cd03227 75 RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDpRDGQA-LAEAILEHLVkgaQVIVITHLPELAELA-DKLIH 152
|
.
gi 2796936914 241 V 241
Cdd:cd03227 153 I 153
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
362-534 |
9.24e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 44.24 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVP-------------------GHFAQTHARP------ELLGR 416
Cdd:PRK13635 33 GEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeetvwdvrrqvgmvfqnpdNQFVGATVQDdvafglENIGV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPCEIVMTEHARLKNEAMKALARYELAggvaeqrfeTLSGGQQARLQILLLEMSGATLLLLDEPTDNLD-------LASA 489
Cdd:PRK13635 113 PREEMVERVDQALRQVGMEDFLNREPH---------RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2796936914 490 EALQAGLDAfdgTVLAVTHDRWFAADFDRYMVFgTDGRVYESPEP 534
Cdd:PRK13635 184 RQLKEQKGI---TVLSITHDLDEAAQADRVIVM-NKGEILEEGTP 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
346-508 |
9.25e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.02 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSH-------FLR------LIAGEEVRHTG--VA-RLGARVV 400
Cdd:COG3845 6 LELRGITKRFggvvanddvSLTVRPGEIHALLGENGAGKSTlmkilygLYQpdsgeiLIDGKPVRIRSprDAiALGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 401 PGHF----AQTHArpE--LLGRTPCEIVMTEHARLKNEAMKALARYELAggV-AEQRFETLSGGQQARLQILLLEMSGAT 473
Cdd:COG3845 86 HQHFmlvpNLTVA--EniVLGLEPTKGGRLDRKAARARIRELSERYGLD--VdPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 2796936914 474 LLLLDEPTDNLDLASAEALQAGLDAF--DG-TVLAVTH 508
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITH 199
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
362-534 |
9.70e-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: 44.02 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSH----FLRLI--AGEEVRHTGV--ARLGARVVPGHFAQTHARPELLGRT------PCEIVMTEha 427
Cdd:cd03244 30 GEKVGIVGRTGSGKSSlllaLFRLVelSSGSILIDGVdiSKIGLHDLRSRISIIPQDPVLFSGTirsnldPFGEYSDE-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 428 rlknEAMKALARYELAGGVAEQRF----------ETLSGGQQ-----ARlqILLlemSGATLLLLDEPTDNLDLASAEAL 492
Cdd:cd03244 108 ----ELWQALERVGLKEFVESLPGgldtvveeggENLSVGQRqllclAR--ALL---RKSKILVLDEATASVDPETDALI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2796936914 493 QAGL-DAF-DGTVLAVTHDRWFAADFDRYMVFGtDGRVYESPEP 534
Cdd:cd03244 179 QKTIrEAFkDCTVLTIAHRLDTIIDSDRILVLD-KGRVVEFDSP 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
162-246 |
1.11e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.10 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 162 DNVKYRDlTTLSGGEQKRLAL-EALLRGpDQTLLLDEPDNYLD----VPGKIWLEQaLRETSKTVLLVSHDRQLLANAvD 236
Cdd:PRK10535 136 DRVEYQP-SQLSGGQQQRVSIaRALMNG-GQVILADEPTGALDshsgEEVMAILHQ-LRDRGHTVIIVTHDPQVAAQA-E 211
|
90
....*....|
gi 2796936914 237 RIVTVESGNV 246
Cdd:PRK10535 212 RVIEIRDGEI 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
357-508 |
1.23e-04 |
|
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: 43.63 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 357 LEIWYGERVAVLGSNGSGKSHFLRLIAGeevrhTGVARLGARVVPGHFAQThARPELLgRTPCEIVMTEHA--------- 427
Cdd:cd03252 23 LRIKPGEVVGIVGRSGSGKSTLTKLIQR-----FYVPENGRVLVDGHDLAL-ADPAWL-RRQVGVVLQENVlfnrsirdn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 428 -RLKNEAM---KALARYELAGG-------------VAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAE 490
Cdd:cd03252 96 iALADPGMsmeRVIEAAKLAGAhdfiselpegydtIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEH 175
|
170 180
....*....|....*....|
gi 2796936914 491 ALQAGL-DAFDG-TVLAVTH 508
Cdd:cd03252 176 AIMRNMhDICAGrTVIIIAH 195
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
13-263 |
1.30e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 43.59 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVT--------------HAGGLGVMRQFIGSLRGAG 78
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslsqQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 79 ESSPggdgrdSRTVQDLLLSvAPVRVK----EAAERLNGAELAMMeredektqmryaqaitdytdaggydievlwdtctm 154
Cdd:PRK11264 95 NLFP------HRTVLENIIE-GPVIVKgepkEEATARARELLAKV----------------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 155 aALGAPYDNVKYRdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLD------VPGKIwleQALRETSKTVLLVSHDR 228
Cdd:PRK11264 133 -GLAGKETSYPRR----LSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgeVLNTI---RQLAQEKRTMVIVTHEM 204
|
250 260 270
....*....|....*....|....*....|....*
gi 2796936914 229 QLLANAVDRIVTVESGNVWIHGGGFATYSEARKDR 263
Cdd:PRK11264 205 SFARDVADRAIFMDQGRIVEQGPAKALFADPQQPR 239
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
362-530 |
1.35e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 43.61 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARvvPGHFAQTHARPELLGRT------PCEIVMTEHArLKNEAMK 435
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQ--PLHQMDEEARAKLRAKHvgfvfqSFMLIPTLNA-LENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 436 ALARYELAGGVAEQRFE----------------TLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDA- 498
Cdd:PRK10584 113 ALLRGESSRQSRNGAKAlleqlglgkrldhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSl 192
|
170 180 190
....*....|....*....|....*....|....*
gi 2796936914 499 ---FDGTVLAVTHDRWFAADFDRYMVFgTDGRVYE 530
Cdd:PRK10584 193 nreHGTTLILVTHDLQLAARCDRRLRL-VNGQLQE 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
362-534 |
1.53e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.59 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVRHTG--------VARLGARVVPGHFAQTHARPE--LLGRT-------PCEIVMT 424
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynnqaITDDNFEKLRKHIGIVFQNPDnqFVGSIvkydvafGLENHAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 425 EHARLKNEAMKALARYELAGgVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF----D 500
Cdd:PRK13648 115 PYDEMHRRVSEALKQVDMLE-RADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVksehN 193
|
170 180 190
....*....|....*....|....*....|....
gi 2796936914 501 GTVLAVTHDRWFAADFDrYMVFGTDGRVYESPEP 534
Cdd:PRK13648 194 ITIISITHDLSEAMEAD-HVIVMNKGTVYKEGTP 226
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-58 |
1.79e-04 |
|
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: 41.98 E-value: 1.79e-04
10 20 30
....*....|....*....|....*....|..
gi 2796936914 27 GTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV 58
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV 33
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-62 |
1.88e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 43.27 E-value: 1.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2796936914 16 LLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG 62
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG 70
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
8-62 |
1.95e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.09 E-value: 1.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 8 HVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAG--DLQPIEGSVTHAG 62
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKG 70
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-59 |
2.02e-04 |
|
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: 42.87 E-value: 2.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLI----RLIagdlQPIEGSVT 59
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLV----ELSSGSIL 62
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
172-268 |
2.14e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 43.15 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRETSK----TVLLVSHDRQLLANAvDRIVTVESGNVW 247
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITHYMEEAVEA-DRIIVMDSGKVV 223
|
90 100
....*....|....*....|.
gi 2796936914 248 IHGGGFATYSEARKDRNERLD 268
Cdd:PRK13633 224 MEGTPKEIFKEVEMMKKIGLD 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
352-509 |
2.16e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 43.14 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 352 MKPFDLEIWYGERVAVLGSNGSGKS----HF---LR------LIAGEEVRHTGVARLGARVVPG---------HFAQTHA 409
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKStlflHFngiLKptsgevLIKGEPIKYDKKSLLEVRKTVGivfqnpddqLFAPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 410 RPELLGRTPCEIVMTEHARLKNEAMKALAryelAGGVAEQRFETLSGGQQARLQIL-LLEMSgATLLLLDEPTDNLDLAS 488
Cdd:PRK13639 98 EDVAFGPLNLGLSKEEVEKRVKEALKAVG----MEGFENKPPHHLSGGQKKRVAIAgILAMK-PEIIVLDEPTSGLDPMG 172
|
170 180
....*....|....*....|....
gi 2796936914 489 AEALQAGLDAFDG---TVLAVTHD 509
Cdd:PRK13639 173 ASQIMKLLYDLNKegiTIIISTHD 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-59 |
2.33e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 2.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVT 59
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT 63
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
362-528 |
2.36e-04 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 43.97 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAG-------------EEVRHTGVARLGARVvpGHFAQthaRPELLGRTPCE-IvmtehA 427
Cdd:COG4618 358 GEVLGVIGPSGSGKSTLARLLVGvwpptagsvrldgADLSQWDREELGRHI--GYLPQ---DVELFDGTIAEnI-----A 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 428 RLKN---EAMKALARyeLAGgVAE------QRFET--------LSGGQQ-----ARlqilllemsgA-----TLLLLDEP 480
Cdd:COG4618 428 RFGDadpEKVVAAAK--LAG-VHEmilrlpDGYDTrigeggarLSGGQRqriglAR----------AlygdpRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2796936914 481 TDNLDLASAEALQAGLDAF---DGTVLAVTHDRWFAADFDRYMVFGtDGRV 528
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALkarGATVVVITHRPSLLAAVDKLLVLR-DGRV 544
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-242 |
2.45e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.59 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 31 ALVGPNGAGKTTLIrliagdlQPIEGSVThagglgvmrqfigslrgaGESSPGGDGrdsrtvqdlllsvapvrvkeaaer 110
Cdd:cd03240 26 LIVGQNGAGKTTII-------EALKYALT------------------GELPPNSKG------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 111 lnGAELAMMEREDEKTqmryAQAITDYTDAGGYDIEVlwdTCTMAAlgapYDNVKY-----------RDLTTLSGGEQK- 178
Cdd:cd03240 57 --GAHDPKLIREGEVR----AQVKLAFENANGKKYTI---TRSLAI----LENVIFchqgesnwpllDMRGRCSGGEKVl 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 179 -----RLALEALLRGPDQTLLLDEPDNYLDvPGKI--WLEQALRETSKT----VLLVSHDRQLLaNAVDRIVTVE 242
Cdd:cd03240 124 asliiRLALAETFGSNCGILALDEPTTNLD-EENIeeSLAEIIEERKSQknfqLIVITHDEELV-DAADHIYRVE 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
346-527 |
2.73e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.75 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpgHFAQT--------- 407
Cdd:PRK11288 5 LSFDGIGKTFpgvkalddiSFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM--RFASTtaalaagva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 408 ------HARPEL-------LGRTPCEIVMTEHARLKNEAMKALARYelagGV---AEQRFETLSGGQQARLQILLLEMSG 471
Cdd:PRK11288 83 iiyqelHLVPEMtvaenlyLGQLPHKGGIVNRRLLNYEAREQLEHL----GVdidPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796936914 472 ATLLLLDEPTDNLDLASAEALQAGLDAF--DGTV-LAVTH--DRWFAADfDRYMVFgTDGR 527
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELraEGRViLYVSHrmEEIFALC-DAITVF-KDGR 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
172-247 |
3.41e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 42.46 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLD--VPGKI--WLEQALRETSKTVLLVSHDRQLLANAvDRIVTVESGNVW 247
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqTGDKIadLLFSLNREHGTTLILVTHDLQLAARC-DRRLRLVNGQLQ 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-542 |
3.97e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 42.34 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 454 LSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF--DGTVLAVTHDRWFAADFDRYMVF--------- 522
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFlyngelvew 233
|
90 100
....*....|....*....|
gi 2796936914 523 GTDGRVYESPEPVWDETRVV 542
Cdd:PRK14246 234 GSSNEIFTSPKNELTEKYVI 253
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
362-529 |
3.99e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.40 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVrhtgvarlgarvvpghfaQTHARPELLGRTPceivmteharlkneamkalarye 441
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLI------------------PNGDNDEWDGITP----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 442 laggVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLD----LASAEALQAGLDAFDGTVLAVTHDrWFAADF- 516
Cdd:cd03222 64 ----VYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHD-LAVLDYl 138
|
170
....*....|....
gi 2796936914 517 -DRYMVFGTDGRVY 529
Cdd:cd03222 139 sDRIHVFEGEPGVY 152
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
167-239 |
4.14e-04 |
|
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: 41.54 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 167 RDLTTLSGGEQKRLAL-EALLRGPDQTL-LLDEPDNYLD------VPGKIwleQALRETSKTVLLVSHDRQLLANAvDRI 238
Cdd:cd03238 83 QKLSTLSGGELQRVKLaSELFSEPPGTLfILDEPSTGLHqqdinqLLEVI---KGLIDLGNTVILIEHNLDVLSSA-DWI 158
|
.
gi 2796936914 239 V 239
Cdd:cd03238 159 I 159
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-246 |
4.26e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 42.26 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 16 LLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVThagglgVMRQFIGSLRGAGESSPGGDGRDSRTVQDL 95
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIV------VNGQTINLVRDKDGQLKVADKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 96 LLSV------------------APVRVkeaaerlngaeLAMMEREDEKTQMRYAQAI-TDYTDAGGYDIEvlwdtctmaa 156
Cdd:PRK10619 94 LTMVfqhfnlwshmtvlenvmeAPIQV-----------LGLSKQEARERAVKYLAKVgIDERAQGKYPVH---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 lgapydnvkyrdlttLSGGEQKRLALEALLRGPDQTLLLDEPDNYLD---VPGKIWLEQALRETSKTVLLVSHDRQLLAN 233
Cdd:PRK10619 153 ---------------LSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARH 217
|
250
....*....|...
gi 2796936914 234 AVDRIVTVESGNV 246
Cdd:PRK10619 218 VSSHVIFLHQGKI 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
366-536 |
4.72e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 43.08 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 366 AVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFaqtHARPELLGRTPCEIVMTEH----------ARLKNEAMK 435
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL---DAVRQSLGMCPQHNILFHHltvaehilfyAQLKGRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 436 AlARYELAG-----GVAEQRFET---LSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFDG--TVLA 505
Cdd:TIGR01257 1037 E-AQLEMEAmledtGLHHKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSgrTIIM 1115
|
170 180 190
....*....|....*....|....*....|...
gi 2796936914 506 VTHdRWFAADF--DRYMVFgTDGRVYESPEPVW 536
Cdd:TIGR01257 1116 STH-HMDEADLlgDRIAII-SQGRLYCSGTPLF 1146
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-533 |
4.85e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 454 LSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF--DGTVLAVTHDRWFAADFDRYMVF--------- 522
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPAQAARVSDYVAFlylgkliev 229
|
90
....*....|.
gi 2796936914 523 GTDGRVYESPE 533
Cdd:PRK14267 230 GPTRKVFENPE 240
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
351-521 |
4.97e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 42.91 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 351 LMKPFDLEIWYGERVAVLGSNGSGKSHFLR------------LIAGEEVR-------HTGVARLGARvvPGHFAQTHARP 411
Cdd:PRK11174 365 LAGPLNFTLPAGQRIALVGPSGAGKTSLLNallgflpyqgslKINGIELReldpeswRKHLSWVGQN--PQLPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 412 ELLGRtpceIVMTEHarlknEAMKALAR-------YELAGGVAEQRFE---TLSGGQQARLQILLLEMSGATLLLLDEPT 481
Cdd:PRK11174 443 VLLGN----PDASDE-----QLQQALENawvseflPLLPQGLDTPIGDqaaGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2796936914 482 DNLDLASAEALQAGLD--AFDGTVLAVTHDRWFAADFDRYMV 521
Cdd:PRK11174 514 ASLDAHSEQLVMQALNaaSRRQTTLMVTHQLEDLAQWDQIWV 555
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-386 |
4.99e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.92 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 15 PLLNDVSFRIGEGTKAALVGPNGAGKttlirliagdlqpiegSVThagGLGVMRqFIGSLRGAGESSPGGDGRDSRTVQD 94
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGK----------------SVT---ALALMR-LLEQAGGLVQCDKMLLRRRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 95 LL-LSVAPVRvkeaaeRLNGAELAMMEREDEKT-------QMRYAQAITDYTDAGGYDievlwdtcTMAALGAPYDNVKY 166
Cdd:PRK10261 90 LSeQSAAQMR------HVRGADMAMIFQEPMTSlnpvftvGEQIAESIRLHQGASREE--------AMVEAKRMLDQVRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 167 RDLTT--------LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALR----ETSKTVLLVSHDRQLLANA 234
Cdd:PRK10261 156 PEAQTilsryphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 235 VDRIV------TVESGNV-WIHGGGFATYSEARKDRNERLDELRrrwdeEHAKLKRLVVMlrqkatyndSMAAPYHAAQT 307
Cdd:PRK10261 236 ADRVLvmyqgeAVETGSVeQIFHAPQHPYTRALLAAVPQLGAMK-----GLDYPRRFPLI---------SLEHPAKQEPP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 308 RLRRFEEAGPPELAPKDQLISMRLRGG---RTAKRAVICENLElsglmkpFDLeiWYGERVAVLGSNGSGKS----HFLR 380
Cdd:PRK10261 302 IEQDTVVDGEPILQVRNLVTRFPLRSGllnRVTREVHAVEKVS-------FDL--WPGETLSLVGESGSGKSttgrALLR 372
|
....*.
gi 2796936914 381 LIAGEE 386
Cdd:PRK10261 373 LVESQG 378
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
362-508 |
6.00e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 42.13 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVRHTG--------------VARLGARVVPgHF----AQTHARPELL--GRtpcei 421
Cdd:PRK13536 67 GECFGLLGPNGAGKSTIARMILGMTSPDAGkitvlgvpvpararLARARIGVVP-QFdnldLEFTVRENLLvfGR----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 422 VMTEHARLKNEAMKALARYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASA----EALQAgLD 497
Cdd:PRK13536 141 YFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARhliwERLRS-LL 219
|
170
....*....|.
gi 2796936914 498 AFDGTVLAVTH 508
Cdd:PRK13536 220 ARGKTILLTTH 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-58 |
6.41e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.10 E-value: 6.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV 58
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-63 |
7.16e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.42 E-value: 7.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAG--DLQpiEGSVTHAGG 63
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGarKIQ--QGRVEVLGG 63
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
13-62 |
7.38e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 7.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG 62
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG 72
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
454-508 |
8.44e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.30 E-value: 8.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 454 LSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAF--DGTVLAVTH 508
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLkdDYTMLLVTR 205
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
169-239 |
9.54e-04 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.06 E-value: 9.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 169 LTTLSGGEQKR--LALEALLRGPDQTL-LLDEPDNYL---DVPGKIWLEQALRETSKTVLLVSHDRQLLANAvDRIV 239
Cdd:cd03271 167 ATTLSGGEAQRikLAKELSKRSTGKTLyILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCA-DWII 242
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-62 |
1.01e-03 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 41.19 E-value: 1.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQP---IEGSVTHAG 62
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDG 69
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
366-518 |
1.15e-03 |
|
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: 39.65 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 366 AVLGSNGSGKSHFLR---LIAGEEVRHTGVARLGArvvPGHFaqtharpellgrtpceivmteharlkneamKALARYEL 442
Cdd:cd03227 25 IITGPNGSGKSTILDaigLALGGAQSATRRRSGVK---AGCI------------------------------VAAVSAEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 443 AggvaeQRFETLSGGQQARLQILLL----EMSGATLLLLDEPTDNLDLASAEAL------QAGLDAfdgTVLAVTHDRWF 512
Cdd:cd03227 72 I-----FTRLQLSGGEKELSALALIlalaSLKPRPLYILDEIDRGLDPRDGQALaeaileHLVKGA---QVIVITHLPEL 143
|
....*.
gi 2796936914 513 AADFDR 518
Cdd:cd03227 144 AELADK 149
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
346-509 |
1.40e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 40.74 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 346 LELSGLMKPF---------DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVPGHFAQTHARPELLgR 416
Cdd:PRK11300 6 LSVSGLMMRFggllavnnvNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVV-R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 417 TPCEI----VMT--------EHARLKN-----------------EAMKALARY-ELAG--GVAEQRFETLSGGQQARLQI 464
Cdd:PRK11300 85 TFQHVrlfrEMTvienllvaQHQQLKTglfsgllktpafrraesEALDRAATWlERVGllEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2796936914 465 LLLEMSGATLLLLDEPTDNLDLASAEALQAGLDA----FDGTVLAVTHD 509
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAElrneHNVTVLLIEHD 213
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
167-245 |
1.70e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 167 RDLTTLSGGEQKRLAL--EALLRGPDQTL-LLDEPDNYL---DVPGKIWLEQALRETSKTVLLVSHDRQLLANAvDRIVT 240
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLayELLAPSKKPTLyVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVA-DYVLE 883
|
....*..
gi 2796936914 241 V--ESGN 245
Cdd:PRK00635 884 LgpEGGN 890
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
454-508 |
1.91e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 40.02 E-value: 1.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796936914 454 LSGGQQARLQI---LLLEmsgATLLLLDEPTDNLD-LASA--EALQAGLdAFDGTVLAVTH 508
Cdd:COG1117 155 LSGGQQQRLCIaraLAVE---PEVLLMDEPTSALDpISTAkiEELILEL-KKDYTIVIVTH 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
356-534 |
1.97e-03 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 40.11 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLI-------AGE---------------EVR-HTG------------------VAr 394
Cdd:TIGR04520 22 SLSIEKGEFVAIIGHNGSGKSTLAKLLnglllptSGKvtvdgldtldeenlwEIRkKVGmvfqnpdnqfvgatveddVA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 395 lgarvvpghFAqtharPELLGRTPCEIVmtehaRLKNEA-----MKALARYELAggvaeqrfeTLSGGQQARLQI---LL 466
Cdd:TIGR04520 101 ---------FG-----LENLGVPREEMR-----KRVDEAlklvgMEDFRDREPH---------LLSGGQKQRVAIagvLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796936914 467 LEMSgatLLLLDEPTDNLD-------LASAEAL--QAGLdafdgTVLAVTHDRWFAADFDRYMVFGtDGRVYESPEP 534
Cdd:TIGR04520 153 MRPD---IIILDEATSMLDpkgrkevLETIRKLnkEEGI-----TVISITHDMEEAVLADRVIVMN-KGKIVAEGTP 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
347-489 |
2.11e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.25 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 347 ELSGLMKPfdleiwyGERVAVLGSNGSGKSHFLRLIAGEEVrhTGVARLGARVVPG-------------------HFAQT 407
Cdd:TIGR00956 781 NVDGWVKP-------GTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRLVNGrpldssfqrsigyvqqqdlHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 408 HARPELLG----RTPCEIVMTEHARLKNEAMKALARYELAGGVAEQRFETLSGGQQARLQILL-LEMSGATLLLLDEPTD 482
Cdd:TIGR00956 852 TVRESLRFsaylRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVeLVAKPKLLLFLDEPTS 931
|
....*..
gi 2796936914 483 NLDLASA 489
Cdd:TIGR00956 932 GLDSQTA 938
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-49 |
2.22e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.22e-03
10 20 30
....*....|....*....|....*....|...
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAG 49
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
167-251 |
2.23e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 167 RDLTTLSGGEQKR--LALEALLRGPDQTL-LLDEPDNYL---DVPGKIWLEQALRETSKTVLLVSHDRQLLANAvDRIVT 240
Cdd:TIGR00630 825 QPATTLSGGEAQRikLAKELSKRSTGRTLyILDEPTTGLhfdDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTA-DYIID 903
|
90
....*....|...
gi 2796936914 241 V--ESGNvwiHGG 251
Cdd:TIGR00630 904 LgpEGGD---GGG 913
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
362-492 |
2.23e-03 |
|
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: 39.66 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 362 GERVAVLGSNGSGKSHFLRLIAGEEVRHTGVA-----------------------------RLGARVVPGHFAQTH--AR 410
Cdd:cd03266 31 GEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgfdvvkepaearrrlgfvsdstglydRLTARENLEYFAGLYglKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 411 PELLGRTpceivmteharlkNEAMKALARYELAggvaEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAE 490
Cdd:cd03266 111 DELTARL-------------EELADRLGMEELL----DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
..
gi 2796936914 491 AL 492
Cdd:cd03266 174 AL 175
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-225 |
2.35e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 16 LLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDL---QPIEGSVTHAGGLG---VMRQFIGSLRGAGESS---Pggdg 86
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfHIGVEGVITYDGITpeeIKKHYRGDVVYNAETDvhfP---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 87 rdSRTVQDLLLSVApvRVKEAAERLNGaelamMEREDektqmrYAQAITDYtdaggydievlwdtcTMAALGAP--YDNV 164
Cdd:TIGR00956 152 --HLTVGETLDFAA--RCKTPQNRPDG-----VSREE------YAKHIADV---------------YMATYGLShtRNTK 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 165 KYRDLTT-LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRET---SKTVLLVS 225
Cdd:TIGR00956 202 VGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSaniLDTTPLVA 266
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-58 |
2.39e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.16 E-value: 2.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2796936914 19 DVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSV 58
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL 70
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-61 |
2.42e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.73 E-value: 2.42e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 14 RPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIE-------GSVTHA 61
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvirGSVAYV 684
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
157-251 |
2.55e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 157 LGAPYDNVKyRDLTTLSGGEQKRLALEALLrGPDQT---LLLDEPdnyldvpgKIWLEQA-----------LRETSKTVL 222
Cdd:TIGR00630 475 VGLDYLSLS-RAAGTLSGGEAQRIRLATQI-GSGLTgvlYVLDEP--------SIGLHQRdnrrlintlkrLRDLGNTLI 544
|
90 100
....*....|....*....|....*....
gi 2796936914 223 LVSHDRQLLANAvDRIVTVESGnVWIHGG 251
Cdd:TIGR00630 545 VVEHDEDTIRAA-DYVIDIGPG-AGEHGG 571
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
356-535 |
3.01e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 39.59 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 356 DLEIWYGERVAVLGSNGSGKSHFLRLIAGEEVRHTGVARLGARVVpghfaQTHARPELlgRTPCEIVMT----------- 424
Cdd:PRK13632 29 SFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI-----SKENLKEI--RKKIGIIFQnpdnqfigatv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 425 --------EHARLKNEAMKALArYELAGGVAEQRF-----ETLSGGQQARLQIlllemsgATLLLL-------DEPTDNL 484
Cdd:PRK13632 102 eddiafglENKKVPPKKMKDII-DDLAKKVGMEDYldkepQNLSGGQKQRVAI-------ASVLALnpeiiifDESTSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 485 D-LASAEALQAGLD---AFDGTVLAVTHDRWFAADFDRYMVFgTDGRVYESPEPV 535
Cdd:PRK13632 174 DpKGKREIKKIMVDlrkTRKKTLISITHDMDEAILADKVIVF-SEGKLIAQGKPK 227
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
339-508 |
3.44e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.24 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 339 RAVICENLELSGLmkpfDLEIWYGERVAVLGSNGSGKSHFLRLIAGeevrHTGVARLGARVVPGHFAQTHARPEL---LG 415
Cdd:CHL00131 14 HASVNENEILKGL----NLSINKGEIHAIMGPNGSGKSTLSKVIAG----HPAYKILEGDILFKGESILDLEPEErahLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 416 -----RTPCEI--VMTE-------HARLKNEAMKALARYELAGGVAE--------QRF------ETLSGGQQARLQILLL 467
Cdd:CHL00131 86 iflafQYPIEIpgVSNAdflrlayNSKRKFQGLPELDPLEFLEIINEklklvgmdPSFlsrnvnEGFSGGEKKRNEILQM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2796936914 468 EMSGATLLLLDEPTDNLDLASAEALQAGLDAF---DGTVLAVTH 508
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITH 209
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
32-246 |
4.29e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 39.78 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 32 LVGPNGAGKTTLIRLIAGDLQPIEGSVthagglgvmrqfigslrgagesspggdgrdsrtvqdlllsvapvrvkeaaeRL 111
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEI---------------------------------------------------LL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 112 NGAELAMMEREDektqmrYAQ---AI-TDY---TDAGGYDIEVLwdtctmAALGAPY-------DNVKYRD--LTT--LS 173
Cdd:COG4615 392 DGQPVTADNREA------YRQlfsAVfSDFhlfDRLLGLDGEAD------PARARELlerleldHKVSVEDgrFSTtdLS 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 174 GGEQKRLAL-EALL--RgpdQTLLLDEpdnyldvpgkiW---------------LEQALRETSKTVLLVSHDRQLLANAv 235
Cdd:COG4615 460 QGQRKRLALlVALLedR---PILVFDE-----------WaadqdpefrrvfyteLLPELKARGKTVIAISHDDRYFDLA- 524
|
250
....*....|.
gi 2796936914 236 DRIVTVESGNV 246
Cdd:COG4615 525 DRVLKMDYGKL 535
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
161-232 |
4.48e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 4.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796936914 161 YDNVKYRDLTTLSGGEQKRLALEALL---RGPDQTLLLDEPDNYLDvPGKI-WLEQALRETSKT---VLLVSHDRQLLA 232
Cdd:pfam13304 226 NGGGGELPAFELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLH-PKLLrRLLELLKELSRNgaqLILTTHSPLLLD 303
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-231 |
4.64e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.00 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 8 HVLPDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAG--DLQPIEGSVTHAGglgvmrqfigslRGAGESSPggd 85
Cdd:PRK09580 8 HVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKG------------KDLLELSP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 86 grDSRTVQDLLLSVA-PVRVKEAAER--LNGAELAMMEREDEKTQMRYaqaitDYTDAGGYDIEVlwdtctmaaLGAPYD 162
Cdd:PRK09580 73 --EDRAGEGIFMAFQyPVEIPGVSNQffLQTALNAVRSYRGQEPLDRF-----DFQDLMEEKIAL---------LKMPED 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796936914 163 NVKYRDLTTLSGGEQKR---LALEALlrGPDqTLLLDEPDNYLDVPG-KIWLE--QALRETSKTVLLVSHDRQLL 231
Cdd:PRK09580 137 LLTRSVNVGFSGGEKKRndiLQMAVL--EPE-LCILDESDSGLDIDAlKIVADgvNSLRDGKRSFIIVTHYQRIL 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-485 |
4.70e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 1 MQVSRLTHVLPDGRPLLNDvSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHagglgvmrQFigslrgages 80
Cdd:PRK10938 4 LQISQGTFRLSDTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQS--------QF---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 81 spggdgrdsRTVQDLLLSVAPVRVKEAAERLNGAELAMMEREDEKTQmryAQAITDYTDAGgydievlwDTCTMAALGAP 160
Cdd:PRK10938 65 ---------SHITRLSFEQLQKLVSDEWQRNNTDMLSPGEDDTGRTT---AEIIQDEVKDP--------ARCEQLAQQFG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 161 YDNVKYRDLTTLSGGE-QKRLALEALLRGPDqTLLLDEPDNYLDVPGKIWLEQALRETSKT-VLLVshdrqLLANAVDRI 238
Cdd:PRK10938 125 ITALLDRRFKYLSTGEtRKTLLCQALMSEPD-LLILDEPFDGLDVASRQQLAELLASLHQSgITLV-----LVLNRFDEI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 239 VTvesgnvwihgggFATYSEARKDRnerldELRRRwDEEHAKLKRLVVMLRQKATYNDSMAAPyhaaqtrlrrfEEAGP- 317
Cdd:PRK10938 199 PD------------FVQFAGVLADC-----TLAET-GEREEILQQALVAQLAHSEQLEGVQLP-----------EPDEPs 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 318 --PELAPKDQLISMRlrggrtakRAVICENLE--LSGLmkpfDLEIWYGERVAVLGSNGSGKSHFLRLI----------- 382
Cdd:PRK10938 250 arHALPANEPRIVLN--------NGVVSYNDRpiLHNL----SWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysnd 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 383 ---------AGEEV----RHTGVA----RLGARVvpghfaQTHARPELL-------GrtpceIVMTEHARLKNEAMKALA 438
Cdd:PRK10938 318 ltlfgrrrgSGETIwdikKHIGYVssslHLDYRV------STSVRNVILsgffdsiG-----IYQAVSDRQQKLAQQWLD 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2796936914 439 RYELAGGVAEQRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLD 485
Cdd:PRK10938 387 ILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
168-234 |
4.86e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 4.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796936914 168 DLTTLSGGEQK------RLALEALLRGPDQTLLLDEPDNYLDVPGKIWL----EQALRETS--KTVLLVSHDRQLLANA 234
Cdd:PRK01156 798 GIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLkdiiEYSLKDSSdiPQVIMISHHRELLSVA 876
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
172-250 |
5.08e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 39.06 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 172 LSGGEQKRLALEALLRGPDQTLLLDEPDNYLDVPGKIWLEQALRET---SKTVLLVSHDRQLLANAVDRIVTVESGNVWI 248
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkanNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
..
gi 2796936914 249 HG 250
Cdd:PRK13631 257 TG 258
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-49 |
5.43e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.06 E-value: 5.43e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2796936914 11 PDGRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAG 49
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG 52
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-62 |
5.61e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 39.18 E-value: 5.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2796936914 17 LNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG 62
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-62 |
6.45e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 38.92 E-value: 6.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2796936914 18 NDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAG 62
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
449-512 |
7.58e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 7.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796936914 449 QRFETLSGGQQARLQILLLEMSGATLLLLDEPTDNLDLASAEALQAGLDAFDGTVLAVTHDRWF 512
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREF 403
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-244 |
9.21e-03 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 37.41 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 13 GRPLLNDVSFRIGEGTKAALVGPNGAGKTTLIRLIAGDLQPIEGSVTHAGglgvmrqfigslrgagesspggdgrdsrtv 92
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG------------------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796936914 93 qdlllsvAPVRVKEAAERLNgAELAMMErEDektqmRYAQAItdytdAGGYDIevlwdtctmaalgapYDNVKYRDLttL 172
Cdd:cd03215 62 -------KPVTRRSPRDAIR-AGIAYVP-ED-----RKREGL-----VLDLSV---------------AENIALSSL--L 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796936914 173 SGGEQKRLAL-EALLRGPDqTLLLDEPDNYLDVPGK--IW-LEQALRETSKTVLLVSHDRQLLANAVDRIVTVESG 244
Cdd:cd03215 106 SGGNQQKVVLaRWLARDPR-VLILDEPTRGVDVGAKaeIYrLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
353-384 |
9.81e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 38.80 E-value: 9.81e-03
10 20 30
....*....|....*....|....*....|..
gi 2796936914 353 KPFDLEIWYGERVAVLGSNGSGKSHFLRLIAG 384
Cdd:PRK10522 340 GPINLTIKRGELLFLIGGNGSGKSTLAMLLTG 371
|
|
| |
