|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-522 |
4.15e-132 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 393.66 E-value: 4.15e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG--TIGLLRQDMPGG------WTLAEALGVAND 88
Cdd:COG0488 12 PLLDDVSLSINPgDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDddltvlDTVLDGDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 89 LE-RLERILAGNGTAGD-----------FDAAD-WTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAP 155
Cdd:COG0488 92 LEaELEELEAKLAEPDEdlerlaelqeeFEALGgWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 156 DLLLLDEPTNNLDAAGRAAIRALMREWRGGVLVASHDRELLDDV-DRILELTAIGARSFGGGWSAFSAARDEDRRRASAE 234
Cdd:COG0488 172 DLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVaTRILELDRGKLTLYPGNYSAYLEQRAERLEQEAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 235 LERADADVRavRQAVQARReakerrdragraFAAKGSepkillgaRAERAQnsggtaqaiSDRRMGRALAEADDARSRVE 314
Cdd:COG0488 252 YAKQQKKIA--KEEEFIRR------------FRAKAR--------KAKQAQ---------SRIKALEKLEREEPPRRDKT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 315 VltplTIALPPsGLPSGANVLAMEGVVAEAGDRRL-GPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRA 393
Cdd:COG0488 301 V----EIRFPP-PERLGKKVLELEGLSKSYGDKTLlDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 394 EG-RIVLLDQQVGLLDPEGTILDNIRRLHPDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALsgSAPPWL 472
Cdd:COG0488 376 ETvKIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLL--LSPPNV 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 518843096 473 IILDEPTNHLDIESVEILENALLSFDGALLVVSHDPSFVERVgFDRVFEV 522
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRV-ATRILEF 502
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-514 |
1.01e-66 |
|
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: 225.20 E-value: 1.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 31 RVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG--TIGLLRQDMPGGWTL------AEALG-VANDLERLERILAGNGT 101
Cdd:TIGR03719 33 KIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPgiKVGYLPQEPQLDPTKtvrenvEEGVAeIKDALDRFNEISAKYAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 102 AGD---------------FDAAD-WTLESRIGAALAQVGLPalPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:TIGR03719 113 PDAdfdklaaeqaelqeiIDAADaWDLDSQLEIAMDALRCP--PWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 166 NLDAAGRAAIRALMREWRGGVLVASHDRELLDDVDR-ILELtaigarsfgggwsafsaardeDRRRA-------SAELER 237
Cdd:TIGR03719 191 HLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGwILEL---------------------DRGRGipwegnySSWLEQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 238 ADAdvravRQAVQARREAKeRRDRAGRAFAAKGSEPKillgARaeraqnsggtaQAISDRRMGR--ALAEADDARsRVEv 315
Cdd:TIGR03719 250 KQK-----RLEQEEKEESA-RQKTLKRELEWVRQSPK----GR-----------QAKSKARLARyeELLSQEFQK-RNE- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 316 ltPLTIALPPsGLPSGANVLAMEGVVAEAGDRRLgpwtlrIDG------PERI-ALKGANGAGKTTLLRIAAGLRAPVSG 388
Cdd:TIGR03719 307 --TAEIYIPP-GPRLGDKVIEAENLTKAFGDKLL------IDDlsfklpPGGIvGVIGPNGAGKSTLFRMITGQEQPDSG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 389 TVRRAEG-RIVLLDQQVGLLDPEGTI-------LDNIRrlhpdAGDEE--AYALCARFAFRNRDARRVVGTLSGGERLRA 458
Cdd:TIGR03719 378 TIEIGETvKLAYVDQSRDALDPNKTVweeisggLDIIK-----LGKREipSRAYVGRFNFKGSDQQKKVGQLSGGERNRV 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 459 GLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSFDGALLVVSHDPSFVERV 514
Cdd:TIGR03719 453 HLAKTLKSGGN--VLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRI 506
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-514 |
2.95e-64 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 218.45 E-value: 2.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG--TIGLLRQDMPggwtLAEAL--------GVA---NDLERLERILAG 98
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPgiKVGYLPQEPQ----LDPEKtvrenveeGVAevkAALDRFNEIYAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 99 NGTAG-DFD--------------AAD-WTLESRIGAALAQVGLPalPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDE 162
Cdd:PRK11819 112 YAEPDaDFDalaaeqgelqeiidAADaWDLDSQLEIAMDALRCP--PWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 163 PTNNLDAAGRAAIRALMREWRGGVLVASHDRELLDDV-DRILELtaigarsfgggwsafsaardeDRRRA-------SAE 234
Cdd:PRK11819 190 PTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVaGWILEL---------------------DRGRGipwegnySSW 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 235 LERADAdvravRQAVQARREAKeRRDRAGRAFAAKGSEPKillgARaeraqnsggtaQAISDRRMGR---ALAEADDARs 311
Cdd:PRK11819 249 LEQKAK-----RLAQEEKQEAA-RQKALKRELEWVRQSPK----AR-----------QAKSKARLARyeeLLSEEYQKR- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 312 rvevLTPLTIALPPsGLPSGANVLAMEGVVAEAGDRRLgpwtlrIDG------PERI-ALKGANGAGKTTLLRIAAGLRA 384
Cdd:PRK11819 307 ----NETNEIFIPP-GPRLGDKVIEAENLSKSFGDRLL------IDDlsfslpPGGIvGIIGPNGAGKSTLFKMITGQEQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 385 PVSGTVRRAEG-RIVLLDQQVGLLDPEGTI-------LDNIRrlhpdAGDEE----AYalCARFAFRNRDARRVVGTLSG 452
Cdd:PRK11819 376 PDSGTIKIGETvKLAYVDQSRDALDPNKTVweeisggLDIIK-----VGNREipsrAY--VGRFNFKGGDQQKKVGVLSG 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 453 GERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSFDGALLVVSHDPSFVERV 514
Cdd:PRK11819 449 GERNRLHLAKTLKQGGN--VLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRI 508
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-512 |
6.94e-61 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 211.35 E-value: 6.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 16 DGPLFQKLTFAI-GTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG--TIGLLRQDMP-------------GGWTL 79
Cdd:PRK11147 15 DAPLLDNAELHIeDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlIVARLQQDPPrnvegtvydfvaeGIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 80 AEALG--------VAND-----LERLERILAgngtagDFDAAD-WTLESRIGAALAQVGLPAlplDRCLRTLSGGERTRV 145
Cdd:PRK11147 95 AEYLKryhdishlVETDpseknLNELAKLQE------QLDHHNlWQLENRINEVLAQLGLDP---DAALSSLSGGWLRKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 146 GIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGGVLVASHDRELLDDV-DRILELTAIGARSFGGGWSAFSAAR 224
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMaTRIVDLDRGKLVSYPGNYDQYLLEK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 225 DEDRR---RASAELERADADVRA-VRQAVQARREAKERRDRAGRAFaakgsepkillgaRAERaqnsggtaqaiSDRR-- 298
Cdd:PRK11147 246 EEALRveeLQNAEFDRKLAQEEVwIRQGIKARRTRNEGRVRALKAL-------------RRER-----------SERRev 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 299 MGRALAEADDArSRvevltpltialppsglpSGANVLAMEGVVAEAGDRRL-GPWTLRIDGPERIALKGANGAGKTTLLR 377
Cdd:PRK11147 302 MGTAKMQVEEA-SR-----------------SGKIVFEMENVNYQIDGKQLvKDFSAQVQRGDKIALIGPNGCGKTTLLK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 378 IAAGLRAPVSGTVRRAEG-RIVLLDQQVGLLDPEGTILDNI----RRLHPDAGDEEAYALCARFAFRNRDARRVVGTLSG 452
Cdd:PRK11147 364 LMLGQLQADSGRIHCGTKlEVAYFDQHRAELDPEKTVMDNLaegkQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSG 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 453 GERLRAGLAAALSgsAPPWLIILDEPTNHLDIESVEILENALLSFDGALLVVSHDPSFVE 512
Cdd:PRK11147 444 GERNRLLLARLFL--KPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVD 501
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-507 |
1.05e-48 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 178.05 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVrrtgtigllrqDMPGGWTLA-----------EALGVANDLER----LER 94
Cdd:PRK10636 28 QKVGLVGKNGCGKSTLLALLKNEISADGGSY-----------TFPGNWQLAwvnqetpalpqPALEYVIDGDReyrqLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 95 ILA-------GNGTA---GDFDAAD-WTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEP 163
Cdd:PRK10636 97 QLHdanerndGHAIAtihGKLDAIDaWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 164 TNNLDAAGRAAIRALMREWRGGVLVASHDRELLDD-VDRILELTAIGARSFGGGWSAFsaardedrrrasaELERAdadV 242
Cdd:PRK10636 177 TNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPiVDKIIHIEQQSLFEYTGNYSSF-------------EVQRA---T 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 243 RAVRQavQARREAKERR--------DRagraFAAKGSEPKillgaraeraqnsggtaQAISDRRMgralaeaddaRSRVE 314
Cdd:PRK10636 241 RLAQQ--QAMYESQQERvahlqsyiDR----FRAKATKAK-----------------QAQSRIKM----------LERME 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 315 VLTPLTIALP-------PSGLPSgaNVLAMEGVVAEAGDRR-LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPV 386
Cdd:PRK10636 288 LIAPAHVDNPfhfsfraPESLPN--PLLKMEKVSAGYGDRIiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 387 SGTVRRAEG-RIVLLDQ-QVGLLDPEGTILDNIRRLHPDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRagLAAAL 464
Cdd:PRK10636 366 SGEIGLAKGiKLGYFAQhQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKAR--LVLAL 443
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 518843096 465 SGSAPPWLIILDEPTNHLDIESVEILENALLSFDGALLVVSHD 507
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHD 486
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-206 |
4.38e-40 |
|
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: 141.82 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRR--TGTIGLLRQdmpggwtlae 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPgDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 82 algvandlerlerilagngtagdfdaadwtlesrigaalaqvglpalpldrclrtLSGGERTRVGIARLVMEAPDLLLLD 161
Cdd:cd03221 71 -------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518843096 162 EPTNNLDAAGRAAIRALMREWRGGVLVASHDRELLDDV-DRILELT 206
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVaTKIIELE 141
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-511 |
4.47e-40 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 151.97 E-value: 4.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--IGLLRQD-------------MPGGWTLAE 81
Cdd:PRK15064 15 PLFENISVKFGGgNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNerLGKLRQDqfafeeftvldtvIMGHTELWE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 82 ALgvandLERlERILAgNGTAGDFD---AAD----------WTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIA 148
Cdd:PRK15064 95 VK-----QER-DRIYA-LPEMSEEDgmkVADlevkfaemdgYTAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 149 RLVMEAPDLLLLDEPTNNLDAAgraAIRalmreWRGGVLVA--------SHDRELLD-------DVDrILELtaigaRSF 213
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDIN---TIR-----WLEDVLNErnstmiiiSHDRHFLNsvcthmaDLD-YGEL-----RVY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 214 GGGWSAFSAARDEDRRRASAELERADADVRAVRQAVqarreakeRRdragraFAAKGSEPKillgaraeraqnsggtaQA 293
Cdd:PRK15064 234 PGNYDEYMTAATQARERLLADNAKKKAQIAELQSFV--------SR------FSANASKAK-----------------QA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 294 ISD-RRMGRALAEADDARSRVevlTPLTIALPPSGLPSgaNVLAMEGVVAEAGDRRL-GPWTLRIDGPERIALKGANGAG 371
Cdd:PRK15064 283 TSRaKQIDKIKLEEVKPSSRQ---NPFIRFEQDKKLHR--NALEVENLTKGFDNGPLfKNLNLLLEAGERLAIIGENGVG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 372 KTTLLRIAAGLRAPVSGTVRRAEgrivllDQQVGL--------LDPEGTILDNIRRLHPDAGDEEAY-ALCARFAFRNRD 442
Cdd:PRK15064 358 KTTLLRTLVGELEPDSGTVKWSE------NANIGYyaqdhaydFENDLTLFDWMSQWRQEGDDEQAVrGTLGRLLFSQDD 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 443 ARRVVGTLSGGERLRAglaaaLSGS---APPWLIILDEPTNHLDIESVEILENALLSFDGALLVVSHDPSFV 511
Cdd:PRK15064 432 IKKSVKVLSGGEKGRM-----LFGKlmmQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFV 498
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-507 |
1.08e-39 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 153.09 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 23 LTFAIGtERVGLVGRNGSGKSTLLRIVAGLAEPSsgtVRRTGTIGLLRQDMPGGWTLAEALGVANDLERLE------RIL 96
Cdd:PLN03073 198 VTLAFG-RHYGLVGRNGTGKTTFLRYMAMHAIDG---IPKNCQILHVEQEVVGDDTTALQCVLNTDIERTQlleeeaQLV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 97 A-----------GNGTAGDFDAAD--------------------WTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRV 145
Cdd:PLN03073 274 AqqrelefetetGKGKGANKDGVDkdavsqrleeiykrlelidaYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRI 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 146 GIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGGVLVASHDRELLDDV-DRILELTAIGARSFGGGWSAFSAAR 224
Cdd:PLN03073 354 ALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVvTDILHLHGQKLVTYKGDYDTFERTR 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 225 DEDRRRAsaeleradadvravrqavQARREAKERRDRAGRAFAAKgsepkilLGARAERAQNSGGTAQAISdrRMGRALA 304
Cdd:PLN03073 434 EEQLKNQ------------------QKAFESNERSRSHMQAFIDK-------FRYNAKRASLVQSRIKALD--RLGHVDA 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 305 EADDARSRVEVLTPltialppSGLPSGANVLAMEGVVAEAGdrrlGPWTLR-----IDGPERIALKGANGAGKTTLLRIA 379
Cdd:PLN03073 487 VVNDPDYKFEFPTP-------DDRPGPPIISFSDASFGYPG----GPLLFKnlnfgIDLDSRIAMVGPNGIGKSTILKLI 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 380 AGLRAPVSGTV-RRAEGRIVLLDQQ-VGLLDPEGTILDNIRRLHPDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLR 457
Cdd:PLN03073 556 SGELQPSSGTVfRSAKVRMAVFSQHhVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSR 635
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 518843096 458 AGLAAALSGSapPWLIILDEPTNHLDIESVEILENALLSFDGALLVVSHD 507
Cdd:PLN03073 636 VAFAKITFKK--PHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHD 683
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-220 |
2.07e-38 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 147.13 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRR--TGTIGLLRQD---MPGGWT 78
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRgDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgeTVKIGYFDQHqeeLDPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 79 LAEALGvandlerlerilagngtagdfDAADWTLESRIGAALAQVGLPAlplDRCL---RTLSGGERTRVGIARLVMEAP 155
Cdd:COG0488 396 VLDELR---------------------DGAPGGTEQEVRGYLGRFLFSG---DDAFkpvGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 156 DLLLLDEPTNNLDAAGRAAIRALMREWRGGVLVASHDRELLDDV-DRILELTAIGARSFGGGWSAF 220
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVaTRILEFEDGGVREYPGGYDDY 517
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-207 |
9.07e-37 |
|
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: 134.91 E-value: 9.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLRQDMPGGWT-LAE 81
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAgEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpIRDAREDYRRRLAyLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 82 ALGVANDL---ERLERILAGNGTAGDFDAADwtlesrigAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLL 158
Cdd:COG4133 83 ADGLKPELtvrENLRFWAALYGLRADREAID--------EALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518843096 159 LLDEPTNNLDAAGRAAIRALMREWR---GGVLVASHDrELLDDVDRILELTA 207
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQ-PLELAAARVLDLGD 204
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
353-522 |
1.28e-36 |
|
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: 132.57 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEG-RIVLLDQqvglldpegtildnirrlhpdagdeeaya 431
Cdd:cd03221 20 SLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvKIGYFEQ----------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 432 lcarfafrnrdarrvvgtLSGGERLRAGLAAALSGsaPPWLIILDEPTNHLDIESVEILENALLSFDGALLVVSHDPSFV 511
Cdd:cd03221 71 ------------------LSGGEKMRLALAKLLLE--NPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFL 130
|
170
....*....|.
gi 518843096 512 ERVgFDRVFEV 522
Cdd:cd03221 131 DQV-ATKIIEL 140
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-519 |
2.31e-36 |
|
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: 141.58 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAFLTLDSVCARTPDG--PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPS---SGTVR------------- 61
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGdvPAVDGVSLTIAPgETVALVGESGSGKSTLALALMGLLPHGgriSGEVLldgrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 62 RTGTIGLLRQD-------MPGGWTLAEALgVANDLERLERilagngtagdfdaadwtlESRIGAALAQVGLPALpLDRCL 134
Cdd:COG1123 81 RGRRIGMVFQDpmtqlnpVTVGDQIAEAL-ENLGLSRAEA------------------RARVLELLEAVGLERR-LDRYP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 135 RTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRG----GVLVASHDREL-LDDVDRILELtaig 209
Cdd:COG1123 141 HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRergtTVLLITHDLGVvAEIADRVVVM---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 210 arsfgggwsafsaardedRRRASAEleraDADVRAVRQAVQARREAKERRDRAGRAFAAKGSEPKILlgaraeraqnsgg 289
Cdd:COG1123 217 ------------------DDGRIVE----DGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLL------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 290 taqaisdrrmgralaEADDarsrvevltpLTIALPpsgLPSGANVLAMEGVvaeagdrrlgpwTLRIDGPERIALKGANG 369
Cdd:COG1123 262 ---------------EVRN----------LSKRYP---VRGKGGVRAVDDV------------SLTLRRGETLGLVGESG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 370 AGKTTLLRIAAGLRAPVSGTVR--------RAEGRIVLLDQQVGL--------LDPEGTILDNIR---RLHPDAGDEE-- 428
Cdd:COG1123 302 SGKSTLARLLLGLLRPTSGSILfdgkdltkLSRRSLRELRRRVQMvfqdpyssLNPRMTVGDIIAeplRLHGLLSRAErr 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 429 --AYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIeSV--EILEnaLL-----SFDG 499
Cdd:COG1123 382 erVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALE--PKLLILDEPTSALDV-SVqaQILN--LLrdlqrELGL 456
|
570 580
....*....|....*....|
gi 518843096 500 ALLVVSHDPSFVERVGfDRV 519
Cdd:COG1123 457 TYLFISHDLAVVRYIA-DRV 475
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-205 |
1.97e-33 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 126.68 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG-PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGLL 69
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKgEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlrelrrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 70 RQD------MPggwTLAE--ALGvandLERLerilagnGTAGDfdaadwTLESRIGAALAQVGLPALpLDRCLRTLSGGE 141
Cdd:COG1122 81 FQNpddqlfAP---TVEEdvAFG----PENL-------GLPRE------EIRERVEEALELVGLEHL-ADRPPHELSGGQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518843096 142 RTRVGIAR-LVMEaPDLLLLDEPTNNLDAAGRAAIRALMREWRG---GVLVASHDRELLDDV-DRILEL 205
Cdd:COG1122 140 KQRVAIAGvLAME-PEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELaDRVIVL 207
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-207 |
3.72e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.31 E-value: 3.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR-----RTGT--------IGLLR 70
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAgECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkpLSAMpppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 71 QD--MPGGwTLAEALgvandlerlERILAGNGTAGDFDAADwtlesrigAALAQVGLPALPLDRCLRTLSGGERTRVGIA 148
Cdd:COG4619 81 QEpaLWGG-TVRDNL---------PFPFQLRERKFDRERAL--------ELLERLGLPPDILDKPVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 149 RLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWR----GGVLVASHDRELLDDV-DRILELTA 207
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVaDRVLTLEA 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-205 |
1.47e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.82 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAFLTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------IGLLRQ 71
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPgEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 72 DMPGGW----TLAE--ALGvandlerlerILAGNGTAGDFDAADWTlesRIGAALAQVGLPALpLDRCLRTLSGGERTRV 145
Cdd:COG1121 83 RAEVDWdfpiTVRDvvLMG----------RYGRRGLFRRPSRADRE---AVDEALERVGLEDL-ADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 146 GIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRG---GVLVASHDRELLDD-VDRILEL 205
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREyFDRVLLL 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-205 |
2.86e-32 |
|
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: 122.96 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 7 LDSVCARTPDG--PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTV-------------RRTGTIGLLR 70
Cdd:cd03225 2 LKNLSFSYPDGarPALDDISLTIKKgEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklslkELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 71 QD------MPggwTLAE--ALGVANDLERLERIlagngtagdfdaadwtlESRIGAALAQVGLPALpLDRCLRTLSGGER 142
Cdd:cd03225 82 QNpddqffGP---TVEEevAFGLENLGLPEEEI-----------------EERVEEALELVGLEGL-RDRSPFTLSGGQK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 143 TRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRG---GVLVASHDRELLDDV-DRILEL 205
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELaDRVIVL 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
23-202 |
1.97e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 121.32 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 23 LTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT------------IGLLRQD--MPGGWTLAEALGVAN 87
Cdd:COG1131 19 VSLTVEPgEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQEpaLYPDLTVRENLRFFA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 88 DLERLERILAgngtagdfdaadwtlESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNL 167
Cdd:COG1131 99 RLYGLPRKEA---------------RERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 518843096 168 DAAGRAAIRALMREWRGG---VLVASHdreLLDDVDRI 202
Cdd:COG1131 163 DPEARRELWELLRELAAEgktVLLSTH---YLEEAERL 197
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-192 |
2.98e-31 |
|
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: 121.30 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGLLR 70
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPgEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 71 QD--MPGGWTLAE--ALGVANDLERLERIlagngTAGDFDAADWtlesrigaALAQVGLPALpLDRCLRTLSGGERTRVG 146
Cdd:COG1120 82 QEppAPFGLTVRElvALGRYPHLGLFGRP-----SAEDREAVEE--------ALERTGLEHL-ADRPVDELSGGERQRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518843096 147 IARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREW---RG-GVLVASHD 192
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLareRGrTVVMVLHD 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
18-205 |
1.61e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 118.02 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------IGLLRQ------DMPGgwTLAE- 81
Cdd:cd03235 13 PVLEDVSFEVKPgEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQrrsidrDFPI--SVRDv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 82 -ALGVANDLERLERIlagngTAGDFDAADwtlesrigAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLL 160
Cdd:cd03235 91 vLMGLYGHKGLFRRL-----SKADKAKVD--------EALERVGLSEL-ADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518843096 161 DEPTNNLDAAGRAAIRALMREWRG---GVLVASHDRELLDD-VDRILEL 205
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEyFDRVLLL 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
23-205 |
2.80e-30 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 118.37 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 23 LTFAIGtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR-------------RTGTIGLLRQDMPG--------GWTLAE 81
Cdd:COG1124 26 LEVAPG-ESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrrrrkaFRRRVQMVFQDPYAslhprhtvDRILAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 82 ALgvandleRLERILAgngtagdfdaadwtLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLD 161
Cdd:COG1124 105 PL-------RIHGLPD--------------REERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518843096 162 EPTNNLDAAGRAAIRAL---MREWRG-GVLVASHDRELLDDV-DRILEL 205
Cdd:COG1124 164 EPTSALDVSVQAEILNLlkdLREERGlTYLFVSHDLAVVAHLcDRVAVM 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-205 |
5.69e-28 |
|
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: 109.26 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 6 TLDSVCARTPDGPLFQKLTFAIG-TERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigllrqdmpggwtlaEALG 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKaGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG----------------KDIA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 85 VANDLERLERIlagngtagdfdaadwtlesrigAALAQvglpalpldrclrtLSGGERTRVGIARLVMEAPDLLLLDEPT 164
Cdd:cd00267 65 KLPLEELRRRI----------------------GYVPQ--------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518843096 165 NNLDAAGRAAIRALMREWRGG---VLVASHDRELLDDV-DRILEL 205
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEgrtVIIVTHDPELAELAaDRVIVL 153
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
30-205 |
5.98e-28 |
|
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: 111.04 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTigLLRQDMPGGWTL--AEALGVA-------NDLERLERILAGNG 100
Cdd:cd03255 31 EFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT--DISKLSEKELAAfrRRHIGFVfqsfnllPDLTALENVELPLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 101 TAGDFDAADwtlESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMR 180
Cdd:cd03255 109 LAGVPKKER---RERAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLR 184
|
170 180
....*....|....*....|....*....
gi 518843096 181 E---WRG-GVLVASHDRELLDDVDRILEL 205
Cdd:cd03255 185 ElnkEAGtTIVVVTHDPELAEYADRIIEL 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-205 |
3.48e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.09 E-value: 3.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 13 RTPDGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG--TIGLLRQDMPGGWTL------AEAL 83
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLtAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSEVPDSLpltvrdLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 84 GVANDLERLERIlagngtagdfDAADwtlESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEP 163
Cdd:NF040873 81 GRWARRGLWRRL----------TRDD---RAAVDDALERVGLADL-AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518843096 164 TNNLDAAGRAAIRALMREWRG---GVLVASHDRELLDDVDRILEL 205
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-192 |
4.06e-27 |
|
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: 107.52 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 6 TLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTigllrqdmpggwtlaealg 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAgEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 85 vanDLERLERIlagngtagdfdaadwTLESRIG---AALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLD 161
Cdd:cd03214 62 ---DLASLSPK---------------ELARKIAyvpQALELLGLAHL-ADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190
....*....|....*....|....*....|....*
gi 518843096 162 EPTNNLDAAGRAA----IRALMREWRGGVLVASHD 192
Cdd:cd03214 123 EPTSHLDIAHQIEllelLRRLARERGKTVVMVLHD 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
353-519 |
4.29e-27 |
|
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: 109.56 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV-----------RRAEGRIVLLDQQVGLldPEG-TILDNIR-- 418
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedvrkepREARRQIGVLPDERGL--YDRlTVRENIRyf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 -RLHPDAGDE---EAYALCARFAFRNrDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENAL 494
Cdd:COG4555 99 aELYGLFDEElkkRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPK--VLLLDEPTNGLDVMARRLLREIL 175
|
170 180
....*....|....*....|....*...
gi 518843096 495 LSF---DGALLVVSHDPSFVERVgFDRV 519
Cdd:COG4555 176 RALkkeGKTVLFSSHIMQEVEAL-CDRV 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-165 |
6.14e-27 |
|
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: 106.19 E-value: 6.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--IGLLRQDMPGGW-TLAEALGVANDLERLERILAGNGTAGDFD 106
Cdd:pfam00005 12 EILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdlTDDERKSLRKEIgYVFQDPQLFPRLTVRENLRLGLLLKGLSK 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 107 AADwtlESRIGAALAQVGLPAL---PLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:pfam00005 92 REK---DARAEEALEKLGLGDLadrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
16-203 |
6.67e-27 |
|
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: 108.79 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 16 DGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVR------RTGTIGLLRQdmpggwtlaeaLGVAND 88
Cdd:COG4555 13 KVPALKDVSFTAKDGEItGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvRKEPREARRQ-----------IGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 89 lerlERILAGNGTA-----------GDFDAAdwtLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDL 157
Cdd:COG4555 82 ----ERGLYDRLTVreniryfaelyGLFDEE---LKKRIEELIELLGLEEF-LDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518843096 158 LLLDEPTNNLDAAGRAAIRALMREWRG---GVLVASHDRELLDDV-DRIL 203
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALcDRVV 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
23-205 |
7.06e-27 |
|
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: 106.71 E-value: 7.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 23 LTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigllrQDMPggwtlaealgvandlERLERILagngt 101
Cdd:cd03230 19 ISLTVEKgEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIK---------------KEPEEVK----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 102 agdfdaadwtleSRIGAALAQVGLPA-LPLDRCLRtLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMR 180
Cdd:cd03230 73 ------------RRIGYLPEEPSLYEnLTVRENLK-LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLR 139
|
170 180
....*....|....*....|....*....
gi 518843096 181 EWR---GGVLVASHDRELLDDV-DRILEL 205
Cdd:cd03230 140 ELKkegKTILLSSHILEEAERLcDRVAIL 168
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-205 |
8.07e-27 |
|
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: 109.02 E-value: 8.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 2 SAFLTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGtvrrtGTIGLLRQDMpGGWTLA 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPgEHWAILGPNGAGKSTLLSLITGDLPPTYG-----NDVRLFGERR-GGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 81 E---ALGV-----ANDLERLERIL-----AGNGTAGDFDAADWTLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGI 147
Cdd:COG1119 75 ElrkRIGLvspalQLRFPRDETVLdvvlsGFFDSIGLYREPTDEQRERARELLELLGLAHL-ADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518843096 148 ARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG-----VLVASHDRELLDDVDRILEL 205
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaptlVLVTHHVEEIPPGITHVLLL 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
30-203 |
1.12e-26 |
|
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: 113.07 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT----------------IGLLRQD--------MPGGWTLAEALGV 85
Cdd:COG1123 292 ETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsrrslrelrrrVQMVFQDpysslnprMTVGDIIAEPLRL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 ANDLERLERilagngtagdfdaadwtlESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIAR-LVMEaPDLLLLDEPT 164
Cdd:COG1123 372 HGLLSRAER------------------RERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARaLALE-PKLLILDEPT 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518843096 165 NNLDAAGRAAIRALMREWR----GGVLVASHDRELLDDV-DRIL 203
Cdd:COG1123 433 SALDVSVQAQILNLLRDLQrelgLTYLFISHDLAVVRYIaDRVA 476
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-205 |
1.18e-26 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 114.16 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG--PLFQKLTFAI--GtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTV---------------RRTgt 65
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIkpG-ERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpaslRRQ-- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 66 IGLLRQD---MPGgwTLAEalgvaNdlerlerILAGNGTAGDfdaadwtleSRIGAALAQVGL----PALP--LDRCL-- 134
Cdd:COG2274 551 IGVVLQDvflFSG--TIRE-----N-------ITLGDPDATD---------EEIIEAARLAGLhdfiEALPmgYDTVVge 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 135 --RTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRILEL 205
Cdd:COG2274 608 ggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTIRLADRIIVL 682
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
30-203 |
2.21e-26 |
|
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: 106.82 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR----------------RTGTIGLLRQD--------MPGGWTLAEALGV 85
Cdd:cd03257 32 ETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdllklsrrlrkiRRKEIQMVFQDpmsslnprMTIGEQIAEPLRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 ANDLERLERILAgngtagdfdaadwtlesRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIAR-LVMEaPDLLLLDEPT 164
Cdd:cd03257 112 HGKLSKKEARKE-----------------AVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARaLALN-PKLLIADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518843096 165 NNLDAAGRAAIRALMREWR----GGVLVASHDRELLDDV-DRIL 203
Cdd:cd03257 174 SALDVSVQAQILDLLKKLQeelgLTLLFITHDLGVVAKIaDRVA 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
334-514 |
5.19e-26 |
|
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: 105.25 E-value: 5.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 334 VLAMEGVVAEAGDRRL-GPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-----------RAEGRIVLLD 401
Cdd:COG4133 2 MLEAENLSCRRGERLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngepirdareDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 402 QQVGlLDPEGTILDNIR---RLHPDAGDEEA-YALCARFAFRNRDARRvVGTLSGGERLRAGLAAALSGSAPpwLIILDE 477
Cdd:COG4133 82 HADG-LKPELTVRENLRfwaALYGLRADREAiDEALEAVGLAGLADLP-VRQLSAGQKRRVALARLLLSPAP--LWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518843096 478 PTNHLDIESVEILENALLSF---DGALLVVSHDPSFVERV 514
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAA 197
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-205 |
9.90e-26 |
|
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: 103.23 E-value: 9.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG--PLFQKLTFAI--GtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTigllrqdmpggwtla 80
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIkpG-EKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 81 ealgvanDLErlerilagngtagDFDAADWTleSRIGAALAQVGLpalpLDRCLRT--LSGGERTRVGIARLVMEAPDLL 158
Cdd:cd03228 65 -------DLR-------------DLDLESLR--KNIAYVPQDPFL----FSGTIREniLSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518843096 159 LLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRILEL 205
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGktVIVIAHRLSTIRDADRIIVL 167
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-205 |
1.52e-25 |
|
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: 110.23 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG-PLFQKLTFAI-GTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGLL 69
Cdd:COG4988 337 IELEDVSFSYPGGrPALDGLSLTIpPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 70 RQD---MPGgwTLAEALGVANDlerlerilagngtagdfDAADWTLEsrigAALAQVGL----PALP--LDRCL----RT 136
Cdd:COG4988 417 PQNpylFAG--TIRENLRLGRP-----------------DASDEELE----AALEAAGLdefvAALPdgLDTPLgeggRG 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518843096 137 LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRILEL 205
Cdd:COG4988 474 LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQADRILVL 544
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-205 |
2.75e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 103.97 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAFLTLDSVCARTPDG----PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR-------------- 61
Cdd:COG1136 1 MSPLLELRNLTKSYGTGegevTALRGVSLSIEAgEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslserel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 62 ---RTGTIGLLRQD---MPGgWTLAE--ALGvandlerleRILAGNGTAGDfdaadwtlESRIGAALAQVGLPALpLDRC 133
Cdd:COG1136 81 arlRRRHIGFVFQFfnlLPE-LTALEnvALP---------LLLAGVSRKER--------RERARELLERVGLGDR-LDHR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 134 LRTLSGGERTRVGIAR-LVMEaPDLLLLDEPTNNLDAAGRAAIRALMREW--RGG--VLVASHDRELLDDVDRILEL 205
Cdd:COG1136 142 PSQLSGGQQQRVAIARaLVNR-PKLILADEPTGNLDSKTGEEVLELLRELnrELGttIVMVTHDPELAARADRVIRL 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
32-191 |
3.58e-25 |
|
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: 103.07 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-----TIGLLRQ-----DMPGgwtLAEALGVANDLERLERILAGNgt 101
Cdd:cd03268 29 YGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyqkNIEALRRigaliEAPG---FYPNLTARENLRLLARLLGIR-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 102 agdfdaadwtlESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMRE 181
Cdd:cd03268 104 -----------KKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILS 171
|
170
....*....|...
gi 518843096 182 WR---GGVLVASH 191
Cdd:cd03268 172 LRdqgITVLISSH 184
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
353-519 |
1.77e-24 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 101.68 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-----------RAEGRIVLLDQQVGlLDPEGTILDNIR--- 418
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardpaEVRRRIGYVPQEPA-LYPDLTVRENLRffa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 RLHP---DAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALL 495
Cdd:COG1131 99 RLYGlprKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPE--LLILDEPTSGLDPEARRELWELLR 175
|
170 180
....*....|....*....|....*..
gi 518843096 496 SF---DGALLVVSHDPSFVERVgFDRV 519
Cdd:COG1131 176 ELaaeGKTVLLSTHYLEEAERL-CDRV 201
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-226 |
2.15e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.82 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG-PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLL----RQDMPGGwT 78
Cdd:COG4178 363 LALEDLTLRTPDGrPLLEDLSLSLKPgERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLflpqRPYLPLG-T 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 79 LAEALgvandlerlerilAGNGTAGDFDaadwtlESRIGAALAQVGLPALP--LDRCL---RTLSGGERTRVGIARLVME 153
Cdd:COG4178 442 LREAL-------------LYPATAEAFS------DAELREALEAVGLGHLAerLDEEAdwdQVLSLGEQQRLAFARLLLH 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 154 APDLLLLDEPTNNLDAAGRAAIRALMRE--WRGGVLVASHDRELLDDVDRILELTAigarsfGGGWSAFSAARDE 226
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGHRSTLAAFHDRVLELTG------DGSWQLLPAEAPA 571
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-203 |
4.85e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 100.36 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 21 QKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGLLRQD---MPGgwTLAEAL 83
Cdd:cd03245 21 DNVSLTIRAgEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldpadlrrnIGYVPQDvtlFYG--TLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 84 GVANDLERLERILAGNGTAGdfdAADWTLESRIGAALaQVGlpalplDRClRTLSGGERTRVGIARLVMEAPDLLLLDEP 163
Cdd:cd03245 99 TLGAPLADDERILRAAELAG---VTDFVNKHPNGLDL-QIG------ERG-RGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518843096 164 TNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRIL 203
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLVDRII 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
353-521 |
7.05e-24 |
|
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: 99.49 E-value: 7.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR---------RAEGRIVLLDQQVGL------LDPEGTILDNI 417
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisklSEKELAAFRRRHIGFvfqsfnLLPDLTALENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 ------RRLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILE 491
Cdd:cd03255 104 elplllAGVPKKERRERAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALAND--PKIILADEPTGNLDSETGKEVM 180
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 492 NALLSF---DG-ALLVVSHDPSFVERvgFDRVFE 521
Cdd:cd03255 181 ELLRELnkeAGtTIVVVTHDPELAEY--ADRIIE 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
353-519 |
9.49e-24 |
|
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: 97.85 E-value: 9.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-----------RAEGRIVLLDQQVGLLdPEGTILDNIRrlh 421
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdikkepeEVKRRIGYLPEEPSLY-ENLTVRENLK--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 422 pdagdeeayalcarfafrnrdarrvvgtLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSF---D 498
Cdd:cd03230 96 ----------------------------LSGGMKQRLALAQALLHDPE--LLILDEPTSGLDPESRREFWELLRELkkeG 145
|
170 180
....*....|....*....|.
gi 518843096 499 GALLVVSHDPSFVERVgFDRV 519
Cdd:cd03230 146 KTILLSSHILEEAERL-CDRV 165
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-205 |
1.03e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 99.36 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG-PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR---------RTGTIGLLRQDM 73
Cdd:COG2884 2 IRFENVSKRYPGGrEALSDVSLEIEKgEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 74 pG----------GWTLAE----ALGVAndlerlerilagnGTAGDfdaadwTLESRIGAALAQVGLP----ALPldrclR 135
Cdd:COG2884 82 -GvvfqdfrllpDRTVYEnvalPLRVT-------------GKSRK------EIRRRVREVLDLVGLSdkakALP-----H 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 136 TLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREW-RGG--VLVASHDRELLDDVD-RILEL 205
Cdd:COG2884 137 ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGttVLIATHDLELVDRMPkRVLEL 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-207 |
1.10e-23 |
|
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: 104.46 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG--PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLRQDmpggwTLA 80
Cdd:COG4987 334 LELEDVSFRYPGAgrPVLDGLSLTLPPgERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdLRDLDED-----DLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 81 EALGVANDLERL------ERILAGNGTAGDfdaadwtleSRIGAALAQVGLP----ALP--LDRCL----RTLSGGERTR 144
Cdd:COG4987 409 RRIAVVPQRPHLfdttlrENLRLARPDATD---------EELWAALERVGLGdwlaALPdgLDTWLgeggRRLSGGERRR 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 145 VGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRILELTA 207
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLERMDRILVLED 544
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
353-520 |
1.54e-23 |
|
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: 104.53 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV---------------RRaegRIVLLDQQVGLLdpEGTILDNI 417
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpaslRR---QIGVVLQDVFLF--SGTIRENI 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 RRLHPDAGDEEAYAlCARFAFRNRDARR-------VVG----TLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIES 486
Cdd:COG2274 570 TLGDPDATDEEIIE-AARLAGLHDFIEAlpmgydtVVGeggsNLSGGQRQRLAIARALLRNPR--ILILDEATSALDAET 646
|
170 180 190
....*....|....*....|....*....|....*.
gi 518843096 487 VEILENALLSFDG--ALLVVSHDPSFVERVgfDRVF 520
Cdd:COG2274 647 EAIILENLRRLLKgrTVIIIAHRLSTIRLA--DRII 680
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-207 |
1.71e-23 |
|
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: 99.05 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCAR--TPDGPL--FQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLRQDMPGGWt 78
Cdd:COG4181 9 IELRGLTKTvgTGAGELtiLKGISLEVEAgESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdLFALDEDARARL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 79 LAEALG-----------------VANDLERlerilagngtAGDFDAADwtlesRIGAALAQVGLPALpLDRCLRTLSGGE 141
Cdd:COG4181 88 RARHVGfvfqsfqllptltalenVMLPLEL----------AGRRDARA-----RARALLERVGLGHR-LDHYPAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 142 RTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREW---RGGVLV-ASHDRELLDDVDRILELTA 207
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnreRGTTLVlVTHDPALAARCDRVLRLRA 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
11-205 |
1.74e-23 |
|
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: 97.81 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 11 CARTPDgPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQDMPGGWT--LAEALGVAN 87
Cdd:TIGR01189 8 CSRGER-MLFEGLSFTLNAgEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlyLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 88 DLERLERIlagngtagDFDAADWTLESR-IGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNN 166
Cdd:TIGR01189 87 ELSALENL--------HFWAAIHGGAQRtIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518843096 167 LDAAGRAAIRALMREW--RGGVLVASHDRELLDDVDRILEL 205
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHlaRGGIVLLTTHQDLGLVEARELRL 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
30-204 |
2.04e-23 |
|
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: 97.26 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTigllrqdmpggwtlaealgvanDLERLERILAgngtagdfdaad 109
Cdd:cd03229 27 EIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE----------------------DLTDLEDELP------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 110 wTLESRIGAALAQVGLPALP--LDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG-- 185
Cdd:cd03229 73 -PLRRRIGMVFQDFALFPHLtvLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlg 151
|
170 180
....*....|....*....|.
gi 518843096 186 --VLVASHDrelLDDVDRILE 204
Cdd:cd03229 152 itVVLVTHD---LDEAARLAD 169
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
2.73e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 99.01 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAFLTLDSVCAR--TPDGPL--FQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------IG 67
Cdd:COG1116 4 AAPALELRGVSKRfpTGGGGVtaLDDVSLTVAAgEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 68 LLRQD---MPggW-TLAE--ALGV-ANDLERLERilagngtagdfdaadwtlESRIGAALAQVGLP----ALPldrclRT 136
Cdd:COG1116 84 VVFQEpalLP--WlTVLDnvALGLeLRGVPKAER------------------RERARELLELVGLAgfedAYP-----HQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 137 LSGGERTRVGIAR-LVMEaPDLLLLDEPTNNLDAAGRAAIRALMRE-WRGG---VLVASHDRE---LLddVDRILELTAI 208
Cdd:COG1116 139 LSGGMRQRVAIARaLAND-PEVLLMDEPFGALDALTRERLQDELLRlWQETgktVLFVTHDVDeavFL--ADRVVVLSAR 215
|
...
gi 518843096 209 GAR 211
Cdd:COG1116 216 PGR 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-200 |
5.10e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 96.88 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG------------TIGLLRQD 72
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 73 MPG--GWTLAEALgvaNDLERLERIlagngtagdfdaADWTLESRIGAALAQVGLpALPLDRCLRTLSGGERTRVGIARL 150
Cdd:cd03264 81 FGVypNFTVREFL---DYIAWLKGI------------PSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518843096 151 VMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHdreLLDDVD 200
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDriVILSTH---IVEDVE 193
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-194 |
5.41e-23 |
|
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: 96.82 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------IGLLRQD 72
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPgEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 73 mpggWTLAEALGVAndlerlERILAGnGTAGDFDAADWtlESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIAR-LV 151
Cdd:cd03259 81 ----YALFPHLTVA------ENIAFG-LKLRGVPKAEI--RARVRELLELVGLEGL-LNRYPHELSGGQQQRVALARaLA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518843096 152 MEaPDLLLLDEPTNNLDAAGRAAIRALMRE-WRGG---VLVASHDRE 194
Cdd:cd03259 147 RE-PSLLLLDEPLSALDAKLREELREELKElQRELgitTIYVTHDQE 192
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-203 |
5.82e-23 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 97.82 E-value: 5.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG-PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT----------------I 66
Cdd:COG3638 3 LELRNLSKRYPGGtPALDDVSLEIERgEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdvtalrgralrrlrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 67 GLLRQDMPggwtLAEALGVandlerLERILAGN--------GTAGDFDAADwtlesRIGA--ALAQVGLPALPLDRClRT 136
Cdd:COG3638 83 GMIFQQFN----LVPRLSV------LTNVLAGRlgrtstwrSLLGLFPPED-----RERAleALERVGLADKAYQRA-DQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 137 LSGGERTRVGIARLVMEAPDLLLLDEPTNNLD-AAGR---AAIRALMREWRGGVLVASHDREL-LDDVDRIL 203
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDpKTARqvmDLLRRIAREDGITVVVNLHQVDLaRRYADRII 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
353-519 |
5.98e-22 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 92.31 E-value: 5.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLrapvsgtVRRAEGRIVLLDQQVGLLDPEgtildnirrlhpdagdeeayal 432
Cdd:cd00267 19 SLTLKAGEIVALVGPNGSGKSTLLRAIAGL-------LKPTSGEILIDGKDIAKLPLE---------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 433 carfafRNRDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSF---DGALLVVSHDPS 509
Cdd:cd00267 70 ------ELRRRIGYVPQLSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPE 141
|
170
....*....|
gi 518843096 510 FVERVgFDRV 519
Cdd:cd00267 142 LAELA-ADRV 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
353-520 |
1.11e-21 |
|
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: 93.55 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-----RAEGRIVLLDQQVGLL--DPE-----GTILDNI--- 417
Cdd:COG1122 21 SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkdITKKNLRELRRKVGLVfqNPDdqlfaPTVEEDVafg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 ---RRLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESVEILENAL 494
Cdd:COG1122 101 penLGLPREEIRERVEEALELVGLEHL-ADRPPHELSGGQKQRVAIAGVL--AMEPEVLVLDEPTAGLDPRGRRELLELL 177
|
170 180
....*....|....*....|....*....
gi 518843096 495 LSFDGA---LLVVSHDPSFVERVgFDRVF 520
Cdd:COG1122 178 KRLNKEgktVIIVTHDLDLVAEL-ADRVI 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
353-519 |
1.33e-21 |
|
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: 92.92 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD-----QQVGLL--DPEG-----TILDNI--- 417
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkelrRKVGLVfqNPDDqffgpTVEEEVafg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 ---RRLHPDAGDEEAYALCARF---AFRNRDarrvVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILE 491
Cdd:cd03225 101 lenLGLPEEEIEERVEEALELVgleGLRDRS----PFTLSGGQKQRVAIAGVLAMDPD--ILLLDEPTAGLDPAGRRELL 174
|
170 180 190
....*....|....*....|....*....|.
gi 518843096 492 NALLSFDGA---LLVVSHDPSFVERVgFDRV 519
Cdd:cd03225 175 ELLKKLKAEgktIIIVTHDLDLLLEL-ADRV 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
360-480 |
2.21e-21 |
|
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: 90.40 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTV------------RRAEGRIVLLDQQVGlLDPEGTILDNIR------RLH 421
Cdd:pfam00005 12 EILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltdderKSLRKEIGYVFQDPQ-LFPRLTVRENLRlglllkGLS 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 422 PDAGDEEAYALCARFA---FRNRDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTN 480
Cdd:pfam00005 91 KREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPK--LLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
329-520 |
3.46e-21 |
|
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: 96.75 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 329 PSGANVLAMEGVVAEAGDRR--LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-----RAEGRIVLLD 401
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGGRpaLDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdLSDLDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 402 QQVGLLD-----PEGTILDNIRRLHPDAGDEEAYALCARFAFRNRDARR------VVG----TLSGGERLRAGLAAALSG 466
Cdd:COG4988 411 RQIAWVPqnpylFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALpdgldtPLGeggrGLSGGQAQRLALARALLR 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 467 SAPpwLIILDEPTNHLDIESVEILENALLSF--DGALLVVSHDPSFVERvgFDRVF 520
Cdd:COG4988 491 DAP--LLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQ--ADRIL 542
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
30-211 |
3.81e-21 |
|
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: 91.76 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------IGLLRQD---MPggW-TLAE--ALGV-ANDLERLER 94
Cdd:cd03293 31 EFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQdalLP--WlTVLDnvALGLeLQGVPKAEA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 95 ilagngtagdfdaadwtlESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA 174
Cdd:cd03293 109 ------------------RERAEELLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518843096 175 IRALM----REWRGGVLVASHDrelLDDV----DRILELTAIGAR 211
Cdd:cd03293 170 LQEELldiwRETGKTVLLVTHD---IDEAvflaDRVVVLSARPGR 211
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-205 |
3.82e-21 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 92.03 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPL----FQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT---------IGLLR 70
Cdd:TIGR02211 2 LKCENLGKRYQEGKLdtrvLKGVSLSIGKgEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQslsklssneRAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 71 QdmpggwtlaEALG-------VANDLERLERI----LAGNGTAGDfdaadwtLESRIGAALAQVGLPAlPLDRCLRTLSG 139
Cdd:TIGR02211 82 N---------KKLGfiyqfhhLLPDFTALENVamplLIGKKSVKE-------AKERAYEMLEKVGLEH-RINHRPSELSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 140 GERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALM----REWRGGVLVASHDRELLDDVDRILEL 205
Cdd:TIGR02211 145 GERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMlelnRELNTSFLVVTHDLELAKKLDRVLEM 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
30-205 |
5.51e-21 |
|
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: 91.16 E-value: 5.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTV----------RRTGTIGLLRQDMpgGWTLAEAlGVANDLerleRILAGN 99
Cdd:cd03226 27 EIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikakERRKSIGYVMQDV--DYQLFTD-SVREEL----LLGLKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 GTAGDFDAADwtlesrigaALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALM 179
Cdd:cd03226 100 LDAGNEQAET---------VLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELI 169
|
170 180 190
....*....|....*....|....*....|
gi 518843096 180 REWRG---GVLVASHDRELLDDV-DRILEL 205
Cdd:cd03226 170 RELAAqgkAVIVITHDYEFLAKVcDRVLLL 199
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-196 |
6.54e-21 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 96.47 E-value: 6.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 15 PDGP-LFQKLTFAIGTE-RVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--IGLLRQDMPGGWTLAealgvANDLE 90
Cdd:PLN03073 519 PGGPlLFKNLNFGIDLDsRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvrMAVFSQHHVDGLDLS-----SNPLL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 91 RLERILAGngtagdfdaadwTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA- 169
Cdd:PLN03073 594 YMMRCFPG------------VPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLd 661
|
170 180
....*....|....*....|....*..
gi 518843096 170 AGRAAIRALMReWRGGVLVASHDRELL 196
Cdd:PLN03073 662 AVEALIQGLVL-FQGGVLMVSHDEHLI 687
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
11-191 |
1.03e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.32 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 11 CARTPDgPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTigllRQDMPGGWTLA--------- 80
Cdd:PRK13539 10 CVRGGR-VLFSGLSFTLAAgEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG----DIDDPDVAEAChylghrnam 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 81 -EALGVANDLERLERILAGNgtagdfdaadwtlESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLL 159
Cdd:PRK13539 85 kPALTVAENLEFWAAFLGGE-------------ELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*
gi 518843096 160 LDEPTNNLDAAGRAAIRALMREW--RGG-VLVASH 191
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRAHlaQGGiVIAATH 185
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-194 |
2.15e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 89.66 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 22 KLTFAIGTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------------IGLLRQDmpggWTLAEALG 84
Cdd:cd03297 16 KIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQ----YALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 85 VANDLERlerilagnGTAGDFDAADWTLESRIgaaLAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPT 164
Cdd:cd03297 92 VRENLAF--------GLKRKRNREDRISVDEL---LDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 165 NNLDAAGRAAIRALMRE----WRGGVLVASHDRE 194
Cdd:cd03297 160 SALDRALRLQLLPELKQikknLNIPVIFVTHDLS 193
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-210 |
2.86e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.08 E-value: 2.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEP---SSGTVRRTGT-----------IGLL 69
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPgEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRrltalpaeqrrIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 70 RQDMP--GGWTLAE--ALGVANDLERLERilagngtagdfdaadwtlESRIGAALAQVGLPALPlDRCLRTLSGGERTRV 145
Cdd:COG4136 82 FQDDLlfPHLSVGEnlAFALPPTIGRAQR------------------RARVEQALEEAGLAGFA-DRDPATLSGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518843096 146 GIARLVMEAPDLLLLDEPTNNLDAAGRAAIRAL----MREWRGGVLVASHDRELLDDVDRILELTAIGA 210
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQH 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-191 |
4.12e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.32 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLR----QDMPggWtLAEALGVANDLER 91
Cdd:PRK13538 15 ILFSGLSFTLNAgELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpIRRQRdeyhQDLL--Y-LGHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 92 LERILAGNGTAGDFDAADwtlesrIGAALAQVGL------PAlpldrclRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEA------LWEALAQVGLagfedvPV-------RQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 518843096 166 NLDAAGRAAIRALMREW--RGG-VLVASH 191
Cdd:PRK13538 159 AIDKQGVARLEALLAQHaeQGGmVILTTH 187
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
5-205 |
4.35e-20 |
|
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: 93.57 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG--PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-------------TIGL 68
Cdd:TIGR01842 317 LSVENVTIVPPGGkkPTLRGISFSLQAgEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 69 LRQD---MPGgwTLAEALGVANDLERLERILAGNGTAGdfdAADWTL------ESRIGAALAqvglpalpldrclrTLSG 139
Cdd:TIGR01842 397 LPQDvelFPG--TVAENIARFGENADPEKIIEAAKLAG---VHELILrlpdgyDTVIGPGGA--------------TLSG 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518843096 140 GERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWR---GGVLVASHDRELLDDVDRILEL 205
Cdd:TIGR01842 458 GQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLGCVDKILVL 526
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
353-520 |
4.57e-20 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 87.49 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD-----QQVGLLdpeGTILDNIRRLHpdagde 427
Cdd:cd03214 19 SLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSpkelaRKIAYV---PQALELLGLAH------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 428 eayalcarFAFRNrdarrvVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDI-ESVEILEnaLL-----SFDGAL 501
Cdd:cd03214 90 --------LADRP------FNELSGGERQRVLLARALAQEPP--ILLLDEPTSHLDIaHQIELLE--LLrrlarERGKTV 151
|
170
....*....|....*....
gi 518843096 502 LVVSHDPSFVERVGfDRVF 520
Cdd:cd03214 152 VMVLHDLNLAARYA-DRVI 169
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-205 |
4.65e-20 |
|
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: 88.62 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--IGLLRQDMPggwTLAEALGVANDLERLerILAGNGtagdFDA 107
Cdd:cd03292 28 EFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvSDLRGRAIP---YLRRKIGVVFQDFRL--LPDRNV----YEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 108 ADWTLE----------SRIGAALAQVGLP----ALPLDrclrtLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRA 173
Cdd:cd03292 99 VAFALEvtgvppreirKRVPAALELVGLShkhrALPAE-----LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 518843096 174 AIRALMREW--RGG-VLVASHDRELLDDVD-RILEL 205
Cdd:cd03292 174 EIMNLLKKInkAGTtVVVATHAKELVDTTRhRVIAL 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
353-520 |
5.34e-20 |
|
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: 87.05 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR----------RAE--GRIVLLDQQVGLLDpeGTILDNIrrl 420
Cdd:cd03228 22 SLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdldLESlrKNIAYVPQDPFLFS--GTIRENI--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 421 hpdagdeeayalcarfafrnrdarrvvgtLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSFDG- 499
Cdd:cd03228 97 -----------------------------LSGGQRQRIAIARALLRDPP--ILILDEATSALDPETEALILEALRALAKg 145
|
170 180
....*....|....*....|..
gi 518843096 500 -ALLVVSHDPSFVERvgFDRVF 520
Cdd:cd03228 146 kTVIVIAHRLSTIRD--ADRII 165
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-205 |
6.45e-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: 86.89 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG--PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIglLRQDMPGGWtlAE 81
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPgESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAD--ISQWDPNEL--GD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 82 ALG-VANDLERLERILAGNgtagdfdaadwtlesrigaalaqvglpalpldrclrTLSGGERTRVGIARLVMEAPDLLLL 160
Cdd:cd03246 77 HVGyLPQDDELFSGSIAEN------------------------------------ILSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518843096 161 DEPTNNLDAAGRAAIRAL---MREWRGGVLVASHDRELLDDVDRILEL 205
Cdd:cd03246 121 DEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLASADRILVL 168
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
34-205 |
7.28e-20 |
|
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: 88.07 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT---------IGLLRQDMpggwtlaealGVANDLERL--ERILAGN--- 99
Cdd:TIGR02673 33 LTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnrlrgrqLPLLRRRI----------GVVFQDFRLlpDRTVYENval 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 --GTAGDfDAADWtlESRIGAALAQVGLP----ALPLdrclrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRA 173
Cdd:TIGR02673 103 plEVRGK-KEREI--QRRVGAALRQVGLEhkadAFPE-----QLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSE 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 518843096 174 AIRALMREW--RG-GVLVASHDRELLDDVD-RILEL 205
Cdd:TIGR02673 175 RILDLLKRLnkRGtTVIVATHDLSLVDRVAhRVIIL 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-202 |
7.61e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.27 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------IGLLRQD- 72
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFDLTIAAG-ERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQEn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 73 -----MpggwTLAE--ALGVANDLeRLerilagngtagdfDAADWtleSRIGAALAQVGLPALpLDRCLRTLSGGERTRV 145
Cdd:COG3840 81 nlfphL----TVAQniGLGLRPGL-KL-------------TAEQR---AQVEQALERVGLAGL-LDRLPGQLSGGQRQRV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 146 GIAR-LVMEAPdLLLLDEPTNNLDAAGRAAIRALMREWRG----GVLVASHDrelLDDVDRI 202
Cdd:COG3840 139 ALARcLVRKRP-ILLLDEPFSALDPALRQEMLDLVDELCRerglTVLMVTHD---PEDAARI 196
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
30-168 |
1.28e-19 |
|
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: 88.01 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT----------------IGLLRQDMPggwtLAEALGVA-NDLE-R 91
Cdd:cd03256 28 EFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQFN----LIERLSVLeNVLSgR 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 92 LERILAGNGTAGDFDAADwtlESRIGAALAQVGLPALPLDRClRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD 168
Cdd:cd03256 104 LGRRSTWRSLFGLFPKEE---KQRALAALERVGLLDKAYQRA-DQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
30-205 |
1.70e-19 |
|
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: 87.20 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLrqdmpggwtLAEALGVANDL---ERLERILAGNGTAGDFD 106
Cdd:cd03220 49 ERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL---------LGLGGGFNPELtgrENIYLNGRLLGLSRKEI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 107 AA--DWTLE-SRIGAAlaqvglpalpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWR 183
Cdd:cd03220 120 DEkiDEIIEfSELGDF----------IDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELL 189
|
170 180
....*....|....*....|....*.
gi 518843096 184 ---GGVLVASHDRELLDDV-DRILEL 205
Cdd:cd03220 190 kqgKTVILVSHDPSSIKRLcDRALVL 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-194 |
2.47e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.39 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAFLTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------IGL 68
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPgEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 69 LRQD------MpggwTLAE--ALGvandLERLerilagngtagDFDAADwtLESRIGAALAQVGLPALpLDRCLRTLSGG 140
Cdd:COG3842 82 VFQDyalfphL----TVAEnvAFG----LRMR-----------GVPKAE--IRARVAELLELVGLEGL-ADRYPHQLSGG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518843096 141 ERTRVGIAR-LVMEaPDLLLLDEPTNNLDAAGRAA----IRALMREWRGGVLVASHDRE 194
Cdd:COG3842 140 QQQRVALARaLAPE-PRVLLLDEPLSALDAKLREEmreeLRRLQRELGITFIYVTHDQE 197
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
301-521 |
2.69e-19 |
|
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: 90.98 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 301 RALAEADDARSRVEVLT--PLTIALPPSGLP-SGANVLAMEGVVA---EAGDRRLGPWTLRIDGPERIALKGANGAGKTT 374
Cdd:COG4987 297 QHLGRVRAAARRLNELLdaPPAVTEPAEPAPaPGGPSLELEDVSFrypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKST 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 375 LLRIAAGLRAPVSGTVR----------RAE--GRIVLLDQQVGLLDpeGTILDNIRRLHPDAGDEEAYALCARFAFRNRD 442
Cdd:COG4987 377 LLALLLRFLDPQSGSITlggvdlrdldEDDlrRRIAVVPQRPHLFD--TTLRENLRLARPDATDEELWAALERVGLGDWL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 443 ARR------VVG----TLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSF--DGALLVVSHDPSF 510
Cdd:COG4987 455 AALpdgldtWLGeggrRLSGGERRRLALARALLRDAP--ILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAG 532
|
250
....*....|.
gi 518843096 511 VERvgFDRVFE 521
Cdd:COG4987 533 LER--MDRILV 541
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
30-195 |
2.71e-19 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 87.55 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG----------------TIGLLRQDMPG--------GWTLAEALGV 85
Cdd:TIGR02769 38 ETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqldrkqrrafrrDVQLVFQDSPSavnprmtvRQIIGEPLRH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 ANDLERLERilagngtagdfdaadwtlESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:TIGR02769 118 LTSLDESEQ------------------KARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 166 NLDAAGRAAIRALMREWR--GGV--LVASHDREL 195
Cdd:TIGR02769 180 NLDMVLQAVILELLRKLQqaFGTayLFITHDLRL 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
353-519 |
4.45e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 86.68 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQVG------LLDPE--GTILD--------- 415
Cdd:COG1121 26 SLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGyvpqraEVDWDfpITVRDvvlmgrygr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 416 -NIRRLHPDAGDEEAYALCARF---AFRNRDarrvVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILE 491
Cdd:COG1121 106 rGLFRRPSRADREAVDEALERVgleDLADRP----IGELSGGQQQRVLLARALAQDPD--LLLLDEPFAGVDAATEEALY 179
|
170 180 190
....*....|....*....|....*....|.
gi 518843096 492 NAL--LSFDG-ALLVVSHDPSFVERVgFDRV 519
Cdd:COG1121 180 ELLreLRREGkTILVVTHDLGAVREY-FDRV 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
334-508 |
4.75e-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: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 334 VLAMEGVVAEAGDRR-LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-------------RAEgRIVL 399
Cdd:COG1120 1 MLEAENLSVGYGGRPvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslsrreLAR-RIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 400 LDQQVGllDPEG-TILDNI---RRLH------PDAGDEEA--YALcARF---AFRNRDarrvVGTLSGGERLRAGLAAAL 464
Cdd:COG1120 80 VPQEPP--APFGlTVRELValgRYPHlglfgrPSAEDREAveEAL-ERTgleHLADRP----VDELSGGERQRVLIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518843096 465 SGSAPpwLIILDEPTNHLDIES-VEILE--NALLSFDG-ALLVVSHDP 508
Cdd:COG1120 153 AQEPP--LLLLDEPTSHLDLAHqLEVLEllRRLARERGrTVVMVLHDL 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-224 |
4.88e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 89.95 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAI-GTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRT--GTIGLLRQDmpggwtlaE 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLeAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIGYYAQD--------H 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 82 ALGVANDLERLERIlAGNGTAGDFDAAdwtlesrIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLD 161
Cdd:PRK15064 392 AYDFENDLTLFDWM-SQWRQEGDDEQA-------VRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMD 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 162 EPTNNLDAagrAAIRAL---MREWRGGVLVASHDRELLDDV-DRILELTAIGARSFGGGWSAFSAAR 224
Cdd:PRK15064 464 EPTNHMDM---ESIESLnmaLEKYEGTLIFVSHDREFVSSLaTRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-209 |
5.18e-19 |
|
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: 84.13 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG-PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLL----RQDMPGGwT 78
Cdd:cd03223 1 IELENLSLATPDGrVLLKDLSFEIKPgDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLflpqRPYLPLG-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 79 LAEALgvandlerlerilagngtagdfdaadwtlesrigaalaqvglpALPLDrclRTLSGGERTRVGIARLVMEAPDLL 158
Cdd:cd03223 80 LREQL-------------------------------------------IYPWD---DVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518843096 159 LLDEPTNNLDAAGRAAIRALMREWRGGVLVASHDRELLDDVDRILELTAIG 209
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-519 |
8.09e-19 |
|
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: 83.80 E-value: 8.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 335 LAMEGVVAEAGDRRlgPWTLR-----IDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-----------RAEGRIV 398
Cdd:cd03246 1 LEVENVSFRYPGAE--PPVLRnvsfsIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqwdpNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 399 -LLDQQVGLLDpeGTILDNIrrlhpdagdeeayalcarfafrnrdarrvvgtLSGGERLRAGLAAALSGSapPWLIILDE 477
Cdd:cd03246 79 gYLPQDDELFS--GSIAENI--------------------------------LSGGQRQRLGLARALYGN--PRILVLDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518843096 478 PTNHLDIESVEILENALLSFDGA---LLVVSHDPSFVERVgfDRV 519
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAgatRIVIAHRPETLASA--DRI 165
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-196 |
1.04e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.55 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAFLTLDSVCARTPDGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--IGLLRQDMPGGW 77
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKIlTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 78 TLAeaLGVandlERLERILAGngtagdfdaadwTLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDL 157
Cdd:PRK09544 81 TLP--LTV----NRFLRLRPG------------TKKEDILPALKRVQAGHL-IDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518843096 158 LLLDEPTNNLDAAGRAA----IRALMREWRGGVLVASHDRELL 196
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVAlydlIDQLRRELDCAVLMVSHDLHLV 184
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-207 |
1.07e-18 |
|
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: 84.47 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 19 LFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----IGLLRQDMPGGWTLAEALGVANDLERL 92
Cdd:cd03231 15 LFSGLSFTLAAgEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 93 ERILAGNGTAGDFDAadwtlesrigaaLAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGR 172
Cdd:cd03231 95 RFWHADHSDEQVEEA------------LARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 518843096 173 AAIRALMREW--RGGVLVAS--HDRELLDDVDRILELTA 207
Cdd:cd03231 162 ARFAEAMAGHcaRGGMVVLTthQDLGLSEAGARELDLGF 200
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
30-209 |
1.43e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.84 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGLLRQDmPG----GWTLAE--ALGVAND-L 89
Cdd:PRK13635 34 EWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwdvrrqVGMVFQN-PDnqfvGATVQDdvAFGLENIgV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ERLERIlagngtagdfdaadwtleSRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:PRK13635 113 PREEMV------------------ERVDQALRQVGMEDF-LNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518843096 170 AGRA----AIRALMREWRGGVLVASHDRELLDDVDRIL-----ELTAIG 209
Cdd:PRK13635 174 RGRRevleTVRQLKEQKGITVLSITHDLDEAAQADRVIvmnkgEILEEG 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-230 |
1.71e-18 |
|
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: 88.45 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 16 DGPLFQKLTF-----AIgterVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGL-----LRQDMPGGWTLAEALGV 85
Cdd:TIGR03719 334 DKLLIDDLSFklppgGI----VGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLayvdqSRDALDPNKTVWEEISG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 ANDLERL-ERILAGNGTAGDFDAADWTLESRIGAalaqvglpalpldrclrtLSGGERTRVGIARLVMEAPDLLLLDEPT 164
Cdd:TIGR03719 410 GLDIIKLgKREIPSRAYVGRFNFKGSDQQKKVGQ------------------LSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 165 NNLDAagrAAIRAL---MREWRGGVLVASHDRELLddvDRIleLTAIGA-------RSFGGGWSAFsaarDEDRRR 230
Cdd:TIGR03719 472 NDLDV---ETLRALeeaLLNFAGCAVVISHDRWFL---DRI--ATHILAfegdshvEWFEGNFSEY----EEDKKR 535
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
353-519 |
1.99e-18 |
|
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: 84.18 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD-----QQVGLL--DPE---GTILDNIRRLHP 422
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDpadlrRNIGYVpqDVTlfyGTLRDNITLGAP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 423 DAGDEEAYAlCARFA----FRNRDAR---RVVG----TLSGGERLRAGLAAALSGSAPPWLiiLDEPTNHLDIESVEILE 491
Cdd:cd03245 104 LADDERILR-AAELAgvtdFVNKHPNgldLQIGergrGLSGGQRQAVALARALLNDPPILL--LDEPTSAMDMNSEERLK 180
|
170 180 190
....*....|....*....|....*....|
gi 518843096 492 NALLSF--DGALLVVSHDPSFVERVgfDRV 519
Cdd:cd03245 181 ERLRQLlgDKTLIIITHRPSLLDLV--DRI 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
353-519 |
2.50e-18 |
|
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: 83.74 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-------RAEGRIVLLDQQ--------------VGL-LDPE 410
Cdd:cd03235 19 SFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkpleKERKRIGYVPQRrsidrdfpisvrdvVLMgLYGH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 411 GTILDNIRRLHPDAGDEeAYALCARFAFRNRDarrvVGTLSGGERLRAGLAAALSGsaPPWLIILDEPTNHLDIESVEIL 490
Cdd:cd03235 99 KGLFRRLSKADKAKVDE-ALERVGLSELADRQ----IGELSGGQQQRVLLARALVQ--DPDLLLLDEPFAGVDPKTQEDI 171
|
170 180 190
....*....|....*....|....*....|..
gi 518843096 491 ENAL--LSFDG-ALLVVSHDPSFVERVgFDRV 519
Cdd:cd03235 172 YELLreLRREGmTILVVTHDLGLVLEY-FDRV 202
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
30-181 |
2.69e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 86.28 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRrtgtIGllrqdmpggwtlaealG-VANDLERLER---------ILAGN 99
Cdd:COG3839 30 EFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL----IG----------------GrDVTDLPPKDRniamvfqsyALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 GTAGD----------FDAADwtLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIAR-LVMEaPDLLLLDEPTNNLD 168
Cdd:COG3839 90 MTVYEniafplklrkVPKAE--IDRRVREAAELLGLEDL-LDRKPKQLSGGQRQRVALGRaLVRE-PKVFLLDEPLSNLD 165
|
170
....*....|...
gi 518843096 169 AAGRAAIRALMRE 181
Cdd:COG3839 166 AKLRVEMRAEIKR 178
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
30-205 |
2.83e-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: 87.73 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtiGLLRQDMPGGWtLAEALGVANDLERLERILAGNGTAGDFDAAD 109
Cdd:TIGR02857 349 ERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG--VPLADADADSW-RDQIAWVPQHPFLFAGTIAENIRLARPDASD 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 110 WTLESRIGAALAQVGLPALP------LDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWR 183
Cdd:TIGR02857 426 AEIREALERAGLDEFVAALPqgldtpIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA 505
|
170 180
....*....|....*....|....
gi 518843096 184 GG--VLVASHDRELLDDVDRILEL 205
Cdd:TIGR02857 506 QGrtVLLVTHRLALAALADRIVVL 529
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
30-211 |
2.90e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG----------------TIGLLRQDMPG--------GWTLAEALGV 85
Cdd:PRK10419 39 ETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplaklnraqrkafrrDIQMVFQDSISavnprktvREIIREPLRH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 ANDLERLERilagngtagdfdaadwtlESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:PRK10419 119 LLSLDKAER------------------LARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518843096 166 NLDAAGRAAIRALMREWRG----GVLVASHD---------RELLDDVDRILELTAIGAR 211
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQqfgtACLFITHDlrlverfcqRVMVMDNGQIVETQPVGDK 239
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-211 |
3.18e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 87.88 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTP--DGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGL 68
Cdd:COG4618 331 LSVENLTVVPPgsKRPILRGVSFSLEPgEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 69 LRQD---MPGgwTLAEA---LGVANDlerlERILAGNGTAGdfdAADWTL------ESRIGAALAqvglpalpldrclrT 136
Cdd:COG4618 411 LPQDvelFDG--TIAENiarFGDADP----EKVVAAAKLAG---VHEMILrlpdgyDTRIGEGGA--------------R 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 137 LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREW--RGG-VLVASHDRELLDDVDRIL-----ELTAI 208
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkaRGAtVVVITHRPSLLAAVDKLLvlrdgRVQAF 547
|
...
gi 518843096 209 GAR 211
Cdd:COG4618 548 GPR 550
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
360-519 |
4.79e-18 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 83.32 E-value: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQ--------VGL--------LDPEGTILDNIR---RL 420
Cdd:cd03257 32 ETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkirrkeIQMvfqdpmssLNPRMTIGEQIAeplRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 421 HPDAGDEEAYALCARFAFR-----NRDARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIES-VEILEnaL 494
Cdd:cd03257 112 HGKLSKKEARKEAVLLLLVgvglpEEVLNRYPHELSGGQRQRVAIARALALN--PKLLIADEPTSALDVSVqAQILD--L 187
|
170 180 190
....*....|....*....|....*....|
gi 518843096 495 L-----SFDGALLVVSHDPSFVERVGfDRV 519
Cdd:cd03257 188 LkklqeELGLTLLFITHDLGVVAKIA-DRV 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
354-518 |
4.88e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 87.31 E-value: 4.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQvgllDP----EGTILDNI-----------R 418
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQ----DPprnvEGTVYDFVaegieeqaeylK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 RLHP---DAGDEEAYALCARFA-------------FRNR----------DARRVVGTLSGGERLRAGLAAALSGSapPWL 472
Cdd:PRK11147 100 RYHDishLVETDPSEKNLNELAklqeqldhhnlwqLENRinevlaqlglDPDAALSSLSGGWLRKAALGRALVSN--PDV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518843096 473 IILDEPTNHLDIESVEILENALLSFDGALLVVSHDPSFVER-----VGFDR 518
Cdd:PRK11147 178 LLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNmatriVDLDR 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
30-181 |
5.88e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.78 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLR---------------QD--------MPGGWTLAEALGV 85
Cdd:COG4608 45 ETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSgrelrplrrrmqmvfQDpyaslnprMTVGDIIAEPLRI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 ANDLERLERilagngtagdfdaadwtlESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:COG4608 125 HGLASKAER------------------RERVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170
....*....|....*.
gi 518843096 166 NLDAAGRAAIRALMRE 181
Cdd:COG4608 187 ALDVSIQAQVLNLLED 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-192 |
6.82e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.68 E-value: 6.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 6 TLDSVCARTPDGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVrrtgtigLLRQDMPGGWT------ 78
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVtGLIGHNGSGKSTLLKMLGRHQPPSEGEI-------LLDAQPLESWSskafar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 79 ----LAEALGVANDLERLERILAG----NGTAGDFDAADwtlESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARL 150
Cdd:PRK10575 86 kvayLPQQLPAAEGMTVRELVAIGrypwHGALGRFGAAD---REKVEEAISLVGLKPLA-HRLVDSLSGGERQRAWIAML 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518843096 151 VMEAPDLLLLDEPTNNLDAAGRAAIRAL---MREWRGGVLVAS-HD 192
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALvhrLSQERGLTVIAVlHD 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
353-522 |
8.11e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.40 E-value: 8.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD----------------QQVGLLdPEGTILDN 416
Cdd:COG1136 28 SLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelarlrrrhigfvfQFFNLL-PELTALEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 417 I------RRLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIES---- 486
Cdd:COG1136 107 ValplllAGVSRKERRERARELLERVGLGDR-LDHRPSQLSGGQQQRVAIARALVNR--PKLILADEPTGNLDSKTgeev 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 518843096 487 VEILENALLSFDGALLVVSHDPSFVERvgFDRVFEV 522
Cdd:COG1136 184 LELLRELNRELGTTIVMVTHDPELAAR--ADRVIRL 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-258 |
1.24e-17 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 85.99 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 22 KLTFAIGTeRVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGL----------LRQDmpggwtlaealgvANDLER 91
Cdd:PRK10636 332 KLNLVPGS-RIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLgyfaqhqlefLRAD-------------ESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 92 LERIlagngtagdfdaADWTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAG 171
Cdd:PRK10636 398 LARL------------APQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 172 RAAIRALMREWRGGVLVASHDRELLDDVDRILELTAIG-ARSFGGGWsafsaardEDRRRASAELER-----ADADVRAV 245
Cdd:PRK10636 466 RQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGkVEPFDGDL--------EDYQQWLSDVQKqenqtDEAPKENN 537
|
250
....*....|...
gi 518843096 246 RQAVQARREAKER 258
Cdd:PRK10636 538 ANSAQARKDQKRR 550
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
32-192 |
1.53e-17 |
|
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: 81.84 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGL-----AEPSSGTVRRTG---------------TIGLLRQD-MPGGWTLAE--ALGVAND 88
Cdd:cd03260 29 TALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKpNPFPGSIYDnvAYGLRLH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 89 LERLERILagngtagdfdaadwtlESRIGAALAQVGLPALPLDR-CLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNL 167
Cdd:cd03260 109 GIKLKEEL----------------DERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSAL 172
|
170 180
....*....|....*....|....*..
gi 518843096 168 DAAGRAAIRALMREWRG--GVLVASHD 192
Cdd:cd03260 173 DPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
30-203 |
2.87e-17 |
|
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: 80.94 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT------------IGLLR--------QDMpggwTLAEALGVANDL 89
Cdd:cd03219 27 EIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarLGIGRtfqiprlfPEL----TVLENVMVAAQA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ERLERILAGNGTAGDFDAADwtlesRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:cd03219 103 RTGSGLLLARARREEREARE-----RAEELLERVGLADL-ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNP 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 518843096 170 AGRAAIRALMREWRG---GVLVASHDRELLDDV-DRIL 203
Cdd:cd03219 177 EETEELAELIRELRErgiTVLLVEHDMDVVMSLaDRVT 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-202 |
3.96e-17 |
|
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: 79.99 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigllrQDMpggwtlaeal 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADgEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG------RDV---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 84 gvaNDLERLERILA---------GNGTAgdFDAADWTLESR------IGAALAQV----GLPALpLDRCLRTLSGGERTR 144
Cdd:cd03301 65 ---TDLPPKDRDIAmvfqnyalyPHMTV--YDNIAFGLKLRkvpkdeIDERVREVaellQIEHL-LDRKPKQLSGGQRQR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518843096 145 VGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRA----LMREWRGGVLVASHDR-ELLDDVDRI 202
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAelkrLQQRLGTTTIYVTHDQvEAMTMADRI 201
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
30-196 |
4.97e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIgllrqdmpgGWTLAEALGVANDL-------------------- 89
Cdd:COG1134 53 ESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV---------SALLELGAGFHPELtgreniylngrllglsrkei 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 -ERLERILagngtagDFdaadwtleSRIGAAlaqvglpalpLDRCLRTLSGGERTRVGIArlVMEA--PDLLLLDEPTnn 166
Cdd:COG1134 124 dEKFDEIV-------EF--------AELGDF----------IDQPVKTYSSGMRARLAFA--VATAvdPDILLVDEVL-- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 518843096 167 ldAAG--------RAAIRALMREWRgGVLVASHDRELL 196
Cdd:COG1134 175 --AVGdaafqkkcLARIRELRESGR-TVIFVSHSMGAV 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
297-513 |
5.95e-17 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 83.49 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 297 RRMGRALAEADDARSRVEVLTPLTIALP---PSGLPSGA---NVLAMEGVVAEAGDRR--LGPWTLRIDGPERIALKGAN 368
Cdd:TIGR02857 278 RQLGAQYHARADGVAAAEALFAVLDAAPrplAGKAPVTAapaSSLEFSGVSVAYPGRRpaLRPVSFTVPPGERVALVGPS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 369 GAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQ-----QVGLLD-----PEGTILDNIRRLHPDAGDEEAYALCARFAF 438
Cdd:TIGR02857 358 GAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdswrdQIAWVPqhpflFAGTIAENIRLARPDASDAEIREALERAGL 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 439 RNRDARRVVGT----------LSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSFDG--ALLVVSH 506
Cdd:TIGR02857 438 DEFVAALPQGLdtpigeggagLSGGQAQRLALARAFLRDAP--LLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTH 515
|
....*..
gi 518843096 507 DPSFVER 513
Cdd:TIGR02857 516 RLALAAL 522
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-207 |
6.86e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 79.79 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR---------------------RTGTIGLLRQ---D 72
Cdd:COG4778 25 PVLDGVSFSVAAgECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwvdlaqaspreilalRRRTIGYVSQflrV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 73 MPGGWTL---AEALgvandlerLERilagngtAGDFDAAdwtlESRIGAALAQVGLP----ALPLdrclRTLSGGERTRV 145
Cdd:COG4778 105 IPRVSALdvvAEPL--------LER-------GVDREEA----RARARELLARLNLPerlwDLPP----ATFSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 146 GIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREW--RGGVLVA-SHDRELLDDV-DRILELTA 207
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTAIIGiFHDEEVREAVaDRVVDVTP 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
34-194 |
1.40e-16 |
|
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: 78.92 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLRQDM------PGGWTLAEALGVANDLERLERILAGNGTagdfd 106
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDSGKILLNGKdITNLPPEKrdisyvPQNYALFPHMTVYKNIAYGLKKRKVDKK----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 107 aadwTLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIAR-LVMEaPDLLLLDEPTNNLDAAGRAAIRALMREWRGG 185
Cdd:cd03299 105 ----EIERKVLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARaLVVN-PKILLLDEPFSALDVRTKEKLREELKKIRKE 178
|
170
....*....|...
gi 518843096 186 ----VLVASHDRE 194
Cdd:cd03299 179 fgvtVLHVTHDFE 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
30-181 |
1.62e-16 |
|
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: 78.78 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT----------------IGLLRQDMPGGWTLAEALGVANDLErle 93
Cdd:cd03258 32 EIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkelrkarrrIGMIFQHFNLLSSRTVFENVALPLE--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 94 riLAGNGTAgdfdaadwTLESRIGAALAQVGLpALPLDRCLRTLSGGERTRVGIAR-LVMEaPDLLLLDEPTNNLDAAGR 172
Cdd:cd03258 109 --IAGVPKA--------EIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARaLANN-PKVLLCDEATSALDPETT 176
|
....*....
gi 518843096 173 AAIRALMRE 181
Cdd:cd03258 177 QSILALLRD 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
335-508 |
1.62e-16 |
|
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: 78.17 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 335 LAMEGVVAEAGDRRL-GPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-----RAEGRIVLLDQQVGL-- 406
Cdd:TIGR01189 1 LAARNLACSRGERMLfEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngtpLAEQRDEPHENILYLgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 407 ---LDPEGTILDNIRRLHPDAGDEEAYALCARFAFRNRD-ARRVVGTLSGGERLRAGLAAALSGSAPPWliILDEPTNHL 482
Cdd:TIGR01189 81 lpgLKPELSALENLHFWAAIHGGAQRTIEDALAAVGLTGfEDLPAAQLSAGQQRRLALARLWLSRRPLW--ILDEPTTAL 158
|
170 180
....*....|....*....|....*....
gi 518843096 483 DIESVEILENAL---LSFDGALLVVSHDP 508
Cdd:TIGR01189 159 DKAGVALLAGLLrahLARGGIVLLTTHQD 187
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
30-202 |
1.63e-16 |
|
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: 78.87 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRrtgtigLLRQDMpggWTLAEAlgvanDLERLER---ILAGNG------ 100
Cdd:COG1127 32 EILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL------VDGQDI---TGLSEK-----ELYELRRrigMLFQGGalfdsl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 101 TAGD---------FDAADWTLESRIGAALAQVGLPA----LPLDrclrtLSGGERTRVGIAR-LVMEaPDLLLLDEPTNN 166
Cdd:COG1127 98 TVFEnvafplrehTDLSEAEIRELVLEKLELVGLPGaadkMPSE-----LSGGMRKRVALARaLALD-PEILLYDEPTAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518843096 167 LDAAGRAAIRALMREWRGG----VLVASHD-RELLDDVDRI 202
Cdd:COG1127 172 LDPITSAVIDELIRELRDElgltSVVVTHDlDSAFAIADRV 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-202 |
1.80e-16 |
|
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: 78.88 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG-PLFQKLTFAI-GTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-------------TIGLL 69
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIaKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 70 RQD---MPGgWTLAEALGVANDLERLERIlagngtagdfdaadwTLESRIGAALAQVGL-PALPLDRCLRTLSGGERTRV 145
Cdd:cd03295 81 IQQiglFPH-MTVEENIALVPKLLKWPKE---------------KIRERADELLALVGLdPAEFADRYPHELSGGQQQRV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 146 GIARLVMEAPDLLLLDEPTNNLDAAGRAA----IRALMREWRGGVLVASHD-RELLDDVDRI 202
Cdd:cd03295 145 GVARALAADPPLLLMDEPFGALDPITRDQlqeeFKRLQQELGKTIVFVTHDiDEAFRLADRI 206
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
30-199 |
2.01e-16 |
|
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: 80.10 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEP---SSGTVR-----------------RTGTIGLLRQD--------MPGGWTLAE 81
Cdd:COG0444 32 ETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfdgedllklsekelrkiRGREIQMIFQDpmtslnpvMTVGDQIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 82 ALGVANDLERLERilagngtagdfdaadwtlESRIGAALAQVGLPAlPLDRCLR---TLSGGERTRVGIAR-LVMEaPDL 157
Cdd:COG0444 112 PLRIHGGLSKAEA------------------RERAIELLERVGLPD-PERRLDRyphELSGGMRQRVMIARaLALE-PKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518843096 158 LLLDEPTNNLDAAGRAAI----RALMREWRGGVLVASHD----RELLDDV 199
Cdd:COG0444 172 LIADEPTTALDVTIQAQIlnllKDLQRELGLAILFITHDlgvvAEIADRV 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
23-192 |
2.41e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.05 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 23 LTFAIGtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-------------TIGLLRQDMpggwTLAEALGVAnDL 89
Cdd:PRK13548 23 LTLRPG-EVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHS----SLSFPFTVE-EV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ERLERILAGNGTAGDFDAADwtlesrigAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVM------EAPDLLLLDEP 163
Cdd:PRK13548 97 VAMGRAPHGLSRAEDDALVA--------AALAQVDLAHL-AGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 164 TNNLDAAG-----RAAiRALMREWRGGVLVASHD 192
Cdd:PRK13548 168 TSALDLAHqhhvlRLA-RQLAHERGLAVIVVLHD 200
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-205 |
2.41e-16 |
|
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: 78.43 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 15 PDGPLFQKLTFAI-GTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-------------TIGLLRQDMPggwtla 80
Cdd:cd03253 12 PGRPVLKDVSFTIpAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTV------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 81 ealgVANDLERlERILAGNGTAGDfdaadwtlESRIGAALA----------------QVGlpalplDRCLRtLSGGERTR 144
Cdd:cd03253 86 ----LFNDTIG-YNIRYGRPDATD--------EEVIEAAKAaqihdkimrfpdgydtIVG------ERGLK-LSGGEKQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518843096 145 VGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRILEL 205
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAHRLSTIVNADKIIVL 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-205 |
2.68e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPL----FQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigllrQDMPGGWTL 79
Cdd:PRK11629 6 LQCDNLCKRYQEGSVqtdvLHNVSFSIGEgEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG------QPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 80 AEA------LG-------VANDLERLERI----LAGNGTAGDfdaadwtLESRIGAALAQVGLPALPLDRClRTLSGGER 142
Cdd:PRK11629 80 AKAelrnqkLGfiyqfhhLLPDFTALENVamplLIGKKKPAE-------INSRALEMLAAVGLEHRANHRP-SELSGGER 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 143 TRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREW--RGGV--LVASHDRELLDDVDRILEL 205
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTafLVVTHDLQLAKRMSRQLEM 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
30-191 |
3.06e-16 |
|
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: 77.79 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG------------TIGLLrqdmPGGWTLAEALGVANDLERLERILA 97
Cdd:cd03266 32 EVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrRLGFV----SDSTGLYDRLTARENLEYFAGLYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 98 GNGTAgdfdaadwtLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRA 177
Cdd:cd03266 108 LKGDE---------LTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE 177
|
170
....*....|....*..
gi 518843096 178 LMREWRGG---VLVASH 191
Cdd:cd03266 178 FIRQLRALgkcILFSTH 194
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
299-520 |
3.06e-16 |
|
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: 81.33 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 299 MGRALA-------------EADDARSRVEVLTpLTIALPPSG--LPSGANVLAMEGVVAEA-GDRR--LGPWTLRIDGPE 360
Cdd:COG4618 281 MGRALApieqaiggwkqfvSARQAYRRLNELL-AAVPAEPERmpLPRPKGRLSVENLTVVPpGSKRpiLRGVSFSLEPGE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 361 RIALKGANGAGKTTLLRIAAGLRAPVSGTVR----------RAE-GRIV-LLDQQVGLLDpeGTILDNIRRLhPDAGDEE 428
Cdd:COG4618 360 VLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgadlsqwdREElGRHIgYLPQDVELFD--GTIAENIARF-GDADPEK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 429 AYAlCARFAfrnrDARRVV---------------GTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENA 493
Cdd:COG4618 437 VVA-AAKLA----GVHEMIlrlpdgydtrigeggARLSGGQRQRIGLARALYGD--PRLVVLDEPNSNLDDEGEAALAAA 509
|
250 260 270
....*....|....*....|....*....|
gi 518843096 494 LLSF--DGA-LLVVSHDPSFVERVgfDRVF 520
Cdd:COG4618 510 IRALkaRGAtVVVITHRPSLLAAV--DKLL 537
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
30-201 |
3.49e-16 |
|
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: 77.97 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR---------------RTGtIGLLRQDMpggwTLAEALGVAndlerlER 94
Cdd:cd03218 27 EIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldgqditklpmhkraRLG-IGYLPQEA----SIFRKLTVE------EN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 95 ILAGNGTAGDfdaADWTLESRIGAALAQVGLPALPLDRCLrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA 174
Cdd:cd03218 96 ILAVLEIRGL---SKKEREEKLEELLEEFHITHLRKSKAS-SLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQD 171
|
170 180 190
....*....|....*....|....*....|.
gi 518843096 175 IRALMREWRG---GVLVASHD-RELLDDVDR 201
Cdd:cd03218 172 IQKIIKILKDrgiGVLITDHNvRETLSITDR 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-203 |
4.30e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 80.98 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG-PLFQKLTFAI--GtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLRQDmpggwTLA 80
Cdd:COG1132 340 IEFENVSFSYPGDrPVLKDISLTIppG-ETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdIRDLTLE-----SLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 81 EALGVAN-DLERLERILAGNGTAGDFDAADwtleSRIGAALAQVGL----PALP--LDRCL----RTLSGGERTRVGIAR 149
Cdd:COG1132 414 RQIGVVPqDTFLFSGTIRENIRYGRPDATD----EEVEEAAKAAQAhefiEALPdgYDTVVgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 150 LVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRIL 203
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAHRLSTIRNADRIL 545
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-202 |
4.71e-16 |
|
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: 77.76 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQD---------MPGGWTLAEALGVAN 87
Cdd:cd03267 35 EALKGISFTIEKgEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKkflrrigvvFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 88 DLERLERILagngtagDFDAADWTLESRIGAALAQVGlpALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNL 167
Cdd:cd03267 115 SFYLLAAIY-------DLPPARFKKRLDELSELLDLE--EL-LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 518843096 168 DAAGRAAIRALMREW---RGG-VLVASHDrelLDDVDRI 202
Cdd:cd03267 185 DVVAQENIRNFLKEYnreRGTtVLLTSHY---MKDIEAL 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
353-519 |
6.04e-16 |
|
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: 76.53 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV---------RRAEGRIVLLDQQVGLLDPEGTILDNIRRLHPD 423
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikaKERRKSIGYVMQDVDYQLFTDSVREELLLGLKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 424 AGDEEAYALC-----ARFAFRNRDARrvvgTLSGGERLRAGLAAA-LSGsapPWLIILDEPTNHLDIESVEILENALLSF 497
Cdd:cd03226 100 LDAGNEQAETvlkdlDLYALKERHPL----SLSGGQKQRLAIAAAlLSG---KDLLIFDEPTSGLDYKNMERVGELIREL 172
|
170 180
....*....|....*....|....*
gi 518843096 498 ---DGALLVVSHDPSFVERVGfDRV 519
Cdd:cd03226 173 aaqGKAVIVITHDYEFLAKVC-DRV 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-203 |
6.94e-16 |
|
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: 80.60 E-value: 6.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGL----LRQDMPGgwTLAEALGVANdlerlerilagngtAGDF 105
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYkpqyISPDYDG--TVEEFLRSAN--------------TDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 106 DAADWtlESRIGAALaqvGLPALpLDRCLRTLSGGERTRVGIAR-LVMEApDLLLLDEPTNNLD-----AAGRaAIRALM 179
Cdd:COG1245 431 GSSYY--KTEIIKPL---GLEKL-LDKNVKDLSGGELQRVAIAAcLSRDA-DLYLLDEPSAHLDveqrlAVAK-AIRRFA 502
|
170 180
....*....|....*....|....*
gi 518843096 180 REWRGGVLVASHDRELLDDV-DRIL 203
Cdd:COG1245 503 ENRGKTAMVVDHDIYLIDYIsDRLM 527
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
30-203 |
7.46e-16 |
|
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: 77.39 E-value: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR--------------------RTGTIGLLRQDMpggwTLAEALGVANDL 89
Cdd:COG0411 31 EIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphriarlgiaRTFQNPRLFPEL----TVLENVLVAAHA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ERLERILAGNGTAGDFDAADWTLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:COG0411 107 RLGRGLLAALLRLPRARREEREARERAEELLERVGLADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNP 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 518843096 170 AGRAAIRALMREWRGG----VLVASHDRELLDDV-DRIL 203
Cdd:COG0411 186 EETEELAELIRRLRDErgitILLIEHDMDLVMGLaDRIV 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-203 |
1.03e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGL----LRQDMPGgwTLAEALGVANDlerlerilagngtagDF 105
Cdd:PRK13409 366 EVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYkpqyIKPDYDG--TVEDLLRSITD---------------DL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 106 DAADWtlESRIGAALaqvGLPALpLDRCLRTLSGGERTRVGIAR-LVMEApDLLLLDEPTNNLD-----AAGRaAIRALM 179
Cdd:PRK13409 429 GSSYY--KSEIIKPL---QLERL-LDKNVKDLSGGELQRVAIAAcLSRDA-DLYLLDEPSAHLDveqrlAVAK-AIRRIA 500
|
170 180
....*....|....*....|....*
gi 518843096 180 REWRGGVLVASHDRELLDDV-DRIL 203
Cdd:PRK13409 501 EEREATALVVDHDIYMIDYIsDRLM 525
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
335-512 |
1.18e-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: 75.69 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 335 LAMEGVVAEAGDRR-LGPWTLRIdGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRR-----------AEGRIVLLDQ 402
Cdd:cd03264 1 LQLENLTKRYGKKRaLDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlkqpqkLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 403 QVGlLDPEGTI---LDNIRRLH--PDAG-DEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILD 476
Cdd:cd03264 80 EFG-VYPNFTVrefLDYIAWLKgiPSKEvKARVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQALVGD--PSILIVD 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 518843096 477 EPTNHLDIESVEILENAL--LSFDGALLVVSHDPSFVE 512
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLseLGEDRIVILSTHIVEDVE 193
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-214 |
1.47e-15 |
|
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: 78.23 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 28 GTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------------IGLLRQDMpggwTLAEALGVANDLE 90
Cdd:TIGR02142 22 GQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIGYVFQEA----RLFPHLSVRGNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 91 RLERILAGNGTAGDFDAAdwtlesrigaaLAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAA 170
Cdd:TIGR02142 98 YGMKRARPSERRISFERV-----------IELLGIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518843096 171 GRAAI----RALMREWRGGVLVASHD-RELLDDVDRILELTAIGARSFG 214
Cdd:TIGR02142 166 RKYEIlpylERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGRVAAAG 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
30-203 |
1.58e-15 |
|
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: 76.70 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQDMpggWTLAEALG--------------VAND----LER 91
Cdd:TIGR04520 29 EFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENL---WEIRKKVGmvfqnpdnqfvgatVEDDvafgLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 92 L----ERIlagngtagdfdaadwtlESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIAR-LVMEaPDLLLLDEPTNN 166
Cdd:TIGR04520 106 LgvprEEM-----------------RKRVDEALKLVGMEDF-RDREPHLLSGGQKQRVAIAGvLAMR-PDIIILDEATSM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518843096 167 LDAAGRAAIRALMREWR--GGVLVAS--HDRELLDDVDRIL 203
Cdd:TIGR04520 167 LDPKGRKEVLETIRKLNkeEGITVISitHDMEEAVLADRVI 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
34-196 |
1.84e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.68 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG----------------TIGLLRQDMpggwTLAEALGVANDLErLERILA 97
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflrrQIGMIFQDH----HLLMDRTVYDNVA-IPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 98 GngtagdfdAADWTLESRIGAALAQVGLpalpLDRCLR---TLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA 174
Cdd:PRK10908 108 G--------ASGDDIRRRVSAALDKVGL----LDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180
....*....|....*....|....*
gi 518843096 175 IRALMREW-RGG--VLVASHDRELL 196
Cdd:PRK10908 176 ILRLFEEFnRVGvtVLMATHDIGLI 200
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-202 |
2.15e-15 |
|
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: 75.10 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 4 FLTLDSVCARTPDGPLFqkltfaigtervGLVGRNGSGKSTLLRIVAGLAEPSSGT--------------VRRTgtIGLL 69
Cdd:cd03265 13 FEAVRGVSFRVRRGEIF------------GLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvrepreVRRR--IGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 70 RQDMpggwTLAEALGVANDLERLERILagnGTAGDfdaadwTLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIAR 149
Cdd:cd03265 79 FQDL----SVDDELTGWENLYIHARLY---GVPGA------ERRERIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 518843096 150 LVMEAPDLLLLDEPTNNLDAAGRAA----IRALMREWRGGVLVASHDRELLDDV-DRI 202
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHvweyIEKLKEEFGMTILLTTHYMEEAEQLcDRV 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-181 |
2.18e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 78.57 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLaEPSSGTVRRTGT--IGL-------LR-------QD--------MPGGWTLAEALGV 85
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQdlDGLsrralrpLRrrmqvvfQDpfgslsprMTVGQIIAEGLRV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 -ANDLERLERilagngtagdfdaadwtlESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIAR-LVMEaPDLLLLDEP 163
Cdd:COG4172 392 hGPGLSAAER------------------RARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARaLILE-PKLLVLDEP 452
|
170
....*....|....*...
gi 518843096 164 TNNLDAAGRAAIRALMRE 181
Cdd:COG4172 453 TSALDVSVQAQILDLLRD 470
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-194 |
2.76e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.11 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSafLTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT------------IG 67
Cdd:COG1118 1 MS--IEVRNISKRFGSFTLLDDVSLEIASgELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnlpprerrVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 68 LLRQD------MpggwTLAE----ALGVA--NDLERLERilagngtagdfdAADWtlesrigaaLAQVGLPALpLDRCLR 135
Cdd:COG1118 79 FVFQHyalfphM----TVAEniafGLRVRppSKAEIRAR------------VEEL---------LELVQLEGL-ADRYPS 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 136 TLSGGERTRVGIAR-LVMEaPDLLLLDEPTNNLDAAGRAAIRALMR----EWRGGVLVASHDRE 194
Cdd:COG1118 133 QLSGGQRQRVALARaLAVE-PEVLLLDEPFGALDAKVRKELRRWLRrlhdELGGTTVFVTHDQE 195
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
347-513 |
2.93e-15 |
|
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: 74.64 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 347 RRLGPWTLRID---GPERIALKGANGAGKTTLLRIAAGLRAPVSGTV-------------------RRaegRIVLLDQQV 404
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrkkinlppqQR---KIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 405 GLLdPEGTILDNI----RRLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTN 480
Cdd:cd03297 85 ALF-PHLNVRENLafglKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARAL--AAQPELLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 518843096 481 HLDIESVEILENAL----LSFDGALLVVSHDPSFVER 513
Cdd:cd03297 161 ALDRALRLQLLPELkqikKNLNIPVIFVTHDLSEAEY 197
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-202 |
3.22e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 78.24 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 19 LFQKLTF-----AIgterVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGL-----LRQDMPGGWTLAEALGVAND 88
Cdd:PRK11819 339 LIDDLSFslppgGI----VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLayvdqSRDALDPNKTVWEEISGGLD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 89 LERLerilagngtaGDFDaadwtLESRigAALAQ-----------VGlpalpldrclrTLSGGERTRVGIARLVMEAPDL 157
Cdd:PRK11819 415 IIKV----------GNRE-----IPSR--AYVGRfnfkggdqqkkVG-----------VLSGGERNRLHLAKTLKQGGNV 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518843096 158 LLLDEPTNNLDAagrAAIRAL---MREWRGGVLVASHDRELLddvDRI 202
Cdd:PRK11819 467 LLLDEPTNDLDV---ETLRALeeaLLEFPGCAVVISHDRWFL---DRI 508
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
30-168 |
3.29e-15 |
|
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: 74.49 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------IGLLRQDMpgG-----WTLAEALGVandlerLERIL 96
Cdd:cd03262 27 EVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltddkknINELRQKV--GmvfqqFNLFPHLTV------LENIT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 97 AGNGTAGDFDAADwtLESRIGAALAQVGLP----ALPldrclRTLSGGERTRVGIAR-LVMEaPDLLLLDEPTNNLD 168
Cdd:cd03262 99 LAPIKVKGMSKAE--AEERALELLEKVGLAdkadAYP-----AQLSGGQQQRVAIARaLAMN-PKVMLFDEPTSALD 167
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
30-203 |
3.79e-15 |
|
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: 74.85 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRrtgtigLLRQDMPGgwtLAEAlgvanDLERLER---ILAGNG------ 100
Cdd:cd03261 27 EILAIIGPSGSGKSTLLRLIVGLLRPDSGEVL------IDGEDISG---LSEA-----ELYRLRRrmgMLFQSGalfdsl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 101 TAGD---------FDAADWTLESRIGAALAQVGLPA----LPLDrclrtLSGGERTRVGIARLVMEAPDLLLLDEPTNNL 167
Cdd:cd03261 93 TVFEnvafplrehTRLSEEEIREIVLEKLEAVGLRGaedlYPAE-----LSGGMKKRVALARALALDPELLLYDEPTAGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518843096 168 DAAGRAAIRALMREWRG----GVLVASHD-RELLDDVDRIL 203
Cdd:cd03261 168 DPIASGVIDDLIRSLKKelglTSIMVTHDlDTAFAIADRIA 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-212 |
5.24e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.37 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 2 SAFLTLDSVCARTPDGPLFQKLTFAIGTERVGLV-GRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLL-----RQDM- 73
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTLkpeiyRQQVs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 74 -----PggwtlaealgvandlerlerILAGNgTAGDFDAADWTL------ESRIGAALAQVGLPALPLDRCLRTLSGGER 142
Cdd:PRK10247 85 ycaqtP--------------------TLFGD-TVYDNLIFPWQIrnqqpdPAIFLDDLERFALPDTILTKNIAELSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 143 TRVGIARLVMEAPDLLLLDEPTNNLDAAGRA----AIRALMREWRGGVLVASHDRELLDDVDRILELTAIGARS 212
Cdd:PRK10247 144 QRISLIRNLQFMPKVLLLDEITSALDESNKHnvneIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEM 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-202 |
5.56e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.56 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG--PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLRQDmpggwTLA 80
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAgEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpIADYSEA-----ALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 81 EALGVANdlerlERI------LAGNGTAGDFDAADwtleSRIGAALAQVGLPAL-----PLDRCL----RTLSGGERTRV 145
Cdd:PRK11160 414 QAISVVS-----QRVhlfsatLRDNLLLAAPNASD----EALIEVLQQVGLEKLleddkGLNAWLgeggRQLSGGEQRRL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 146 GIAR-LVMEAPdLLLLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRI 202
Cdd:PRK11160 485 GIARaLLHDAP-LLLLDEPTEGLDAETERQILELLAEHAQNktVLMITHRLTGLEQFDRI 543
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-194 |
5.73e-15 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 76.29 E-value: 5.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 33 GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTI---GLLRQDMPG-----GWTLAEA-----LGVANDLERLERILAGN 99
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdSARGIFLPPhrrriGYVFQEArlfphLSVRGNLLYGRKRAPRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 GTAGDFDAAdwtlesrigaaLAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAI---- 175
Cdd:COG4148 109 ERRISFDEV-----------VELLGIGHL-LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIlpyl 176
|
170
....*....|....*....
gi 518843096 176 RALMREWRGGVLVASHDRE 194
Cdd:COG4148 177 ERLRDELDIPILYVSHSLD 195
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
354-519 |
6.58e-15 |
|
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: 73.72 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-------RAEGRIVLLDQQVGL------LDPEGTILDNI--- 417
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkltDDKKNINELRQKVGMvfqqfnLFPHLTVLENItla 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 ----RRLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESV-EILEN 492
Cdd:cd03262 101 pikvKGMSKAEAEERALELLEKVGLADK-ADAYPAQLSGGQQQRVAIARAL--AMNPKVMLFDEPTSALDPELVgEVLDV 177
|
170 180
....*....|....*....|....*....
gi 518843096 493 AL-LSFDG-ALLVVSHDPSFVERVGfDRV 519
Cdd:cd03262 178 MKdLAEEGmTMVVVTHEMGFAREVA-DRV 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-204 |
7.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.08 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT---------------IGLLRQdMPGgWTLAEalgvandlERLER 94
Cdd:PRK13637 34 EFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVditdkkvklsdirkkVGLVFQ-YPE-YQLFE--------ETIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 95 ILA-GNGTAGdfdAADWTLESRIGAALAQVGLPALPL-DRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGR 172
Cdd:PRK13637 104 DIAfGPINLG---LSEEEIENRVKRAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 518843096 173 ----AAIRALMREWRGGVLVASHDRElldDVDRILE 204
Cdd:PRK13637 181 deilNKIKELHKEYNMTIILVSHSME---DVAKLAD 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
339-519 |
8.13e-15 |
|
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: 74.14 E-value: 8.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 339 GVVAEAGDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV---------------RRAEGRIVLLDQQ 403
Cdd:cd03256 7 SKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalRQLRRQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 404 VGLLdPEGTILDNI--------------RRLHPDAGDEEAYALCARFAFRNRDARRvVGTLSGGERLRAGLAAALSGSap 469
Cdd:cd03256 87 FNLI-ERLSVLENVlsgrlgrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQR-ADQLSGGQQQRVAIARALMQQ-- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518843096 470 PWLIILDEPTNHLDIESVEILENALLSF---DGALLVVS-HDPSFVERVgFDRV 519
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRInreEGITVIVSlHQVDLAREY-ADRI 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
353-519 |
8.35e-15 |
|
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: 72.60 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-------RAEGRIVLLDQQVGL------LDPEGTILDNIrr 419
Cdd:cd03229 20 SLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILidgedltDLEDELPPLRRRIGMvfqdfaLFPHLTVLENI-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 420 lhpdagdeeAYAlcarfafrnrdarrvvgtLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESVEILENALLS--- 496
Cdd:cd03229 98 ---------ALG------------------LSGGQQQRVALARAL--AMDPDVLLLDEPTSALDPITRREVRALLKSlqa 148
|
170 180
....*....|....*....|....
gi 518843096 497 -FDGALLVVSHDPSFVERVGfDRV 519
Cdd:cd03229 149 qLGITVVLVTHDLDEAARLA-DRV 171
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
334-514 |
1.26e-14 |
|
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: 73.58 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 334 VLAMEGVVAEAGDRR-LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSG-TVR---RAEGRIVLLD--QQVGL 406
Cdd:COG1119 3 LLELRNVTVRRGGKTiLDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgERRGGEDVWElrKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 407 LDPE--------GTILDNI---------RRLHPDAGDEE-AYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSa 468
Cdd:COG1119 83 VSPAlqlrfprdETVLDVVlsgffdsigLYREPTDEQRErARELLELLGLAHL-ADRPFGTLSQGEQRRVLIARALVKD- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518843096 469 pPWLIILDEPTNHLDIESVEILENAL--LSFDG--ALLVVSHD----PSFVERV 514
Cdd:COG1119 161 -PELLILDEPTAGLDLGARELLLALLdkLAAEGapTLVLVTHHveeiPPGITHV 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
360-514 |
1.32e-14 |
|
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: 72.95 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRaEGRIV-LLDQQVGlLDPEGTILDNIRRL-----HPDAGDEEAYALC 433
Cdd:cd03220 49 ERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RGRVSsLLGLGGG-FNPELTGRENIYLNgrllgLSRKEIDEKIDEI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 434 ARFAFRNRDARRVVGTLSGGERLRagLAAALSGSAPPWLIILDEPT----NHLDIESVEILENaLLSFDGALLVVSHDPS 509
Cdd:cd03220 127 IEFSELGDFIDLPVKTYSSGMKAR--LAFAIATALEPDILLIDEVLavgdAAFQEKCQRRLRE-LLKQGKTVILVSHDPS 203
|
....*
gi 518843096 510 FVERV 514
Cdd:cd03220 204 SIKRL 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
364-521 |
1.50e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.78 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 364 LKGANGAGKTTLLRIAAGLRAPVSGTV--------RRAEGRIVLLDQQVG-------LLdPEGTILDN------IRRLHP 422
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsRLKRREIPYLRRRIGvvfqdfrLL-PDRTVYENvalplrVTGKSR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 423 DAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIE-SVEILE-----NALls 496
Cdd:COG2884 112 KEIRRRVREVLDLVGLSDK-AKALPHELSGGEQQRVAIARALVNR--PELLLADEPTGNLDPEtSWEIMElleeiNRR-- 186
|
170 180
....*....|....*....|....*.
gi 518843096 497 fdG-ALLVVSHDPSFVERVGFdRVFE 521
Cdd:COG2884 187 --GtTVLIATHDLELVDRMPK-RVLE 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
30-164 |
1.71e-14 |
|
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: 72.85 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------------IGLLRQDMpggwtlaealGVANDLERLERI 95
Cdd:cd03224 27 EIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGR----------RIFPELTVEENL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 96 LAGnGTAGDFDAADWTLES------RIGAALAQVGlpalpldrclRTLSGGERTRVGIARLVMEAPDLLLLDEPT 164
Cdd:cd03224 97 LLG-AYARRRAKRKARLERvyelfpRLKERRKQLA----------GTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
35-199 |
1.81e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 74.62 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 35 VGRNGSGKSTLLRIVAGLAEPSSGTVRRTG---------TIGLLRQDM------------PG---GWTLAEALGVANDLE 90
Cdd:PRK11308 47 VGESGCGKSTLARLLTMIETPTGGELYYQGqdllkadpeAQKLLRQKIqivfqnpygslnPRkkvGQILEEPLLINTSLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 91 RLERilagngtagdfdaadwtlESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAA 170
Cdd:PRK11308 127 AAER------------------REKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 518843096 171 GRAAIRALM----REWRGGVLVASHD----RELLDDV 199
Cdd:PRK11308 189 VQAQVLNLMmdlqQELGLSYVFISHDlsvvEHIADEV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
353-519 |
1.92e-14 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 72.17 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRR----------AEGRIVLLDQQVGLLdPEGTILDNI----R 418
Cdd:cd03259 20 SLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvppERRNIGMVFQDYALF-PHLTVAENIafglK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 RLHPDAGDEEAYALCARFAFRNRD-ARRVVGTLSGGERLRAGLAAALsgsAP-PWLIILDEPTNHLDIESVEILENALL- 495
Cdd:cd03259 99 LRGVPKAEIRARVRELLELVGLEGlLNRYPHELSGGQQQRVALARAL---ARePSLLLLDEPLSALDAKLREELREELKe 175
|
170 180
....*....|....*....|....*..
gi 518843096 496 ---SFDGALLVVSHDPSFVERVGfDRV 519
Cdd:cd03259 176 lqrELGITTIYVTHDQEEALALA-DRI 201
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
30-168 |
2.09e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 72.72 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------IGLLRQDMpG-------------------------- 75
Cdd:COG1126 28 EVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdltdskkdINKLRRKV-Gmvfqqfnlfphltvlenvtlapikvk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 76 GWTLAEALGVANDLerlerilagngtagdfdaadwtlesrigaaLAQVGLP----ALPldrclRTLSGGERTRVGIAR-L 150
Cdd:COG1126 107 KMSKAEAEERAMEL------------------------------LERVGLAdkadAYP-----AQLSGGQQQRVAIARaL 151
|
170
....*....|....*...
gi 518843096 151 VMEaPDLLLLDEPTNNLD 168
Cdd:COG1126 152 AME-PKVMLFDEPTSALD 168
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-203 |
2.96e-14 |
|
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: 70.80 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQDmpggwTLAEALGVANDLERLeril 96
Cdd:cd03247 16 QVLKNLSLELKQgEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-----ALSSLISVLNQRPYL---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 97 agngtagdFDAadwTLESRIGaalaqvglpalpldrclRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA-AGRAAI 175
Cdd:cd03247 87 --------FDT---TLRNNLG-----------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPiTERQLL 138
|
170 180
....*....|....*....|....*....
gi 518843096 176 RALMREWRG-GVLVASHDRELLDDVDRIL 203
Cdd:cd03247 139 SLIFEVLKDkTLIWITHHLTGIEHMDKIL 167
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
360-520 |
3.19e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.20 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVR----------RAE--GRIVLLDQQVGLLDpeGTILDNIRRLHPDAGDE 427
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdirdltLESlrRQIGVVPQDTFLFS--GTIRENIRYGRPDATDE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 428 EAYAlCARFAFRNRDARR-------VVG----TLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENAL-- 494
Cdd:COG1132 445 EVEE-AAKAAQAHEFIEAlpdgydtVVGergvNLSGGQRQRIAIARALLKDPP--ILILDEATSALDTETEALIQEALer 521
|
170 180
....*....|....*....|....*.
gi 518843096 495 LSFDGALLVVSHDPSFVERVgfDRVF 520
Cdd:COG1132 522 LMKGRTTIVIAHRLSTIRNA--DRIL 545
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
5-191 |
3.74e-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: 71.37 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------IGLLRQDM 73
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQG-EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 74 pggwTLAEALGVANDLErLERILAGNGTAGDfdaadwtlESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIAR-LVM 152
Cdd:cd03298 80 ----NLFAHLTVEQNVG-LGLSPGLKLTAED--------RQAIEVALARVGLAGL-EKRLPGELSGGERQRVALARvLVR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518843096 153 EAPdLLLLDEPTNNLDAAGRAAIRALM----REWRGGVLVASH 191
Cdd:cd03298 146 DKP-VLLLDEPFAALDPALRAEMLDLVldlhAETKMTVLMVTH 187
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
363-514 |
4.17e-14 |
|
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: 71.09 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD---QQVG-LLD-----PEGTILDNIRRLH--PDAGDEEAYA 431
Cdd:cd03268 30 GFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIealRRIGaLIEapgfyPNLTARENLRLLArlLGIRKKRIDE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 432 LCARFAFRNRDARRvVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENALLS---FDGALLVVSHDP 508
Cdd:cd03268 110 VLDVVGLKDSAKKK-VKGFSLGMKQRLGIALALLGN--PDLLILDEPTNGLDPDGIKELRELILSlrdQGITVLISSHLL 186
|
....*.
gi 518843096 509 SFVERV 514
Cdd:cd03268 187 SEIQKV 192
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-207 |
5.08e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 3 AFLTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVrrtgTIGLLR-QDMP------ 74
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEgEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL----FIGEKRmNDVPpaergv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 75 ----GGWTLAEALGVANDLErLERILAGNGTAgdfdaadwTLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARL 150
Cdd:PRK11000 78 gmvfQSYALYPHLSVAENMS-FGLKLAGAKKE--------EINQRVNQVAEVLQLAHL-LDRKPKALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 151 VMEAPDLLLLDEPTNNLDAAGRAAIRA----LMREWRGGVLVASHDR-ELLDDVDRILELTA 207
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIeisrLHKRLGRTMIYVTHDQvEAMTLADKIVVLDA 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
30-202 |
5.41e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.19 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------IGLLRQDmpggWTLAEALGVAND-------LER 91
Cdd:PRK10851 29 QMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQH----YALFRHMTVFDNiafgltvLPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 92 LERilaGNGTAgdfdaadwtLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAG 171
Cdd:PRK10851 105 RER---PNAAA---------IKAKVTQLLEMVQLAHLA-DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 518843096 172 RAAIRALMREWR-----GGVLVaSHDRELLDDV-DRI 202
Cdd:PRK10851 172 RKELRRWLRQLHeelkfTSVFV-THDQEEAMEVaDRV 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
353-519 |
5.66e-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: 71.44 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLR-----APVSGTVRRAEGRIVLLDQ-------QVGLL----DP-EGTILD 415
Cdd:cd03260 20 SLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVdvlelrrRVGMVfqkpNPfPGSIYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 416 NIR---RLHPDAGDEEAYAL---CARFA--FRNRDARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESV 487
Cdd:cd03260 100 NVAyglRLHGIKLKEELDERveeALRKAalWDEVKDRLHALGLSGGQQQRLCLARAL--ANEPEVLLLDEPTSALDPIST 177
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 488 EILENALLSF--DGALLVVSHDPSFVERVGfDRV 519
Cdd:cd03260 178 AKIEELIAELkkEYTIVIVTHNMQQAARVA-DRT 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-513 |
5.83e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.45 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 366 GANGAGKTTLLRIAAGLRAPVSGTVR---RAEGRIVLldQQVGLLdPE--G-----TILDNIR---RLH---PDAGDEEA 429
Cdd:COG4152 34 GPNGAGKTTTIRIILGILAPDSGEVLwdgEPLDPEDR--RRIGYL-PEerGlypkmKVGEQLVylaRLKglsKAEAKRRA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 430 YALCARFAFRNRDARRvVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENALLSF--DGA-LLVVSH 506
Cdd:COG4152 111 DEWLERLGLGDRANKK-VEELSKGNQQKVQLIAALLHD--PELLILDEPFSGLDPVNVELLKDVIRELaaKGTtVIFSSH 187
|
....*..
gi 518843096 507 DPSFVER 513
Cdd:COG4152 188 QMELVEE 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-202 |
6.33e-14 |
|
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: 71.00 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 21 QKLTFAIG-TERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----IGLLRQDM---PGGWTLAEALGVANDLER 91
Cdd:cd03263 19 DDLSLNVYkGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdRKAARQSLgycPQFDALFDELTVREHLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 92 LERILAGNGTAGDFDaADWTLEsrigaalaQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAG 171
Cdd:cd03263 99 YARLKGLPKSEIKEE-VELLLR--------VLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
170 180 190
....*....|....*....|....*....|...
gi 518843096 172 RAAIRALMREWRGG--VLVASHDrelLDDVDRI 202
Cdd:cd03263 169 RRAIWDLILEVRKGrsIILTTHS---MDEAEAL 198
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
334-491 |
7.22e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 334 VLAMEGVVAEAGDRRL-GPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-----RAEGRIVLLDQQVGL- 406
Cdd:PRK13538 1 MLEARNLACERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepIRRQRDEYHQDLLYLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 407 ----LDPEGTILDNIR---RLHPDAGDEEAYALCARFAFRNR-DArrVVGTLSGGERLRAGLAAALSGSAPPWliILDEP 478
Cdd:PRK13538 81 hqpgIKTELTALENLRfyqRLHGPGDDEALWEALAQVGLAGFeDV--PVRQLSAGQQRRVALARLWLTRAPLW--ILDEP 156
|
170
....*....|...
gi 518843096 479 TNHLDIESVEILE 491
Cdd:PRK13538 157 FTAIDKQGVARLE 169
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
10-203 |
8.28e-14 |
|
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: 71.22 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 10 VCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-----------TIGLLRQDMPGGW 77
Cdd:cd03296 8 VSKRFGDFVALDDVSLDIPSgELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 78 TLAEALGVANDLERLERILAGNGTagdfdaadwTLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDL 157
Cdd:cd03296 88 HMTVFDNVAFGLRVKPRSERPPEA---------EIRAKVHELLKLVQLDWLA-DRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518843096 158 LLLDEPTNNLDAAGRAAIRALMREWRGGVLVAS----HDR-ELLDDVDRIL 203
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTvfvtHDQeEALEVADRVV 208
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
34-183 |
1.03e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.88 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-------------TIGLLRQDmpggwtlaealgvaNDLE-RLE-RILAG 98
Cdd:COG4604 32 LIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvattpsrelakRLAILRQE--------------NHINsRLTvRELVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 99 NG----TAGDFDAADWTLesrIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAagRAA 174
Cdd:COG4604 98 FGrfpySKGRLTAEDREI---IDEAIAYLDLEDLA-DRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM--KHS 171
|
....*....
gi 518843096 175 iRALMREWR 183
Cdd:COG4604 172 -VQMMKLLR 179
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-519 |
1.05e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.30 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGL--AEPSSGTV----------------RRTGT 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEgEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 66 I-----GLLRQDMPGGWTLAEAlgVANDLER-----LERILAGNGtagdfdaaDWTLESRIGAALAQVGLPALP-LDRCL 134
Cdd:TIGR03269 81 PcpvcgGTLEPEEVDFWNLSDK--LRRRIRKriaimLQRTFALYG--------DDTVLDNVLEALEEIGYEGKEaVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 135 ----------------RTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAG----RAAIRALMREWRGGVLVASHDRE 194
Cdd:TIGR03269 151 dliemvqlshrithiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 195 LLDDV-DR--ILELTAIgarsfgggwsafsaardedrrrasAELERADADVRAVRQAVQARREAKErrdragrafaakgs 271
Cdd:TIGR03269 231 VIEDLsDKaiWLENGEI------------------------KEEGTPDEVVAVFMEGVSEVEKECE-------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 272 epkILLGARAERAQNSggTAQAISDRRmgralaeaddarsrvevltpltialppsGLpsganVLAMEGVvaeagdrrlgp 351
Cdd:TIGR03269 273 ---VEVGEPIIKVRNV--SKRYISVDR----------------------------GV-----VKAVDNV----------- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 352 wTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-------------------RAEGRIVLLDQQVGLLdPEGT 412
Cdd:TIGR03269 304 -SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewvdmtkpgpdgrgRAKRYIGILHQEYDLY-PHRT 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 413 ILDNIRR-LHPDAGDEEA-----YALCArFAFRNRDARRVV----GTLSGGERLRAGLAAALSGSapPWLIILDEPTNHL 482
Cdd:TIGR03269 382 VLDNLTEaIGLELPDELArmkavITLKM-VGFDEEKAEEILdkypDELSEGERHRVALAQVLIKE--PRIVILDEPTGTM 458
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 518843096 483 D-IESVEILE---NALLSFDGALLVVSHDPSFVERVgFDRV 519
Cdd:TIGR03269 459 DpITKVDVTHsilKAREEMEQTFIIVSHDMDFVLDV-CDRA 498
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
360-508 |
1.10e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 73.55 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTV------------RRAEGRIVLLDQQVGLLDpeGTILDNIRRLHPDAGDE 427
Cdd:TIGR02868 362 ERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssldqDEVRRRVSVCAQDAHLFD--TTVRENLRLARPDATDE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 428 EAYALCARFAFRNRDARRVVG----------TLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSF 497
Cdd:TIGR02868 440 ELWAALERVGLADWLRALPDGldtvlgeggaRLSGGERQRLALARALLADAP--ILLLDEPTEHLDAETADELLEDLLAA 517
|
170
....*....|...
gi 518843096 498 DG--ALLVVSHDP 508
Cdd:TIGR02868 518 LSgrTVVLITHHL 530
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
341-484 |
1.15e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 341 VAEAGdrRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRApvsgtvrrAEGRIVLLDQQVGLLDPEGtiLDNIR-- 418
Cdd:COG4138 6 VAVAG--RLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP--------GQGEILLNGRPLSDWSAAE--LARHRay 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 -----------------RLH-PDAGDEEA-----YALCARFAFRNRDARRvVGTLSGGERLRAGLAAAL-----SGSAPP 470
Cdd:COG4138 74 lsqqqsppfampvfqylALHqPAGASSEAveqllAQLAEALGLEDKLSRP-LTQLSGGEWQRVRLAAVLlqvwpTINPEG 152
|
170
....*....|....
gi 518843096 471 WLIILDEPTNHLDI 484
Cdd:COG4138 153 QLLLLDEPMNSLDV 166
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
30-201 |
1.23e-13 |
|
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: 70.38 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLL----RQDMPGGWTLAEA-----LGVANDLER-LERIlag 98
Cdd:TIGR04406 28 EIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdITHLpmheRARLGIGYLPQEAsifrkLTVEENIMAvLEIR--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 99 ngtaGDFDAADwtLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRAL 178
Cdd:TIGR04406 105 ----KDLDRAE--REERLEALLEEFQISHL-RDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKI 177
|
170 180
....*....|....*....|....*..
gi 518843096 179 MREWRG---GVLVASHD-RELLDDVDR 201
Cdd:TIGR04406 178 IKHLKErgiGVLITDHNvRETLDICDR 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-203 |
1.24e-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: 70.51 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-TIGLLRQDMPggwtlAEALGVANDLerLERILAGNGTAGDFdaa 108
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIK-----ADYEGTVRDL--LSSITKDFYTHPYF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 109 dwtlESRIGAALAQVGLpalpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGR----AAIRALMREWRG 184
Cdd:cd03237 96 ----KTEIAKPLQIEQI----LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFAENNEK 167
|
170 180
....*....|....*....|
gi 518843096 185 GVLVASHDRELLDDV-DRIL 203
Cdd:cd03237 168 TAFVVEHDIIMIDYLaDRLI 187
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-192 |
1.40e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAePSSGTVRrtgtigLLRQDMpGGWTLAEalgvandLERLERILAGNGTAG------ 103
Cdd:COG4138 23 ELIHLIGPNGAGKSTLLARMAGLL-PGQGEIL------LNGRPL-SDWSAAE-------LARHRAYLSQQQSPPfampvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 104 ---DFDAADWTLESRIGAALAQV----GLPALpLDRCLRTLSGGERTRVGIARLVME-------APDLLLLDEPTNNLDA 169
Cdd:COG4138 88 qylALHQPAGASSEAVEQLLAQLaealGLEDK-LSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*.
gi 518843096 170 AGRAAIRALMREWR---GGVLVASHD 192
Cdd:COG4138 167 AQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-203 |
1.52e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.79 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 7 LDSVCARTPDG-PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQDMPGgwtLAEALG 84
Cdd:PRK13644 4 LENVSYSYPDGtPALENINLVIKKgEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQG---IRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 85 VAndLERLERILAGNGTAGD--FDAADWTL-----ESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDL 157
Cdd:PRK13644 81 IV--FQNPETQFVGRTVEEDlaFGPENLCLppieiRKRVDRALAEIGLEKYR-HRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518843096 158 LLLDEPTNNLDA-AGRAAIRALMREWRGG--VLVASHDRELLDDVDRIL 203
Cdd:PRK13644 158 LIFDEVTSMLDPdSGIAVLERIKKLHEKGktIVYITHNLEELHDADRII 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-521 |
1.88e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.92 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGtvrrtgtigllRQDMPGGWtlaealgvANDLER---------LERILAGN--- 99
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLG-----------DYEEEPSW--------DEVLKRfrgtelqnyFKKLYNGEikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 ---------------GTAGD-FDAADwtlESRIGAALA-QVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDE 162
Cdd:PRK13409 163 vhkpqyvdlipkvfkGKVRElLKKVD---ERGKLDEVVeRLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 163 PTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLD---DVDRILeltaigarsFG--GGWSAFSaardedrrrasael 235
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELAEGkyVLVVEHDLAVLDylaDNVHIA---------YGepGAYGVVS-------------- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 236 eradaDVRAVRQAVQA------RREAKERRDRAgrafaakgsepkILLGARAERaqnsggtaqaisdrrmgralaEADDA 309
Cdd:PRK13409 296 -----KPKGVRVGINEylkgylPEENMRIRPEP------------IEFEERPPR---------------------DESER 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 310 RSRVEVlTPLTIALPPSGLpsganvlamegvVAEAGDRRLGpwtlridgpERIALKGANGAGKTTLLRIAAGLRAPVSGT 389
Cdd:PRK13409 338 ETLVEY-PDLTKKLGDFSL------------EVEGGEIYEG---------EVIGIVGPNGIGKTTFAKLLAGVLKPDEGE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 390 VRrAEGRIVLLDQQVGLlDPEGTILDNIRRLHPDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSAP 469
Cdd:PRK13409 396 VD-PELKISYKPQYIKP-DYDGTVEDLLRSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDAD 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 470 pwLIILDEPTNHLDIE---SV-----EILENallsFDGALLVVSHDPSFVERVGfDR--VFE 521
Cdd:PRK13409 474 --LYLLDEPSAHLDVEqrlAVakairRIAEE----REATALVVDHDIYMIDYIS-DRlmVFE 528
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-205 |
2.26e-13 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 69.82 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 15 PDGPL-FQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTV----------------RRTGTIglLRQDMPGG 76
Cdd:cd03252 12 PDGPViLDNISLRIKPgEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladpawlrRQVGVV--LQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 77 WTLAEALGVANDLERLERILAGNGTAGdfdAADWTLESRIG--AALAQVGLpalpldrclrTLSGGERTRVGIARLVMEA 154
Cdd:cd03252 90 RSIRDNIALADPGMSMERVIEAAKLAG---AHDFISELPEGydTIVGEQGA----------GLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518843096 155 PDLLLLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRILEL 205
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAHRLSTVKNADRIIVM 209
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-206 |
2.34e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 69.42 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigllRQ-DMPGgwtlAEALGVANDLERLERILAGNGTAGDFDAA 108
Cdd:TIGR01184 12 EFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-----KQiTEPG----PDRMVVFQNYSLLPWLTVRENIALAVDRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 109 DWTL-----ESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIR-ALMREW 182
Cdd:TIGR01184 83 LPDLskserRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQeELMQIW 161
|
170 180
....*....|....*....|....*...
gi 518843096 183 ---RGGVLVASHD-RELLDDVDRILELT 206
Cdd:TIGR01184 162 eehRVTVLMVTHDvDEALLLSDRVVMLT 189
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-192 |
2.42e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAePSSGTVRRTGTigLLRQdmpggWTLAEalgvandLERLERILAGNGTAGdFDAAD 109
Cdd:PRK03695 23 EILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQ--PLEA-----WSAAE-------LARHRAYLSQQQTPP-FAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 110 WTLESRIGAALAQVGLPALPLD-------------RCLRTLSGGERTRVGIARLVME-APD------LLLLDEPTNNLDA 169
Cdd:PRK03695 87 FQYLTLHQPDKTRTEAVASALNevaealglddklgRSVNQLSGGEWQRVRLAAVVLQvWPDinpagqLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*.
gi 518843096 170 AGRAAIRALMREW---RGGVLVASHD 192
Cdd:PRK03695 167 AQQAALDRLLSELcqqGIAVVMSSHD 192
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
354-508 |
2.88e-13 |
|
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: 68.67 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRivlLDQQVGLLDPEG-------------TILDNIRRL 420
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP---LDFQRDSIARGLlylghapgikttlSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 421 HPDAGDEEAYALCARFAFRNRDaRRVVGTLSGGERLRAGLAAALSGSAPPWliILDEPTNHLDIESVEILENAL---LSF 497
Cdd:cd03231 98 HADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLW--ILDEPTTALDKAGVARFAEAMaghCAR 174
|
170
....*....|.
gi 518843096 498 DGALLVVSHDP 508
Cdd:cd03231 175 GGMVVLTTHQD 185
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
30-205 |
2.89e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.42 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTiGLLRQDMPGGWTL-AEALGVA----------NDLE--RLERIL 96
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQ-PLHQMDEEARAKLrAKHVGFVfqsfmliptlNALEnvELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 97 AGNGTAgdfdaadwtlESRIGAA--LAQVGLpALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA 174
Cdd:PRK10584 116 RGESSR----------QSRNGAKalLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190
....*....|....*....|....*....|....*
gi 518843096 175 IRALM----REWRGGVLVASHDRELLDDVDRILEL 205
Cdd:PRK10584 185 IADLLfslnREHGTTLILVTHDLQLAARCDRRLRL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
363-520 |
3.01e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 68.85 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTVR--------RAEGRIVLLDQQVGLLdPEGTILDNIR---RLH---PDAGDEE 428
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldiAARNRIGYLPEERGLY-PKMKVIDQLVylaQLKglkKEEARRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 429 AYALCARFAFRNRDARRvVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENALLSFDGA---LLVVS 505
Cdd:cd03269 109 IDEWLERLELSEYANKR-VEELSKGNQQKVQFIAAVIHD--PELLILDEPFSGLDPVNVELLKDVIRELARAgktVILST 185
|
170
....*....|....*
gi 518843096 506 HDPSFVERVGfDRVF 520
Cdd:cd03269 186 HQMELVEELC-DRVL 199
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
16-192 |
3.02e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.66 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 16 DGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGLLRQDMPggwtLAE 81
Cdd:PRK11231 14 TKRILNDLSLSLPTGKItALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLPQHHL----TPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 82 ALGVandlerleRILAGNGTA------GDFDAADwtlESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAP 155
Cdd:PRK11231 90 GITV--------RELVAYGRSpwlslwGRLSAED---NARVNQAMEQTRINHLA-DRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518843096 156 DLLLLDEPTNNLDAAGRAAIRALMREWRGG---VLVASHD 192
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQgktVVTVLHD 197
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-194 |
3.10e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.73 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGTERVGLV-GRNGSGKSTLLRIVAGLAEPSSGTVRRTGTigllRQDMPGG------- 76
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVlGPSGCGKTTLLNLIAGFVPYQHGSITLDGK----PVEGPGAergvvfq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 77 ------WTLAEAlGVANDLErleriLAGNGTAgdfdaadwTLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARL 150
Cdd:PRK11248 78 negllpWRNVQD-NVAFGLQ-----LAGVEKM--------QRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518843096 151 VMEAPDLLLLDEPTNNLDAAGRAAIRA-LMREWRGG---VLVASHDRE 194
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTlLLKLWQETgkqVLLITHDIE 190
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-194 |
3.15e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.89 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAfLTLDSVCARTPDG----PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTI--------G 67
Cdd:COG4525 1 MSM-LTVRHVSVRYPGGgqpqPALQDVSLTIESgEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 68 LLRQD---MPggWtlaeaLGVANDLErLERILAGNGTAGDFDAADwtlesrigAALAQVGLPALPlDRCLRTLSGGERTR 144
Cdd:COG4525 80 VVFQKdalLP--W-----LNVLDNVA-FGLRLRGVPKAERRARAE--------ELLALVGLADFA-RRRIWQLSGGMRQR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518843096 145 VGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRAL-MREWRG---GVLVASHDRE 194
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQELlLDVWQRtgkGVFLITHSVE 196
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
23-205 |
3.16e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 68.85 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 23 LTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG---------TIGLLrqdmPGGWTLAEALGVANDLERL 92
Cdd:cd03269 19 ISFSVEKGEIfGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYL----PEERGLYPKMKVIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 93 ERiLAGNGTAgdfDAADWTLEsrigaALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGR 172
Cdd:cd03269 95 AQ-LKGLKKE---EARRRIDE-----WLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 518843096 173 AAIRALMREWRGG---VLVASHDRELLDDV-DRILEL 205
Cdd:cd03269 165 ELLKDVIRELARAgktVILSTHQMELVEELcDRVLLL 201
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-198 |
3.32e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGTERVGL-VGRNGSGKSTLLRIVAGLAEPSSGTvrrtGTIGLLRQDMPGGWTLAEALGvandlerleril 96
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLiVGASGSGKSTLLRLLAGALKGTPVA----GCVDVPDNQFGREASLIDAIG------------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 97 agngTAGDFDAAdwtlesriGAALAQVGLPALPL-DRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA--AGRA 173
Cdd:COG2401 108 ----RKGDFKDA--------VELLNAVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqtAKRV 175
|
170 180
....*....|....*....|....*..
gi 518843096 174 A--IRALMREWRGGVLVASHDRELLDD 198
Cdd:COG2401 176 ArnLQKLARRAGITLVVATHHYDVIDD 202
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-175 |
3.38e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGTVR---RTGTIGLLRQDMPggwTLAEALGVA-----NDL--ERLERILAGNGT 101
Cdd:PRK13634 36 VAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigeRVITAGKKNKKLK---PLRKKVGIVfqfpeHQLfeETVEKDICFGPM 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 102 agDFDAADWTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIAR-LVMEaPDLLLLDEPTNNLDAAGRAAI 175
Cdd:PRK13634 113 --NFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGvLAME-PEVLVLDEPTAGLDPKGRKEM 184
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
32-199 |
3.66e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.86 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGTVR--------RTGTIGL--LRQDMPGGWTLAEALGVANDLerLERILAGngt 101
Cdd:PRK13641 36 VALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpETGNKNLkkLRKKVSLVFQFPEAQLFENTV--LKDVEFG--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 102 AGDFDAADWTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMRE 181
Cdd:PRK13641 111 PKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD 190
|
170 180
....*....|....*....|.
gi 518843096 182 W-RGG--VLVASHDrelLDDV 199
Cdd:PRK13641 191 YqKAGhtVILVTHN---MDDV 208
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
30-192 |
6.08e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR---RTGTI-------------------GLLRQDMPGGWTLAEALGvAN 87
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLrdlyalseaerrrllrtewGFVHQHPRDGLRMQVSAG-GN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 88 DLERLerILAGNGTAGDF--DAADWtlesrigaaLAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:PRK11701 112 IGERL--MAVGARHYGDIraTAGDW---------LERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTG 180
|
170 180 190
....*....|....*....|....*....|.
gi 518843096 166 NLDAAGRAA----IRALMREWRGGVLVASHD 192
Cdd:PRK11701 181 GLDVSVQARlldlLRGLVRELGLAVVIVTHD 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
32-203 |
6.28e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.94 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGTvrrtgtigLLRQDMPggwtlaeaLGVANDLERL----ERIL--------AGN 99
Cdd:PRK11247 41 VAVVGRSGCGKSTLLRLLAGLETPSAGE--------LLAGTAP--------LAEAREDTRLmfqdARLLpwkkvidnVGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 GTAGDfdaadWTLESRigAALAQVGL-------PAlpldrclrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGR 172
Cdd:PRK11247 105 GLKGQ-----WRDAAL--QALAAVGLadranewPA--------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 518843096 173 ----AAIRALMREWRGGVLVASHD-RELLDDVDRIL 203
Cdd:PRK11247 170 iemqDLIESLWQQHGFTVLLVTHDvSEAVAMADRVL 205
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-181 |
6.32e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 4 FLTLDSVCARTPDGPLFQKLTFAI--GTeRVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------IGLLR 70
Cdd:PRK11432 6 FVVLKNITKRFGSNTVIDNLNLTIkqGT-MVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 71 QD------MPGGWTLAEAL---GVANDlERLERIlagngtagdfdaadwtlesriGAALAQVGLPALPlDRCLRTLSGGE 141
Cdd:PRK11432 85 QSyalfphMSLGENVGYGLkmlGVPKE-ERKQRV---------------------KEALELVDLAGFE-DRYVDQISGGQ 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518843096 142 RTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMRE 181
Cdd:PRK11432 142 QQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRE 181
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-202 |
6.63e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 68.42 E-value: 6.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------IGLLRQD 72
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEgEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 73 mpggWTLAEALGVANDLE---RLERIlagngtagdfDAADwtLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIAR 149
Cdd:cd03300 81 ----YALFPHLTVFENIAfglRLKKL----------PKAE--IKERVAEALDLVQLEGY-ANRKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518843096 150 -LVMEaPDLLLLDEPTNNLDAAGRAA----IRALMREWRGGVLVASHDR-ELLDDVDRI 202
Cdd:cd03300 144 aLVNE-PKVLLLDEPLGALDLKLRKDmqleLKRLQKELGITFVFVTHDQeEALTMSDRI 201
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
25-196 |
7.03e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 69.06 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 25 FAIGTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-------------TIGLLRQDmPGGWTLAEALgvandler 91
Cdd:PRK13652 26 IAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevrkFVGLVFQN-PDDQIFSPTV-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 92 lERILAGNGTAGDFDAAdwTLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAG 171
Cdd:PRK13652 97 -EQDIAFGPINLGLDEE--TVAHRVSSALHMLGLEEL-RDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180
....*....|....*....|....*....
gi 518843096 172 RAA----IRALMREWRGGVLVASHDRELL 196
Cdd:PRK13652 173 VKElidfLNDLPETYGMTVIFSTHQLDLV 201
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
32-168 |
7.43e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG---------TIGLLRQDMPGGWTLAEALGVANDLErleriLAGNGTA 102
Cdd:PRK09536 32 VGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsarAASRRVASVPQDTSLSFEFDVRQVVE-----MGRTPHR 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 103 GDFDAADWTLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD 168
Cdd:PRK09536 107 SRFDTWTETDRAAVERAMERTGVAQF-ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
353-519 |
1.01e-12 |
|
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: 67.74 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEgrIVLLDQQVGLLDPEGTILDNIRRLHPDAGDEEAYAL 432
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 433 CAR------FAFRNRDARRV------------VGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENAL 494
Cdd:cd03267 119 LAAiydlppARFKKRLDELSelldleelldtpVRQLSLGQRMRAEIAAALLHE--PEILFLDEPTIGLDVVAQENIRNFL 196
|
170 180
....*....|....*....|....*....
gi 518843096 495 LSF----DGALLVVSHDPSFVERVGfDRV 519
Cdd:cd03267 197 KEYnrerGTTVLLTSHYMKDIEALA-RRV 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
352-522 |
1.14e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 352 WTLRIDGPERIALKGANGAGKTTLLRIAAG--LRAPVSGTVRRAEGRIvllDQQVGLLD---PEGTILDNIRRLHpDAGD 426
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQF---GREASLIDaigRKGDFKDAVELLN-AVGL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 427 EEAYALCARFAfrnrdarrvvgTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENALLSF----DGALL 502
Cdd:COG2401 125 SDAVLWLRRFK-----------ELSTGQKFRFRLALLLAER--PKLLVIDEFCSHLDRQTAKRVARNLQKLarraGITLV 191
|
170 180
....*....|....*....|....*...
gi 518843096 503 VVSHDPSFVE--------RVGFDRVFEV 522
Cdd:COG2401 192 VATHHYDVIDdlqpdlliFVGYGGVPEE 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
360-508 |
1.21e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD-----QQVGLLD---PEGTILDNI---RRLHpDAGDEE 428
Cdd:PRK13539 29 EALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeacHYLGHRNamkPALTVAENLefwAAFL-GGEELD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 429 AYALCARFAFrNRDARRVVGTLSGGERLRAGLAAALSGSAPPWliILDEPTNHLDIESVEILENAL---LSFDGALLVVS 505
Cdd:PRK13539 108 IAAALEAVGL-APLAHLPFGYLSAGQKRRVALARLLVSNRPIW--ILDEPTAALDAAAVALFAELIrahLAQGGIVIAAT 184
|
...
gi 518843096 506 HDP 508
Cdd:PRK13539 185 HIP 187
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
360-520 |
1.32e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.41 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRaEGRIV-LLDQQVGlLDPEGTILDNIR---RLH--PDAGDEEAYALC 433
Cdd:COG1134 53 ESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-NGRVSaLLELGAG-FHPELTGRENIYlngRLLglSRKEIDEKFDEI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 434 ARFA----FRNRDarrvVGTLSGGERLRagLAAALSGSAPPWLIILDEPTnhldieSV--------------EILENAll 495
Cdd:COG1134 131 VEFAelgdFIDQP----VKTYSSGMRAR--LAFAVATAVDPDILLVDEVL------AVgdaafqkkclarirELRESG-- 196
|
170 180
....*....|....*....|....*
gi 518843096 496 sfdGALLVVSHDPSFVERVgFDRVF 520
Cdd:COG1134 197 ---RTVIFVSHSMGAVRRL-CDRAI 217
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-203 |
1.39e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.58 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 23 LTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG------------TIGL-------LRQDMPggwtLAEA 82
Cdd:COG4586 41 ISFTIEPgEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrrkefarRIGVvfgqrsqLWWDLP----AIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 83 LGVandLERLERIlagngtagdfDAADWtlESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDE 162
Cdd:COG4586 117 FRL---LKAIYRI----------PDAEY--KKRLDELVELLDLGEL-LDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518843096 163 PTNNLDAAGRAAIRALMREW--RGG--VLVASHDrelLDDV----DRIL 203
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYnrERGttILLTSHD---MDDIealcDRVI 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
363-519 |
1.48e-12 |
|
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: 67.14 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTV----------RRAEGRIVLLDQQVGLLDPEGTILDNIR---RLH---PDAGD 426
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdRKAARQSLGYCPQFDALFDELTVREHLRfyaRLKglpKSEIK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 427 EEAYALCARF---AFRNRDARrvvgTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSFDG--AL 501
Cdd:cd03263 112 EEVELLLRVLgltDKANKRAR----TLSGGMKRKLSLAIALIGGPS--VLLLDEPTSGLDPASRRAIWDLILEVRKgrSI 185
|
170
....*....|....*...
gi 518843096 502 LVVSHDPSFVERVGfDRV 519
Cdd:cd03263 186 ILTTHSMDEAEALC-DRI 202
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
363-484 |
1.57e-12 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 67.53 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTV-----------RRAEGRIVLLDQQVGLLDPEGTILDNI---RRLH------- 421
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVdlagvdlhglsRRARARRVALVEQDSDTAVPLTVRDVValgRIPHrslwagd 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518843096 422 PDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDI 484
Cdd:TIGR03873 111 SPHDAAVVDRALARTELSHL-ADRDMSTLSGGERQRVHVARALAQE--PKLLLLDEPTNHLDV 170
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
353-519 |
1.61e-12 |
|
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: 65.80 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAE-----------GRIVLLDQQVGLLDpeGTILDNIRRlh 421
Cdd:cd03247 22 SLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalsSLISVLNQRPYLFD--TTLRNNLGR-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 422 pdagdeeayalcaRFafrnrdarrvvgtlSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDiesvEILENALLSF---- 497
Cdd:cd03247 98 -------------RF--------------SGGERQRLALARILLQDAP--IVLLDEPTVGLD----PITERQLLSLifev 144
|
170 180
....*....|....*....|....
gi 518843096 498 --DGALLVVSHDPSFVERvgFDRV 519
Cdd:cd03247 145 lkDKTLIWITHHLTGIEH--MDKI 166
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
30-203 |
1.66e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.83 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-------------TIGLLRQDmPG----GWTLAE--ALGVANDLE 90
Cdd:PRK13650 34 EWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirhKIGMVFQN-PDnqfvGATVEDdvAFGLENKGI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 91 RLErilagngtagdfdaadwTLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAA 170
Cdd:PRK13650 113 PHE-----------------EMKERVNEALELVGMQDFK-EREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518843096 171 GR----AAIRALMREWRGGVLVASHDrelLDDV---DRIL 203
Cdd:PRK13650 175 GRleliKTIKGIRDDYQMTVISITHD---LDEValsDRVL 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
30-164 |
1.87e-12 |
|
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: 66.93 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigllrQDMpGGWTLAE--ALGVA---------NDLERLERILAG 98
Cdd:COG0410 30 EIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG------EDI-TGLPPHRiaRLGIGyvpegrrifPSLTVEENLLLG 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 99 NGTAGDFDAADWTLES------RIGAALAQVGlpalpldrclRTLSGGERTRVGIARLVMEAPDLLLLDEPT 164
Cdd:COG0410 103 AYARRDRAEVRADLERvyelfpRLKERRRQRA----------GTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
30-192 |
1.97e-12 |
|
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: 69.31 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigLLRQDMPGGWTLAEALGVANDLERLERILAGNGTAGDFDAAD 109
Cdd:TIGR02868 362 ERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG---VPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATD 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 110 wtleSRIGAALAQVGL----PALP--LDRCL----RTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALM 179
Cdd:TIGR02868 439 ----EELWAALERVGLadwlRALPdgLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL 514
|
170
....*....|....*
gi 518843096 180 REWRGG--VLVASHD 192
Cdd:TIGR02868 515 LAALSGrtVVLITHH 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-199 |
2.70e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 13 RTPDGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTI------GLL--RQDMPGGWTLAEAL 83
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVtGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrGLLalRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 84 GVANDLER-LERILAGNGTAGDfdaadwTLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIA-RLVMEApDLLLLD 161
Cdd:PRK13638 90 IFYTDIDSdIAFSLRNLGVPEA------EITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAgALVLQA-RYLLLD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518843096 162 EPTNNLDAAGRAAIRALMREWRGG---VLVASHDRELLDDV 199
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEI 202
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
354-512 |
2.76e-12 |
|
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: 66.59 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLL---DQQVGL------LDPEGTILDNIrrlhpda 424
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppeKRDISYvpqnyaLFPHMTVYKNI------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 425 gdeeAYALCARFAFRNRDARRV----------------VGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESVE 488
Cdd:cd03299 93 ----AYGLKKRKVDKKEIERKVleiaemlgidhllnrkPETLSGGEQQRVAIARAL--VVNPKILLLDEPFSALDVRTKE 166
|
170 180
....*....|....*....|....*...
gi 518843096 489 ILENALL----SFDGALLVVSHDpsFVE 512
Cdd:cd03299 167 KLREELKkirkEFGVTVLHVTHD--FEE 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-203 |
2.96e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.10 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 14 TPDG-PLFQKLTFAI-GTERVGLVGRNGSGKSTLLRIVAGLAePSSGTVRRTGTigLLRQDMPGGWTlaEALG-VANDLE 90
Cdd:PRK11174 359 SPDGkTLAGPLNFTLpAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGI--ELRELDPESWR--KHLSwVGQNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 91 RLERILAGNGTAGDFDAADwtleSRIGAALAQVG----LPALPL-------DRCLRtLSGGERTRVGIARLVMEAPDLLL 159
Cdd:PRK11174 434 LPHGTLRDNVLLGNPDASD----EQLQQALENAWvsefLPLLPQgldtpigDQAAG-LSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518843096 160 LDEPTNNLDA-AGRAAIRALMREWRG-GVLVASHDRELLDDVDRIL 203
Cdd:PRK11174 509 LDEPTASLDAhSEQLVMQALNAASRRqTTLMVTHQLEDLAQWDQIW 554
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
362-490 |
2.98e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 362 IALKGANGAGKTTLLRIAAGLRAPVSGTV------------RRAEGRIVLLDQQvgLLDPEGTildNIRRLhpdagdeEA 429
Cdd:PRK11231 31 TALIGPNGCGKSTLLKCFARLLTPQSGTVflgdkpismlssRQLARRLALLPQH--HLTPEGI---TVREL-------VA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 430 Y------ALCARFAFRNRD--------------ARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDI-ESVE 488
Cdd:PRK11231 99 YgrspwlSLWGRLSAEDNArvnqameqtrinhlADRRLTDLSGGQRQRAFLAMVLAQDTP--VVLLDEPTTYLDInHQVE 176
|
..
gi 518843096 489 IL 490
Cdd:PRK11231 177 LM 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-202 |
3.03e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 33 GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTigLLRQDMPggwTLAEALGVA---------NDLERLERILAGN--GT 101
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEILLDGE--PVRFRSP---RDAQAAGIAiihqelnlvPNLSVAENIFLGRepRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 102 AGDFDAAdwTLESRIGAALAQVGLPaLPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMRE 181
Cdd:COG1129 109 GGLIDWR--AMRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRR 185
|
170 180
....*....|....*....|....*...
gi 518843096 182 WRG---GVLVASHDrelLDDV----DRI 202
Cdd:COG1129 186 LKAqgvAIIYISHR---LDEVfeiaDRV 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-521 |
3.27e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.04 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGtvrrtgtigllRQDMPGGWtlaealgvanD--LER---------LERILAGN- 99
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLG-----------DYDEEPSW----------DevLKRfrgtelqdyFKKLANGEi 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 -----------------GTAGD-FDAADwtlESRIGAALA-QVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLL 160
Cdd:COG1245 161 kvahkpqyvdlipkvfkGTVRElLEKVD---ERGKLDELAeKLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 161 DEPTNNLD-----AAGRaAIRALMREWRgGVLVASHDRELLD---DVDRILeltaigarsFG--GGWSAFSaardedrrr 230
Cdd:COG1245 237 DEPSSYLDiyqrlNVAR-LIRELAEEGK-YVLVVEHDLAILDylaDYVHIL---------YGepGVYGVVS--------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 231 asaeleradaDVRAVRQAVQA------RREAKERRDRAgrafaakgsepkILLGARAERAQNSGGTaqaisdrrmgraLA 304
Cdd:COG1245 297 ----------KPKSVRVGINQyldgylPEENVRIRDEP------------IEFEVHAPRREKEEET------------LV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 305 EADDarsrvevltpLTIALPPSGLpsganvlamegvVAEAGDRRLGpwtlridgpERIALKGANGAGKTTLLRIAAGLRA 384
Cdd:COG1245 343 EYPD----------LTKSYGGFSL------------EVEGGEIREG---------EVLGIVGPNGIGKTTFAKILAGVLK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 385 PVSGTVRRAEgRIVLLDQQVGlLDPEGTILDNIRRLHPDAGDEEAYalcarfafRNRDARRV---------VGTLSGGER 455
Cdd:COG1245 392 PDEGEVDEDL-KISYKPQYIS-PDYDGTVEEFLRSANTDDFGSSYY--------KTEIIKPLgleklldknVKDLSGGEL 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 456 LRAGLAAALSGSAPpwLIILDEPTNHLDIES----VEILENALLSFDGALLVVSHDPSFVERVGfDR--VFE 521
Cdd:COG1245 462 QRVAIAACLSRDAD--LYLLDEPSAHLDVEQrlavAKAIRRFAENRGKTAMVVDHDIYLIDYIS-DRlmVFE 530
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
33-181 |
3.29e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 67.80 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 33 GLVGRNGSGKSTLLRIVAGLAEPSSGTV-------------------RRTGTI----GLLRQDmpggwTLAEalGVANDL 89
Cdd:COG1135 35 GIIGYSGAGKSTLIRCINLLERPTSGSVlvdgvdltalserelraarRKIGMIfqhfNLLSSR-----TVAE--NVALPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ErleriLAGngtagdFDAADwtLESRIGAALAQVGLP----ALPldrclRTLSGGERTRVGIAR-LVMEaPDLLLLDEPT 164
Cdd:COG1135 108 E-----IAG------VPKAE--IRKRVAELLELVGLSdkadAYP-----SQLSGGQKQRVGIARaLANN-PKVLLCDEAT 168
|
170
....*....|....*..
gi 518843096 165 NNLDAAGRAAIRALMRE 181
Cdd:COG1135 169 SALDPETTRSILDLLKD 185
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-176 |
3.75e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.56 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 23 LTFAIGtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTigllrqdmpggwtlaealgVANDLERLERILA----- 97
Cdd:PRK11650 25 LDVADG-EFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR-------------------VVNELEPADRDIAmvfqn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 98 ----------GN--------GTAGDfdaadwTLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLL 159
Cdd:PRK11650 85 yalyphmsvrENmayglkirGMPKA------EIEERVAEAARILELEPL-LDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170
....*....|....*..
gi 518843096 160 LDEPTNNLDAAGRAAIR 176
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMR 174
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-203 |
4.10e-12 |
|
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: 64.76 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigllRQDMPGGWTLAEALGVANDLErlERilAGNGTAGDFDAAD 109
Cdd:cd03215 27 EIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG-----KPVTRRSPRDAIRAGIAYVPE--DR--KREGLVLDLSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 110 wtlesrigaalaQVGLPALpldrclrtLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWR---GGV 186
Cdd:cd03215 98 ------------NIALSSL--------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAV 157
|
170
....*....|....*...
gi 518843096 187 LVASHD-RELLDDVDRIL 203
Cdd:cd03215 158 LLISSElDELLGLCDRIL 175
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-205 |
4.49e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.75 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG--PLFQKLTFAI--GTeRVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGL-LRQDMPggWTL 79
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIprGS-WTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGItLTAKTV--WDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 80 AEALGVAndLERLERILAGnGTAGDfDAAdWTLESR----------IGAALAQVGLPALpLDRCLRTLSGGERTRVGIAR 149
Cdd:PRK13640 83 REKVGIV--FQNPDNQFVG-ATVGD-DVA-FGLENRavprpemikiVRDVLADVGMLDY-IDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 150 LVMEAPDLLLLDEPTNNLDAAGRAAI----RALMREWRGGVLVASHDRELLDDVDRILEL 205
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQIlkliRKLKKKNNLTVISITHDIDEANMADQVLVL 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-202 |
5.24e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 63.99 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQDMpggwtLAEALGVAndlerlerilagngtagdfdaad 109
Cdd:cd03216 27 EVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR-----DARRAGIA----------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 110 wtlesrigaalaqvglpalpldrCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRG---GV 186
Cdd:cd03216 79 -----------------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAV 135
|
170
....*....|....*..
gi 518843096 187 LVASHD-RELLDDVDRI 202
Cdd:cd03216 136 IFISHRlDEVFEIADRV 152
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-202 |
6.35e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------------IGLLRQDmpggwtlaeaLGVANDLERLERILAGN 99
Cdd:PRK09700 36 LLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQE----------LSVIDELTVLENLYIGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 GTAGDF---DAADWTlESRIGAA--LAQVGLpALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA 174
Cdd:PRK09700 106 HLTKKVcgvNIIDWR-EMRVRAAmmLLRVGL-KVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDY 183
|
170 180 190
....*....|....*....|....*....|..
gi 518843096 175 IRALMREWRG---GVLVASHD-RELLDDVDRI 202
Cdd:PRK09700 184 LFLIMNQLRKegtAIVYISHKlAEIRRICDRY 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
30-203 |
8.15e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR--------------RTGTIGLLRQDMpgGWTLaEALGVANDLERLERI 95
Cdd:PRK11264 30 EVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslsqQKGLIRQLRQHV--GFVF-QNFNLFPHRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 96 LAGNGTAGDFDAADWTLESRigAALAQVGLpALPLDRCLRTLSGGERTRVGIAR-LVMEaPDLLLLDEPTNNLDA--AGR 172
Cdd:PRK11264 107 IEGPVIVKGEPKEEATARAR--ELLAKVGL-AGKETSYPRRLSGGQQQRVAIARaLAMR-PEVILFDEPTSALDPelVGE 182
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 173 --AAIRALMREWRGGVLVaSHDRELLDDV-DRIL 203
Cdd:PRK11264 183 vlNTIRQLAQEKRTMVIV-THEMSFARDVaDRAI 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-205 |
8.61e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAFLTLDSVCARTPDGP----LFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT---------I 66
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEeqveVLKGISLDIYAgEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvatldadaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 67 GLLRQDMPG----GWTLAEALGVANDLErLERILAGNGTAgdfdaadwTLESRIGAALAQVGLpALPLDRCLRTLSGGER 142
Cdd:PRK10535 81 AQLRREHFGfifqRYHLLSHLTAAQNVE-VPAVYAGLERK--------QRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 143 TRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRG---GVLVASHDRELLDDVDRILEL 205
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQVAAQAERVIEI 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-203 |
9.55e-12 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 64.44 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 8 DSVCAR-TPDGPL-FQKLTFAI-GTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG----TIGL--LR-------Q 71
Cdd:cd03244 6 KNVSLRyRPNLPPvLKNISFSIkPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdisKIGLhdLRsrisiipQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 72 D---MPGgwTLAEAL---GVANDlERLERILAGNGTAGDFDAADWTLESRIgaalaqvglpalplDRCLRTLSGGERTRV 145
Cdd:cd03244 86 DpvlFSG--TIRSNLdpfGEYSD-EELWQALERVGLKEFVESLPGGLDTVV--------------EEGGENLSVGQRQLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 146 GIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRIL 203
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDctVLTIAHRLDTIIDSDRIL 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
353-513 |
9.77e-12 |
|
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: 64.55 E-value: 9.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSG----------TVRRAEGR----IVLldQQVGLLdpEGTILDNIR 418
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGqilidgidirDISRKSLRsmigVVL--QDTFLF--SGTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 RLHPDAGDEEAYALCARFAFRNRDARR------VVG----TLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESVE 488
Cdd:cd03254 99 LGRPNATDEEVIEAAKEAGAHDFIMKLpngydtVLGenggNLSQGERQLLAIARAM--LRDPKILILDEATSNIDTETEK 176
|
170 180
....*....|....*....|....*..
gi 518843096 489 ILENALLS-FDG-ALLVVSHDPSFVER 513
Cdd:cd03254 177 LIQEALEKlMKGrTSIIIAHRLSTIKN 203
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
5-197 |
9.95e-12 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 64.97 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGlaEPSSGTVRrtGTIGLLRQD---MP------ 74
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKgEIHAIMGPNGSGKSTLSKTIAG--HPSYEVTS--GTILFKGQDlleLEpderar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 75 GGWTLA-----EALGVANDL---ERLERILAGNGTaGDFDAADWtlESRIGAALAQVGLPALPLDRCLRT-LSGGERTRV 145
Cdd:TIGR01978 77 AGLFLAfqypeEIPGVSNLEflrSALNARRSARGE-EPLDLLDF--EKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 146 GIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRG---GVLVASHDRELLD 197
Cdd:TIGR01978 154 EILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLLN 208
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-191 |
1.01e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 16 DGPLFQKLTFAIGTERVGLV-GRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQDMPGGWTLAEALGVANDLERLER 94
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 95 ILAGNGTAGdfdaadWTLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAG--- 171
Cdd:PRK13543 103 LHFLCGLHG------RRAKQMPGSALAIVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGitl 175
|
170 180
....*....|....*....|.
gi 518843096 172 -RAAIRALMREwRGGVLVASH 191
Cdd:PRK13543 176 vNRMISAHLRG-GGAALVTTH 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
333-507 |
1.04e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 333 NVLAMEGVVAEAGDRR-LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEG-RIVLLDQQVGLLDPE 410
Cdd:PRK09544 3 SLVSLENVSVSFGQRRvLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 411 GTILDNIRRLHPDAGDEEAYALCARF-AFRNRDARrvVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIES--- 486
Cdd:PRK09544 83 PLTVNRFLRLRPGTKKEDILPALKRVqAGHLIDAP--MQKLSGGETQRVLLARALLNR--PQLLVLDEPTQGVDVNGqva 158
|
170 180
....*....|....*....|..
gi 518843096 487 -VEILENALLSFDGALLVVSHD 507
Cdd:PRK09544 159 lYDLIDQLRRELDCAVLMVSHD 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
360-519 |
1.06e-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: 64.77 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTV-------------RRAEGRIVLLDQQVGLLdPEGTILDNIR-------- 418
Cdd:cd03219 27 EIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditglpphEIARLGIGRTFQIPRLF-PELTVLENVMvaaqartg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 --------RLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEIL 490
Cdd:cd03219 106 sglllaraRREEREARERAEELLERVGLADL-ADRPAGELSYGQQRRLEIARALATD--PKLLLLDEPAAGLNPEETEEL 182
|
170 180 190
....*....|....*....|....*....|..
gi 518843096 491 ENALLS---FDGALLVVSHDPSFVERVGfDRV 519
Cdd:cd03219 183 AELIRElreRGITVLLVEHDMDVVMSLA-DRV 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
363-519 |
1.07e-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: 63.22 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSgtvrraeGRIVLLDQQVGLLDPegtildnirrlhpdagdeeayalcarfafrnRD 442
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPDS-------GEILVDGKEVSFASP-------------------------------RD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 443 ARR----VVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENAL--LSFDG-ALLVVSHDPSFVERVG 515
Cdd:cd03216 72 ARRagiaMVYQLSVGERQMVEIARALARNAR--LLILDEPTAALTPAEVERLFKVIrrLRAQGvAVIFISHRLDEVFEIA 149
|
....
gi 518843096 516 fDRV 519
Cdd:cd03216 150 -DRV 152
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
353-513 |
1.19e-11 |
|
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: 64.38 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRA---------EGRIVLLDQQVG------LLDPEGTILDNI 417
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAgqdlfaldeDARARLRARHVGfvfqsfQLLPTLTALENV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 -----RRLHPDAGdEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILEN 492
Cdd:COG4181 112 mlpleLAGRRDAR-ARARALLERVGLGHR-LDHYPAQLSGGEQQRVALARAFATE--PAILFADEPTGNLDAATGEQIID 187
|
170 180
....*....|....*....|....*..
gi 518843096 493 ALlsFD-----GA-LLVVSHDPSFVER 513
Cdd:COG4181 188 LL--FElnrerGTtLVLVTHDPALAAR 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-226 |
1.20e-11 |
|
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: 65.26 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQD---MPGgwTLAEAL--GVANDLER 91
Cdd:cd03291 51 PVLKNINLKIEKgEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFswiMPG--TIKENIifGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 92 LERILAGNGTAGD---FDAADWTLesrigaaLAQVGLpalpldrclrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD 168
Cdd:cd03291 129 YKSVVKACQLEEDitkFPEKDNTV-------LGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518843096 169 AAGRAAIR-----ALMREwRGGVLVAShDRELLDDVDRILELTAiGARSFGGGWSAFSAARDE 226
Cdd:cd03291 192 VFTEKEIFescvcKLMAN-KTRILVTS-KMEHLKKADKILILHE-GSSYFYGTFSELQSLRPD 251
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-199 |
1.21e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.53 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 15 PDGPLFQKLTFAIGTE-----RVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQDMPGGWTLAEALGVANDL 89
Cdd:PRK13643 13 PNSPFASRALFDIDLEvkkgsYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ---ERLERILAGNGTAG--DFDAADWTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPT 164
Cdd:PRK13643 93 pesQLFEETVLKDVAFGpqNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 518843096 165 NNLDAAGRAAIRAL---MREWRGGVLVASHdreLLDDV 199
Cdd:PRK13643 173 AGLDPKARIEMMQLfesIHQSGQTVVLVTH---LMDDV 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
354-519 |
1.23e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.77 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-------------RAEGRIVLLDQQVGL------LDPEGTIL 414
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslsQQKGLIRQLRQHVGFvfqnfnLFPHRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 415 DNI-------RRLHPDAGDEEAYALCARFAFRNRD---ARRvvgtLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDI 484
Cdd:PRK11264 104 ENIiegpvivKGEPKEEATARARELLAKVGLAGKEtsyPRR----LSGGQQQRVAIARAL--AMRPEVILFDEPTSALDP 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 518843096 485 ESV-EILEN--ALLSFDGALLVVSHDPSFVERVGfDRV 519
Cdd:PRK11264 178 ELVgEVLNTirQLAQEKRTMVIVTHEMSFARDVA-DRA 214
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
30-206 |
2.10e-11 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 63.79 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR------RTGTIGLLRQDMpggwtlaeALgVANDLERLERILAGNGTAG 103
Cdd:cd03251 29 ETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvRDYTLASLRRQI--------GL-VSQDVFLFNDTVAENIAYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 104 DFDAADWTLESRIGAALAQVGLPALPL-------DRCLRtLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD----AAGR 172
Cdd:cd03251 100 RPGATREEVEEAARAANAHEFIMELPEgydtvigERGVK-LSGGQRQRIAIARALLKDPPILILDEATSALDteseRLVQ 178
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 173 AAIRALMRewRGGVLVASHDRELLDDVDRILELT 206
Cdd:cd03251 179 AALERLMK--NRTTFVIAHRLSTIENADRIVVLE 210
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
349-506 |
2.18e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 349 LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV-------RRAE-GRIVLLDQQVGLLDPEGTILDNIRRL 420
Cdd:PRK13543 27 FGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDrSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 421 ------HPDAGDEEAYALCARFAFrnrdARRVVGTLSGGERLRAGLAAALSGSAPPWLiiLDEPTNHLDIESVEILENAL 494
Cdd:PRK13543 107 cglhgrRAKQMPGSALAIVGLAGY----EDTLVRQLSAGQKKRLALARLWLSPAPLWL--LDEPYANLDLEGITLVNRMI 180
|
170
....*....|....*
gi 518843096 495 ---LSFDGALLVVSH 506
Cdd:PRK13543 181 sahLRGGGAALVTTH 195
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
353-495 |
2.38e-11 |
|
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: 63.26 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQVGL------LDPEGTILDNIrrlhpdagd 426
Cdd:cd03293 24 SLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYvfqqdaLLPWLTVLDNV--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 427 eeAYALCARFAFRNRDARRV------VG----------TLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESVEIL 490
Cdd:cd03293 95 --ALGLELQGVPKAEARERAeellelVGlsgfenayphQLSGGMRQRVALARAL--AVDPDVLLLDEPFSALDALTREQL 170
|
....*
gi 518843096 491 ENALL 495
Cdd:cd03293 171 QEELL 175
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
353-515 |
2.60e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.68 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV---------RRAEGRIVLLDQQVGL------LDPEGTILDN- 416
Cdd:PRK11629 29 SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmskLSSAAKAELRNQKLGFiyqfhhLLPDFTALENv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 417 -----IRRLHPDAGDEEAYALCARFAFRNRDARRvVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILE 491
Cdd:PRK11629 109 ampllIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNN--PRLVLADEPTGNLDARNADSIF 185
|
170 180
....*....|....*....|....*...
gi 518843096 492 NALLSFD----GALLVVSHDPSFVERVG 515
Cdd:PRK11629 186 QLLGELNrlqgTAFLVVTHDLQLAKRMS 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-207 |
2.73e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.37 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 31 RVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGLLRQDmPGGWTLAE------ALGVAN-DLE 90
Cdd:PRK13647 33 KTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevnaenekwvrskVGLVFQD-PDDQVFSStvwddvAFGPVNmGLD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 91 RLErilagngtagdfdaadwtLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAA 170
Cdd:PRK13647 112 KDE------------------VERRVEEALKAVRMWDFR-DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518843096 171 GRAAIRALMREW-RGG--VLVASHDREL-LDDVDRILELTA 207
Cdd:PRK13647 173 GQETLMEILDRLhNQGktVIVATHDVDLaAEWADQVIVLKE 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
34-199 |
3.00e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.00 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------------IGLLRQdMPGGWTLAEALgvandlerLERIL 96
Cdd:PRK13649 38 FIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstsknkdikqirkkVGLVFQ-FPESQLFEETV--------LKDVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 97 AGngtAGDFDAADWTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIR 176
Cdd:PRK13649 109 FG---PQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELM 185
|
170 180
....*....|....*....|....*..
gi 518843096 177 ALMREW-RGG---VLVaSHdreLLDDV 199
Cdd:PRK13649 186 TLFKKLhQSGmtiVLV-TH---LMDDV 208
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-521 |
3.01e-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: 63.58 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 349 LGPWTLRIDG-----PERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQVGLlDPEGTILDNIRRLHPD 423
Cdd:cd03237 10 LGEFTLEVEGgsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKA-DYEGTVRDLLSSITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 424 AGdEEAYalcarfaFRNRDAR---------RVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENAL 494
Cdd:cd03237 89 FY-THPY-------FKTEIAKplqieqildREVPELSGGELQRVAIAACLSKDAD--IYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190
....*....|....*....|....*....|...
gi 518843096 495 LSF----DGALLVVSHDPSFVERVGfDR--VFE 521
Cdd:cd03237 159 RRFaennEKTAFVVEHDIIMIDYLA-DRliVFE 190
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
32-170 |
3.12e-11 |
|
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: 62.57 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPS--SGTVRRTGT----------IGLLRQD--MPGGWTLAEALgvandlerlerila 97
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRpldkrsfrkiIGYVPQDdiLHPTLTVRETL-------------- 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 98 gngtagDFDAadwtlesrigaalaqvglpalpldrCLRTLSGGERTRVGIAR-LVMEaPDLLLLDEPTNNLDAA 170
Cdd:cd03213 104 ------MFAA-------------------------KLRGLSGGERKRVSIALeLVSN-PSLLFLDEPTSGLDSS 145
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
30-207 |
3.21e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.96 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTigllRQDMPGGWTLAEALGVAndLERLERILAGNGTAGD--FDA 107
Cdd:PRK13642 34 EWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE----LLTAENVWNLRRKIGMV--FQNPDNQFVGATVEDDvaFGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 108 ADWTLE-----SRIGAALAQVGLPALPLDRCLRtLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMRE- 181
Cdd:PRK13642 108 ENQGIPreemiKRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEi 186
|
170 180
....*....|....*....|....*....
gi 518843096 182 ---WRGGVLVASHDRELLDDVDRILELTA 207
Cdd:PRK13642 187 kekYQLTVLSITHDLDEAASSDRILVMKA 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
353-513 |
4.01e-11 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 63.02 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR--------------RAEGRIVLldQQVGLLDpeGTILDNIR 418
Cdd:cd03251 22 SLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdytlaslRRQIGLVS--QDVFLFN--DTVAENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 RLHPDAGDEEayalcARFAFRNRDARR-----------VVG----TLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLD 483
Cdd:cd03251 98 YGRPGATREE-----VEEAARAANAHEfimelpegydtVIGergvKLSGGQRQRIAIARALLKDPP--ILILDEATSALD 170
|
170 180 190
....*....|....*....|....*....|..
gi 518843096 484 IESVEILENAL--LSFDGALLVVSHDPSFVER 513
Cdd:cd03251 171 TESERLVQAALerLMKNRTTFVIAHRLSTIEN 202
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
32-195 |
4.09e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.69 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAG-LAEP-SSGTVRRTGTIGLlrqdmpGGWTLAEAlgVANDLERLERILAGNGTAG-DFDAA 108
Cdd:PRK13547 30 TALLGRNGAGKSTLLKALAGdLTGGgAPRGARVTGDVTL------NGEPLAAI--DAPRLARLRAVLPQAAQPAfAFSAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 109 DWTLESR-----------------IGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLV---------MEAPDLLLLDE 162
Cdd:PRK13547 102 EIVLLGRypharragalthrdgeiAWQALALAGATAL-VGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDE 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 518843096 163 PTNNLDAAGR----AAIRALMREWRGGVLVASHDREL 195
Cdd:PRK13547 181 PTAALDLAHQhrllDTVRRLARDWNLGVLAIVHDPNL 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-205 |
4.36e-11 |
|
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: 62.87 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 13 RTPDGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-------------TIGLLRQD-MPGGW 77
Cdd:cd03248 23 TRPDTLVLQDVSFTLHPGEVtALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSLVGQEpVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 78 TLAEALGVANDLERLERI--LAGNGTAGDFDAAdwtLESRIGAALAQVGlpalpldrclRTLSGGERTRVGIARLVMEAP 155
Cdd:cd03248 103 SLQDNIAYGLQSCSFECVkeAAQKAHAHSFISE---LASGYDTEVGEKG----------SQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518843096 156 DLLLLDEPTNNLDAAGRAAIRALMREW--RGGVLVASHDRELLDDVDRILEL 205
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVERADQILVL 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-192 |
4.96e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.71 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 2 SAFLTLDSVCARTPDGP-LFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIglLRQDMPGGWTL 79
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVtAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP--IDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 80 AEALGVANDLERLERILAGNGTAGDFDAADWTL-----ESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIAR-LVME 153
Cdd:PRK13636 81 RESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLpedevRKRVDNALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGvLVME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518843096 154 aPDLLLLDEPTNNLDAAGRAAIRALMREWRGG----VLVASHD 192
Cdd:PRK13636 160 -PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElgltIIIATHD 201
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
30-201 |
5.09e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 62.74 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR---------------RTGtIGLLRQdmpggwtlaEA-----LGVANDL 89
Cdd:COG1137 30 EIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldgedithlpmhkraRLG-IGYLPQ---------EAsifrkLTVEDNI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ---------------ERLERILAgngtagDFDAadwtleSRIGAALAQvglpalpldrclrTLSGGERTRVGIAR-LVME 153
Cdd:COG1137 100 lavlelrklskkereERLEELLE------EFGI------THLRKSKAY-------------SLSGGERRRVEIARaLATN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518843096 154 aPDLLLLDEPTNNLDAAGRAAIRALMREW--RG-GVLVASHD-RELLDDVDR 201
Cdd:COG1137 155 -PKFILLDEPFAGVDPIAVADIQKIIRHLkeRGiGVLITDHNvRETLGICDR 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-349 |
5.34e-11 |
|
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: 65.70 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQD---MPGgwTLAEAL--GVANDLER 91
Cdd:TIGR01271 440 PVLKNISFKLEKgQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTswiMPG--TIKDNIifGLSYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 92 LERILAGNGTAGDFDaadwTLESRIGAALAQVGLpalpldrclrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAG 171
Cdd:TIGR01271 518 YTSVIKACQLEEDIA----LFPEKDKTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 172 RAAI------RALMREWRggVLVAShDRELLDDVDRILELTAiGARSFGGGWSAFSAARDEdrrrASAELERADA--DVR 243
Cdd:TIGR01271 584 EKEIfesclcKLMSNKTR--ILVTS-KLEHLKKADKILLLHE-GVCYFYGTFSELQAKRPD----FSSLLLGLEAfdNFS 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 244 AVRQAvQARREAKERRDRAGRAFAAKGSEPKillgaraeraqnsggtaqAISDRRMGralAEADDARSRVEVLTPLTIAL 323
Cdd:TIGR01271 656 AERRN-SILTETLRRVSIDGDSTVFSGPETI------------------KQSFKQPP---PEFAEKRKQSIILNPIASAR 713
|
330 340
....*....|....*....|....*....
gi 518843096 324 PPSGL---PSGANVLAMEGVVAEAGDRRL 349
Cdd:TIGR01271 714 KFSFVqmgPQKAQATTIEDAVREPSERKF 742
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
30-168 |
5.50e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.11 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGL----------AEPSSGTVRRTGTI-GLLRQDMPGGWTLAEALGVANDLERLERILAG 98
Cdd:PRK09984 31 EMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLaRDIRKSRANTGYIFQQFNLVNRLSVLENVLIG 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 99 NGTAGDF--DAADW---TLESRIGAALAQVGLPALPLDRcLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD 168
Cdd:PRK09984 111 ALGSTPFwrTCFSWftrEQKQRALQALTRVGMVHFAHQR-VSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-197 |
5.78e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.77 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGtvrrtgtigllRQDMPGGWT--LAEALGvaNDL-ERLERILAGN--------- 99
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLG-----------KFDDPPDWDeiLDEFRG--SELqNYFTKLLEGDvkvivkpqy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 ---------GTAGD-FDAADWT--LESRIgaalAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNL 167
Cdd:cd03236 96 vdlipkavkGKVGElLKKKDERgkLDELV----DQLELRHV-LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 168 DAAGR----AAIRALMREWRgGVLVASHDRELLD 197
Cdd:cd03236 171 DIKQRlnaaRLIRELAEDDN-YVLVVEHDLAVLD 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
445-522 |
5.94e-11 |
|
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: 61.85 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 445 RVVGTLSGGER------LRAGLAAALSGSAPPwlIILDEPTNHLDIES-----VEILENALLSFDGALLVVSHDPSFVER 513
Cdd:cd03240 111 DMRGRCSGGEKvlasliIRLALAETFGSNCGI--LALDEPTTNLDEENieeslAEIIEERKSQKNFQLIVITHDEELVDA 188
|
....*....
gi 518843096 514 VgfDRVFEV 522
Cdd:cd03240 189 A--DHIYRV 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
354-520 |
6.06e-11 |
|
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: 62.13 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSgtvrraeGRIVLLDQQVGLLDPEG----------------TILDNI 417
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS-------GRVLINGVDVTAAPPADrpvsmlfqennlfahlTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 R-----RLHPDAGDEEA-YALCARFAFRNRDARRvVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDiesvEILE 491
Cdd:cd03298 92 GlglspGLKLTAEDRQAiEVALARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKP--VLLLDEPFAALD----PALR 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 518843096 492 NALLSF--------DGALLVVSHDPSFVERVGFDRVF 520
Cdd:cd03298 165 AEMLDLvldlhaetKMTVLMVTHQPEDAKRLAQRVVF 201
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-202 |
6.35e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.20 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 23 LTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG---------TIGL------LRQDMP-----------G 75
Cdd:COG4152 20 VSFTVPKGEIfGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepldpedrrRIGYlpeergLYPKMKvgeqlvylarlK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 76 GWTLAEALGVANDLerLERilagngtagdFDAADWtlesrigaalaqvglpalpLDRCLRTLSGGERTRVGIARLVMEAP 155
Cdd:COG4152 100 GLSKAEAKRRADEW--LER----------LGLGDR-------------------ANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 518843096 156 DLLLLDEPTNNLD--AAG--RAAIRALMREwrgG--VLVASHDrelLDDVDRI 202
Cdd:COG4152 149 ELLILDEPFSGLDpvNVEllKDVIRELAAK---GttVIFSSHQ---MELVEEL 195
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
353-483 |
6.60e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.95 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR---RAEGRIVLLDQQVGL------LDPEGTILDNI------ 417
Cdd:PRK10851 22 SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgTDVSRLHARDRKVGFvfqhyaLFRHMTVFDNIafgltv 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 --RRLHPDAG--DEEAYALCARFAFrNRDARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLD 483
Cdd:PRK10851 102 lpRRERPNAAaiKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARAL--AVEPQILLLDEPFGALD 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
33-164 |
7.98e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.28 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 33 GLVGRNGSGKSTLLRIVAGLAEPSSGTV---------------RRTGtIGLLRQDMpggwTLAEALGVAndlerlERILA 97
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEIlidgkpvrirsprdaIALG-IGMVHQHF----MLVPNLTVA------ENIVL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518843096 98 GNGTAGDFdAADW-TLESRIGAALAQVGLPaLPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPT 164
Cdd:COG3845 104 GLEPTKGG-RLDRkAARARIRELSERYGLD-VDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
360-519 |
8.10e-11 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 62.00 E-value: 8.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTV-----------RRAEGRIVLLDQQVGLLdPEGTILDNIR---RLHPDAG 425
Cdd:cd03266 32 EVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgfdvvkepAEARRRLGFVSDSTGLY-DRLTARENLEyfaGLYGLKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 426 DEEAYA---LCARFAFRNRDARRvVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILEN---ALLSFDG 499
Cdd:cd03266 111 DELTARleeLADRLGMEELLDRR-VGGFSTGMRQKVAIARALVHD--PPVLLLDEPTTGLDVMATRALREfirQLRALGK 187
|
170 180
....*....|....*....|
gi 518843096 500 ALLVVSHDPSFVERVGfDRV 519
Cdd:cd03266 188 CILFSTHIMQEVERLC-DRV 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
353-483 |
1.01e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 62.41 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQVG-------LLdPEGTILDNI------RR 419
Cdd:COG1116 31 SLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGvvfqepaLL-PWLTVLDNValglelRG 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 420 LHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLD 483
Cdd:COG1116 110 VPKAERRERARELLELVGLAGF-EDAYPHQLSGGMRQRVAIARALAND--PEVLLMDEPFGALD 170
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-202 |
1.04e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 61.91 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------IGLLRQD--MPGGWTLAE--ALGVANDL----- 89
Cdd:PRK10771 26 ERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQEnnLFSHLTVAQniGLGLNPGLklnaa 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 --ERLERILAgngtagdfdaadwtlesrigaalaQVGLPALpLDRCLRTLSGGERTRVGIAR-LVMEAPdLLLLDEPTNN 166
Cdd:PRK10771 106 qrEKLHAIAR------------------------QMGIEDL-LARLPGQLSGGQRQRVALARcLVREQP-ILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518843096 167 LDAAGRAAIRALM----REWRGGVLVASHDrelLDDVDRI 202
Cdd:PRK10771 160 LDPALRQEMLTLVsqvcQERQLTLLMVSHS---LEDAARI 196
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
30-203 |
1.37e-10 |
|
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: 63.58 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG------TIGLLRQDMpggwtlaeALgVANDLERLERILAGN---G 100
Cdd:TIGR02203 359 ETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladyTLASLRRQV--------AL-VSQDVVLFNDTIANNiayG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 101 TAGDFDAADwtLESRIGAALAQVGLPALPLDrcLRT--------LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAG- 171
Cdd:TIGR02203 430 RTEQADRAE--IERALAAAYAQDFVDKLPLG--LDTpigengvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESe 505
|
170 180 190
....*....|....*....|....*....|....*
gi 518843096 172 ---RAAIRALMREWRGgvLVASHDRELLDDVDRIL 203
Cdd:TIGR02203 506 rlvQAALERLMQGRTT--LVIAHRLSTIEKADRIV 538
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
362-519 |
1.40e-10 |
|
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: 60.64 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 362 IALKGANGAGKTTLLRIAAGLRAP--VSGTVrraegrivlldqqvgLLDPEGTILDNIRR----------LHPDAGDEEA 429
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGlgVSGEV---------------LINGRPLDKRSFRKiigyvpqddiLHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 430 --YALCARfafrnrdarrvvgTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENAL--LSFDGALLVVS 505
Cdd:cd03213 103 lmFAAKLR-------------GLSGGERKRVSIALELVSN--PSLLFLDEPTSGLDSSSALQVMSLLrrLADTGRTIICS 167
|
170
....*....|....*
gi 518843096 506 -HDPSFVERVGFDRV 519
Cdd:cd03213 168 iHQPSSEIFELFDKL 182
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
360-479 |
1.49e-10 |
|
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: 60.91 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQ------VGLLdPEG-------TILDNIR-------R 419
Cdd:cd03224 27 EIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraragIGYV-PEGrrifpelTVEENLLlgayarrR 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518843096 420 LHPDAGDEEAYALCARFA-FRNRDArrvvGTLSGGERLRAGLAAALSGSapPWLIILDEPT 479
Cdd:cd03224 106 AKRKARLERVYELFPRLKeRRKQLA----GTLSGGEQQMLAIARALMSR--PKLLLLDEPS 160
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
30-203 |
1.52e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.54 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT------------IGLLR--------QDMpggwTLAEALGVANDL 89
Cdd:PRK11300 32 EIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhieglpghqiarMGVVRtfqhvrlfREM----TVIENLLVAQHQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ERLERILAGNGTAGDFDAADWTLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPtnnldA 169
Cdd:PRK11300 108 QLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHA-NRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP-----A 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518843096 170 AG---------RAAIRALMREWRGGVLVASHDRELLDDV-DRIL 203
Cdd:PRK11300 182 AGlnpketkelDELIAELRNEHNVTVLLIEHDMKLVMGIsDRIY 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
360-519 |
1.56e-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: 61.36 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTV---------------RRAEGRIVLLDQQVGLLDpEGTILDNI------- 417
Cdd:cd03261 27 EILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlidgedisglseaelYRLRRRMGMLFQSGALFD-SLTVFENVafplreh 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 RRLhPDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESVEILENALLSF 497
Cdd:cd03261 106 TRL-SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARAL--ALDPELLLYDEPTAGLDPIASGVIDDLIRSL 182
|
170 180
....*....|....*....|....*.
gi 518843096 498 DGAL----LVVSHDPSFVERVGfDRV 519
Cdd:cd03261 183 KKELgltsIMVTHDLDTAFAIA-DRI 207
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-207 |
1.56e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 60.89 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAI-GTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR----RTGTIGLLRqdmpggwtLAEALG-VANDLER 91
Cdd:cd03369 22 PVLKNVSFKVkAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgiDISTIPLED--------LRSSLTiIPQDPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 92 LERILAGNgtagdFDAADWTLESRIGAAL--AQVGLpalpldrclrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:cd03369 94 FSGTIRSN-----LDPFDEYSDEEIYGALrvSEGGL----------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 518843096 170 AGRAAIRALMREWRGG--VLVASHDRELLDDVDRILELTA 207
Cdd:cd03369 159 ATDALIQKTIREEFTNstILTIAHRLRTIIDYDKILVMDA 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
360-513 |
1.59e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVR---------RAEGRIVLLDQQVG------LLDPEGTILDNI------R 418
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplhqmDEEARAKLRAKHVGfvfqsfMLIPTLNALENVelpallR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 RLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENALLS-- 496
Cdd:PRK10584 117 GESSRQSRNGAKALLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGR--PDVLFADEPTGNLDRQTGDKIADLLFSln 193
|
170
....*....|....*....
gi 518843096 497 --FDGALLVVSHDPSFVER 513
Cdd:PRK10584 194 reHGTTLILVTHDLQLAAR 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
30-203 |
1.79e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 61.64 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRrtgTIGLLRQDMPGGWTLAEALG----------VANDLErlERILAGN 99
Cdd:PRK13633 37 EFLVILGRNGSGKSTIAKHMNALLIPSEGKVY---VDGLDTSDEENLWDIRNKAGmvfqnpdnqiVATIVE--EDVAFGP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 GTAGdfdAADWTLESRIGAALAQVGL-------PALpldrclrtLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGR 172
Cdd:PRK13633 112 ENLG---IPPEEIRERVDESLKKVGMyeyrrhaPHL--------LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190
....*....|....*....|....*....|....*
gi 518843096 173 ----AAIRALMREWRGGVLVASHDRELLDDVDRIL 203
Cdd:PRK13633 181 revvNTIKELNKKYGITIILITHYMEEAVEADRII 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
30-199 |
1.92e-10 |
|
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: 60.23 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLA--EPSSGTVRRTGtigllrQDMpggwtlaealgvaNDLERLERILAGNGTAgdfda 107
Cdd:cd03217 27 EVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG------EDI-------------TDLPPEERARLGIFLA----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 108 adWTLESRIgaalaqvglPALPLDRCLR----TLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWR 183
Cdd:cd03217 83 --FQYPPEI---------PGVKNADFLRyvneGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLR 151
|
170
....*....|....*....
gi 518843096 184 G---GVLVASHDRELLDDV 199
Cdd:cd03217 152 EegkSVLIITHYQRLLDYI 170
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
353-513 |
2.25e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR----------RAEGRIVLLDQQ------VGLLDPEGTILDN 416
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgeplaklnRAQRKAFRRDIQmvfqdsISAVNPRKTVREI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 417 IR-------RLHPDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDI----E 485
Cdd:PRK10419 112 IReplrhllSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVE--PKLLILDEAVSNLDLvlqaG 189
|
170 180
....*....|....*....|....*...
gi 518843096 486 SVEILENALLSFDGALLVVSHDPSFVER 513
Cdd:PRK10419 190 VIRLLKKLQQQFGTACLFITHDLRLVER 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
361-517 |
2.43e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.96 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 361 RIALKGANGAGKTTLLRIAA--------------------------GLRAPVSGTVRRA---EGRIVLLDQQVGLL---- 407
Cdd:PLN03073 205 HYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvgddttALQCVLNTDIERTqllEEEAQLVAQQRELEfete 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 408 --------------DPEGTILDNI-RRLH---PDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSgsAP 469
Cdd:PLN03073 285 tgkgkgankdgvdkDAVSQRLEEIyKRLElidAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALF--IE 362
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518843096 470 PWLIILDEPTNHLDIESVEILENALLSFDGALLVVSHDPSFVERVGFD 517
Cdd:PLN03073 363 PDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTD 410
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
33-181 |
2.57e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 62.13 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 33 GLVGRNGSGKSTLLRIVAGLAEPSSGTV-------------------RRTGTI----GLLRQDmpggwTLAEalGVANDL 89
Cdd:PRK11153 35 GVIGASGAGKSTLIRCINLLERPTSGRVlvdgqdltalsekelrkarRQIGMIfqhfNLLSSR-----TVFD--NVALPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ErleriLAGngtagdFDAADwtLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:PRK11153 108 E-----LAG------TPKAE--IKARVTELLELVGLSDKA-DRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
|
170
....*....|..
gi 518843096 170 AGRAAIRALMRE 181
Cdd:PRK11153 174 ATTRSILELLKD 185
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
360-507 |
2.58e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.94 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-------------RAEGRIVLLdQQVGLLDPEgTILDNIR------RL 420
Cdd:PRK13548 29 EVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladwspaeLARRRAVLP-QHSSLSFPF-TVEEVVAmgraphGL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 421 HPDAGD---EEAYALCARFAFRNRDARrvvgTLSGGERLRAGLAAAL-----SGSAPPWLiILDEPTNHLDI----ESVE 488
Cdd:PRK13548 107 SRAEDDalvAAALAQVDLAHLAGRDYP----QLSGGEQQRVQLARVLaqlwePDGPPRWL-LLDEPTSALDLahqhHVLR 181
|
170
....*....|....*....
gi 518843096 489 ILENALLSFDGALLVVSHD 507
Cdd:PRK13548 182 LARQLAHERGLAVIVVLHD 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-209 |
2.80e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.16 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGLLRQDmPG----GWTL 79
Cdd:PRK13632 23 NALKNVSFEINEgEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItiskenlkeirkkIGIIFQN-PDnqfiGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 80 AE--ALGVAN---DLERLERILAgngtagdfDAADwtlesrigaalaQVGLPALpLDRCLRTLSGGERTRVGIARLVMEA 154
Cdd:PRK13632 102 EDdiAFGLENkkvPPKKMKDIID--------DLAK------------KVGMEDY-LDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 155 PDLLLLDEPTNNLDAAGRAAIRALMREWRGG----VLVASHDRELLDDVDRIL-----ELTAIG 209
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkktLISITHDMDEAILADKVIvfsegKLIAQG 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-205 |
3.14e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.82 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 15 PDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGLLRQDmPGGW--T 78
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPgEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVALVGQE-PVLFsgS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 79 LAEALGVANDLERLERILAGNGTAG--DFDAAD-WTLESRIGAALAQvglpalpldrclrtLSGGERTRVGIARLVMEAP 155
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANahDFIMEFpNGYDTEVGEKGSQ--------------LSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 518843096 156 DLLLLDEPTNNLDAAGRAAIRALMREWRGGVLVASHDRELLDDVDRILEL 205
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVL 686
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
429-514 |
3.77e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.49 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 429 AYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSFDGALLVVSHDP 508
Cdd:PRK10636 129 AASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSD--LLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDR 206
|
....*.
gi 518843096 509 SFVERV 514
Cdd:PRK10636 207 DFLDPI 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-181 |
3.86e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.54 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 3 AFLTLDSVCARTPDGplfqKLTfaigtervGLVGRNGSGKSTLLRIVAGLAEPSSGTVrrtgtiglLRQDMPGGwtlaea 82
Cdd:PRK13648 21 ASFTLKDVSFNIPKG----QWT--------SIVGHNGSGKSTIAKLMIGIEKVKSGEI--------FYNNQAIT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 83 lgvANDLERLER---ILAGN------GTAGDFDAAdWTLE----------SRIGAALAQVGLpalpLDRC---LRTLSGG 140
Cdd:PRK13648 75 ---DDNFEKLRKhigIVFQNpdnqfvGSIVKYDVA-FGLEnhavpydemhRRVSEALKQVDM----LERAdyePNALSGG 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518843096 141 ERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMRE 181
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRK 187
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
353-513 |
4.00e-10 |
|
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: 59.73 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRA--------EGRIVLLDQQVGL------LDPEGTILDN-- 416
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlrGRAIPYLRRKIGVvfqdfrLLPDRNVYENva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 417 ----IRRLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILEN 492
Cdd:cd03292 101 faleVTGVPPREIRKRVPAALELVGLSHK-HRALPAELSGGEQQRVAIARAIVNS--PTILIADEPTGNLDPDTTWEIMN 177
|
170 180
....*....|....*....|....
gi 518843096 493 ALLSFD--GALLVVS-HDPSFVER 513
Cdd:cd03292 178 LLKKINkaGTTVVVAtHAKELVDT 201
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-191 |
4.07e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.50 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 36 GRNGSGKSTLLRIVAGLAEPSSGTVR-RTGTIGLLRQdmPGGWTLAEALGVANDLERLERILagngtagdFDAADWTLES 114
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYyKNCNINNIAK--PYCTYIGHNLGLKLEMTVFENLK--------FWSEIYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 115 RIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRAL--MREWRGG-VLVASH 191
Cdd:PRK13541 103 TLYAAIHYFKLHDL-LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLivMKANSGGiVLLSSH 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
346-507 |
4.24e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 346 DRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLrAPVSGTVRRAeGRIVL-------------LDQQV-------- 404
Cdd:PRK03695 9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFA-GQPLEawsaaelarhrayLSQQQtppfampv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 405 ----GLLDPEGTildnirrlHPDAGDEEAYALCARFAFRNRDARRVvGTLSGGERLRAGLAAAL-----SGSAPPWLIIL 475
Cdd:PRK03695 87 fqylTLHQPDKT--------RTEAVASALNEVAEALGLDDKLGRSV-NQLSGGEWQRVRLAAVVlqvwpDINPAGQLLLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 518843096 476 DEPTNHLDIESVEILE---NALLSFDGALLVVSHD 507
Cdd:PRK03695 158 DEPMNSLDVAQQAALDrllSELCQQGIAVVMSSHD 192
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
364-506 |
5.25e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 364 LKGANGAGKTTLLRIAAGLRAPVSGTVrRAEGRIVLLD-----QQVGL------LDPEGTILDN-IRRLHPDAGDEEAYA 431
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEI-LFERQSIKKDlctyqKQLCFvghrsgINPYLTLRENcLYDIHFSPGAVGITE 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518843096 432 LCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSAPPWLiiLDEPTNHLDIESVEILENALLSF---DGALLVVSH 506
Cdd:PRK13540 111 LCRLFSLEHL-IDYPCGLLSSGQKRQVALLRLWMSKAKLWL--LDEPLVALDELSLLTIITKIQEHrakGGAVLLTSH 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
340-510 |
5.89e-10 |
|
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: 58.32 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 340 VVAEAGDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQVGLLdPEGTILDNIrr 419
Cdd:cd03223 8 LATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-PLGTLREQL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 420 lhpdagdeeAYALcarfafrnrdaRRVvgtLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESVEILENALLSFDG 499
Cdd:cd03223 85 ---------IYPW-----------DDV---LSGGEQQRLAFARLL--LHKPKFVFLDEATSALDEESEDRLYQLLKELGI 139
|
170
....*....|.
gi 518843096 500 ALLVVSHDPSF 510
Cdd:cd03223 140 TVISVGHRPSL 150
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-195 |
5.94e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.09 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG---------------TIGLLRQ---DMPGGWTLAE--ALGVAN-D 88
Cdd:PRK13639 29 EMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkksllevrkTVGIVFQnpdDQLFAPTVEEdvAFGPLNlG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 89 LERLErilagngtagdfdaadwtLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD 168
Cdd:PRK13639 109 LSKEE------------------VEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD 169
|
170 180 190
....*....|....*....|....*....|
gi 518843096 169 AAGRAAIRALMREW-RGG--VLVASHDREL 195
Cdd:PRK13639 170 PMGASQIMKLLYDLnKEGitIIISTHDVDL 199
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
30-181 |
6.50e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG------------TIGLLRQDMpgG--------W-------TLAEA 82
Cdd:PRK11124 29 ETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdkAIRELRRNV--GmvfqqynlWphltvqqNLIEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 83 ----LGVAND--LERLERILAGNGTAgdfDAADwtlesrigaalaqvglpALPLDrclrtLSGGERTRVGIARLVMEAPD 156
Cdd:PRK11124 107 pcrvLGLSKDqaLARAEKLLERLRLK---PYAD-----------------RFPLH-----LSGGQQQRVAIARALMMEPQ 161
|
170 180
....*....|....*....|....*
gi 518843096 157 LLLLDEPTNNLDAAGRAAIRALMRE 181
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRE 186
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
30-205 |
6.65e-10 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 59.16 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR------RTGTIGLLRQDMpgGWTLAEALGVANDLerLERILAGNGTAG 103
Cdd:cd03254 30 ETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidiRDISRKSLRSMI--GVVLQDTFLFSGTI--MENIRLGRPNAT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 104 DfdaadwtleSRIGAALAQVGLP----ALP--LDRCLR----TLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRA 173
Cdd:cd03254 106 D---------EEVIEAAKEAGAHdfimKLPngYDTVLGenggNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 174 AIRALMREWRGG--VLVASHDRELLDDVDRILEL 205
Cdd:cd03254 177 LIQEALEKLMKGrtSIIIAHRLSTIKNADKILVL 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
360-479 |
6.94e-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: 59.23 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLrapvsgtVRRAEGRIVLLDQQVGLLD------------PEG-------TILDNIR-- 418
Cdd:COG0410 30 EIVALLGRNGAGKTTLLKAISGL-------LPPRSGSIRFDGEDITGLPphriarlgigyvPEGrrifpslTVEENLLlg 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518843096 419 -RLHPDAGD-----EEAYALCARFA-FRNRDArrvvGTLSGGERLRAGLAAALSGSapPWLIILDEPT 479
Cdd:COG0410 103 aYARRDRAEvradlERVYELFPRLKeRRRQRA----GTLSGGEQQMLAIGRALMSR--PKLLLLDEPS 164
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-202 |
7.21e-10 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 59.96 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTV------------------RRTgTIGLLRQD---MPGGWTLAEalgVANDLErl 92
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVlidgqdiaamsrkelrelRRK-KISMVFQSfalLPHRTVLEN---VAFGLE-- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 93 eriLAGNGTAgdfdaadwTLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGR 172
Cdd:cd03294 129 ---VQGVPRA--------EREERAAEALELVGLEGW-EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 173 AAIR----ALMREWRGGVLVASHDrelLDDVDRI 202
Cdd:cd03294 197 REMQdellRLQAELQKTIVFITHD---LDEALRL 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-203 |
8.05e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.49 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT----------------IGLLRQD--------MPGGWTLAEALGV 85
Cdd:PRK15079 48 ETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKdllgmkddewravrsdIQMIFQDplaslnprMTIGEIIAEPLRT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 AN-DLERLErilagngtagdfdaadwtLESRIGAALAQVGLpaLP--LDRCLRTLSGGERTRVGIARLVMEAPDLLLLDE 162
Cdd:PRK15079 128 YHpKLSRQE------------------VKDRVKAMMLKVGL--LPnlINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 518843096 163 PTNNLDAAGRAAI----RALMREWRGGVLVASHDRELLDDV-DRIL 203
Cdd:PRK15079 188 PVSALDVSIQAQVvnllQQLQREMGLSLIFIAHDLAVVKHIsDRVL 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
360-494 |
8.82e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.13 E-value: 8.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVR----------RAEGR--IVLLDQQVGLLDPegTILDNIRRLHPDAGDE 427
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdirtvtRASLRrnIAVVFQDAGLFNR--SIEDNIRVGRPDATDE 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 428 EAYALCARFAFRNRDARR------VVG----TLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENAL 494
Cdd:PRK13657 440 EMRAAAERAQAHDFIERKpdgydtVVGergrQLSGGERQRLAIARALLKDPP--ILILDEATSALDVETEAKVKAAL 514
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
16-180 |
9.07e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 60.23 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 16 DGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSsgtvrrTGTIGLLRQDMPGGWTLAEA-LGVANDLERLE 93
Cdd:PRK13536 53 DKAVVNGLSFTVASgECFGLLGPNGAGKSTIARMILGMTSPD------AGKITVLGVPVPARARLARArIGVVPQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 94 R--------ILAGNGtagdFDAADWTLESRIGAALAQVGLPAlPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:PRK13536 127 LeftvrenlLVFGRY----FGMSTREIEAVIPSLLEFARLES-KADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170
....*....|....*
gi 518843096 166 NLDAAGRAAIRALMR 180
Cdd:PRK13536 202 GLDPHARHLIWERLR 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
353-519 |
9.20e-10 |
|
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: 59.13 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV---------------RRAEGRIVLLDQQVGLLDPEgTILDNI 417
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdltllsgkelRKARRRIGMIFQHFNLLSSR-TVFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 rrlhpdagdeeAYAL-CARFAFRNRDAR-----RVVG----------TLSGGERLRAGLAAALSGSapPWLIILDEPTNH 481
Cdd:cd03258 104 -----------ALPLeIAGVPKAEIEERvlellELVGledkadaypaQLSGGQKQRVGIARALANN--PKVLLCDEATSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518843096 482 LDIESVE-ILEnaLLS-----FDGALLVVSHDPSFVERVGfDRV 519
Cdd:cd03258 171 LDPETTQsILA--LLRdinreLGLTIVLITHEMEVVKRIC-DRV 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
30-192 |
1.17e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKST----LLRIVAGLAE------PSSGTVRRT-----GTIGLLRQDmPGGwTLAEALGVANDLERLER 94
Cdd:PRK15134 313 ETLGLVGESGSGKSTtglaLLRLINSQGEiwfdgqPLHNLNRRQllpvrHRIQVVFQD-PNS-SLNPRLNVLQIIEEGLR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 95 ILAGNGTAGDfdaadwtLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA 174
Cdd:PRK15134 391 VHQPTLSAAQ-------REQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQ 463
|
170 180
....*....|....*....|..
gi 518843096 175 IRALMR----EWRGGVLVASHD 192
Cdd:PRK15134 464 ILALLKslqqKHQLAYLFISHD 485
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
353-506 |
1.28e-09 |
|
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: 58.78 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV---------------RRAegrIVLLDQQVGLLDpeGTILDNI 417
Cdd:cd03253 21 SFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlidgqdirevtldslRRA---IGVVPQDTVLFN--DTIGYNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 RRLHPDAGDEEAYALC-----ARFAFRNRDA-RRVVG----TLSGGERLRAGLAAALSgSAPPwLIILDEPTNHLDIES- 486
Cdd:cd03253 96 RYGRPDATDEEVIEAAkaaqiHDKIMRFPDGyDTIVGerglKLSGGEKQRVAIARAIL-KNPP-ILLLDEATSALDTHTe 173
|
170 180
....*....|....*....|.
gi 518843096 487 VEILENALLSFDG-ALLVVSH 506
Cdd:cd03253 174 REIQAALRDVSKGrTTIVIAH 194
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
354-483 |
1.39e-09 |
|
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: 58.50 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV----RRAEGRIVlLDQQVGL------LDPEGTILDNI------ 417
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPV-QERNVGFvfqhyaLFRHMTVFDNVafglrv 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 --RRLHPDAG--DEEAYALCaRFAFRNRDARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLD 483
Cdd:cd03296 102 kpRSERPPEAeiRAKVHELL-KLVQLDWLADRYPAQLSGGQRQRVALARAL--AVEPKVLLLDEPFGALD 168
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
353-519 |
1.40e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 58.90 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD-------------QQVGLLdPEGTILDNIR- 418
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPphriarlgiartfQNPRLF-PELTVLENVLv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 --------------------RLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEP 478
Cdd:COG0411 103 aaharlgrgllaallrlpraRREEREARERAEELLERVGLADR-ADEPAGNLSYGQQRRLEIARALATE--PKLLLLDEP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 518843096 479 T---NHLDIES-VEILENALLSFDGALLVVSHDPSFVERVGfDRV 519
Cdd:COG0411 180 AaglNPEETEElAELIRRLRDERGITILLIEHDMDLVMGLA-DRI 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
353-515 |
1.55e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.57 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSG-------TVRRAEGRIVLLDQQVGL------LDPEGTILDN--- 416
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglKVNDPKVDERLIRQEAGMvfqqfyLFPHLTALENvmf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 417 ----IRRLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIE-SVEILE 491
Cdd:PRK09493 101 gplrVRGASKEEAEKQARELLAKVGLAER-AHHYPSELSGGQQQRVAIARAL--AVKPKLMLFDEPTSALDPElRHEVLK 177
|
170 180
....*....|....*....|....*.
gi 518843096 492 --NALLSFDGALLVVSHDPSFVERVG 515
Cdd:PRK09493 178 vmQDLAEEGMTMVIVTHEIGFAEKVA 203
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-168 |
1.60e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.56 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGTV-------------RRTGTIGLLRQD-MPG---GWTLAEALGVA-------- 86
Cdd:COG1101 35 VTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklpeyKRAKYIGRVFQDpMMGtapSMTIEENLALAyrrgkrrg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 87 -------NDLERLERILA--GNGtagdfdaadwtLESRIGaalAQVGLpalpldrclrtLSGGERTRVGIARLVMEAPDL 157
Cdd:COG1101 115 lrrgltkKRRELFRELLAtlGLG-----------LENRLD---TKVGL-----------LSGGQRQALSLLMATLTKPKL 169
|
170
....*....|.
gi 518843096 158 LLLDEPTNNLD 168
Cdd:COG1101 170 LLLDEHTAALD 180
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
334-506 |
1.74e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.24 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 334 VLAMEGVVAeagdrrLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLrAPVSG--TVRRAEGRIVLLDQ--------- 402
Cdd:PRK11174 357 ILSPDGKTL------AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGslKINGIELRELDPESwrkhlswvg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 403 QVGLLdPEGTILDNIRRLHPDAGDEEAYALCAR---------------FAFRNRDARrvvgtLSGGERLRAGLAAALSGs 467
Cdd:PRK11174 430 QNPQL-PHGTLRDNVLLGNPDASDEQLQQALENawvseflpllpqgldTPIGDQAAG-----LSVGQAQRLALARALLQ- 502
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518843096 468 aPPWLIILDEPTNHLDIESVEILENAL--LSFDGALLVVSH 506
Cdd:PRK11174 503 -PCQLLLLDEPTASLDAHSEQLVMQALnaASRRQTTLMVTH 542
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
30-181 |
2.04e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG------------TIGLLRQDMpgG-----WTLAEALGVANDL-ER 91
Cdd:COG4161 29 ETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpsekAIRLLRQKV--GmvfqqYNLWPHLTVMENLiEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 92 LERILAGNGTAGDFDAADwtlesrigaALAQVGLP----ALPLdrclrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNL 167
Cdd:COG4161 107 PCKVLGLSKEQAREKAMK---------LLARLRLTdkadRFPL-----HLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170
....*....|....
gi 518843096 168 DAAGRAAIRALMRE 181
Cdd:COG4161 173 DPEITAQVVEIIRE 186
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-168 |
2.21e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.06 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQDMPGGWTLAEALGVANDLERLERILAGNGTAGDFDAADWT 111
Cdd:PRK10619 34 ISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLRTRLTMVFQHFNLWSHMTVLENV 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518843096 112 LES--------------RIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD 168
Cdd:PRK10619 114 MEApiqvlglskqeareRAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALD 184
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
353-494 |
2.30e-09 |
|
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: 60.31 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAeGRIVLlDQQVGLLDPeGTILDNIrrLHPDAGDEEAYAL 432
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS-GRISF-SPQTSWIMP-GTIKDNI--IFGLSYDEYRYTS 520
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 433 CARFA--------FRNRDaRRVVG----TLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIES-VEILENAL 494
Cdd:TIGR01271 521 VIKACqleedialFPEKD-KTVLGeggiTLSGGQRARISLARAVYKDAD--LYLLDSPFTHLDVVTeKEIFESCL 592
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
353-521 |
2.38e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.82 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEG-RIVLLDQQVGLldPEGTILD-----NIRRLHPDAGD 426
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGaRVLFLPQRPYL--PLGTLREallypATAEAFSDAEL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 427 EEAYALC--ARFAFRNRDARRVVGTLSGGERLRAGLAAALSgSAPPWLiILDEPTNHLDIESVEILENALLS--FDGALL 502
Cdd:COG4178 461 REALEAVglGHLAERLDEEADWDQVLSLGEQQRLAFARLLL-HKPDWL-FLDEATSALDEENEAALYQLLREelPGTTVI 538
|
170
....*....|....*....
gi 518843096 503 VVSHDPSFVErvGFDRVFE 521
Cdd:COG4178 539 SVGHRSTLAA--FHDRVLE 555
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-206 |
2.83e-09 |
|
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: 56.85 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLR-IVAGLaepsSGTVRRTGTIGLLRQDMPG-GWTLAEA-LGVANDLERLERILAgngtagDFDAADW 110
Cdd:cd03240 27 IVGQNGAGKTTIIEaLKYAL----TGELPPNSKGGAHDPKLIReGEVRAQVkLAFENANGKKYTITR------SLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 111 TLESRIGAALAqvgLPALPLDRClrtlSGGERT------RVGIARLVMEAPDLLLLDEPTNNLDAAGRA-AIRALMREWR 183
Cdd:cd03240 97 VIFCHQGESNW---PLLDMRGRC----SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERK 169
|
170 180
....*....|....*....|....*..
gi 518843096 184 GG----VLVASHDRELLDDVDRILELT 206
Cdd:cd03240 170 SQknfqLIVITHDEELVDAADHIYRVE 196
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-203 |
3.22e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.20 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR------RTGTIGLLRQDMpgGWTLAEALgvandleRLERILAGNGTAG 103
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdiRTVTRASLRRNI--AVVFQDAG-------LFNRSIEDNIRVG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 104 DFDAADwtLESRIGAALAQV---------GLPALPLDRClRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA 174
Cdd:PRK13657 433 RPDATD--EEMRAAAERAQAhdfierkpdGYDTVVGERG-RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509
|
170 180 190
....*....|....*....|....*....|.
gi 518843096 175 IRALMREWRGG--VLVASHDRELLDDVDRIL 203
Cdd:PRK13657 510 VKAALDELMKGrtTFIIAHRLSTVRNADRIL 540
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
328-483 |
3.25e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 58.28 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 328 LPSGANVLAMEGVVAEAGDRRL-GPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAE----GRIVLLDQ 402
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDKLVvDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 403 QVGL------LDPEGTILDNIRRLH-----PDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSapPW 471
Cdd:PRK13537 81 RVGVvpqfdnLDPDFTVRENLLVFGryfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND--PD 158
|
170
....*....|..
gi 518843096 472 LIILDEPTNHLD 483
Cdd:PRK13537 159 VLVLDEPTTGLD 170
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
353-483 |
3.35e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 58.62 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV----RRAEGRIVLLDQQVGL------LDPEGTILDNIrrlhp 422
Cdd:COG1118 22 SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlngRDLFTNLPPRERRVGFvfqhyaLFPHMTVAENI----- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 423 dagdeeAYALCARFAFRNRDARRV----------------VGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLD 483
Cdd:COG1118 97 ------AFGLRVRPPSKAEIRARVeellelvqlegladryPSQLSGGQRQRVALARAL--AVEPEVLLLDEPFGALD 165
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
335-520 |
3.95e-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: 56.38 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 335 LAMEGVVAEAGDRR-LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPvsgtvRRAEGRIVLLDQQVGLLDPEgti 413
Cdd:cd03217 1 LEIKDLHVSVGGKEiLKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKY-----EVTEGEILFKGEDITDLPPE--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 414 ldniRRlhpdagdeeayALCARF-AF---------RNRDARRVVG-TLSGGERLRAGLAAALSgsAPPWLIILDEPTNHL 482
Cdd:cd03217 73 ----ER-----------ARLGIFlAFqyppeipgvKNADFLRYVNeGFSGGEKKRNEILQLLL--LEPDLAILDEPDSGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 518843096 483 DIESVEILENA---LLSFDGALLVVSHDPSFVERVGFDRVF 520
Cdd:cd03217 136 DIDALRLVAEVinkLREEGKSVLIITHYQRLLDYIKPDRVH 176
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
352-519 |
3.96e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 57.07 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 352 WTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSgtvrraeGRIVLLDQQVGLLDPEG----------------TILD 415
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDS-------GRILWNGQDLTALPPAErpvsmlfqennlfphlTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 416 NI-----RRLHPDAGDEEA-YALCARFAFRNRDARRvVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDI----E 485
Cdd:COG3840 91 NIglglrPGLKLTAEQRAQvEQALERVGLAGLLDRL-PGQLSGGQRQRVALARCLVRKRP--ILLLDEPFSALDPalrqE 167
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 486 SVEILENALLSFDGALLVVSHDPSFVERVGfDRV 519
Cdd:COG3840 168 MLDLVDELCRERGLTVLMVTHDPEDAARIA-DRV 200
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-181 |
3.99e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 19 LFQKLTFAIgtervglVGRNGSGKSTLLRIVAGLAEPSSGTV-------------RRTGTIGLLRQDMPG--------GW 77
Cdd:PRK15112 36 LREGQTLAI-------IGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdysYRSQRIRMIFQDPSTslnprqriSQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 78 TLAEALGVANDLERLERilagngtagdfdaadwtlESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDL 157
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQR------------------EKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180
....*....|....*....|....
gi 518843096 158 LLLDEPTNNLDAAGRAAIRALMRE 181
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLE 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
34-203 |
4.14e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 58.42 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigllrQDMPGgwTLAE-----------AL--------GVANDLeRLER 94
Cdd:PRK09452 45 LLGPSGCGKTTVLRLIAGFETPDSGRIMLDG------QDITH--VPAEnrhvntvfqsyALfphmtvfeNVAFGL-RMQK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 95 ILAGNgtagdfdaadwtLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA 174
Cdd:PRK09452 116 TPAAE------------ITPRVMEALRMVQLEEFA-QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ 182
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 175 ----IRALMREWRGGVLVASHDR-ELLDDVDRIL 203
Cdd:PRK09452 183 mqneLKALQRKLGITFVFVTHDQeEALTMSDRIV 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-170 |
4.77e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.68 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGL--------------AEPSSGTVRRTGTIGLLrqdmpggwTLAEALGVANDLERLERI 95
Cdd:TIGR02633 28 ECVGLCGENGAGKSTLMKILSGVyphgtwdgeiywsgSPLKASNIRDTERAGIV--------IIHQELTLVPELSVAENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 96 LAGN-----GTAGDFDAadwtLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAA 170
Cdd:TIGR02633 100 FLGNeitlpGGRMAYNA----MYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK 175
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
353-478 |
5.25e-09 |
|
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: 56.90 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-------------RAEGRIVLLDQQVGLLDpEGTILDNIR- 418
Cdd:TIGR04406 21 SLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILidgqdithlpmheRARLGIGYLPQEASIFR-KLTVEENIMa 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 419 ------RLHPDAGDEEAYALCARFAF-RNRDARrvVGTLSGGERLRAGLAAALsgSAPPWLIILDEP 478
Cdd:TIGR04406 100 vleirkDLDRAEREERLEALLEEFQIsHLRDNK--AMSLSGGERRRVEIARAL--ATNPKFILLDEP 162
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-205 |
5.28e-09 |
|
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: 56.32 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 23 LTFAIGtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQD---MPGgwTLAE--ALGVANDLERLERILA 97
Cdd:cd03250 26 LEVPKG-ELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEpwiQNG--TIREniLFGKPFDEERYEKVIK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 98 GNGTAGDFDAADWTLESRIGaalaQVGLpalpldrclrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAI-- 175
Cdd:cd03250 103 ACALEPDLEILPDGDLTEIG----EKGI----------NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfe 168
|
170 180 190
....*....|....*....|....*....|..
gi 518843096 176 RALMREWRGG--VLVASHDRELLDDVDRILEL 205
Cdd:cd03250 169 NCILGLLLNNktRILVTHQLQLLPHADQIVVL 200
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-381 |
5.37e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 35 VGRNGSGKSTLLRIVAGLAEPSSGTVR-RTGTIGLLrqdmpggwtlaealgvanDLERLERILAG----NGT----AGDF 105
Cdd:PRK10938 35 VGANGSGKSALARALAGELPLLSGERQsQFSHITRL------------------SFEQLQKLVSDewqrNNTdmlsPGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 106 D----AADWTLESRIGAAL-----AQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIR 176
Cdd:PRK10938 97 DtgrtTAEIIQDEVKDPARceqlaQQFGITAL-LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 177 ALMREWRGG----VLVASHDRELLDDVDRILELtaigarsfgggwsafsaardedrrrasaeleradADVRAVRQAvqar 252
Cdd:PRK10938 176 ELLASLHQSgitlVLVLNRFDEIPDFVQFAGVL----------------------------------ADCTLAETG---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 253 reakERRDRAGRAFAAKgsepkillGARAERAQNSggtaqaisdrrmgrALAEADDARSRVEvltpltialppsgLPSGA 332
Cdd:PRK10938 218 ----EREEILQQALVAQ--------LAHSEQLEGV--------------QLPEPDEPSARHA-------------LPANE 258
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 518843096 333 NVLAMEGVVAEAGDRR-LGPWTLRIDGPERIALKGANGAGKTTLLRIAAG 381
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPiLHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
34-197 |
7.51e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 56.23 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLA--EPSSGTVR---------------RTGtIGLLRQDmPggwtlAEALGVANdlERLERIL 96
Cdd:COG0396 31 IMGPNGSGKSTLAKVLMGHPkyEVTSGSILldgedilelspderaRAG-IFLAFQY-P-----VEIPGVSV--SNFLRTA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 97 AGNGTAGDFDAADWtlESRIGAALAQVGLPALPLDRCL-RTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAagrAAI 175
Cdd:COG0396 102 LNARRGEELSAREF--LKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDI---DAL 176
|
170 180
....*....|....*....|....*...
gi 518843096 176 RAL------MREWRGGVLVASHDRELLD 197
Cdd:COG0396 177 RIVaegvnkLRSPDRGILIITHYQRILD 204
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
30-181 |
7.59e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 56.25 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG--------TIGLLRQdmpggwtlaEALGVAND------LERLERI 95
Cdd:PRK09493 28 EVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvDERLIRQ---------EAGMVFQQfylfphLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 96 LAG----NGtAGDFDAADWTLEsrigaALAQVGLpALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAG 171
Cdd:PRK09493 99 MFGplrvRG-ASKEEAEKQARE-----LLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170
....*....|
gi 518843096 172 RAAIRALMRE 181
Cdd:PRK09493 172 RHEVLKVMQD 181
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
30-206 |
7.63e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.02 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTV----------RRTGTIGLLRQDMPGGWTLAEALGVANDLERleRIlagn 99
Cdd:PRK13651 34 EFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKEKEKVLEKLVIQKTRFKKIKKIKEIRR--RV---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 GTAgdFDAADWTL-ESRI------GAA----------------LAQVGLPALPLDRCLRTLSGGERTRVGIAR-LVMEaP 155
Cdd:PRK13651 108 GVV--FQFAEYQLfEQTIekdiifGPVsmgvskeeakkraakyIELVGLDESYLQRSPFELSGGQKRRVALAGiLAME-P 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518843096 156 DLLLLDEPTNNLDAAGRAAIRALMRE-WRGG--VLVASHdrelldDVDRILELT 206
Cdd:PRK13651 185 DFLVFDEPTAGLDPQGVKEILEIFDNlNKQGktIILVTH------DLDNVLEWT 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
353-506 |
7.83e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.13 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR----------RAEGRIVLLDQQVGLLdPEGTILDNIRR-LH 421
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlngqdhtttpPSRRPVSMLFQENNLF-SHLTVAQNIGLgLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 422 P----DAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLD----IESVEILENA 493
Cdd:PRK10771 98 PglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP--ILLLDEPFSALDpalrQEMLTLVSQV 175
|
170
....*....|...
gi 518843096 494 LLSFDGALLVVSH 506
Cdd:PRK10771 176 CQERQLTLLMVSH 188
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-192 |
8.22e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG--TIGLLRQDMPGGWTLAEALGVANDLERLERILAGN-GTAGDFDAADW 110
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLASGKISILGqpTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRyGHMGWLRRAKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 111 TLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRG---GVL 187
Cdd:PRK15056 118 RDRQIVTAALARVDMVEFR-HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDegkTML 196
|
....*
gi 518843096 188 VASHD 192
Cdd:PRK15056 197 VSTHN 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-175 |
9.20e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 56.74 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAFLTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigllrQDMPGGWTL 79
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRgECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG------EPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 80 AEA-LGVANDLERLERilagngtagDFDAADWTLE-SR---IGAALAQVGLPAL--------PLDRCLRTLSGGERTRVG 146
Cdd:PRK13537 78 ARQrVGVVPQFDNLDP---------DFTVRENLLVfGRyfgLSAAAARALVPPLlefaklenKADAKVGELSGGMKRRLT 148
|
170 180
....*....|....*....|....*....
gi 518843096 147 IARLVMEAPDLLLLDEPTNNLDAAGRAAI 175
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
345-483 |
9.42e-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: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 345 GDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD---QQVGL------LDPEGTILD 415
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPphkRPVNTvfqnyaLFPHLTVFE 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 416 NI------RRLHPD---AGDEEAYALCARFAFRNRDARRvvgtLSGGERLRAGLAAALSGSapPWLIILDEPTNHLD 483
Cdd:cd03300 92 NIafglrlKKLPKAeikERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNE--PKVLLLDEPLGALD 162
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-179 |
9.90e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.97 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAG-----------LA---EPSSGTVRRTGtigLLRQD--MPGGWTLAEALgVANDLERLE 93
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGriqgnnftgtiLAnnrKPTKQILKRTG---FVTQDdiLYPHLTVRETL-VFCSLLRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 94 RilagngtagdfdaadwTLESRIGAALAQVGLPALPLDRC---------LRTLSGGERTRVGIARLVMEAPDLLLLDEPT 164
Cdd:PLN03211 171 K----------------SLTKQEKILVAESVISELGLTKCentiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170
....*....|....*
gi 518843096 165 NNLDAAgrAAIRALM 179
Cdd:PLN03211 235 SGLDAT--AAYRLVL 247
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
363-490 |
9.95e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.72 E-value: 9.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTVR--------------RAEGrIVLLDQQVGLLdPEGTILDNI---------RR 419
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfrsprdaQAAG-IAIIHQELNLV-PNLSVAENIflgreprrgGL 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518843096 420 LHPDAGDEEAYALCARFAFrNRDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEIL 490
Cdd:COG1129 112 IDWRAMRRRARELLARLGL-DIDPDTPVGDLSVAQQQLVEIARALSRDAR--VLILDEPTASLTEREVERL 179
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
361-514 |
1.00e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 361 RIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEG-RIVLLDQ------QVGLLDpegTIL-------------DNIRRL 420
Cdd:PRK15064 29 RYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNeRLGKLRQdqfafeEFTVLD---TVImghtelwevkqerDRIYAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 421 hPDAGDEEAYA---LCARFA-FRNRDARRVVGTL------------------SGGERLRAGLAAALSgsAPPWLIILDEP 478
Cdd:PRK15064 106 -PEMSEEDGMKvadLEVKFAeMDGYTAEARAGELllgvgipeeqhyglmsevAPGWKLRVLLAQALF--SNPDILLLDEP 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 518843096 479 TNHLDIESVEILENALLSFDGALLVVSHDPSFVERV 514
Cdd:PRK15064 183 TNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSV 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
335-483 |
1.16e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 55.34 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 335 LAMEGVVAEAGDRR-LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLL---DQQVGL---- 406
Cdd:cd03301 1 VELENVTKRFGNVTaLDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppkDRDIAMvfqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 407 --LDPEGTILDNI------RRLHPDAGDEeayalcarfafRNRDARRVVG----------TLSGGERLRAGLAAALSGSA 468
Cdd:cd03301 81 yaLYPHMTVYDNIafglklRKVPKDEIDE-----------RVREVAELLQiehlldrkpkQLSGGQRQRVALGRAIVREP 149
|
170
....*....|....*
gi 518843096 469 PPWLiiLDEPTNHLD 483
Cdd:cd03301 150 KVFL--MDEPLSNLD 162
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
363-486 |
1.47e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTVR-----------RA--EGRIVLLDQQVGLLdPEGTILDNI------------ 417
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILylgkevtfngpKSsqEAGIGIIHQELNLI-PQLTIAENIflgrefvnrfgr 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518843096 418 ---RRLHpdagdEEAYALCARFAFRnRDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHL-DIES 486
Cdd:PRK10762 113 idwKKMY-----AEADKLLARLNLR-FSSDKLVGELSIGEQQMVEIAKVLSFESK--VIIMDEPTDALtDTET 177
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
32-205 |
1.68e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG------TIGLLRQDMpggwtlaeALgVANDLERLERILAGNGTAG-D 104
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslSHSVLRQGV--------AM-VQQDPVVLADTFLANVTLGrD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 105 FDaadwtlESRIGAALAQVGLPALpldrcLRTLSGGERTRVG---------------IARLVMEAPDLLLLDEPTNNLDA 169
Cdd:PRK10790 441 IS------EEQVWQALETVQLAEL-----ARSLPDGLYTPLGeqgnnlsvgqkqllaLARVLVQTPQILILDEATANIDS 509
|
170 180 190
....*....|....*....|....*....|....*...
gi 518843096 170 AGRAAIRALMREWR--GGVLVASHDRELLDDVDRILEL 205
Cdd:PRK10790 510 GTEQAIQQALAAVRehTTLVVIAHRLSTIVEADTILVL 547
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
16-200 |
1.69e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 16 DGPLFQKLTFAIgtERVGLV---GRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIglLRQDMPggwTLAEAL-------GV 85
Cdd:PRK13540 13 DQPLLQQISFHL--PAGGLLhlkGSNGAGKTTLLKLIAGLLNPEKGEILFERQS--IKKDLC---TYQKQLcfvghrsGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 ANDLERLERILagngtagdFDAADWTLESRIGAALAQVGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:PRK13540 86 NPYLTLRENCL--------YDIHFSPGAVGITELCRLFSLEHL-IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 518843096 166 NLDAAGRAAIRALMREWR---GGVLVASHDRELLDDVD 200
Cdd:PRK13540 157 ALDELSLLTIITKIQEHRakgGAVLLTSHQDLPLNKAD 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
360-519 |
2.26e-08 |
|
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: 54.99 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVRraegrivLLDQQVGLLDPEG---------------------TILDNIR 418
Cdd:COG1127 32 EILAIIGGSGSGKSVLLKLIIGLLRPDSGEIL-------VDGQDITGLSEKElyelrrrigmlfqggalfdslTVFENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 ---RLHPDAGDEEAYALcARFAFRN---RDAR-RVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESVEILE 491
Cdd:COG1127 105 fplREHTDLSEAEIREL-VLEKLELvglPGAAdKMPSELSGGMRKRVALARAL--ALDPEILLYDEPTAGLDPITSAVID 181
|
170 180 190
....*....|....*....|....*....|..
gi 518843096 492 NALL----SFDGALLVVSHDPSFVERVGfDRV 519
Cdd:COG1127 182 ELIRelrdELGLTSVVVTHDLDSAFAIA-DRV 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
335-519 |
2.27e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.07 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 335 LAMEGVVAEAGDRR-LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR-------RAEGRIVLLDQQVGL 406
Cdd:PRK11247 13 LLLNAVSKRYGERTvLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtaplaEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 407 LdPEGTILDNIrrlhpdagdeeAYALCARFAFRNRDARRVVG----------TLSGGERLRAGLAAALSGSapPWLIILD 476
Cdd:PRK11247 93 L-PWKKVIDNV-----------GLGLKGQWRDAALQALAAVGladranewpaALSGGQKQRVALARALIHR--PGLLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 518843096 477 EPTNHLD----IESVEILENALLSFDGALLVVSHDPSfvERVGF-DRV 519
Cdd:PRK11247 159 EPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVS--EAVAMaDRV 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
30-201 |
2.40e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.90 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTV--------------RRTGTIGLLRQDMpggwTLAEALGVANDLERLERI 95
Cdd:PRK10895 30 EIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplhaRARRGIGYLPQEA----SIFRRLSVYDNLMAVLQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 96 LAGNGTAGDFDAADWTLESRIGAALAqvglpalplDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAI 175
Cdd:PRK10895 106 RDDLSAEQREDRANELMEEFHIEHLR---------DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
170 180 190
....*....|....*....|....*....|
gi 518843096 176 RALMREWRG---GVLVASHD-RELLDDVDR 201
Cdd:PRK10895 177 KRIIEHLRDsglGVLITDHNvRETLAVCER 206
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-199 |
2.66e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 56.23 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKS----TLLRIVAGLAEPSSGTVR-----------------RTGTIGLLRQD--------MPGGWTLA 80
Cdd:COG4172 37 ETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfdgqdllglserelrriRGNRIAMIFQEpmtslnplHTIGKQIA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 81 EALgvandleRLERILAGngtagdfDAAdwtlESRIGAALAQVGL--PALPLDRCLRTLSGGERTRVGIARLVMEAPDLL 158
Cdd:COG4172 117 EVL-------RLHRGLSG-------AAA----RARALELLERVGIpdPERRLDAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518843096 159 LLDEPTNNLDAAGRAAIRALMREWRG----GVLVASHD----RELLDDV 199
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQRelgmALLLITHDlgvvRRFADRV 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
354-484 |
2.78e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.00 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD-----QQVGLLDPEGTILDNIR---------- 418
Cdd:PRK09536 24 LSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSaraasRRVASVPQDTSLSFEFDvrqvvemgrt 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 419 ----RLHP-----DAGDEEAYALCARFAFRNRDarrvVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDI 484
Cdd:PRK09536 104 phrsRFDTwtetdRAAVERAMERTGVAQFADRP----VTSLSGGERQRVLLARALAQATP--VLLLDEPTASLDI 172
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-168 |
3.13e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.65 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 36 GRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------------IGLLRQDmpggwtlaealgvandlERL--ERIL 96
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrrIGYVFQD-----------------ARLfpHYKV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 97 AGNGTAG--DFDAADWtleSRIGAALaqvGLPALpLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD 168
Cdd:PRK11144 94 RGNLRYGmaKSMVAQF---DKIVALL---GIEPL-LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
353-507 |
3.34e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 55.61 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPvsgtvrrAEGRIVLLDQQVGL----------------LDPEGTILDN 416
Cdd:PRK11607 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP-------TAGQIMLDGVDLSHvppyqrpinmmfqsyaLFPHMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 417 IR------RLHPD---AGDEEAYALCARFAFrnrdARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLD---- 483
Cdd:PRK11607 112 IAfglkqdKLPKAeiaSRVNEMLGLVHMQEF----AKRKPHQLSGGQRQRVALARSLAKR--PKLLLLDEPMGALDkklr 185
|
170 180
....*....|....*....|....*....
gi 518843096 484 ----IESVEILENAllsfdGALLV-VSHD 507
Cdd:PRK11607 186 drmqLEVVDILERV-----GVTCVmVTHD 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
353-483 |
3.61e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 55.49 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPvsgtvrrAEGRIVLLDQQVGLLDPEG----------------TILDN 416
Cdd:COG3842 25 SLSIEPGEFVALLGPSGCGKTTLLRMIAGFETP-------DSGRILLDGRDVTGLPPEKrnvgmvfqdyalfphlTVAEN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 417 I------RRLHPDAGDEEAYALCARF---AFrnrdARRVVGTLSGGERLRAGLAAALsgsAP-PWLIILDEPTNHLD 483
Cdd:COG3842 98 VafglrmRGVPKAEIRARVAELLELVgleGL----ADRYPHQLSGGQQQRVALARAL---APePRVLLLDEPLSALD 167
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
33-169 |
4.36e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 53.81 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 33 GLVGRNGSGKSTLLRIVAGLAEPS---SGTV------RRTGT----IGLLRQDMpggwTLAEALGVANDLERLERILAGN 99
Cdd:cd03234 37 AILGSSGSGKTTLLDAISGRVEGGgttSGQIlfngqpRKPDQfqkcVAYVRQDD----ILLPGLTVRETLTYTAILRLPR 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 100 GTAGDFDAADWTLESRIGAALAQVGlpalplDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:cd03234 113 KSSDAIRKKRVEDVLLRDLALTRIG------GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
353-507 |
4.65e-08 |
|
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: 53.53 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGT--------VRRAEG---RIVLLDQQVGlLDPEGTILDNIR--- 418
Cdd:cd03265 20 SFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREvrrRIGIVFQDLS-VDDELTGWENLYiha 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 RLHPDAGDE------EAYALCARFAFRNrdarRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESV----E 488
Cdd:cd03265 99 RLYGVPGAErreridELLDFVGLLEAAD----RLVKTYSGGMRRRLEIARSLVHR--PEVLFLDEPTIGLDPQTRahvwE 172
|
170
....*....|....*....
gi 518843096 489 ILENALLSFDGALLVVSHD 507
Cdd:cd03265 173 YIEKLKEEFGMTILLTTHY 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
363-496 |
4.92e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTV--------RRAEGRIVlldQQVGLLDPEGTILDNI-------RRLHPD---- 423
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqHYASKEVA---RRIGLLAQNATTPGDItvqelvaRGRYPHqplf 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518843096 424 ----AGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDI-ESVEILEnaLLS 496
Cdd:PRK10253 114 trwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA--IMLLDEPTTWLDIsHQIDLLE--LLS 187
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
119-205 |
5.20e-08 |
|
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: 52.71 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 119 ALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPD--LLLLDEPTNNLDaagRAAIRALMREWRG------GVLVAS 190
Cdd:cd03238 70 FLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQDINQLLEVIKGlidlgnTVILIE 146
|
90
....*....|....*
gi 518843096 191 HDRELLDDVDRILEL 205
Cdd:cd03238 147 HNLDVLSSADWIIDF 161
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
354-494 |
5.22e-08 |
|
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: 54.48 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAeGRIVlLDQQVGLLDPeGTILDNIrrLHPDAGDEEAYALC 433
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS-GRIS-FSSQFSWIMP-GTIKENI--IFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 434 AR--------FAFRNRDaRRVVG----TLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIES-VEILENAL 494
Cdd:cd03291 133 VKacqleediTKFPEKD-NTVLGeggiTLSGGQRARISLARAVYKDAD--LYLLDSPFGYLDVFTeKEIFESCV 203
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
34-181 |
6.41e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-------------IGLLRQD--MPGGWTLAEALGVAndlERLERILAG 98
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarrIGLLAQNatTPGDITVQELVARG---RYPHQPLFT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 99 NGTAGDFDAadwtlesrIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRAL 178
Cdd:PRK10253 115 RWRKEDEEA--------VTKAMQATGITHLA-DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
...
gi 518843096 179 MRE 181
Cdd:PRK10253 186 LSE 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
137-199 |
7.01e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.10 E-value: 7.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518843096 137 LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRG----GVLVASHD----RELLDDV 199
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNlsivRKLADRV 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
30-170 |
7.13e-08 |
|
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: 53.04 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEpssGTVRRTGTIGLlrqdmpGGWTLAEALgvandlERLERILAGNGtAGDFDAAD 109
Cdd:cd03233 34 EMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGDIHY------NGIPYKEFA------EKYPGEIIYVS-EEDVHFPT 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518843096 110 WTLESRIGAALAQVGlpalplDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAA 170
Cdd:cd03233 98 LTVRETLDFALRCKG------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
353-483 |
7.14e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.45 E-value: 7.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV-----------RRAEGRIVLLdQQVGLLDPEGTILDNI---- 417
Cdd:PRK13536 61 SFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvparaRLARARIGVV-PQFDNLDLEFTVRENLlvfg 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 418 RRLHPDAGD-EEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLD 483
Cdd:PRK13536 140 RYFGMSTREiEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND--PQLLILDEPTTGLD 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
353-485 |
7.48e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.48 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRA-----------EGRIVLLDQQVGL------LDPEGTILD 415
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfdfsktpsDKAIRELRRNVGMvfqqynLWPHLTVQQ 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 416 N-------IRRLHPDAGDEEAYALCARFAFRNRdARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIE 485
Cdd:PRK11124 102 NlieapcrVLGLSKDQALARAEKLLERLRLKPY-ADRFPLHLSGGQQQRVAIARAL--MMEPQVLLFDEPTAALDPE 175
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
353-478 |
8.19e-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: 53.32 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV-------------RRAEGRIVLLDQQVGLLDpEGTILDNIR- 418
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmhKRARLGIGYLPQEASIFR-KLTVEENILa 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518843096 419 --RLHPDAGDE---EAYALCARF---AFRNRDArrvvGTLSGGERLRAGLAAALsgSAPPWLIILDEP 478
Cdd:cd03218 99 vlEIRGLSKKEreeKLEELLEEFhitHLRKSKA----SSLSGGERRRVEIARAL--ATNPKFLLLDEP 160
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
334-492 |
8.21e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.83 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 334 VLAMEGVVAEAGD-RRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLR-------------AP-VSGTVRRAEGR-I 397
Cdd:TIGR02633 1 LLEMKGIVKTFGGvKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgeiywsgSPlKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 398 VLLDQQVGLLdPEGTILDNI----------RRLHPDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGS 467
Cdd:TIGR02633 81 VIIHQELTLV-PELSVAENIflgneitlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180
....*....|....*....|....*
gi 518843096 468 APpwLIILDEPTNHLDIESVEILEN 492
Cdd:TIGR02633 160 AR--LLILDEPSSSLTEKETEILLD 182
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
30-181 |
8.25e-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: 54.83 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLRQDmpggwTLAEALGVA-------NDLERlERILAGNGT 101
Cdd:COG5265 385 KTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdIRDVTQA-----SLRAAIGIVpqdtvlfNDTIA-YNIAYGRPD 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 102 AGD---FDAADwtlesrigaaLAQVG--LPALPL-------DRCLRtLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:COG5265 459 ASEeevEAAAR----------AAQIHdfIESLPDgydtrvgERGLK-LSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170
....*....|..
gi 518843096 170 AGRAAIRALMRE 181
Cdd:COG5265 528 RTERAIQAALRE 539
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-169 |
8.36e-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: 53.31 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 15 PDGPLFQKLTFAI-GTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTV---------------RRTgtIGLLRQD---MPG 75
Cdd:cd03249 14 PDVPILKGLSLTIpPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrwlRSQ--IGLVSQEpvlFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 76 gwTLAEalgvandlerlerilagNGTAGDFDAADWTLESRIGAALA-------------QVGlpalplDRCLrTLSGGER 142
Cdd:cd03249 92 --TIAE-----------------NIRYGKPDATDEEVEEAAKKANIhdfimslpdgydtLVG------ERGS-QLSGGQK 145
|
170 180
....*....|....*....|....*..
gi 518843096 143 TRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDA 172
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
30-168 |
8.69e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.46 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-----------IGLLRQD---MPGgWTLAE--ALGVAND-LERL 92
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrpINMMFQSyalFPH-MTVEQniAFGLKQDkLPKA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 93 ErilagngtagdfdaadwtLESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD 168
Cdd:PRK11607 125 E------------------IASRVNEMLGLVHMQEFA-KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-194 |
1.18e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.02 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG-----TIGLLRQDM---PGGWTLAEALGVANDLERLERiLAGNGT 101
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksiltNISDVHQNMgycPQFDAIDDLLTGREHLYLYAR-LRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 102 AGDFDAADWTLESrigaalaqVGLpALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRA----AIRA 177
Cdd:TIGR01257 2045 EEIEKVANWSIQS--------LGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRmlwnTIVS 2115
|
170
....*....|....*..
gi 518843096 178 LMREWRgGVLVASHDRE 194
Cdd:TIGR01257 2116 IIREGR-AVVLTSHSME 2131
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
348-513 |
1.39e-07 |
|
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: 53.57 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 348 RLGPWTLRID----GPERIALKGANGAGKTTLLRIAAGLRAPVSGTVrRAEGRiVLLDQQVGL----------------- 406
Cdd:COG4148 10 RRGGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRI-RLGGE-VLQDSARGIflpphrrrigyvfqear 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 407 LDPEGTILDNIRrlhpdagdeeaYALcaRFAFRNRDA----------------RRVVGTLSGGERLRAGLAAALSGSapP 470
Cdd:COG4148 88 LFPHLSVRGNLL-----------YGR--KRAPRAERRisfdevvellgighllDRRPATLSGGERQRVAIGRALLSS--P 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518843096 471 WLIILDEPTNHLDIES-VEI---LENALLSFDGALLVVSHDPSFVER 513
Cdd:COG4148 153 RLLLMDEPLAALDLARkAEIlpyLERLRDELDIPILYVSHSLDEVAR 199
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
30-256 |
1.48e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.87 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------------IGLL-----RQDMPGGWTLAEALGVANdLE 90
Cdd:COG1129 279 EILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVpedrkGEGLVLDLSIRENITLAS-LD 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 91 RLERilagngtAGDFDAAdwTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAA 170
Cdd:COG1129 358 RLSR-------GGLLDRR--RERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 171 GRAAIRALMRE--WRG-GVLVASHD-RELLDDVDRILELTaigarsfgggwsafsaardedRRRASAELERADADVRAVR 246
Cdd:COG1129 429 AKAEIYRLIRElaAEGkAVIVISSElPELLGLSDRILVMR---------------------EGRIVGELDREEATEEAIM 487
|
250
....*....|
gi 518843096 247 QAVQARREAK 256
Cdd:COG1129 488 AAATGGAAAA 497
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
353-494 |
1.55e-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: 52.54 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVrraegrivLLD-------------QQVGLLDPE-----GTIL 414
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI--------LLDgvdirdlnlrwlrSQIGLVSQEpvlfdGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 415 DNIRRLHPDAGDEEAYALCaRFA----FRNRDARR---VVG----TLSGGERLRAGLAAALSGSapPWLIILDEPTNHLD 483
Cdd:cd03249 95 ENIRYGKPDATDEEVEEAA-KKAnihdFIMSLPDGydtLVGergsQLSGGQKQRIAIARALLRN--PKILLLDEATSALD 171
|
170
....*....|.
gi 518843096 484 IESVEILENAL 494
Cdd:cd03249 172 AESEKLVQEAL 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-169 |
1.62e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAFLTLDSVCARTPDGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGtigllrQDMPGGWTl 79
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVhALMGENGAGKSTLLKILSGNYQPDAGSILIDG------QEMRFAST- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 80 AEAL--GVA---------NDLERLERILAGN--GTAGDFDAAdwTLESRIGAALAQVGL---PALPldrcLRTLSGGERT 143
Cdd:PRK11288 74 TAALaaGVAiiyqelhlvPEMTVAENLYLGQlpHKGGIVNRR--LLNYEAREQLEHLGVdidPDTP----LKYLSIGQRQ 147
|
170 180
....*....|....*....|....*.
gi 518843096 144 RVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSA 173
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-205 |
1.95e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.44 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPD-----GPLfqKLTFAIGtERVGLVGRNGSGKSTLLRIVAGLAEPSSGtvrrtgtiGLLRQDMP---GG 76
Cdd:PRK10522 323 LELRNVTFAYQDngfsvGPI--NLTIKRG-ELLFLIGGNGSGKSTLAMLLTGLYQPQSG--------EILLDGKPvtaEQ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 77 WTLAEAL--GVANDLERLERILAGNGTAGDfdaadwtlesrigAALAQVGLPALPLDRCLR---------TLSGGERTRV 145
Cdd:PRK10522 392 PEDYRKLfsAVFTDFHLFDQLLGPEGKPAN-------------PALVEKWLERLKMAHKLEledgrisnlKLSKGQKKRL 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 146 GIARLVMEAPDLLLLDEPTNNLDAAGR----AAIRALMREWRGGVLVASHDRELLDDVDRILEL 205
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDPHFRrefyQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEM 522
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
363-513 |
2.87e-07 |
|
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: 51.32 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVL-----LDQQVGLLDPE-----GTILDNIRRLHPDAGDEEAYAL 432
Cdd:cd03248 44 ALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkyLHSKVSLVGQEpvlfaRSLQDNIAYGLQSCSFECVKEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 433 CARFAFRN----------RDARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENALLSF--DGA 500
Cdd:cd03248 124 AQKAHAHSfiselasgydTEVGEKGSQLSGGQKQRVAIARALIRN--PQVLILDEATSALDAESEQQVQQALYDWpeRRT 201
|
170
....*....|...
gi 518843096 501 LLVVSHDPSFVER 513
Cdd:cd03248 202 VLVIAHRLSTVER 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-484 |
2.91e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------------IGLLRQdmpggwtlaEALGVANdLERLERILAG- 98
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQ---------EPLLFPN-LSVKENILFGl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 99 NGTAGDfdaadwtlESRIGAALAQVGLpALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA---- 174
Cdd:PRK15439 112 PKRQAS--------MQKMKQLLAALGC-QLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERlfsr 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 175 IRALMREWRGGVLVASHDRELLDDVDRIleltaigarsfgggwsafSAARDEDRRRASAELERADADVravrqaVQArre 254
Cdd:PRK15439 183 IRELLAQGVGIVFISHKLPEIRQLADRI------------------SVMRDGTIALSGKTADLSTDDI------IQA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 255 akerrdragrafaakgsepkILLGARAERAQNSGGTAQAISDRRMGRAlaeADDARSRVEVLTPltialppsglpsganv 334
Cdd:PRK15439 236 --------------------ITPAAREKSLSASQKLWLELPGNRRQQA---AGAPVLTVEDLTG---------------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 335 lamEGVVAEAGDRRLGpwtlridgpERIALKGANGAGKTTLLRIAAGLRAPVSGTV--------------RRAEGRIVLL 400
Cdd:PRK15439 277 ---EGFRNISLEVRAG---------EILGLAGVVGAGRTELAETLYGLRPARGGRImlngkeinalstaqRLARGLVYLP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 401 D--QQVGL---------------------LDP--EGTILDNIRRlhpdagdeeayALCARFAfrnrDARRVVGTLSGGER 455
Cdd:PRK15439 345 EdrQSSGLyldaplawnvcalthnrrgfwIKParENAVLERYRR-----------ALNIKFN----HAEQAARTLSGGNQ 409
|
490 500
....*....|....*....|....*....
gi 518843096 456 LRAGLAAALsgSAPPWLIILDEPTNHLDI 484
Cdd:PRK15439 410 QKVLIAKCL--EASPQLLIVDEPTRGVDV 436
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
34-208 |
2.92e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.09 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT----------IGLLRQDMPGGWTLAEALGVANDLERleRILAGngtAG 103
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDDItithktkdkyIRPVRKRIGMVFQFPESQLFEDTVER--EIIFG---PK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 104 DFDAADWTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWR 183
Cdd:PRK13646 113 NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQ 192
|
170 180
....*....|....*....|....*....
gi 518843096 184 ----GGVLVASHDrelLDDVDRILELTAI 208
Cdd:PRK13646 193 tdenKTIILVSHD---MNEVARYADEVIV 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-203 |
2.95e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.11 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 5 LTLDSVCARTPDG-PLFQKLTFAI--GtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRrtgtigLLRQDMpGGWTLAE 81
Cdd:COG3845 258 LEVENLSVRDDRGvPALKDVSLEVraG-EILGIAGVAGNGQSELAEALAGLRPPASGSIR------LDGEDI-TGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 82 --ALGVANDLErlERIlaGNGTAGDFDAAD---------------WTLESRIGAALAQ------------VGLPAlpldr 132
Cdd:COG3845 330 rrRLGVAYIPE--DRL--GRGLVPDMSVAEnlilgryrrppfsrgGFLDRKAIRAFAEelieefdvrtpgPDTPA----- 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518843096 133 clRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWR---GGVLVASHDrelLDDV----DRIL 203
Cdd:COG3845 401 --RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdagAAVLLISED---LDEIlalsDRIA 473
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
366-483 |
2.97e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.25 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 366 GANGAGKTTLLRIAAGLRAPVSGTvrraegrIVLLDQQVGLLDPEG-----------------TILDN------IRRLHP 422
Cdd:PRK10247 40 GPSGCGKSTLLKIVASLISPTSGT-------LLFEGEDISTLKPEIyrqqvsycaqtptlfgdTVYDNlifpwqIRNQQP 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 423 dagDEEAY-ALCARFAFRNRDARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLD 483
Cdd:PRK10247 113 ---DPAIFlDDLERFALPDTILTKNIAELSGGEKQRISLIRNL--QFMPKVLLLDEITSALD 169
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
353-519 |
3.20e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.91 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR--------------RAegRIVLLDQQVGLLDpeGTILDNIR 418
Cdd:PRK11160 360 SLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngqpiadyseaalRQ--AISVVSQRVHLFS--ATLRDNLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 RLHPDAGDEEayaLCarfafrnrDARRVVG--------------------TLSGGERLRAGLAAALSGSAPpwLIILDEP 478
Cdd:PRK11160 436 LAAPNASDEA---LI--------EVLQQVGleklleddkglnawlgeggrQLSGGEQRRLGIARALLHDAP--LLLLDEP 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 518843096 479 TNHLDIES-VEILENaLLSF--DGALLVVSHDPSFVERvgFDRV 519
Cdd:PRK11160 503 TEGLDAETeRQILEL-LAEHaqNKTVLMITHRLTGLEQ--FDRI 543
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
345-511 |
3.21e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.05 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 345 GDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAeGRIV------LLDQQVGLL--DPE-----G 411
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-GREVnaenekWVRSKVGLVfqDPDdqvfsS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 412 TILDNI------RRLHPDAGD---EEAYALCARFAFRNRDARRvvgtLSGGERLRAGLAAALsgSAPPWLIILDEPTNHL 482
Cdd:PRK13647 96 TVWDDVafgpvnMGLDKDEVErrvEEALKAVRMWDFRDKPPYH----LSYGQKKRVAIAGVL--AMDPDVIVLDEPMAYL 169
|
170 180 190
....*....|....*....|....*....|..
gi 518843096 483 DIESVEILENAL--LSFDGALLVVS-HDPSFV 511
Cdd:PRK13647 170 DPRGQETLMEILdrLHNQGKTVIVAtHDVDLA 201
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
34-205 |
3.21e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.16 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRrTGTIGLLRQDMPGGWTLAEALGVANDLERLERILAGNGTAGDFDAADWTLE 113
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQ-VGDIYIGDKKNNHELITNPYSKKIKNFKELRRRVSMVFQFPEYQLFKDTIE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 114 ------------SRIGAA------LAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAI 175
Cdd:PRK13631 136 kdimfgpvalgvKKSEAKklakfyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM 215
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 176 RALMREWRGG---VLVASHDRE-LLDDVDRILEL 205
Cdd:PRK13631 216 MQLILDAKANnktVFVITHTMEhVLEVADEVIVM 249
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
366-513 |
3.40e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.05 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 366 GANGAGKTTLLRiAAGLrapvsgtvrraegrIVLLDQQVGLldpegtildniRRLHPDAGDEEAYALcARFAFrnrdarr 445
Cdd:cd03227 28 GPNGSGKSTILD-AIGL--------------ALGGAQSATR-----------RRSGVKAGCIVAAVS-AELIF------- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518843096 446 VVGTLSGGERLRAGLAAALSGSA--PPWLIILDEPTNHLDIESVEILENALLSF--DGA-LLVVSHDPSFVER 513
Cdd:cd03227 74 TRLQLSGGEKELSALALILALASlkPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAqVIVITHLPELAEL 146
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-192 |
3.54e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 16 DGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQDM--PGGWTLAEALGVA----ND 88
Cdd:PRK14246 22 DKAILKDITIKIPNNSIfGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfqIDAIKLRKEVGMVfqqpNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 89 LERL---ERILAGNGTAGDFDAADwtLESRIGAALAQVGLPALPLDRC---LRTLSGGERTRVGIARLVMEAPDLLLLDE 162
Cdd:PRK14246 102 FPHLsiyDNIAYPLKSHGIKEKRE--IKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|..
gi 518843096 163 PTNNLDAAGRAAIRALMREWRG--GVLVASHD 192
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
335-495 |
3.73e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 51.62 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 335 LAMEGVVAE-AGDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIV-------LLDQQVGL 406
Cdd:PRK11248 2 LQISHLYADyGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaergVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 407 LdPEGTILDNI------RRLHPDAGDEEAYALCARFAFRNRDARRvVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTN 480
Cdd:PRK11248 82 L-PWRNVQDNVafglqlAGVEKMQRLEIAHQMLKKVGLEGAEKRY-IWQLSGGQRQRVGIARAL--AANPQLLLLDEPFG 157
|
170
....*....|....*
gi 518843096 481 HLDIESVEILENALL 495
Cdd:PRK11248 158 ALDAFTREQMQTLLL 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
137-181 |
4.62e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.00 E-value: 4.62e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 518843096 137 LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMRE 181
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFE 194
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
354-505 |
4.70e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.17 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGL----RAP----------------VSGTVRRAEGRIVLLDQQVGLLDpEGTI 413
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAgshiellgrtvqregrLARDIRKSRANTGYIFQQFNLVN-RLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 414 LDNIrrLHPDAGDEEAYALCARFAFRNRDAR------RV---------VGTLSGGERLRAGLAAALSGSAPpwLIILDEP 478
Cdd:PRK09984 104 LENV--LIGALGSTPFWRTCFSWFTREQKQRalqaltRVgmvhfahqrVSTLSGGQQQRVAIARALMQQAK--VILADEP 179
|
170 180 190
....*....|....*....|....*....|
gi 518843096 479 TNHLDIESVEILENALLSF---DGALLVVS 505
Cdd:PRK09984 180 IASLDPESARIVMDTLRDInqnDGITVVVT 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
136-203 |
6.54e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 6.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 136 TLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREW----RGGVLVASHDRELLDDVDRIL 203
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELakkdKGIIIISSEMPELLGITDRIL 462
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-180 |
7.44e-07 |
|
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: 49.55 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEpsSGTVrrTGTIGLlrqdmpggwtlaealgvaNDLERLERILAGNGTAGDFDAADWTLE 113
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGRKT--AGVI--TGEILI------------------NGRPLDKNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 114 SRigaalaqvglPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMR 180
Cdd:cd03232 96 VR----------EALRFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-181 |
7.49e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.68 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAE---------------------PSSGTVRRTGTIGLLRQDMPGgWTLAEALGVANDLERL 92
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNRLIElypearvsgevyldgqdifkmDVIELRRRVQMVFQIPNPIPN-LSIFENVALGLKLNRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 93 ERILAgngtagdfdaadwTLESRIGAALAQVGLPALPLDRC---LRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:PRK14247 113 VKSKK-------------ELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDP 179
|
170
....*....|..
gi 518843096 170 AGRAAIRALMRE 181
Cdd:PRK14247 180 ENTAKIESLFLE 191
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
30-164 |
7.55e-07 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 50.22 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTigllrqdmpggwtlaealgvanDLERL---ERILAGNG--TAGD 104
Cdd:TIGR03410 27 EVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGE----------------------DITKLpphERARAGIAyvPQGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 105 FDAADWTLESRIgaalaQVGLPALP--------------------LDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPT 164
Cdd:TIGR03410 85 EIFPRLTVEENL-----LTGLAALPrrsrkipdeiyelfpvlkemLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-164 |
9.86e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 1 MSAFLTLDSVCARTPDGPLFQKLTFAIGT-ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIgllRQDMPGGWTL 79
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQgEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD---ITDWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 80 AEALGVANDLERL--ERILAGNGTAGDFDAADWTLESRIGAALAQvgLPALPLDRCLR--TLSGGERTRVGIARLVMEAP 155
Cdd:PRK11614 79 REAVAIVPEGRRVfsRMTVEENLAMGGFFAERDQFQERIKWVYEL--FPRLHERRIQRagTMSGGEQQMLAIGRALMSQP 156
|
....*....
gi 518843096 156 DLLLLDEPT 164
Cdd:PRK11614 157 RLLLLDEPS 165
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
353-522 |
9.87e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 51.65 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD----------------QQVGLLdPEGTILDN 416
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalaqlrrehfgfifQRYHLL-SHLTAAQN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 417 IRRLHPDAGDEE------AYALCARFAFRNRDARRvVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEIL 490
Cdd:PRK10535 107 VEVPAVYAGLERkqrllrAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMNGGQ--VILADEPTGALDSHSGEEV 183
|
170 180 190
....*....|....*....|....*....|....*
gi 518843096 491 ENAL--LSFDG-ALLVVSHDPSFVERVgfDRVFEV 522
Cdd:PRK10535 184 MAILhqLRDRGhTVIIVTHDPQVAAQA--ERVIEI 216
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
363-513 |
1.01e-06 |
|
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: 48.86 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLR---IAAGLRAPVSGTVRRAEGRIVLLDQQVGLLDpegtilDNIRRLHPDagdeeayalcarfafr 439
Cdd:cd03238 25 VVTGVSGSGKSTLVNeglYASGKARLISFLPKFSRNKLIFIDQLQFLID------VGLGYLTLG---------------- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 440 nrdarRVVGTLSGGERLRAGLAAALSGSAPPWLIILDEPTNHLDIESVEILENA---LLSFDGALLVVSHDPSFVER 513
Cdd:cd03238 83 -----QKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVikgLIDLGNTVILIEHNLDVLSS 154
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
362-509 |
1.04e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 50.87 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 362 IALKGANGAGKTTLLRIAAGLRAPVSG---------TVRRAEGR-IVLLDQQVGLLdPEGTILDNIR---RLHPDAGDE- 427
Cdd:PRK11432 35 VTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedvTHRSIQQRdICMVFQSYALF-PHMSLGENVGyglKMLGVPKEEr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 428 -----EAYALCARFAFRNrdarRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDI-------ESVEILENall 495
Cdd:PRK11432 114 kqrvkEALELVDLAGFED----RYVDQISGGQQQRVALARAL--ILKPKVLLFDEPLSNLDAnlrrsmrEKIRELQQ--- 184
|
170
....*....|....
gi 518843096 496 SFDGALLVVSHDPS 509
Cdd:PRK11432 185 QFNITSLYVTHDQS 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
363-519 |
1.11e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTVR-------------RAEGRIVLLDQQVGLLDpEGTILDN--IRRlHP----- 422
Cdd:PRK09700 35 ALLGENGAGKSTLMKVLSGIHEPTKGTITinninynkldhklAAQLGIGIIYQELSVID-ELTVLENlyIGR-HLtkkvc 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 423 --DAGD-----EEAYALCARFAFRnRDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEIL---EN 492
Cdd:PRK09700 113 gvNIIDwremrVRAAMMLLRVGLK-VDLDEKVANLSISHKQMLEIAKTLMLDAK--VIIMDEPTSSLTNKEVDYLfliMN 189
|
170 180
....*....|....*....|....*..
gi 518843096 493 ALLSFDGALLVVSHDPSFVERVGfDRV 519
Cdd:PRK09700 190 QLRKEGTAIVYISHKLAEIRRIC-DRY 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
353-520 |
1.70e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.58 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGT----------VRRAEGRIVLLDQ-QVGLLDPE----------- 410
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSivvngqtinlVRDKDGQLKVADKnQLRLLRTRltmvfqhfnlw 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 411 --GTILDNIRR-------LHPDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSgsAPPWLIILDEPTNH 481
Cdd:PRK10619 105 shMTVLENVMEapiqvlgLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALA--MEPEVLLFDEPTSA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518843096 482 LDIESV-EILE--NALLSFDGALLVVSHDPSFVERVGFDRVF 520
Cdd:PRK10619 183 LDPELVgEVLRimQQLAEEGKTMVVVTHEMGFARHVSSHVIF 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
137-203 |
1.77e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 1.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518843096 137 LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG----VLVASHDRELLDDVDRIL 203
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEglsiILVSSEMPEVLGMSDRIL 466
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
112-215 |
1.78e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 112 LESRIgAALAQVGLPALPLDRCLRTLSGGERTRVGIAR-LVMEAPDLL-LLDEPTNNL---DAAGRAAIRALMREWRGGV 186
Cdd:PRK00635 453 LKSRL-SILIDLGLPYLTPERALATLSGGEQERTALAKhLGAELIGITyILDEPSIGLhpqDTHKLINVIKKLRDQGNTV 531
|
90 100
....*....|....*....|....*....
gi 518843096 187 LVASHDRELLDDVDRILELTAiGARSFGG 215
Cdd:PRK00635 532 LLVEHDEQMISLADRIIDIGP-GAGIFGG 559
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
34-202 |
2.00e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLaepssgTVRRTGtigllrQDMPGGWTLAEALGVANDLERLERILAGNGTAGDFDAADWTLE 113
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGL------IISETG------QTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFPEYQLFQETIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 114 SRIGAALAQVG---------------LPALPLDRCLRT---LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAI 175
Cdd:PRK13645 110 KDIAFGPVNLGenkqeaykkvpellkLVQLPEDYVKRSpfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDF 189
|
170 180 190
....*....|....*....|....*....|.
gi 518843096 176 RALM----REWRGGVLVASHDrelLDDVDRI 202
Cdd:PRK13645 190 INLFerlnKEYKKRIIMVTHN---MDQVLRI 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
353-513 |
2.39e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.49 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD-----QQVGLLDPE-----GTILDNIRRLHP 422
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhhylhRQVALVGQEpvlfsGSVRENIAYGLT 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 423 DAGDEEAYALcARFAFRN-------RDARRVVGT----LSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILE 491
Cdd:TIGR00958 581 DTPDEEIMAA-AKAANAHdfimefpNGYDTEVGEkgsqLSGGQKQRIAIARALVRK--PRVLILDEATSALDAECEQLLQ 657
|
170 180
....*....|....*....|..
gi 518843096 492 NALLSFDGALLVVSHDPSFVER 513
Cdd:TIGR00958 658 ESRSRASRTVLLIAHRLSTVER 679
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-203 |
2.53e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 50.02 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 16 DGPLFQKLTFAIGTER-VGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTG------TIGLLRQDMpggwtlaeALgVAND 88
Cdd:PRK11176 355 EVPALRNINFKIPAGKtVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdyTLASLRNQV--------AL-VSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 89 LERLERILAGNGT--AGDFdaadWTLESRIGAALAQVGLPAL-PLDRCLRT--------LSGGERTRVGIAR-LVMEAPd 156
Cdd:PRK11176 426 VHLFNDTIANNIAyaRTEQ----YSREQIEEAARMAYAMDFInKMDNGLDTvigengvlLSGGQRQRIAIARaLLRDSP- 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 518843096 157 LLLLDEPTNNLDAAGRAAIRALMREWRGG--VLVASHDRELLDDVDRIL 203
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNrtSLVIAHRLSTIEKADEIL 549
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
366-522 |
2.56e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 48.42 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 366 GANGAGKTTLLR-IAAGLRAPVSGTvRRAEGRIVLLDQQVGLLDPEGTILDN------IRRLHPDAGDEEAYALCARFAF 438
Cdd:cd03279 35 GPTGAGKSTILDaITYALYGKTPRY-GRQENLRSVFAPGEDTAEVSFTFQLGgkkyrvERSRGLDYDQFTRIVLLPQGEF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 439 RnRDARRVVGTLSGGERLRAGLAAAL--------SGSAPPWLIILDEPTNHLDIESVEILENAL--LSFDGAL-LVVSHD 507
Cdd:cd03279 114 D-RFLARPVSTLSGGETFLASLSLALalsevlqnRGGARLEALFIDEGFGTLDPEALEAVATALelIRTENRMvGVISHV 192
|
170
....*....|....*
gi 518843096 508 PSFVERvgFDRVFEV 522
Cdd:cd03279 193 EELKER--IPQRLEV 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
34-181 |
2.69e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.88 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGtVRRTGTIGLLRQDMpggwtlaeaLGVANDLERLER------------------- 94
Cdd:COG1117 42 LIGPSGCGKSTLLRCLNRMNDLIPG-ARVEGEILLDGEDI---------YDPDVDVVELRRrvgmvfqkpnpfpksiydn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 95 ILAGNGTAGDFDAADwtLESRIGAALAQVGL----------PALpldrclrTLSGGERTRVGIAR-LVMEaPDLLLLDEP 163
Cdd:COG1117 112 VAYGLRLHGIKSKSE--LDEIVEESLRKAALwdevkdrlkkSAL-------GLSGGQQQRLCIARaLAVE-PEVLLMDEP 181
|
170
....*....|....*...
gi 518843096 164 TNNLDAAGRAAIRALMRE 181
Cdd:COG1117 182 TSALDPISTAKIEELILE 199
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
47-504 |
2.78e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 50.26 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 47 RIVAGLAEPSSGTVRRTGTIGLLRQDMPGGWTLAEAL------GVANDLERL----------------ERILAGNGTAGD 104
Cdd:COG3321 801 PVLTGLVRQCLAAAGDAVVLPSLRRGEDELAQLLTALaqlwvaGVPVDWSALypgrgrrrvplptypfQREDAAAALLAA 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 105 FDAADWTLESRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTnNLDAAGRAAIRALMREWRG 184
Cdd:COG3321 881 ALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA-ALLALAAAAAAAAAALAAA 959
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 185 GVLVASHDRELLDDVDRILELTAIGARSFGGGWSAFSAARDEDRRRASAELERADADVRAVRQAVQARREAKERRDRAGR 264
Cdd:COG3321 960 EAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAA 1039
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 265 AFAAKGSEPKILLGARAERAQNSGGTAQAISDRRMGRALAEADDARSRVEVLTPLTIALPPSGLPSGANVLAMEGVVAEA 344
Cdd:COG3321 1040 AAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAA 1119
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 345 GDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQVGLLDPEGTILDNIRRLHPDA 424
Cdd:COG3321 1120 AAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAA 1199
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 425 GDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSAPPWLIILDEPTNHLDIESVEILENALLSFDGALLVV 504
Cdd:COG3321 1200 LLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAA 1279
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-507 |
2.93e-06 |
|
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: 48.90 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 364 LKGANGAGKTTLLRIAAGLRAPVSGT-------------------------VRRAEGRIVLLDQQVGLLdP---EGTILD 415
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkLLEGDVKVIVKPQYVDLI-PkavKGKVGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 416 NIRRLHPDAGDEEayaLCARFAFRN-RDarRVVGTLSGGERLRAGLAAALSGSAPPWLiiLDEPTNHLDIE---SVEILE 491
Cdd:cd03236 110 LLKKKDERGKLDE---LVDQLELRHvLD--RNIDQLSGGELQRVAIAAALARDADFYF--FDEPSSYLDIKqrlNAARLI 182
|
170
....*....|....*.
gi 518843096 492 NALLSFDGALLVVSHD 507
Cdd:cd03236 183 RELAEDDNYVLVVEHD 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
353-486 |
3.24e-06 |
|
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: 48.25 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD-----QQVGLLDPE-----GTILDNIRRLHP 422
Cdd:cd03252 22 SLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADpawlrRQVGVVLQEnvlfnRSIRDNIALADP 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 423 DAGDEEAYAlCARFAFRNRDARR-------VVG----TLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIES 486
Cdd:cd03252 102 GMSMERVIE-AAKLAGAHDFISElpegydtIVGeqgaGLSGGQRQRIAIARALIHN--PRILIFDEATSALDYES 173
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
30-162 |
3.31e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLlrqdmpggwtLAEALGVANDLERLERI-LAG---------- 98
Cdd:PRK13545 51 EIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL----------IAISSGLNGQLTGIENIeLKGlmmgltkeki 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 99 -NGTAGDFDAADwtlesrIGAALAQvglPalpldrcLRTLSGGERTRVGIARLVMEAPDLLLLDE 162
Cdd:PRK13545 121 kEIIPEIIEFAD------IGKFIYQ---P-------VKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
360-486 |
3.32e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.93 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRA-----EGRIVLLdQQVGL-------LDPEGTILDN---IRRLH--P 422
Cdd:COG4586 49 EIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpfKRRKEFA-RRIGVvfgqrsqLWWDLPAIDSfrlLKAIYriP 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 423 DAgdeeayalcarfAFRNRDARRV------------VGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIES 486
Cdd:COG4586 128 DA------------EYKKRLDELVelldlgelldtpVRQLSLGQRMRCELAAALLHR--PKILFLDEPTIGLDVVS 189
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
354-515 |
3.89e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLL--DQQVGLLDPEGTiLDNIRRLHPDAGDE---- 427
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfEQLQKLVSDEWQ-RNNTDMLSPGEDDTgrtt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 428 --------EAYALCARFA--FRNRD--ARRVVgTLSGGERLRAGLAAALSgsAPPWLIILDEPTNHLDIESVEILENAL- 494
Cdd:PRK10938 103 aeiiqdevKDPARCEQLAqqFGITAllDRRFK-YLSTGETRKTLLCQALM--SEPDLLILDEPFDGLDVASRQQLAELLa 179
|
170 180
....*....|....*....|....*..
gi 518843096 495 -LSFDGALLVV-----SHDPSFVERVG 515
Cdd:PRK10938 180 sLHQSGITLVLvlnrfDEIPDFVQFAG 206
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
30-205 |
4.13e-06 |
|
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: 49.35 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT------IGLLRQDMpgGWTLAEALGVANDLerLERILAG---NG 100
Cdd:TIGR01193 501 SKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidRHTLRQFI--NYLPQEPYIFSGSI--LENLLLGakeNV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 101 TAGDFDAADWTLESRIGAALAQVGLPAlPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA-AGRAAIRALM 179
Cdd:TIGR01193 577 SQDEIWAACEIAEIKDDIENMPLGYQT-ELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTiTEKKIVNNLL 655
|
170 180
....*....|....*....|....*.
gi 518843096 180 REWRGGVLVASHDRELLDDVDRILEL 205
Cdd:TIGR01193 656 NLQDKTIIFVAHRLSVAKQSDKIIVL 681
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
297-391 |
4.18e-06 |
|
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: 49.41 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 297 RRMGRALAEADDARSrvevltpltiALPPSGLPSGANVLAMEGVV----AEAGDR--RLGPWTLRIDGPERIALKGANGA 370
Cdd:COG4615 300 EELELALAAAEPAAA----------DAAAPPAPADFQTLELRGVTyrypGEDGDEgfTLGPIDLTIRRGELVFIVGGNGS 369
|
90 100
....*....|....*....|.
gi 518843096 371 GKTTLLRIAAGLRAPVSGTVR 391
Cdd:COG4615 370 GKSTLAKLLTGLYRPESGEIL 390
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
360-506 |
4.44e-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: 49.63 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAeGRIVL-----LDQQVGLLdPEGTILDNIRrlhpdAGDEEAYaLCA 434
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVA-GKSILtnisdVHQNMGYC-PQFDAIDDLL-----TGREHLY-LYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 435 RFAFRNRD------------------ARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLS 496
Cdd:TIGR01257 2038 RLRGVPAEeiekvanwsiqslglslyADRLAGTYSGGNKRKLSTAIALIGCPP--LVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170
....*....|...
gi 518843096 497 F---DGALLVVSH 506
Cdd:TIGR01257 2116 IireGRAVVLTSH 2128
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-202 |
5.65e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGL--------------AEPSSGTVRRT--GTIGLLRQDMpggwTLAEALGVAndlerlE 93
Cdd:PRK13549 32 EIVSLCGENGAGKSTLMKVLSGVyphgtyegeiifegEELQASNIRDTerAGIAIIHQEL----ALVKELSVL------E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 94 RILAGN--GTAG--DFDAadwtLESRIGAALAQVGL---PALPldrcLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNN 166
Cdd:PRK13549 102 NIFLGNeiTPGGimDYDA----MYLRAQKLLAQLKLdinPATP----VGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 518843096 167 LDAAGRAAIRALMREWR-GGV--LVASHDrelLDDVDRI 202
Cdd:PRK13549 174 LTESETAVLLDIIRDLKaHGIacIYISHK---LNEVKAI 209
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
137-212 |
6.28e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 137 LSGGERTRVGIA-RLVME-----APDLLLLDEPTNNLDAAGRAAIRALM-REWRG--GVLVASHDRELLDDVDRILELTA 207
Cdd:PRK03918 789 LSGGERIALGLAfRLALSlylagNIPLLILDEPTPFLDEERRRKLVDIMeRYLRKipQVIIVSHDEELKDAADYVIRVSL 868
|
....*
gi 518843096 208 IGARS 212
Cdd:PRK03918 869 EGGVS 873
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
30-172 |
6.95e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.46 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIV--------------------AGLAEPSSGTVRRTGTIGLL-RQDMPGGWTLaealgvand 88
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRSInrmndlnpevtitgsivyngHNIYSPRTDTVDLRKEIGMVfQQPNPFPMSI--------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 89 lerLERILAGNGTAGDFDAAdwTLESRIGAALAQVGLPALPLDRCLRT---LSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:PRK14239 103 ---YENVVYGLRLKGIKDKQ--VLDEAVEKSLKGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
....*....
gi 518843096 166 NLD--AAGR 172
Cdd:PRK14239 178 ALDpiSAGK 186
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
136-212 |
7.56e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 136 TLSGGERT------RVGIARLVMEAPDLLLLDEPTNNLDAAGRAA----IRALMREWRG--GVLVASHDRELLDDVDRIL 203
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNlkdiIEYSLKDSSDipQVIMISHHRELLSVADVAY 880
|
....*....
gi 518843096 204 ELTAIGARS 212
Cdd:PRK01156 881 EVKKSSGSS 889
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
341-513 |
7.88e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.51 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 341 VAEAGDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAG-LRAPVSGTVRRAEGRIVLLDQQVGLLDPegTILDNIRR 419
Cdd:PRK13547 9 VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAPRGARVTGDVTLNGEPLAAIDA--PRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 420 LHPDAGdEEAYALCAR----------------FAFRNRD--------------ARRVVGTLSGGERLRAGLAAALS---- 465
Cdd:PRK13547 87 VLPQAA-QPAFAFSAReivllgrypharragaLTHRDGEiawqalalagatalVGRDVTTLSGGELARVQFARVLAqlwp 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 466 ---GSAPPWLIILDEPTNHLDIESVEILENAL--LSFD---GALLVVsHDPSFVER 513
Cdd:PRK13547 166 phdAAQPPRYLLLDEPTAALDLAHQHRLLDTVrrLARDwnlGVLAIV-HDPNLAAR 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
353-483 |
7.92e-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: 47.27 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGlRAPVSGTvrrAEGRIVLLDQQvglLDPEgTILDNIR------RLHPDAGD 426
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGT---TSGQILFNGQP---RKPD-QFQKCVAyvrqddILLPGLTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518843096 427 EEAYALCARFAFRNR--DARR--------------------VVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLD 483
Cdd:cd03234 99 RETLTYTAILRLPRKssDAIRkkrvedvllrdlaltriggnLVKGISGGERRRVSIAVQLLWD--PKVLILDEPTSGLD 175
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
349-489 |
8.43e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 47.39 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 349 LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVrRAEGRIVL------LDQQVGLLDPEGTIldNIR---- 418
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEV-LVDGLDVAttpsreLAKRLAILRQENHI--NSRltvr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 419 -------------RLHPDagDEEAYALCARF----AFRNR--DarrvvgTLSGGERLRAGLAAALSGSAPpwLIILDEPT 479
Cdd:COG4604 94 elvafgrfpyskgRLTAE--DREIIDEAIAYldleDLADRylD------ELSGGQRQRAFIAMVLAQDTD--YVLLDEPL 163
|
170
....*....|.
gi 518843096 480 NHLDIE-SVEI 489
Cdd:COG4604 164 NNLDMKhSVQM 174
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-202 |
9.46e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------------IGLL---RQD--MPGGWTLAEALGVANDLE 90
Cdd:PRK09700 290 EILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYItesRRDngFFPNFSIAQNMAISRSLK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 91 rleriLAG-NGTAGDFDAADwtlESRIG-AALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD 168
Cdd:PRK09700 370 -----DGGyKGAMGLFHEVD---EQRTAeNQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 518843096 169 AAGRAAIRALMR----EWRGGVLVASHDRELLDDVDRI 202
Cdd:PRK09700 442 VGAKAEIYKVMRqladDGKVILMVSSELPEIITVCDRI 479
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-515 |
9.66e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.35 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGL------RAPVSGTVRRAEGRIVLLD-----QQVGLLD------PEGTILD 415
Cdd:PRK14246 30 TIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDaiklrKEVGMVFqqpnpfPHLSIYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 416 NIrrlhpdagdeeAYALCARFAFRNRDARRVV---------------------GTLSGGERLRAGLAAALSgsAPPWLII 474
Cdd:PRK14246 110 NI-----------AYPLKSHGIKEKREIKKIVeeclrkvglwkevydrlnspaSQLSGGQQQRLTIARALA--LKPKVLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518843096 475 LDEPTNHLDIESVEILENAL--LSFDGALLVVSHDPSFVERVG 515
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLIteLKNEIAIVIVSHNPQQVARVA 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
342-487 |
9.81e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 47.20 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 342 AEAGDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIaaglrapVSGTVRRAEGRIVLLDQQV-------------GLLD 408
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYM-------VVGIVPRDAGNIIIDDEDIsllplhararrgiGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 409 PEGTIL------DNI-------RRLHPDAGDEEAYALCARFAFRNrdARRVVG-TLSGGERLRAGLAAALsgSAPPWLII 474
Cdd:PRK10895 85 QEASIFrrlsvyDNLmavlqirDDLSAEQREDRANELMEEFHIEH--LRDSMGqSLSGGERRRVEIARAL--AANPKFIL 160
|
170
....*....|...
gi 518843096 475 LDEPTNHLDIESV 487
Cdd:PRK10895 161 LDEPFAGVDPISV 173
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
353-479 |
1.00e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.80 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLriaaglrAPVSGTVRRAEGRIVLLDQQVG------LLDPEGTILDNIRRLHPDAGD 426
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTTLL-------GTLCGDPRATSGRIVFDGKDITdwqtakIMREAVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 427 EEAYALCARFAFRNRDARRV-----------------VGTLSGGERLRAGLAAALsgSAPPWLIILDEPT 479
Cdd:PRK11614 98 EENLAMGGFFAERDQFQERIkwvyelfprlherriqrAGTMSGGEQQMLAIGRAL--MSQPRLLLLDEPS 165
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-181 |
1.10e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.37 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 14 TPDG-PLFQKLTFAI-GTERVGLVGRNGSGKSTLLrivaglaepsSGTVRRTGTIGLLRQDMPgGW------TLAEALGV 85
Cdd:TIGR01271 1228 TEAGrAVLQDLSFSVeGGQRVGLLGRTGSGKSTLL----------SALLRLLSTEGEIQIDGV-SWnsvtlqTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 ANdlerlERILAGNGT-AGDFDAADWTLESRIGAALAQVGLPAL------PLDRCLR----TLSGGERTRVGIARLVMEA 154
Cdd:TIGR01271 1297 IP-----QKVFIFSGTfRKNLDPYEQWSDEEIWKVAEEVGLKSVieqfpdKLDFVLVdggyVLSNGHKQLMCLARSILSK 1371
|
170 180
....*....|....*....|....*..
gi 518843096 155 PDLLLLDEPTNNLDAAGRAAIRALMRE 181
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
366-507 |
1.14e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 366 GANGAGKTTLLR-IAAGLRAPVSG-----------------------------TVRRAEGRIV------------LLDQQ 403
Cdd:COG0419 30 GPNGAGKSTILEaIRYALYGKARSrsklrsdlinvgseeasvelefehggkryRIERRQGEFAefleakpserkeALKRL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 404 VGLldpegTILDNIRRLHPDAGDEEAYALCARFAFRNRDARRV--------VGTLSGGERLRAGLAAALSgsappwlIIL 475
Cdd:COG0419 110 LGL-----EIYEELKERLKELEEALESALEELAELQKLKQEILaqlsgldpIETLSGGERLRLALADLLS-------LIL 177
|
170 180 190
....*....|....*....|....*....|..
gi 518843096 476 DepTNHLDIESVEILENALLSfdgaLLVVSHD 507
Cdd:COG0419 178 D--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-208 |
1.29e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVrrtgtigllrqdmpggwtlaealgVANDLERLERILAgngtagdfdaad 109
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGV------------------------IYIDGEDILEEVL------------ 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 110 wtlesrigaalaqVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRGG---- 185
Cdd:smart00382 47 -------------DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLllks 113
|
170 180 190
....*....|....*....|....*....|....
gi 518843096 186 -----VLVASHDRELLDD------VDRILELTAI 208
Cdd:smart00382 114 eknltVILTTNDEKDLGPallrrrFDRRIVLLLI 147
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
442-514 |
1.39e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 442 DARRVVGTLSGGERLRAGLAAAL--------SGSAPPWLIILDEPTNHLDIES----VEILEnALLSFDGALLVVSHDPS 509
Cdd:TIGR00618 943 GSVRPSATLSGGETFLASLSLALaladllstSGGTVLDSLFIDEGFGSLDEDSldraIGILD-AIREGSKMIGIISHVPE 1021
|
....*
gi 518843096 510 FVERV 514
Cdd:TIGR00618 1022 FRERI 1026
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-291 |
1.39e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 22 KLTFAIGTervglvgrNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQDmpgGWTLaEALGVAN----DLERLERIla 97
Cdd:PTZ00243 687 KLTVVLGA--------TGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ---AWIM-NATVRGNilffDEEDAARL-- 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 98 gngtagdfdaADWTLESRIGAALAQVGlpalpldRCLRT--------LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:PTZ00243 753 ----------ADAVRVSQLEADLAQLG-------GGLETeigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 170 -AGRAAIRALMR-EWRGGVLV-ASHDRELLDDVDRILELtAIGARSFGGGWSAFSA-----------ARDEDRRRASAEL 235
Cdd:PTZ00243 816 hVGERVVEECFLgALAGKTRVlATHQVHVVPRADYVVAL-GDGRVEFSGSSADFMRtslyatlaaelKENKDSKEGDADA 894
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 236 ERADADVRAVRQAVQARREAKERRDRAGRAFAAKGSEPKILLgARAERAqnSGGTA 291
Cdd:PTZ00243 895 EVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALDAAAGRLM-TREEKA--SGSVP 947
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
112-215 |
1.45e-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: 46.48 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 112 LESRIG-----AALAQVGLPALPLDRCLRTLSGGERTRVGIAR-LVMEAPDLL-LLDEPTNNLDAAGRAAIRALMREWR- 183
Cdd:cd03270 108 LFARVGirerlGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATqIGSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRLRd 187
|
90 100 110
....*....|....*....|....*....|....
gi 518843096 184 --GGVLVASHDRELLDDVDRILELtAIGARSFGG 215
Cdd:cd03270 188 lgNTVLVVEHDEDTIRAADHVIDI-GPGAGVHGG 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
450-513 |
1.70e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 47.32 E-value: 1.70e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 450 LSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENAL--LSFDGALLVVSHDPSFVER 513
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSP--ILILDEATSALDTESERAIQAALdeLQKNRTSLVIAHRLSTIEK 544
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-199 |
1.95e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 33 GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------------IGLLRQDMpggwTLAEALGVAndlerlERILAG 98
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevtfngpkssqeagIGIIHQEL----NLIPQLTIA------ENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 99 NGTAGDFDAADWT-LESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRA 177
Cdd:PRK10762 104 REFVNRFGRIDWKkMYAEADKLLARLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFR 182
|
170 180 190
....*....|....*....|....*....|
gi 518843096 178 LMREWRG---GVLVASHdR-----ELLDDV 199
Cdd:PRK10762 183 VIRELKSqgrGIVYISH-RlkeifEICDDV 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
334-490 |
2.12e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 334 VLAMEGVVAEAGD-RRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAG-----------------LRApvsGTVRRAEG 395
Cdd:PRK13549 5 LLEMKNITKTFGGvKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifegeeLQA---SNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 396 R-IVLLDQQVGLLdPEGTILDNI---------RRLHPDAGDEEAYALCARFAFrNRDARRVVGTLSGGERLRAGLAAALS 465
Cdd:PRK13549 82 AgIAIIHQELALV-KELSVLENIflgneitpgGIMDYDAMYLRAQKLLAQLKL-DINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180
....*....|....*....|....*
gi 518843096 466 GSAPpwLIILDEPTNHLDIESVEIL 490
Cdd:PRK13549 160 KQAR--LLILDEPTASLTESETAVL 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
130-203 |
2.51e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 130 LDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMR---EWRGGVLVASHDrelLDDV----DRI 202
Cdd:PRK15439 397 AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRsiaAQNVAVLFISSD---LEEIeqmaDRV 473
|
.
gi 518843096 203 L 203
Cdd:PRK15439 474 L 474
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-205 |
2.57e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 119 ALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEA---PDLLLLDEPTNNLDAAG-RAAIRALMREWRGG--VLVASHD 192
Cdd:PRK00635 792 ALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGhtVVIIEHN 871
|
90
....*....|...
gi 518843096 193 RELLDDVDRILEL 205
Cdd:PRK00635 872 MHVVKVADYVLEL 884
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
137-207 |
2.75e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.80 E-value: 2.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 137 LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWR----GGVLVASHDrelLDDVDRILELTA 207
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN---LHQVSRLSDFTA 222
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
359-509 |
2.80e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 359 PERIA-LKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRI--------VLLDQQVGlLDPEGTILDNIR---RLHPDAgd 426
Cdd:PRK13541 25 PSAITyIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniakpycTYIGHNLG-LKLEMTVFENLKfwsEIYNSA-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 427 EEAYALCARFAFRNRDARRVVgTLSGGERLRAGLAAALSGSAPPWLiiLDEPTNHLDIESVEILENALL---SFDGALLV 503
Cdd:PRK13541 102 ETLYAAIHYFKLHDLLDEKCY-SLSSGMQKIVAIARLIACQSDLWL--LDEVETNLSKENRDLLNNLIVmkaNSGGIVLL 178
|
....*.
gi 518843096 504 VSHDPS 509
Cdd:PRK13541 179 SSHLES 184
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
445-507 |
2.93e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518843096 445 RVVGTLSGGERLRAGLA--AALS----GSAPpwLIILDEPTNHLDIES----VEILENALLSFDgALLVVSHD 507
Cdd:PRK03918 784 RPLTFLSGGERIALGLAfrLALSlylaGNIP--LLILDEPTPFLDEERrrklVDIMERYLRKIP-QVIIVSHD 853
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-170 |
2.97e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.58 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPS---SGTVRRTGTI----------GLLRQD--MPGGWTLAEALGVANDL----- 89
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPidakemraisAYVQQDdlFIPTLTVREHLMFQAHLrmprr 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ----ERLERILAGNGTAGDFDAADwtleSRIGAAlaqvglpalplDRcLRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:TIGR00955 132 vtkkEKRERVDEVLQALGLRKCAN----TRIGVP-----------GR-VKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
....*
gi 518843096 166 NLDAA 170
Cdd:TIGR00955 196 GLDSF 200
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
359-511 |
3.44e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 359 PERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGrivlldqqvglldpegtildnirrlhpdagdeEAYALCARFAF 438
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG--------------------------------EDILEEVLDQL 49
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518843096 439 RNRDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSFDGALLVVSHDPSFV 511
Cdd:smart00382 50 LLIIVGGKKASGSGELRLRLALALARKLKPD--VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
138-192 |
3.46e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.87 E-value: 3.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 518843096 138 SGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALM----REWRGGVLVASHD 192
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTAIIMITHD 221
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
137-202 |
3.55e-05 |
|
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: 44.49 E-value: 3.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518843096 137 LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGR----AAIRALMREWRGGVLVASHDRELLDDV-DRI 202
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEEGKKTALVVEHDLAVLDYLsDRI 142
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
363-479 |
3.59e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.17 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPvsgtvrrAEGRIVLLDQQVGLLDPE-----G--------------TILDNI------ 417
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQP-------DSGEILIDGKPVRIRSPRdaialGigmvhqhfmlvpnlTVAENIvlglep 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 418 ---RRLHPDAGDEEAYALCARFAFrNRDARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPT 479
Cdd:COG3845 108 tkgGRLDRKAARARIRELSERYGL-DVDPDAKVEDLSVGEQQRVEILKALYRGAR--ILILDEPT 169
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
34-206 |
4.17e-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: 43.89 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLR-IVAGLAEPSSGTVRRTGTigllrqdmpggwtlAEALGVAndLERLERILagngtagdfdaadwtl 112
Cdd:cd03227 26 ITGPNGSGKSTILDaIGLALGGAQSATRRRSGV--------------KAGCIVA--AVSAELIF---------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 113 eSRIGaalaqvglpalpldrclrtLSGGERTRVGIA-----RLVMEAPdLLLLDEPTNNLDAAGRAAIRALMREWRGG-- 185
Cdd:cd03227 74 -TRLQ-------------------LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKga 132
|
170 180
....*....|....*....|..
gi 518843096 186 -VLVASHDRELLDDVDRILELT 206
Cdd:cd03227 133 qVIVITHLPELAELADKLIHIK 154
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-215 |
4.33e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 120 LAQVGLPALPLDRCLRTLSGGERTRVGIA-----RLVMEapdLLLLDEPTNNL---DaaGRAAIRALMREWRGG--VLVA 189
Cdd:TIGR00630 472 LIDVGLDYLSLSRAAGTLSGGEAQRIRLAtqigsGLTGV---LYVLDEPSIGLhqrD--NRRLINTLKRLRDLGntLIVV 546
|
90 100
....*....|....*....|....*.
gi 518843096 190 SHDRELLDDVDRILELTAiGARSFGG 215
Cdd:TIGR00630 547 EHDEDTIRAADYVIDIGP-GAGEHGG 571
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
344-490 |
4.68e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.16 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 344 AGDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV-----------RRAEGRIV-LLDQQvgLLDPEG 411
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEIlldaqpleswsSKAFARKVaYLPQQ--LPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 412 TildNIRRL-----HPDAGD------------EEAYALCARFAFrnrdARRVVGTLSGGERLRAGLAAALSGSAPpwLII 474
Cdd:PRK10575 100 M---TVRELvaigrYPWHGAlgrfgaadrekvEEAISLVGLKPL----AHRLVDSLSGGERQRAWIAMLVAQDSR--CLL 170
|
170
....*....|....*..
gi 518843096 475 LDEPTNHLDI-ESVEIL 490
Cdd:PRK10575 171 LDEPTSALDIaHQVDVL 187
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
353-519 |
4.87e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 45.47 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLrapvsgtVRRAEGRIV-----LLDQQ------------------VGLLDP 409
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGL-------VKATDGEVAwlgkdLLGMKddewravrsdiqmifqdpLASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 410 EGTILDNI----RRLHPDAGDEE----AYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSgsAPPWLIILDEPTNH 481
Cdd:PRK15079 114 RMTIGEIIaeplRTYHPKLSRQEvkdrVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALI--LEPKLIICDEPVSA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 518843096 482 LDI----ESVEILENALLSFDGALLVVSHDPSFVERVGfDRV 519
Cdd:PRK15079 192 LDVsiqaQVVNLLQQLQREMGLSLIFIAHDLAVVKHIS-DRV 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-61 |
4.95e-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: 45.94 E-value: 4.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 5 LTLDSVC---ARTPDGPLFQ----KLTFAIGtERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR 61
Cdd:COG4615 328 LELRGVTyryPGEDGDEGFTlgpiDLTIRRG-ELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL 390
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-169 |
6.99e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 6.99e-05
10 20 30
....*....|....*....|....*....|....*
gi 518843096 135 RTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
363-506 |
7.00e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.29 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTVrRAEGR--------------IVLLDQQVGLLdPEGTILDNIRRLHpdagdee 428
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSI-LIDGQemrfasttaalaagVAIIYQELHLV-PEMTVAENLYLGQ------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 429 ayaLCARFAFRNR------------------DARRVVGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLDIESVEIL 490
Cdd:PRK11288 105 ---LPHKGGIVNRrllnyeareqlehlgvdiDPDTPLKYLSIGQRQMVEIAKALARNAR--VIAFDEPTSSLSAREIEQL 179
|
170
....*....|....*....
gi 518843096 491 E---NALLSFDGALLVVSH 506
Cdd:PRK11288 180 FrviRELRAEGRVILYVSH 198
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
120-514 |
8.07e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 45.23 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 120 LAQVGLPALP--LDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA----IRALMREWRGGVLVASHDR 193
Cdd:PRK10261 150 LDQVRIPEAQtiLSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQilqlIKVLQKEMSMGVIFITHDM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 194 ELLDDV-DRILELTAIGARSFGGGWSAFSAARDEDRRRASAELERadadVRAVRQAVQARREAKERRDRAGRafaakgSE 272
Cdd:PRK10261 230 GVVAEIaDRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAVPQ----LGAMKGLDYPRRFPLISLEHPAK------QE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 273 PKILLGARAEraqnsggtaqaisdrrmGRALAEADDARSRVevltPLTialppSGLpsgANVLAMEGVVAEAGDRRLGPw 352
Cdd:PRK10261 300 PPIEQDTVVD-----------------GEPILQVRNLVTRF----PLR-----SGL---LNRVTREVHAVEKVSFDLWP- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 tlridgPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLL----------DQQV------GLLDPEGTILDN 416
Cdd:PRK10261 350 ------GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgklqalrrDIQFifqdpyASLDPRQTVGDS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 417 I-------RRLHPDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEI 489
Cdd:PRK10261 424 ImeplrvhGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALN--PKVIIADEAVSALDVSIRGQ 501
|
410 420
....*....|....*....|....*....
gi 518843096 490 LENALL----SFDGALLVVSHDPSFVERV 514
Cdd:PRK10261 502 IINLLLdlqrDFGIAYLFISHDMAVVERI 530
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
32-69 |
8.12e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 8.12e-05
10 20 30
....*....|....*....|....*....|....*...
gi 518843096 32 VGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLL 69
Cdd:PRK13546 53 IGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI 90
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
448-515 |
8.49e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 448 GTLSGGER------LRAGLAAALSGSAPpwLIILDEPTNHLDIESVEILENALLSF--------DGALLVVSHDPSFVER 513
Cdd:TIGR00606 1198 GRCSAGQKvlasliIRLALAETFCLNCG--IIALDEPTTNLDRENIESLAHALVEIiksrsqqrNFQLLVITHDEDFVEL 1275
|
..
gi 518843096 514 VG 515
Cdd:TIGR00606 1276 LG 1277
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-208 |
8.50e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 45.02 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLRQDMPGGWTLAEALGVANDLERLERILAGNGTAGDFDAADWTL 112
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 113 ESRIGAAL---AQVGLP----ALPLDrclrtLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIR----ALMRE 181
Cdd:PRK10070 139 EERREKALdalRQVGLEnyahSYPDE-----LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdelvKLQAK 213
|
170 180
....*....|....*....|....*..
gi 518843096 182 WRGGVLVASHDrelLDDVDRILELTAI 208
Cdd:PRK10070 214 HQRTIVFISHD---LDEAMRIGDRIAI 237
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-205 |
1.08e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 119 ALAQVGLPALPLDRCLRTLSGGERTRVGIAR---LVMEAPDLLLLDEPTNNLDAAGRAAIRALMREWRG---GVLVASHD 192
Cdd:PRK00635 1682 ALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKflyLPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSlghSVIYIDHD 1761
|
90
....*....|...
gi 518843096 193 RELLDDVDRILEL 205
Cdd:PRK00635 1762 PALLKQADYLIEM 1774
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
350-483 |
1.09e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 44.02 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 350 GPWTlridgperiALKGANGAGKTTLLRIAAGLRAPVSGtvrrAEGRIVLLDQQVGlldpEGTILDNIRRL-----HPD- 423
Cdd:PRK13640 33 GSWT---------ALIGHNGSGKSTISKLINGLLLPDDN----PNSKITVDGITLT----AKTVWDIREKVgivfqNPDn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 424 ------AGDEEAYALCARFAFRN------RDARRVVG----------TLSGGERLRAGLAAALsgSAPPWLIILDEPTNH 481
Cdd:PRK13640 96 qfvgatVGDDVAFGLENRAVPRPemikivRDVLADVGmldyidsepaNLSGGQKQRVAIAGIL--AVEPKIIILDESTSM 173
|
..
gi 518843096 482 LD 483
Cdd:PRK13640 174 LD 175
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-203 |
1.15e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 32 VGLVGRNGSGKSTLLRIVAG-LAEPSSGTVRRTGTIGLLRQDmpgGWTLAEAL------GVANDLERLERilagngtAGD 104
Cdd:PLN03130 646 VAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGTVAYVPQV---SWIFNATVrdnilfGSPFDPERYER-------AID 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 105 FDAADWTLESRIGAALAQVGlpalplDRCLrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA-AGRAAI-RALMREW 182
Cdd:PLN03130 716 VTALQHDLDLLPGGDLTEIG------ERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFdKCIKDEL 788
|
170 180
....*....|....*....|...
gi 518843096 183 RGG--VLVaSHDRELLDDVDRIL 203
Cdd:PLN03130 789 RGKtrVLV-TNQLHFLSQVDRII 810
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
99-181 |
1.25e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.00 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 99 NGTAGDFD---------AADWtleSRIGAALAQVGLpalpldrclrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA 169
Cdd:PRK14243 118 NGYKGDMDelverslrqAALW---DEVKDKLKQSGL----------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP 184
|
90
....*....|..
gi 518843096 170 AGRAAIRALMRE 181
Cdd:PRK14243 185 ISTLRIEELMHE 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-208 |
1.33e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTV----RRTGTIG-----LLRQDM---------------PGGWTLAEALgv 85
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIifngQRIDTLSpgklqALRRDIqfifqdpyasldprqTVGDSIMEPL-- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 86 andleRLERILAGNGTAgdfdaadwtleSRIGAALAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTN 165
Cdd:PRK10261 429 -----RVHGLLPGKAAA-----------ARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 518843096 166 NLDAAGRAAIRALM----REWRGGVLVASHDRELlddVDRILELTAI 208
Cdd:PRK10261 493 ALDVSIRGQIINLLldlqRDFGIAYLFISHDMAV---VERISHRVAV 536
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-168 |
1.35e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 16 DGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT--------------IGLLRQDmPGGWT-- 78
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTyAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskIGVVSQD-PLLFSns 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 79 ----LAEALGVANDLERLERILAGNGT----------------AGDFDAADWTLESR--------------------IGA 118
Cdd:PTZ00265 476 iknnIKYSLYSLKDLEALSNYYNEDGNdsqenknkrnscrakcAGDLNDMSNTTDSNeliemrknyqtikdsevvdvSKK 555
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 119 ALAQVGLPALP------LDRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLD 168
Cdd:PTZ00265 556 VLIHDFVSALPdkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
119-205 |
1.39e-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: 43.76 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 119 ALAQVGLPALPLDRCLRTLSGGERTRVGIAR-LVMEAP--DLLLLDEPTNNLDAAG-RAAIRALMREWRGG--VLVASHD 192
Cdd:cd03271 152 TLCDVGLGYIKLGQPATTLSGGEAQRIKLAKeLSKRSTgkTLYILDEPTTGLHFHDvKKLLEVLQRLVDKGntVVVIEHN 231
|
90
....*....|...
gi 518843096 193 RELLDDVDRILEL 205
Cdd:cd03271 232 LDVIKCADWIIDL 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
116-203 |
1.54e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.43 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 116 IGAALAQVGL----PALPLDRclrtLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALM----REWRGGVL 187
Cdd:TIGR02633 383 IGSAIQRLKVktasPFLPIGR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInqlaQEGVAIIV 458
|
90
....*....|....*.
gi 518843096 188 VASHDRELLDDVDRIL 203
Cdd:TIGR02633 459 VSSELAEVLGLSDRVL 474
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-483 |
1.78e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.15 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 366 GANGAGKTTLLRIaaglrapVSGTVRRAEGRIVLLDQQVGLL--------------DP------EGTILDNI-------- 417
Cdd:COG1101 39 GSNGAGKSTLLNA-------IAGSLPPDSGSILIDGKDVTKLpeykrakyigrvfqDPmmgtapSMTIEENLalayrrgk 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 418 -RRLHP--DAGDEEAY-ALCARFA--FRNR-DARrvVGTLSGGER----LragLAAALSgsaPPWLIILDEPTNHLD 483
Cdd:COG1101 112 rRGLRRglTKKRRELFrELLATLGlgLENRlDTK--VGLLSGGQRqalsL---LMATLT---KPKLLLLDEHTAALD 180
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
354-483 |
1.85e-04 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 43.78 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 354 LRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSgtvrraeGRIVLLDQQVGLLDPEG----------------TILDNI 417
Cdd:PRK09452 35 LTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDS-------GRIMLDGQDITHVPAENrhvntvfqsyalfphmTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 rrlhpdagdeeAYAL------CARFAFRNRDARRVV----------GTLSGGERLRAGLAAALSGSapPWLIILDEPTNH 481
Cdd:PRK09452 108 -----------AFGLrmqktpAAEITPRVMEALRMVqleefaqrkpHQLSGGQQQRVAIARAVVNK--PKVLLLDESLSA 174
|
..
gi 518843096 482 LD 483
Cdd:PRK09452 175 LD 176
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
357-483 |
2.45e-04 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 43.52 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 357 DGpERIALKGANGAGKTTLLRIAAGLRAPVSGTVrRAEGRIVL-LD----------QQVGLLdPEGTILDNIrrlhpdag 425
Cdd:COG3839 28 DG-EFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI-LIGGRDVTdLPpkdrniamvfQSYALY-PHMTVYENI-------- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 426 deeAYAL-CARFAFRNRDAR---------------RVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLD 483
Cdd:COG3839 97 ---AFPLkLRKVPKAEIDRRvreaaellgledlldRKPKQLSGGQRQRVALGRAL--VREPKVFLLDEPLSNLD 165
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
34-192 |
2.71e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLR-IVAGLAEPSSGT------------------------------VRRTGTIGLLRQDMPGgwTLAEA 82
Cdd:COG0419 28 IVGPNGAGKSTILEaIRYALYGKARSRsklrsdlinvgseeasvelefehggkryriERRQGEFAEFLEAKPS--ERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 83 LGVANDLERLERIlagngtAGDFDAADWTLESRIGAALAQVGLPALPLDRC-----LRTLSGGERTRVGIARLVMeapdl 157
Cdd:COG0419 106 LKRLLGLEIYEEL------KERLKELEEALESALEELAELQKLKQEILAQLsgldpIETLSGGERLRLALADLLS----- 174
|
170 180 190
....*....|....*....|....*....|....*
gi 518843096 158 LLLDepTNNLDAAGRAAIRALMREwrggVLVASHD 192
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
366-491 |
2.84e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.14 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 366 GANGAGKTTLLRIAAGLRAPVSGTV---------------RRAEGRIVLLDQQVGLLDpEGTILDNIrrlhpdagdeeAY 430
Cdd:COG1135 38 GYSGAGKSTLIRCINLLERPTSGSVlvdgvdltalserelRAARRKIGMIFQHFNLLS-SRTVAENV-----------AL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518843096 431 AL-CARFAFRNRDAR-----RVVG----------TLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIES-VEILE 491
Cdd:COG1135 106 PLeIAGVPKAEIRKRvaellELVGlsdkadaypsQLSGGQKQRVGIARALANN--PKVLLCDEATSALDPETtRSILD 181
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
366-483 |
2.97e-04 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 42.63 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 366 GANGAGKTTLLRIAAGLRAPVSGTV------------------RRAegRIVLLDQQVGLLdPEGTILDNIrrlhpdagde 427
Cdd:cd03294 57 GLSGSGKSTLLRCINRLIEPTSGKVlidgqdiaamsrkelrelRRK--KISMVFQSFALL-PHRTVLENV---------- 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 428 eAYALCAR---FAFRNRDARRVV-------------GTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLD 483
Cdd:cd03294 124 -AFGLEVQgvpRAEREERAAEALelvglegwehkypDELSGGMQQRVGLARAL--AVDPDILLMDEAFSALD 192
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
30-181 |
3.94e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKStllriVAGLAepssgtvrrtgTIGLLrqDMPGGwTLAEALGV-ANDLERLE----RILAGNGTAGD 104
Cdd:PRK11022 34 EVVGIVGESGSGKS-----VSSLA-----------IMGLI--DYPGR-VMAEKLEFnGQDLQRISekerRNLVGAEVAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 105 FDAA------DWTLESRIGAA-------------------LAQVGLP--ALPLDRCLRTLSGGERTRVGIARLVMEAPDL 157
Cdd:PRK11022 95 FQDPmtslnpCYTVGFQIMEAikvhqggnkktrrqraidlLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180
....*....|....*....|....
gi 518843096 158 LLLDEPTNNLDAAGRAAIRALMRE 181
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLE 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-206 |
3.95e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 22 KLTFAIGTeRVGLVGRNGSGKSTLLRIVAG---LAEPSSGTVRrtGTIGLLRQDmpgGW----TLAEALGVANDLERlER 94
Cdd:PLN03232 637 NLEIPVGS-LVAIVGGTGEGKTSLISAMLGelsHAETSSVVIR--GSVAYVPQV---SWifnaTVRENILFGSDFES-ER 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 95 IlagnGTAGDFDAADWTLESRIGAALAQVGLPALpldrclrTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDA-AGRA 173
Cdd:PLN03232 710 Y----WRAIDVTALQHDLDLLPGRDLTEIGERGV-------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQ 778
|
170 180 190
....*....|....*....|....*....|....*.
gi 518843096 174 AIRALMREWRGG---VLVaSHDRELLDDVDRILELT 206
Cdd:PLN03232 779 VFDSCMKDELKGktrVLV-TNQLHFLPLMDRIILVS 813
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
364-513 |
4.28e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.78 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 364 LKGANGAGKTTLLRIAAGLRAPVSGTV--------RRAEGRIVLLDQQVGL------LDPEGTILDN------------- 416
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIwfsghditRLKNREVPFLRRQIGMifqdhhLLMDRTVYDNvaipliiagasgd 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 417 -IRRLHPDAGDEEAYAlcarfafrnRDARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENALL 495
Cdd:PRK10908 113 dIRRRVSAALDKVGLL---------DKAKNFPIQLSGGEQQRVGIARAVVNK--PAVLLADEPTGNLDDALSEGILRLFE 181
|
170 180
....*....|....*....|.
gi 518843096 496 SFDG---ALLVVSHDPSFVER 513
Cdd:PRK10908 182 EFNRvgvTVLMATHDIGLISR 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
363-417 |
5.22e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.73 E-value: 5.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLD----QQVG--------LLDPEGTILDNI 417
Cdd:PRK15439 41 ALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakaHQLGiylvpqepLLFPNLSVKENI 107
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
31-189 |
6.18e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 31 RVGLVGRNGSGKSTLLRIVAGlaepssgtVRR--TGTIGLLRQD----------------MPGGW--TLAEALGVANDLE 90
Cdd:NF033858 29 MVGLIGPDGVGKSSLLSLIAG--------ARKiqQGRVEVLGGDmadarhrravcpriayMPQGLgkNLYPTLSVFENLD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 91 ---RL------ERilagngtagdfdaadwtlESRIGAALAQVGLPALPlDRCLRTLSGGERTRVGIARLVMEAPDLLLLD 161
Cdd:NF033858 101 ffgRLfgqdaaER------------------RRRIDELLRATGLAPFA-DRPAGKLSGGMKQKLGLCCALIHDPDLLILD 161
|
170 180 190
....*....|....*....|....*....|...
gi 518843096 162 EPTNNLDAAGRAAIRAL---MREWRGG--VLVA 189
Cdd:NF033858 162 EPTTGVDPLSRRQFWELidrIRAERPGmsVLVA 194
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
353-483 |
6.73e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 41.65 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIV---------LLDQQVGLL--DPEG-----TILDN 416
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdikQIRKKVGLVfqFPESqlfeeTVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 417 IRRLHPDAG--DEEAYALCarfafrnRDARRVVGT-----------LSGGERLRAGLAAALsgSAPPWLIILDEPTNHLD 483
Cdd:PRK13649 107 VAFGPQNFGvsQEEAEALA-------REKLALVGIseslfeknpfeLSGGQMRRVAIAGIL--AMEPKILVLDEPTAGLD 177
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
33-205 |
6.91e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.39 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 33 GLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGT-IGLLRQDmpggwTLAEALGVANDLERL-ERILAGNGTAGDFDAADW 110
Cdd:PRK10789 345 GICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpLTKLQLD-----SWRSRLAVVSQTPFLfSDTVANNIALGRPDATQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 111 TLESriGAALAQVGLPALPLDRCLRT--------LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREW 182
Cdd:PRK10789 420 EIEH--VARLASVHDDILRLPQGYDTevgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW 497
|
170 180
....*....|....*....|....*
gi 518843096 183 RGG--VLVASHDRELLDDVDRILEL 205
Cdd:PRK10789 498 GEGrtVIISAHRLSALTEASEILVM 522
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-194 |
6.94e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGlAEPSS--------GTVRRTG-TIgllrqdmpggWTLAEALG-VANDLERLERIlagNGTA- 102
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSGeTI----------WDIKKHIGyVSSSLHLDYRV---STSVr 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 103 -----GDFD---------------AADWtlesrigaaLAQVGLPALPLDRCLRTLSGGERTRVGIARLVMEAPDLLLLDE 162
Cdd:PRK10938 357 nvilsGFFDsigiyqavsdrqqklAQQW---------LDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDE 427
|
170 180 190
....*....|....*....|....*....|....*.
gi 518843096 163 PTNNLDAAGRAAIR----ALMREWRGGVLVASHDRE 194
Cdd:PRK10938 428 PLQGLDPLNRQLVRrfvdVLISEGETQLLFVSHHAE 463
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
126-203 |
7.22e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 126 PALPLDRclrtLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALM----REWRGGVLVASHDRELLDDVDR 201
Cdd:PRK13549 399 PELAIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLInqlvQQGVAIIVISSELPEVLGLSDR 474
|
..
gi 518843096 202 IL 203
Cdd:PRK13549 475 VL 476
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
363-514 |
8.46e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.37 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLR-----IAAGLRAPVSGTVRRAEGRIVLLD-------QQVGLLD------PEGTILDNIR---RLH 421
Cdd:PRK14267 34 ALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDvdpievrREVGMVFqypnpfPHLTIYDNVAigvKLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 422 PDAGDEEAYALCARFAFRNRDARRVV--------GTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESVEILENA 493
Cdd:PRK14267 114 GLVKSKKELDERVEWALKKAALWDEVkdrlndypSNLSGGQRQRLVIARAL--AMKPKILLMDEPTANIDPVGTAKIEEL 191
|
170 180
....*....|....*....|...
gi 518843096 494 LLSF--DGALLVVSHDPSFVERV 514
Cdd:PRK14267 192 LFELkkEYTIVLVTHSPAQAARV 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
363-513 |
1.01e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 41.30 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRAPVSGTV---------RRAEGRIVLLDQQVGLL--DPEGTIL-DNIRR----------L 420
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTTGTVtvdditithKTKDKYIRPVRKRIGMVfqFPESQLFeDTVEReiifgpknfkM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 421 HPDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIES----VEILENALLS 496
Cdd:PRK13646 117 NLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMN--PDIIVLDEPTAGLDPQSkrqvMRLLKSLQTD 194
|
170
....*....|....*..
gi 518843096 497 FDGALLVVSHDPSFVER 513
Cdd:PRK13646 195 ENKTIILVSHDMNEVAR 211
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
364-483 |
1.06e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 41.15 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 364 LKGANGAGKTTLLRIAAGLRAPVSGTV-------RRAEGRIVLLDQQVGLL--DPEGTIldnirrLHPDAGDEEAYALCA 434
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkplDYSKRGLLALRQQVATVfqDPEQQI------FYTDIDSDIAFSLRN 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518843096 435 RFAFRNRDARRV----------------VGTLSGGERLRAGLAAALSGSAPpwLIILDEPTNHLD 483
Cdd:PRK13638 106 LGVPEAEITRRVdealtlvdaqhfrhqpIQCLSHGQKKRVAIAGALVLQAR--YLLLDEPTAGLD 168
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
222-468 |
1.11e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 222 AARDEDRRRASAELERADADVRAVRQAVQARREAKERRDRAGRAFAAKGSEPKILLGARAERAQNSGGTAQAISDRRMGR 301
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 302 ALAEADDARSR----VEVLTPLTIALPPSGLPSGANVLAMEGVVAEAGDRRLGPWTLRI------DGPERIALKGANGAG 371
Cdd:COG1196 493 LLLLLEAEADYegflEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvveddeVAAAAIEYLKAAKAG 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 372 KTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQVGLLDPEGTILDNIRRLHPDAGDEEAYALCARFAFRNRDARRVVGTLS 451
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
250
....*....|....*..
gi 518843096 452 GGERLRAGLAAALSGSA 468
Cdd:COG1196 653 GEGGSAGGSLTGGSRRE 669
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
316-391 |
1.16e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518843096 316 LTPLTIALPPSGLPSGANVLAMEGVVAEAGDRR--LGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVR 391
Cdd:PRK10522 304 LAPYKAEFPRPQAFPDWQTLELRNVTFAYQDNGfsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL 381
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
335-512 |
1.20e-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: 41.22 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 335 LAMEGVVAEAGDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQVGLLDPEGTIL 414
Cdd:pfam13304 126 ERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 415 DNIRRLHPDAGDEEAYalcaRFAFRNRDARRVVGTLSGGE-RLRAGLAAALSGSAPPWLIILDEPTNHLDIESVE-ILE- 491
Cdd:pfam13304 206 IEKSLLVDDRLRERGL----ILLENGGGGELPAFELSDGTkRLLALLAALLSALPKGGLLLIDEPESGLHPKLLRrLLEl 281
|
170 180
....*....|....*....|..
gi 518843096 492 -NALLSFDGALLVVSHDPSFVE 512
Cdd:pfam13304 282 lKELSRNGAQLILTTHSPLLLD 303
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-199 |
1.44e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.45 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 14 TPDGPLFQKLTFAIGTERV-GLVGRNGSGKSTLLRIVAGLAEPSsgtVRRTGtiGLLRQDmpGGWTLAEAL---GVANDL 89
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVlALVGGSGSGKSLTCAAALGILPAG---VRQTA--GRVLLD--GKPVAPCALrgrKIATIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 90 ER---------------LERILAGNGTAGDfdaadwtleSRIGAALAQVGL--PALPLDRCLRTLSGGERTRVGIARLVM 152
Cdd:PRK10418 86 QNprsafnplhtmhthaRETCLALGKPADD---------ATLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518843096 153 -EAPdLLLLDEPTNNLDAAGRAAI----RALMREWRGGVLVASHD----RELLDDV 199
Cdd:PRK10418 157 cEAP-FIIADEPTTDLDVVAQARIldllESIVQKRALGMLLVTHDmgvvARLADDV 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-207 |
1.67e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 18 PLFQKLTFAI-GTERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVR----RTGTIGLlrqdmpggWTLAEALGVANDLERL 92
Cdd:PLN03130 1253 PVLHGLSFEIsPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILidgcDISKFGL--------MDLRKVLGIIPQAPVL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 93 erilaGNGTA-------GDFDAAD-WtlESRIGAALAQV------GLPAlpldrclRTLSGGERTRVG------IARLVM 152
Cdd:PLN03130 1325 -----FSGTVrfnldpfNEHNDADlW--ESLERAHLKDVirrnslGLDA-------EVSEAGENFSVGqrqllsLARALL 1390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518843096 153 EAPDLLLLDEPTNNLDAAGRAAIRALMR-EWRG-GVLVASHDRELLDDVDRILELTA 207
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIReEFKScTMLIIAHRLNTIIDCDRILVLDA 1447
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
360-507 |
1.79e-03 |
|
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: 39.48 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 360 ERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVLLDQQVglldpegtildnirrlhpdagdeeayalcarfafr 439
Cdd:cd03222 26 EVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI----------------------------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518843096 440 nrdarrvvgTLSGGERLRAGLAAALSGSAPPWLIilDEPTNHLDIESVEILENALLSF----DGALLVVSHD 507
Cdd:cd03222 71 ---------DLSGGELQRVAIAAALLRNATFYLF--DEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHD 131
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
376-519 |
2.15e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 40.82 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 376 LRIAAGLRApvsgtvRRAEGRIVLLDQQVGLLDPEgtildniRRLhpdagdeeayalcARFAFRnrdarrvvgtLSGGER 455
Cdd:COG4172 119 LRLHRGLSG------AAARARALELLERVGIPDPE-------RRL-------------DAYPHQ----------LSGGQR 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518843096 456 LRAGLAAALSGSapPWLIILDEPTNHLDIeSV--EILEnaLL-----SFDGALLVVSHDPSFVERVGfDRV 519
Cdd:COG4172 163 QRVMIAMALANE--PDLLIADEPTTALDV-TVqaQILD--LLkdlqrELGMALLLITHDLGVVRRFA-DRV 227
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
34-168 |
2.73e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.77 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 34 LVGRNGSGKSTLLRIVAGLA--EPSSGTVRRTGT--IGLLRQDMPG-GWTLA-----EALGVAN---------------D 88
Cdd:PRK09580 32 IMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKdlLELSPEDRAGeGIFMAfqypvEIPGVSNqfflqtalnavrsyrG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 89 LERLERilagngtagdFDAADWtLESRIgaalAQVGLPALPLDRCLRT-LSGGERTRVGIARLVMEAPDLLLLDEPTNNL 167
Cdd:PRK09580 112 QEPLDR----------FDFQDL-MEEKI----ALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGL 176
|
.
gi 518843096 168 D 168
Cdd:PRK09580 177 D 177
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
353-506 |
2.82e-03 |
|
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: 39.32 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLlrIAAGLRApvsgtVRRAEGRIVLLDQQVGLL--------------DP---EGTILD 415
Cdd:cd03369 28 SFKVKAGEKIGIVGRTGAGKSTL--ILALFRF-----LEAEEGKIEIDGIDISTIpledlrssltiipqDPtlfSGTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 416 NIRRLHpDAGDEEAYAlcarfafrnrdARRVVG---TLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIES-VEILE 491
Cdd:cd03369 101 NLDPFD-EYSDEEIYG-----------ALRVSEgglNLSQGQRQLLCLARALLKR--PRVLVLDEATASIDYATdALIQK 166
|
170
....*....|....*.
gi 518843096 492 NALLSFDGA-LLVVSH 506
Cdd:cd03369 167 TIREEFTNStILTIAH 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-203 |
3.01e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 40.28 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 30 ERVGLVGRNGSGKSTLLRIVAGLAEPSSGTVRRTGTIGLLRQdmPGGwtlAEALGVANDLE--RLERILAGNGTA----- 102
Cdd:PRK11288 280 EIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRS--PRD---AIRAGIMLCPEdrKAEGIIPVHSVAdnini 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 103 ---GDFDAADWTLESRIGAALAQVGLPALPL-----DRCLRTLSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAA 174
Cdd:PRK11288 355 sarRHHLRAGCLINNRWEAENADRFIRSLNIktpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHE 434
|
170 180 190
....*....|....*....|....*....|...
gi 518843096 175 IRALMREW--RG-GVLVASHD-RELLDDVDRIL 203
Cdd:PRK11288 435 IYNVIYELaaQGvAVLFVSSDlPEVLGVADRIV 467
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
118-192 |
3.03e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 39.69 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 118 AALAQVGLPALPLDRCLRT---LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGRAAIRALMREW--RGGVLVASHD 192
Cdd:PRK14271 142 ARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHN 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
450-506 |
3.05e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 39.37 E-value: 3.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 518843096 450 LSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESVEILENALLSF--DGALLVVSH 506
Cdd:PRK14239 149 LSGGQQQRVCIARVLATS--PKIILLDEPTSALDPISAGKIEETLLGLkdDYTMLLVTR 205
|
|
| T2SSE |
pfam00437 |
Type II/IV secretion system protein; This family contains components of both the Type II ... |
259-466 |
3.73e-03 |
|
Type II/IV secretion system protein; This family contains components of both the Type II protein secretion system (T2SS), including Type 4 pilus (T4P), and Type IV protein secretion system (T4SS) from Gram-negative bacteria. VirB11 ATPase is a subunit of the Agrobacterium tumefaciens transfer DNA (T-DNA) transfer system, a type IV secretion pathway required for delivery of T-DNA and effector proteins to plant cells during infection. The cytoplasmic T2S E ATPase is a Zn-containing protein thought to provide the mechanical force for the secretion process. T2S-E contains Walker A and B motifs, that are essential for secretion and ATPase activity. ATPase PulE and XcpR from Klebsiella oxytoca and Pseudomonas aeruginosa respectively are required for protein secretion via the T2SS. ATPase PilB is required for T4P extension.
Pssm-ID: 425681 [Multi-domain] Cd Length: 269 Bit Score: 39.19 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 259 RDRAGRAFAAKGSEPKILLGARAERAQNSggTAQAISDRRM---GRALAEADDARSRVEVLTPLTI--------ALPPSG 327
Cdd:pfam00437 27 RFRVDGVLREIPFPDADALARLISRIKVM--ARLDISERRPpqdGRLPLRIGGKGVRVRVSTLPTAggeklvirLLDPSN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 328 LPSGANVLAMEGVVAEAGDRRL-GPWTLridgperIALKGANGAGKTTLLRIAaglrapvSGTVRRAEGRIVLLDQQVGL 406
Cdd:pfam00437 105 VALSLDELGMTGAQDEALLEFLrQPRGN-------ILVTGPTGSGKTTTLYAA-------LGELNTRDENIVTVEDPVEI 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 407 LDPEgtilDNIRRLHPDAGDEEAYALcaRFAFRNRDARRVVGTLSGGERLRAGLAAALSG 466
Cdd:pfam00437 171 QLEG----INQVQLNARAGVTFADLL--RAILRQDPDRIMVGEIRDLETAEIALQAANTG 224
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
363-509 |
4.27e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.83 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 363 ALKGANGAGKTTLLRIAAGLRA--------PVSGTVRRAE--GRIVLLDQQVGLLDPEGTILDNI-----RRLHPDAGDE 427
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAGRKTggyiegdiRISGFPKKQEtfARISGYCEQNDIHSPQVTVRESLiysafLRLPKEVSKE 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 428 EAYALCARFA----FRN-RDArrVVGT-----LSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDIESVEILENALL-S 496
Cdd:PLN03140 990 EKMMFVDEVMelveLDNlKDA--IVGLpgvtgLSTEQRKRLTIAVEL--VANPSIIFMDEPTSGLDARAAAIVMRTVRnT 1065
|
170
....*....|....*
gi 518843096 497 FDGALLVVS--HDPS 509
Cdd:PLN03140 1066 VDTGRTVVCtiHQPS 1080
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
445-508 |
4.34e-03 |
|
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: 38.78 E-value: 4.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518843096 445 RVVGTLSGGERLRAGLAAALSGSAPPWLIILDEPT-------NHLDIESVEILENAllsfDGALLVVSHDP 508
Cdd:cd03270 133 RSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSiglhprdNDRLIETLKRLRDL----GNTVLVVEHDE 199
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
334-507 |
5.15e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 38.92 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 334 VLAMEGVV----AEAGDRRLGPWTLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTVRRAEGRIVL-----LDQQV 404
Cdd:PRK13642 4 ILEVENLVfkyeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAenvwnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 405 GLL--DPE-----GTILDNIRRLHPDAGD---------EEAYALCARFAFRNRDARRvvgtLSGGERLRAGLAAALsgSA 468
Cdd:PRK13642 84 GMVfqNPDnqfvgATVEDDVAFGMENQGIpreemikrvDEALLAVNMLDFKTREPAR----LSGGQKQRVAVAGII--AL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 518843096 469 PPWLIILDEPTNHLD----IESVEILENALLSFDGALLVVSHD 507
Cdd:PRK13642 158 RPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
449-496 |
5.17e-03 |
|
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: 38.75 E-value: 5.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 518843096 449 TLSGGERLRAGLAAALS-GSAPPWLIILDEPTNHLDIESVEILENALLS 496
Cdd:cd03271 169 TLSGGEAQRIKLAKELSkRSTGKTLYILDEPTTGLHFHDVKKLLEVLQR 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
137-202 |
7.78e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 7.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 137 LSGGERTRVGIARLVMEAPDLLLLDEPTNNLDAAGR----AAIRALMREWRGGVLVASHDRELLDDVDRI 202
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKyeiyTIINELAAEGKGVIVISSELPELLGMCDRI 474
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
362-484 |
7.86e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 38.23 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 362 IALKGANGAGKTTLLRIAAGLRAPVSGTV--------------RRAEGRIVLLDQQVGlLDPE---GTILDNIRRLH--- 421
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdysyRSQRIRMIFQDPSTS-LNPRqriSQILDFPLRLNtdl 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518843096 422 -PDAGDEEAYALCARFAFRNRDARRVVGTLSGGERLRAGLAAALsgSAPPWLIILDEPTNHLDI 484
Cdd:PRK15112 121 ePEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARAL--ILRPKVIIADEALASLDM 182
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
353-519 |
8.22e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 38.48 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 353 TLRIDGPERIALKGANGAGKTTLLRIAAGLRAPVSGTV---------------RRAEGRIVLLDQQVGLLDPEGTILDNI 417
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakisdaelREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518843096 418 RrlhpdAGDEEAYALCARFAFRNRDARRVVG----------TLSGGERLRAGLAAALSGSapPWLIILDEPTNHLDIESV 487
Cdd:PRK10070 128 A-----FGMELAGINAEERREKALDALRQVGlenyahsypdELSGGMRQRVGLARALAIN--PDILLMDEAFSALDPLIR 200
|
170 180 190
....*....|....*....|....*....|....*.
gi 518843096 488 EILENALLSFDG----ALLVVSHDPSFVERVGfDRV 519
Cdd:PRK10070 201 TEMQDELVKLQAkhqrTIVFISHDLDEAMRIG-DRI 235
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