|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-482 |
4.14e-118 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 356.30 E-value: 4.14e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 6 AEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG--TFAYIPQ----LEEAAVR 78
Cdd:COG0488 1 LENLSKSFGGRPLLdDVS-LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQepplDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 79 EV------------QDYA-------------------------------------LMGKLGISRVQAE----IMSGGEET 105
Cdd:COG0488 80 DTvldgdaelraleAELEeleaklaepdedlerlaelqeefealggweaearaeeILSGLGFPEEDLDrpvsELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 106 RLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEYWGGYSDYLA 185
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 186 QKEAERNRQLAQYQQAEAERERLEQAISEKKVQARRldqksraagknstesggrlahqksqgSKQkklhtaARQMQRRIE 265
Cdd:COG0488 240 QRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARK--------------------------AKQ------AQSRIKALE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 266 ALDGVSAPEELWSVQFYHSEVLELHHPLpVTGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE 345
Cdd:COG0488 288 KLEREEPPRRDKTVEIRFPPPERLGKKV-LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 346 ---G-VVIAPKAEIGYFDQTGYKFTRNQNVMAYMQEGSDY-SVPDIRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARL 420
Cdd:COG0488 367 pdsGtVKLGETVKIGYFDQHQEELDPDKTVLDELRDGAPGgTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKL 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 421 LLGRYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQLQ 482
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-470 |
2.61e-63 |
|
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: 214.80 E-value: 2.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 15 GRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGrIPLQY-GKIERQ-----GTFAYIPQLE---------EAAVRE 79
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDFnGEARPQpgikvGYLPQEPQLDptktvrenvEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 80 VQD--------YALMG-------KLG--ISRVQAEI------------------------------MSGGEETRLKIAQA 112
Cdd:TIGR03719 96 IKDaldrfneiSAKYAepdadfdKLAaeQAELQEIIdaadawdldsqleiamdalrcppwdadvtkLSGGERRRVALCRL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 113 LEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEYWGGYSDYLAQKEAern 192
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQK--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 193 rQLAQYQQAEAERerleqaiseKKVQARRLDQkSRAAGKnstesgGRLAHQKSQGSKQKKLhtAARQMQRRIEALDGVSA 272
Cdd:TIGR03719 253 -RLEQEEKEESAR---------QKTLKRELEW-VRQSPK------GRQAKSKARLARYEEL--LSQEFQKRNETAEIYIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 273 P-EELWSVqfyhseVLELHHplpvtgheLCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE----GV 347
Cdd:TIGR03719 314 PgPRLGDK------VIEAEN--------LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQpdsgTI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 348 VIAPKAEIGYFDQTGYKFTRNQNVMAYMQEGSD------YSVPDiRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLL 421
Cdd:TIGR03719 380 EIGETVKLAYVDQSRDALDPNKTVWEEISGGLDiiklgkREIPS-RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTL 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1752069711 422 LGRYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISHDTRLVERVA 470
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIA 507
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-470 |
3.99e-53 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 187.63 E-value: 3.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTL-------LGRIPLQYG-KIerqGTFAYIPQLEEA---------AVREVQD-----------Y 83
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMagvdkefEGEARPAPGiKV---GYLPQEPQLDPEktvrenveeGVAEVKAaldrfneiyaaY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 84 A--------LMGKLGisRVQAEI------------------------------MSGGEETRLKIAQALEDNVHGIMADEP 125
Cdd:PRK11819 113 AepdadfdaLAAEQG--ELQEIIdaadawdldsqleiamdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 126 TSHLDRAGIDFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEYWGGYSDYLAQKEAernrQLAQYQQAEAER 205
Cdd:PRK11819 191 TNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAK----RLAQEEKQEAAR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 206 erleqaiseKKVQARRLDQkSRAAGKnstesgGRLAHQKSQGSKQKKLhtAARQMQRRIEALDGVSAP-EELWSVqfyhs 284
Cdd:PRK11819 267 ---------QKALKRELEW-VRQSPK------ARQAKSKARLARYEEL--LSEEYQKRNETNEIFIPPgPRLGDK----- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 285 eVLELHHplpvtgheLCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE----GVVIAPKAEIGYFDQ 360
Cdd:PRK11819 324 -VIEAEN--------LSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQpdsgTIKIGETVKLAYVDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 361 TGYKFTRNQNVMAYMQEGSDY------SVPDiRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPG 434
Cdd:PRK11819 395 SRDALDPNKTVWEEISGGLDIikvgnrEIPS-RAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
490 500 510
....*....|....*....|....*....|....*.
gi 1752069711 435 NFLDIPAMEALETMMREYPGTIVFISHDTRLVERVA 470
Cdd:PRK11819 474 NDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIA 509
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-481 |
1.02e-51 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 183.17 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 31 RIGLVGANGAGKSTLLKTLLG---------------RIplqyGKIeRQGTFAY--------------------------- 68
Cdd:PRK15064 29 RYGLIGANGCGKSTFMKILGGdlepsagnvsldpneRL----GKL-RQDQFAFeeftvldtvimghtelwevkqerdriy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 69 -IPQLEE-----AAVREVQdYA--------------LMGkLGISRVQAE-IMSG---GEETRLKIAQALEDNVHGIMADE 124
Cdd:PRK15064 104 aLPEMSEedgmkVADLEVK-FAemdgytaearagelLLG-VGIPEEQHYgLMSEvapGWKLRVLLAQALFSNPDILLLDE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 125 PTSHLDRAGIDFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEYWGGYSDYLAQKEAERNRQLAQYQQAEAE 204
Cdd:PRK15064 182 PTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQARERLLADNAKKKAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 205 rerleqaISEKKVQARRLdqksrAAGKnstesggrlahqksqgSKQKKLHTAARQMQRrIEaLDGVSA-----PeelwSV 279
Cdd:PRK15064 262 -------IAELQSFVSRF-----SANA----------------SKAKQATSRAKQIDK-IK-LEEVKPssrqnP----FI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 280 QFYHSEVLelhHPLPVTGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDR---EEGVV-IAPKAEI 355
Cdd:PRK15064 308 RFEQDKKL---HRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGElepDSGTVkWSENANI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 356 GYFDQ-TGYKFTRNQNVMAYM----QEGSDYSVpdIRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLL 430
Cdd:PRK15064 385 GYYAQdHAYDFENDLTLFDWMsqwrQEGDDEQA--VRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 431 DEPGNFLDIPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK15064 463 DEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-467 |
7.93e-47 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 171.67 E-value: 7.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 19 LDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI-----------------ERQGT-FAYIPQ-LEEAA--- 76
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarlqqdpprNVEGTvYDFVAEgIEEQAeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 77 ---------VREVQDYALMGKLgiSRVQAEI-----------------------------MSGGEETRLKIAQALEDNVH 118
Cdd:PRK11147 99 kryhdishlVETDPSEKNLNEL--AKLQEQLdhhnlwqlenrinevlaqlgldpdaalssLSGGWLRKAALGRALVSNPD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 119 GIMADEPTSHLDRAGIDFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEYWGGYSDYLAQKE---------- 188
Cdd:PRK11147 177 VLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEealrveelqn 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 189 AERNRQLAQyqqaeaererlEQAISEKKVQARRL--DQKSRAAGKNSTEsggRLAHQKSQGSKQKKLHTAARQmqRRIea 266
Cdd:PRK11147 257 AEFDRKLAQ-----------EEVWIRQGIKARRTrnEGRVRALKALRRE---RSERREVMGTAKMQVEEASRS--GKI-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 267 ldgvsapeelwsvqfyhseVLELHhplpvtghELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREEG 346
Cdd:PRK11147 319 -------------------VFEME--------NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 347 ----VVIAPKAEIGYFDQTGYKFTRNQNVMAYMQEG-SDYSVPDI-RAVLSSMG---FTPEDVRKELSMLSGGEIIKLQL 417
Cdd:PRK11147 372 dsgrIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGkQEVMVNGRpRHVLGYLQdflFHPKRAMTPVKALSGGERNRLLL 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1752069711 418 ARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISHDTRLVE 467
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVD 501
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-172 |
1.52e-46 |
|
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: 158.38 E-value: 1.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT--FAYIPQLeeaavrevq 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTvkIGYFEQL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 82 dyalmgklgisrvqaeimSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTGALLIISHDRDLLDRV 161
Cdd:cd03221 72 ------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQV 133
|
170
....*....|.
gi 1752069711 162 ADKIWELKDGR 172
Cdd:cd03221 134 ATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
295-480 |
4.32e-44 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 151.83 E-value: 4.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 295 VTGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDRE---EGVVI-APKAEIGYFDQtgykftrnqn 370
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELepdEGIVTwGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 371 vmaymqegsdysvpdiravlssmgftpedvrkelsmLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMR 450
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 1752069711 451 EYPGTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-482 |
6.46e-44 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 163.80 E-value: 6.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 31 RIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAY------IPQLEEAAVREVQD---------------------- 82
Cdd:PRK10636 29 KVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLawvnqeTPALPQPALEYVIDgdreyrqleaqlhdanerndgh 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 83 ---------------------YALMGKLGISRVQAE----IMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFL 137
Cdd:PRK10636 109 aiatihgkldaidawtirsraASLLHGLGFSNEQLErpvsDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 138 VSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEYWGGYSDYlaqkEAERNRQLAQyqqaeaererlEQAISEKKV 217
Cdd:PRK10636 189 EKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF----EVQRATRLAQ-----------QQAMYESQQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 218 QarrldqksraagknstesggRLAHQKSQGSKQKKLHTAARQMQRRIEALDGVS--APEEL---WSVQFYHSEVLelhhP 292
Cdd:PRK10636 254 E--------------------RVAHLQSYIDRFRAKATKAKQAQSRIKMLERMEliAPAHVdnpFHFSFRAPESL----P 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 293 LPVTGHE-LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI----RDREEGVVIAPKAEIGYFDQTGYKFTR 367
Cdd:PRK10636 310 NPLLKMEkVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLagelAPVSGEIGLAKGIKLGYFAQHQLEFLR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 368 -NQNVMAYMQEGSDYSVPD-IRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEAL 445
Cdd:PRK10636 390 aDESPLQHLARLAPQELEQkLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
490 500 510
....*....|....*....|....*....|....*..
gi 1752069711 446 ETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQLQ 482
Cdd:PRK10636 470 TEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-186 |
1.98e-41 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 154.84 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 2 LLIKAEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERqGT---FAYIPQLEEA-- 75
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLdDLS-LRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GEtvkIGYFDQHQEEld 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 76 ----AVREVQDYA----------LMGKLGIS--RVQAEI--MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFL 137
Cdd:COG0488 392 pdktVLDELRDGApggteqevrgYLGRFLFSgdDAFKPVgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 138 VSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEYWGGYSDYLAQ 186
Cdd:COG0488 472 EEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
300-483 |
2.53e-38 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 146.36 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---G-VVIAPKAEIGYFDQTGYkFTRNQNVMAYM 375
Cdd:COG0488 4 LSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEpdsGeVSIPKGLRIGYLPQEPP-LDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 376 QEG---------------SDYSVPD------------------------IRAVLSSMGFTPEDVRKELSMLSGGEIIKLQ 416
Cdd:COG0488 83 LDGdaelraleaeleeleAKLAEPDedlerlaelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWRRRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752069711 417 LARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQLQR 483
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTL 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
298-480 |
2.16e-29 |
|
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: 112.72 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIgYFDqtgykftrnqnvmaymqe 377
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAI----AGLLKPTSGEI-LID------------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 378 GSDYSVPDIRAVLSSMGFTPEdvrkelsmLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYPG--- 454
Cdd:cd00267 60 GKDIAKLPLEELRRRIGYVPQ--------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegr 131
|
170 180
....*....|....*....|....*.
gi 1752069711 455 TIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:cd00267 132 TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
300-481 |
1.23e-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: 108.64 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRdreeGVVIAPKAEIGYFdqtGYKFTRNQnvmaymqegs 379
Cdd:cd03230 6 LSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL----GLLKPDSGEIKVL---GKDIKKEP---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 380 dysvpdiRAVLSSMGFTPEDVR-------KELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMREY 452
Cdd:cd03230 69 -------EEVKRRIGYLPEEPSlyenltvRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL 141
|
170 180 190
....*....|....*....|....*....|..
gi 1752069711 453 ---PGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03230 142 kkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
300-481 |
3.24e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 105.67 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---------------RDREEGVVIAPKAEIGYFDQTGYK 364
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALadldpptsgeiyldgKPLSAMPPPEWRRQVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 365 FTrnQNVMAYMQE-----GSDYSVPDIRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDI 439
Cdd:COG4619 86 WG--GTVRDNLPFpfqlrERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752069711 440 PAMEALETMMREYP----GTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:COG4619 164 ENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
100-481 |
3.22e-25 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 109.18 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 100 SGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEYWGG 179
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGD 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 180 YSDYLAQKEAERNRQLAQYQQAEAERERLEQAISEKKVQARRldqksraagknstesggrlahqksqgskqkklhtaARQ 259
Cdd:PLN03073 426 YDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKR-----------------------------------ASL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 260 MQRRIEALDGVSAPEELWSVQFYHsevLELHHPLPVTGHELCK-------QLGDKVILDRVSFQFPLGGKIAITGGNGAG 332
Cdd:PLN03073 471 VQSRIKALDRLGHVDAVVNDPDYK---FEFPTPDDRPGPPIISfsdasfgYPGGPLLFKNLNFGIDLDSRIAMVGPNGIG 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 333 KTTLLNMIRDREE---GVVI-APKAEIGYFDQ---TGYKFTRNQnvMAYMQEGSDySVPD--IRAVLSSMGFTPEDVRKE 403
Cdd:PLN03073 548 KSTILKLISGELQpssGTVFrSAKVRMAVFSQhhvDGLDLSSNP--LLYMMRCFP-GVPEqkLRAHLGSFGVTGNLALQP 624
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 404 LSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PLN03073 625 MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
298-481 |
8.49e-25 |
|
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: 102.63 E-value: 8.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVV-----------IAPKAEIGYF-DQTG 362
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaglLKPDSGSIlidgedvrkepREARRQIGVLpDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 363 --YKFTRNQNVMAYmqeGSDYSVPD------IRAVLSSMGFTPEDVRKeLSMLSGGEIIKLQLARLLLGRYNILLLDEPG 434
Cdd:COG4555 85 lyDRLTVRENIRYF---AELYGLFDeelkkrIEELIELLGLEEFLDRR-VGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752069711 435 NFLDIPAMEALETMMREY---PGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:COG4555 161 NGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-481 |
9.43e-24 |
|
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: 104.21 E-value: 9.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRD---VLDIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIP----------------LQYGKIERQ 63
Cdd:COG1123 4 LLEVRDLSVRYPGGDvpaVDGVS-LTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevlldgrdlLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 64 GTFAYIPQ-------------------------LEEAAVREVQDYALMGKLGISRVQAEIMSGGEETRLKIAQALEDNVH 118
Cdd:COG1123 83 RRIGMVFQdpmtqlnpvtvgdqiaealenlglsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 119 GIMADEPTSHLD---RAGIDFLVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRITEywggysDYLAQKEAERNRQ 194
Cdd:COG1123 163 LLIADEPTTALDvttQAEILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVE------DGPPEEILAAPQA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 195 LAQYQQAEAERERLEQAISEKKVqarrldqksraagknstesggrlahqksqgskqkklhtaarqmqrriealdgvsape 274
Cdd:COG1123 237 LAAVPRLGAARGRAAPAAAAAEP--------------------------------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 275 elwsvqfyhseVLELHHplpVTGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIAP 351
Cdd:COG1123 260 -----------LLEVRN---LSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLlglLRPTSGSILFD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 352 KAEI-GYFDQTGYKFTRN-----QN----------VMAYMQEG----SDYSVPDIRA----VLSSMGFTPEDVRKELSML 407
Cdd:COG1123 326 GKDLtKLSRRSLRELRRRvqmvfQDpysslnprmtVGDIIAEPlrlhGLLSRAERRErvaeLLERVGLPPDLADRYPHEL 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 408 SGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA----MEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-172 |
1.67e-23 |
|
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: 96.55 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 5 KAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-------------FAYIPQ 71
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKdiaklpleelrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 LeeaavrevqdyalmgklgisrvqaeimSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTG---AL 148
Cdd:cd00267 81 L---------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTV 133
|
170 180
....*....|....*....|....
gi 1752069711 149 LIISHDRDLLDRVADKIWELKDGR 172
Cdd:cd00267 134 IIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
300-481 |
1.87e-23 |
|
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: 97.12 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIGYFDQTGYKFTRNQ--NVMAYM-Q 376
Cdd:cd03214 5 LSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTL----AGLLKPSSGEILLDGKDLASLSPKElaRKIAYVpQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 377 egsdysvpdiraVLSSMGFTPEdVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIP----AMEALETMMREY 452
Cdd:cd03214 81 ------------ALELLGLAHL-ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAhqieLLELLRRLARER 147
|
170 180
....*....|....*....|....*....
gi 1752069711 453 PGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03214 148 GKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-190 |
2.94e-23 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 102.66 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 24 LELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIE--RQGTFAYIPQLEEA-----------------------AVR 78
Cdd:PRK15064 340 LLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsENANIGYYAQDHAYdfendltlfdwmsqwrqegddeqAVR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 79 evqdyALMGKLGIS----RVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTGALLIISHD 154
Cdd:PRK15064 420 -----GTLGRLLFSqddiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHD 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 1752069711 155 RDLLDRVADKIWELKDGRITEYWGGYSDYLAQKEAE 190
Cdd:PRK15064 495 REFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGIE 530
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-191 |
5.76e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 97.47 E-value: 5.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 1 MLLIKAEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT--------FAYIPQ 71
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLeDVS-LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 LEEAA------VREVqdyALMGKLG-------------------ISRVQAE------I--MSGGEETRLKIAQALEDNVH 118
Cdd:COG1121 83 RAEVDwdfpitVRDV---VLMGRYGrrglfrrpsradreavdeaLERVGLEdladrpIgeLSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 119 GIMADEPTSHLDRAGI-DF--LVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRIteYWGGYSDYLAQKEAER 191
Cdd:COG1121 160 LLLLDEPFAGVDAATEeALyeLLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV--AHGPPEEVLTPENLSR 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
298-481 |
2.70e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.52 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVV-----------IAPKAEIGY-FDQTG 362
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlglLRPTSGEVrvlgedvardpAEVRRRIGYvPQEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 363 Y--KFTRNQNVMAYmqeGSDYSVPD------IRAVLSSMGFTpEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPG 434
Cdd:COG1131 84 LypDLTVRENLRFF---ARLYGLPRkearerIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752069711 435 NFLDIPAMEALETMMREY--PGTIVFIS-HDTRLVERVADQVYVLKKGQL 481
Cdd:COG1131 160 SGLDPEARRELWELLRELaaEGKTVLLStHYLEEAERLCDRVAIIDKGRI 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-233 |
2.77e-22 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 100.02 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 30 DRIGLVGANGAGKSTLLKTLLGRIPLQYGKIeRQGT---FAYIPQLEEA--AVREVQDYALMGKL-----GISR------ 93
Cdd:PRK11147 346 DKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTkleVAYFDQHRAEldPEKTVMDNLAEGKQevmvnGRPRhvlgyl 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 94 -------------VQAeiMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTGALLIISHDRDLLDR 160
Cdd:PRK11147 425 qdflfhpkramtpVKA--LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDN 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 161 VADKIWELK-DGRITEYWGGYSDylaqkeaernrqlAQYQQAEAERERLEQAISEKKVQARRLDQKSRAAGKNS 233
Cdd:PRK11147 503 TVTECWIFEgNGKIGRYVGGYHD-------------ARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSKKLS 563
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
295-476 |
3.46e-22 |
|
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: 94.08 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 295 VTGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVV-----------IAPKAEIGY-FD 359
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILaglLPPSAGEVlwngepirdarEDYRRRLAYlGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 360 QTGYK--FTRNQNVMAYMQ-EGSDYSVPDIRAVLSSMGFTP-EDVRkeLSMLSGGEIIKLQLARLLLGRYNILLLDEPGN 435
Cdd:COG4133 83 ADGLKpeLTVRENLRFWAAlYGLRADREAIDEALEAVGLAGlADLP--VRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752069711 436 FLDIPAMEALETMMREYP---GTIVFISHDTRLVErvADQVYVL 476
Cdd:COG4133 161 ALDAAGVALLAELIAAHLargGAVLLTTHQPLELA--AARVLDL 202
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-173 |
1.32e-21 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 93.95 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-------------FAY 68
Cdd:COG1120 1 MLEAENLSVGYGGRPVLdDVS-LSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 69 IPQLEEAA----VREV-----------------QDYAL----MGKLGIS-----RVQAeiMSGGEETRLKIAQALednVH 118
Cdd:COG1120 80 VPQEPPAPfgltVRELvalgryphlglfgrpsaEDREAveeaLERTGLEhladrPVDE--LSGGERQRVLIARAL---AQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 119 G---IMADEPTSHLD-RAGIDFL--VSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:COG1120 155 EpplLLLDEPTSHLDlAHQLEVLelLRRLARERGrTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-174 |
1.56e-21 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 91.73 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 5 KAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI-------------ERQGTFAYIPQ 71
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlaslspkELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 leeaavrevqdyaLMGKLGIS----RVQAEiMSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLY 144
Cdd:cd03214 81 -------------ALELLGLAhladRPFNE-LSGGERQRVLLARALAQEPPILLLDEPTSHLDiahQIELLELLRRLARE 146
|
170 180 190
....*....|....*....|....*....|.
gi 1752069711 145 TG-ALLIISHDRDLLDRVADKIWELKDGRIT 174
Cdd:cd03214 147 RGkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-173 |
1.90e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 91.31 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLD-IDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT------------FAYIP 70
Cdd:cd03230 1 IEVRNLSKRYGKKTALDdIS-LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkepeevkrrIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 71 Q----LEEAAVREVQDYalmgklgisrvqaeimSGGEETRLKIAQALednVHG---IMADEPTSHLDRAGIDFLVSRLKL 143
Cdd:cd03230 80 EepslYENLTVRENLKL----------------SGGMKQRLALAQAL---LHDpelLILDEPTSGLDPESRREFWELLRE 140
|
170 180 190
....*....|....*....|....*....|...
gi 1752069711 144 YT---GALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03230 141 LKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
305-480 |
3.71e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 90.13 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVViapkaeigYFDQtgykftrnqnvmaymQEGSDY 381
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLlrlYDPTSGEI--------LIDG---------------VDLRDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 382 SVPDIRavlSSMGFTPED-------VRKELsmLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA----MEALETMMR 450
Cdd:cd03228 70 DLESLR---KNIAYVPQDpflfsgtIRENI--LSGGQRQRIAIARALLRDPPILILDEATSALDPETealiLEALRALAK 144
|
170 180 190
....*....|....*....|....*....|
gi 1752069711 451 EYpgTIVFISHDTRLVERvADQVYVLKKGQ 480
Cdd:cd03228 145 GK--TVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
305-480 |
8.23e-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: 90.60 E-value: 8.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIAPKAEIGYFD------QTGYKF--TRNQNVMA 373
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnglLGPTSGEVLVDGKDLTKLSlkelrrKVGLVFqnPDDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 YMQEgsdysvpDIRAVLSSMGFTPEDVRK-----------------ELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNF 436
Cdd:cd03225 92 TVEE-------EVAFGLENLGLPEEEIEErveealelvgleglrdrSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752069711 437 LDIPAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:cd03225 165 LDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-165 |
9.05e-21 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 90.29 E-value: 9.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 5 KAEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT--------FAYIPQLEEA 75
Cdd:cd03235 1 EVEDLTVSYGGHPVLeDVS-FEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 76 A------VREVQDYALMGKLG----ISRVQAEI--------------------MSGGEETRLKIAQALEDNVHGIMADEP 125
Cdd:cd03235 80 DrdfpisVRDVVLMGLYGHKGlfrrLSKADKAKvdealervglseladrqigeLSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1752069711 126 TSHLDRAGI-DF--LVSRLKLYTGALLIISHDRDLLDRVADKI 165
Cdd:cd03235 160 FAGVDPKTQeDIyeLLRELRREGMTILVVTHDLGLVLEYFDRV 202
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-174 |
1.15e-20 |
|
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: 90.01 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 6 AEEIVVEY-MGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI----------ERQGTFAYIPQ--- 71
Cdd:cd03226 2 IENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikakERRKSIGYVMQdvd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 ---------------LEEAAVREVQDYALMGKLGISRVQAE---IMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG 133
Cdd:cd03226 82 yqlftdsvreelllgLKELDAGNEQAETVLKDLDLYALKERhplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752069711 134 IDF---LVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRIT 174
Cdd:cd03226 162 MERvgeLIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-229 |
1.87e-20 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 94.47 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIE-----RQGTFAYiPQLE---- 73
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGlakgiKLGYFAQ-HQLEflra 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 74 -------------EAAVREVQDYalMGKLGISRVQ----AEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDF 136
Cdd:PRK10636 391 desplqhlarlapQELEQKLRDY--LGGFGFQGDKvteeTRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 137 LVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEYWGGYSDYlAQKEAERNRQlaQYQQAEAERERleqaiSEKK 216
Cdd:PRK10636 469 LTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY-QQWLSDVQKQ--ENQTDEAPKEN-----NANS 540
|
250
....*....|...
gi 1752069711 217 VQARRlDQKSRAA 229
Cdd:PRK10636 541 AQARK-DQKRREA 552
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
305-480 |
2.00e-19 |
|
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: 91.15 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR--DRE-EG-VVIAPKAEIGYFDQTGY---KFTRNQNVMAYMQE 377
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAgvDKDfNGeARPQPGIKVGYLPQEPQldpTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 378 GSD-----------YSVPD--IRAVLSSMGFTPE----------DVRKELSM--------------LSGGEIIKLQLARL 420
Cdd:TIGR03719 96 IKDaldrfneisakYAEPDadFDKLAAEQAELQEiidaadawdlDSQLEIAMdalrcppwdadvtkLSGGERRRVALCRL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 421 LLGRYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGR 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
298-481 |
2.91e-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: 87.02 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-RdreegvVIAPKA-EIGYFDQTGYKFTRNQ--NVMA 373
Cdd:COG1120 5 ENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALaG------LLKPSSgEVLLDGRDLASLSRRElaRRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 YM-QE---GSDYSVPDIraVLssMG----------FTPEDVR----------------KELSMLSGGEIIKLQLARLLLG 423
Cdd:COG1120 79 YVpQEppaPFGLTVREL--VA--LGryphlglfgrPSAEDREaveealertglehladRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 424 RYNILLLDEPGNFLDIP----AMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAhqleVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
305-481 |
3.82e-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: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRdreeGVVIAPKAEIGYFdqtGYKFTRNQNVMAYM--QEGSDYS 382
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIL----GLLPPTSGTVRLF---GKPPRRARRRIGYVpqRAEVDWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 383 VP---------------------------DIRAVLSSMGFtpEDVRKE-LSMLSGGEiikLQ---LARLLLGRYNILLLD 431
Cdd:COG1121 90 FPitvrdvvlmgrygrrglfrrpsradreAVDEALERVGL--EDLADRpIGELSGGQ---QQrvlLARALAQDPDLLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 432 EPGNFLDIPAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:COG1121 165 EPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
304-479 |
4.25e-19 |
|
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: 85.66 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 304 LGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRdreeGVVIAPKAEIGYFdqtGYKFTRNQNVMAYM--QEGSDY 381
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL----GLLKPTSGSIRVF---GKPLEKERKRIGYVpqRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 382 SVP-DIRAVLsSMGFTP-------------EDVR-------------KELSMLSGGEIIKLQLARLLLGRYNILLLDEPG 434
Cdd:cd03235 82 DFPiSVRDVV-LMGLYGhkglfrrlskadkAKVDealervglseladRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752069711 435 NFLDIPAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKG 479
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
305-481 |
7.27e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 89.89 E-value: 7.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVV---------IAPKA---EIGYFDQTGYKFTRN- 368
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlglYEPTSGRIlidgidlrqIDPASlrrQIGVVLQDVFLFSGTi 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 369 -QNVMAYmqeGSDYSVPDIRAVLSSMGFTpEDVRK-------EL----SMLSGGEIIKLQLARLLLGRYNILLLDEPGNF 436
Cdd:COG2274 566 rENITLG---DPDATDEEIIEAARLAGLH-DFIEAlpmgydtVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752069711 437 LDiPAMEA--LETMMREYPG-TIVFISHDTRLVeRVADQVYVLKKGQL 481
Cdd:COG2274 642 LD-AETEAiiLENLRRLLKGrTVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
305-481 |
1.01e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 89.24 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-RD---------REEGVVIA------PKAEIGyfdqTGYKFT-- 366
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILnGEvllddgriiYEQDLIVArlqqdpPRNVEG----TVYDFVae 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 367 -------------------------RNQNVMAYMQEGSDYS-----VPDIRAVLSSMGFTPEdvrKELSMLSGGEIIKLQ 416
Cdd:PRK11147 90 gieeqaeylkryhdishlvetdpseKNLNELAKLQEQLDHHnlwqlENRINEVLAQLGLDPD---AALSSLSGGWLRKAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752069711 417 LARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-172 |
1.17e-18 |
|
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: 83.39 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG----TFAYIPQLEEAAVRE 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 80 V-QDYALMGKLGISRVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTG-ALLIISHD 154
Cdd:cd03229 81 VfQDFALFPHLTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDpitRREVRALLKSLQAQLGiTVVLVTHD 160
|
170
....*....|....*...
gi 1752069711 155 RDLLDRVADKIWELKDGR 172
Cdd:cd03229 161 LDEAARLADRVVVLRDGK 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
298-480 |
1.53e-18 |
|
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: 83.87 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRD---REEGVV--------IAPKAEIGYF-DQTG-YK 364
Cdd:cd03269 4 ENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiilPDSGEVlfdgkpldIAARNRIGYLpEERGlYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 365 FTRNQNVMAYMQEGSDYSVPDIRA----VLSSMGFTPEDVRKeLSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIP 440
Cdd:cd03269 84 KMKVIDQLVYLAQLKGLKKEEARRrideWLERLELSEYANKR-VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1752069711 441 AMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:cd03269 163 NVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
305-481 |
2.60e-18 |
|
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: 83.92 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI----RDRE-----EGVVIAPKAEIGYFDQTGYKFT--RNQNVMA 373
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllKPTSgevlvDGKDITKKNLRELRRKVGLVFQnpDDQLFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 YMQEgsdysvpDIRAVLSSMGFTPEDVR-----------------KELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNF 436
Cdd:COG1122 92 TVEE-------DVAFGPENLGLPREEIRerveealelvglehladRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752069711 437 LDIPAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:COG1122 165 LDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
305-481 |
7.98e-18 |
|
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: 85.97 E-value: 7.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVV---------IAPKA---EIGYFDQTGYKF--TR 367
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlgfLPPYSGSIlingvdlsdLDPASwrrQIAWVPQNPYLFagTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 368 NQNVMAYMQEGSDysvPDIRAVLSSMGFTpeDVRKEL------------SMLSGGEIIKLQLARLLLGRYNILLLDEPGN 435
Cdd:COG4988 428 RENLRLGRPDASD---EELEAALEAAGLD--EFVAALpdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752069711 436 FLDIPA----MEALETMMREYpgTIVFISHDTRLVERvADQVYVLKKGQL 481
Cdd:COG4988 503 HLDAETeaeiLQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRI 549
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-173 |
9.06e-18 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 82.38 E-value: 9.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYM-GRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfayipQLEEAAVREvq 81
Cdd:COG1122 1 IELENLSFSYPgGTPALdDVS-LSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK-----DITKKNLRE-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 82 dyaLMGKLGI-----------SRVQAEIMSG-------GEETRLKIAQALED---------NVH-------------GIM 121
Cdd:COG1122 73 ---LRRKVGLvfqnpddqlfaPTVEEDVAFGpenlglpREEIRERVEEALELvglehladrPPHelsggqkqrvaiaGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 122 A--------DEPTSHLDRAGIDFLVSRLKLYTGA---LLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:COG1122 150 AmepevlvlDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
310-433 |
1.12e-17 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 79.61 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---------------RDREEGVVIAPKAEIGYFDQ--------TGYKFT 366
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIagllsptegtilldgQDLTDDERKSLRKEIGYVFQdpqlfprlTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 367 R-NQNVMAYMQEGSDYSVPDIRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEP 433
Cdd:pfam00005 81 RlGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
305-462 |
2.25e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.79 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI--RDRE-EG-VVIAPKAEIGYFDQTGY---KFTRNQNVMAYMQE 377
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagVDKEfEGeARPAPGIKVGYLPQEPQldpEKTVRENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 378 GSD-----------YSVP--DIRAVLSSMGFTPE----------DVRKELSM--------------LSGGEIIKLQLARL 420
Cdd:PRK11819 98 VKAaldrfneiyaaYAEPdaDFDALAAEQGELQEiidaadawdlDSQLEIAMdalrcppwdakvtkLSGGERRRVALCRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1752069711 421 LLGRYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISHD 462
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
298-480 |
2.32e-17 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 79.54 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIGYFDQTGYKFTRN-----QNVM 372
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCI----AGLEEPDSGSILIDGEDLTDLEDElpplrRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 373 AYMQEGsdysvpdirAVLSSMgftpeDVRKELSM-LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPAMEA-----LE 446
Cdd:cd03229 80 MVFQDF---------ALFPHL-----TVLENIALgLSGGQQQRVALARALAMDPDVLLLDEPTSALD-PITRRevralLK 144
|
170 180 190
....*....|....*....|....*....|....
gi 1752069711 447 TMMREYPGTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:cd03229 145 SLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-197 |
2.39e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 84.82 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMG--RDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfaYIPQLEEAAVREV- 80
Cdd:COG4987 334 LELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV--DLRDLDEDDLRRRi 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 81 ----QDYAL----------MGKLGIS---------RVQ-------------------AEIMSGGEETRLKIAQALEDNVH 118
Cdd:COG4987 412 avvpQRPHLfdttlrenlrLARPDATdeelwaaleRVGlgdwlaalpdgldtwlgegGRRLSGGERRRLALARALLRDAP 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 119 GIMADEPTSHLDRAGIDFLVSRLKLYTG--ALLIISHDRDLLDRvADKIWELKDGRITEYwGGYSDYLAQKeaERNRQLA 196
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGLER-MDRILVLEDGRIVEQ-GTHEELLAQN--GRYRQLY 567
|
.
gi 1752069711 197 Q 197
Cdd:COG4987 568 Q 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-175 |
3.74e-17 |
|
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: 84.04 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVL--DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-------------FAY 68
Cdd:COG4988 337 IELEDVSFSYPGGRPAldGLS-LTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 69 IPQ--------LEE---------------AAVREVQDYALMGKL--GI-SRV--QAEIMSGGEETRLKIAQALEDNVHGI 120
Cdd:COG4988 416 VPQnpylfagtIREnlrlgrpdasdeeleAALEAAGLDEFVAALpdGLdTPLgeGGRGLSGGQAQRLALARALLRDAPLL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752069711 121 MADEPTSHLDRAGIDFLVSRL-KLYTG-ALLIISHDRDLLDRvADKIWELKDGRITE 175
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALrRLAKGrTVILITHRLALLAQ-ADRILVLDDGRIVE 551
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-174 |
7.72e-17 |
|
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: 77.85 E-value: 7.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLD-IDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGtfayipqlEEAAVREVQD 82
Cdd:cd03216 1 LELRGITKRFGGVKALDgVS-LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------KEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 83 yalMGKLGISRV-QaeiMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFL---VSRLKLYTGALLIISHDRDLL 158
Cdd:cd03216 72 ---ARRAGIAMVyQ---LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLfkvIRRLRAQGVAVIFISHRLDEV 145
|
170
....*....|....*.
gi 1752069711 159 DRVADKIWELKDGRIT 174
Cdd:cd03216 146 FEIADRVTVLRDGRVV 161
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-172 |
1.05e-16 |
|
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: 78.66 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 16 RDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-------------FAYIPQ----------- 71
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklslkelrrkVGLVFQnpddqffgptv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 ------------LEEAAVREVQDYALmGKLGISRVQAEI---MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDF 136
Cdd:cd03225 94 eeevafglenlgLPEEEIEERVEEAL-ELVGLEGLRDRSpftLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRE 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1752069711 137 LVSRLKLYTGA---LLIISHDRDLLDRVADKIWELKDGR 172
Cdd:cd03225 173 LLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
300-482 |
1.89e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.05 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreegvviapkaeigyfdqTGYKFTRNQNVMAYMQEGS 379
Cdd:PRK13548 8 LSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL--------------------SGELSPDSGEVRLNGRPLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 380 DYSVPD---IRAVL---SSMGF--TPEDV------------------------RKELSM--------LSGGEIIKLQLAR 419
Cdd:PRK13548 68 DWSPAElarRRAVLpqhSSLSFpfTVEEVvamgraphglsraeddalvaaalaQVDLAHlagrdypqLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 420 LLL------GRYNILLLDEPGNFLDI----PAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQLQ 482
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-183 |
4.74e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 81.06 E-value: 4.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 31 RIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT---------------FAYIPQLEEA----AVREVQDYALMGKLGI 91
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvrmavfsqhhvdgldLSSNPLLYMMrcfpGVPEQKLRAHLGSFGV 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 92 SRVQA----EIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTGALLIISHDRDLLDRVADKIWE 167
Cdd:PLN03073 617 TGNLAlqpmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWV 696
|
170
....*....|....*.
gi 1752069711 168 LKDGRITEYWGGYSDY 183
Cdd:PLN03073 697 VSEGKVTPFHGTFHDY 712
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
309-481 |
5.62e-16 |
|
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: 80.58 E-value: 5.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 309 ILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR---DREEGVV------IAPKAE------IGYFDQTGYKFT---RNqN 370
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrflDPQSGSItlggvdLRDLDEddlrrrIAVVPQRPHLFDttlRE-N 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 371 V-MAYmQEGSDysvPDIRAVLSSMGFTP--EDVRKELSM--------LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDi 439
Cdd:COG4987 429 LrLAR-PDATD---EELWAALERVGLGDwlAALPDGLDTwlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLD- 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752069711 440 PAMEA--LETMMREYPG-TIVFISHDTRLVERvADQVYVLKKGQL 481
Cdd:COG4987 504 AATEQalLADLLEALAGrTVLLITHRLAGLER-MDRILVLEDGRI 547
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-172 |
8.78e-16 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 75.11 E-value: 8.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRD--VLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI-------------ERQGTFAY 68
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdldleSLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 69 IPQ---LEEAAVREvqdyalmgklgisrvqaEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYT 145
Cdd:cd03228 81 VPQdpfLFSGTIRE-----------------NILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALA 143
|
170 180
....*....|....*....|....*....
gi 1752069711 146 G--ALLIISHDRDLLDRvADKIWELKDGR 172
Cdd:cd03228 144 KgkTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
305-481 |
1.29e-15 |
|
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: 76.38 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI----RDRE-----EGVVIAPKAEIGYFDQTGYKFtrnQNVMA-- 373
Cdd:COG1124 16 RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALagleRPWSgevtfDGRPVTRRRRKAFRRRVQMVF---QDPYAsl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 -------------YMQEGSDYSVPDIRAVLSSMGFTPEDVRKELSMLSGGEiikLQ---LARLLLGRYNILLLDEPGNFL 437
Cdd:COG1124 93 hprhtvdrilaepLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQ---RQrvaIARALILEPELLLLDEPTSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752069711 438 DIP----AMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:COG1124 170 DVSvqaeILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-176 |
1.67e-15 |
|
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: 75.62 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRD-----VLDIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT------------ 65
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkaLDDVS-FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 66 ----FAYIPQ---------------LEE-----------AAVREVQDYALMGkLGISRVQAEI----MSGGEETRLKIAQ 111
Cdd:cd03257 80 rrkeIQMVFQdpmsslnprmtigeqIAEplrihgklskkEARKEAVLLLLVG-VGLPEEVLNRypheLSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 112 ALEDNVHGIMADEPTSHLD---RAGIDFLVSRLK-LYTGALLIISHDRDLLDRVADKIWELKDGRITEY 176
Cdd:cd03257 159 ALALNPKLLIADEPTSALDvsvQAQILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
306-481 |
2.27e-15 |
|
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: 73.89 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRdreeGVVIAPKAEIgYFDQTgykftrnqNVMAYMQEGSDY-SVP 384
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT----GDLKPQQGEI-TLDGV--------PVSDLEKALSSLiSVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 385 DIRAVLSSmgftpEDVRKELSM-LSGGEIIKLQLARLLLGRYNILLLDEPGNFLD-IPAMEALETMMREYPG-TIVFISH 461
Cdd:cd03247 81 NQRPYLFD-----TTLRNNLGRrFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQLLSLIFEVLKDkTLIWITH 155
|
170 180
....*....|....*....|
gi 1752069711 462 DTRLVERVaDQVYVLKKGQL 481
Cdd:cd03247 156 HLTGIEHM-DKILFLENGKI 174
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-195 |
2.75e-15 |
|
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: 78.05 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT--FAYIPQLEEA---------AVREVQDYALMGKLGI-SRV----- 94
Cdd:TIGR03719 351 VGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvkLAYVDQSRDAldpnktvweEISGGLDIIKLGKREIpSRAyvgrf 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 95 ---------QAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTGALLIISHDRDLLDRVADKI 165
Cdd:TIGR03719 431 nfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHI 510
|
170 180 190
....*....|....*....|....*....|..
gi 1752069711 166 --WElKDGRITEYWGGYSDYlaqkEAERNRQL 195
Cdd:TIGR03719 511 laFE-GDSHVEWFEGNFSEY----EEDKKRRL 537
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
307-481 |
3.62e-15 |
|
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: 74.45 E-value: 3.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 307 KVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI--RDR-EEGVVI--------APKAEIGYF--DQTGYKF-------- 365
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggLDRpTSGEVRvdgtdiskLSEKELAAFrrRHIGFVFqsfnllpd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 366 -TRNQNVMA---YMQEGSDYSVPDIRAVLSSMGFtPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEP-GNfLDIP 440
Cdd:cd03255 97 lTALENVELpllLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPtGN-LDSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752069711 441 A----MEALETMMREYPGTIVFISHDTRLVERvADQVYVLKKGQL 481
Cdd:cd03255 175 TgkevMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
305-461 |
5.26e-15 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 74.74 E-value: 5.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI----------------RDReEGVVIAP-KAEIGYFDQT-GYKFT 366
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgdlpptygndvrlfgERR-GGEDVWElRKRIGLVSPAlQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 367 RNQNVmaymqegsdysvpdIRAVLS----SMG----FTPEDVRK------ELSM----------LSGGEIIKLQLARLLL 422
Cdd:COG1119 93 RDETV--------------LDVVLSgffdSIGlyrePTDEQRERarelleLLGLahladrpfgtLSQGEQRRVLIARALV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1752069711 423 GRYNILLLDEPGNFLDIPAME----ALETMMREYPGTIVFISH 461
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARElllaLLDKLAAEGAPTLVLVTH 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-173 |
5.48e-15 |
|
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: 72.63 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRD--VLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGtfAYIPQLEEAAVRE-- 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--ADISQWDPNELGDhv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 80 ---VQDYALM-GKLgisrvqAE-IMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG---IDFLVSRLKLYTGALLII 151
Cdd:cd03246 79 gylPQDDELFsGSI------AEnILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGeraLNQAIAALKAAGATRIVI 152
|
170 180
....*....|....*....|..
gi 1752069711 152 SHDRDLLdRVADKIWELKDGRI 173
Cdd:cd03246 153 AHRPETL-ASADRILVLEDGRV 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
300-481 |
5.79e-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: 74.08 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIAPKAEIGYFDQTGYKFTRN-------- 368
Cdd:cd03261 6 LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIvglLRPDSGEVLIDGEDISGLSEAELYRLRRrmgmlfqs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 369 ----------QNVMAYMQEGSDYSVPDIRA-VLSSMGFT--PEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGN 435
Cdd:cd03261 86 galfdsltvfENVAFPLREHTRLSEEEIREiVLEKLEAVglRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752069711 436 FLDIPAMEALETMMR----EYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03261 166 GLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
309-481 |
1.32e-14 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 72.67 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 309 ILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---------RDREEGVVIAPKAE---IGYFDQT-GYKFTRN--QNVMA 373
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILaglikessgSILLNGKPIKAKERrksIGYVMQDvDYQLFTDsvREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 YMQEGSDYSVPDIRAVLSSMGFTPEDVRKELSmLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYP 453
Cdd:cd03226 95 LGLKELDAGNEQAETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELA 173
|
170 180 190
....*....|....*....|....*....|.
gi 1752069711 454 G---TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03226 174 AqgkAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-195 |
1.46e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT--FAYIPQLEEA---------AVREVQDYALMGKLGI-SRV----- 94
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETvkLAYVDQSRDAldpnktvweEISGGLDIIKVGNREIpSRAyvgrf 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 95 ---------QAEIMSGGEETRLKIAQAL--EDNVhgIMADEPTSHLD----RAgidfLVSRLKLYTGALLIISHDRDLLD 159
Cdd:PRK11819 433 nfkggdqqkKVGVLSGGERNRLHLAKTLkqGGNV--LLLDEPTNDLDvetlRA----LEEALLEFPGCAVVISHDRWFLD 506
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752069711 160 RVADKI--WElKDGRITEYWGGYSDYlaqkEAERNRQL 195
Cdd:PRK11819 507 RIATHIlaFE-GDSQVEWFEGNFQEY----EEDKKRRL 539
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
305-481 |
1.61e-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: 72.60 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREEGVVIAPKA-EIGYFDQTGYKftRNQNVMA---------- 373
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEgEVLLDGKDIYD--LDVDVLElrrrvgmvfq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 --YMQEGSDYSvpDIRAVLSSMGFTPEDVRKE-----LSM---------------LSGGEIIKLQLARLLLGRYNILLLD 431
Cdd:cd03260 89 kpNPFPGSIYD--NVAYGLRLHGIKLKEELDErveeaLRKaalwdevkdrlhalgLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 432 EPGNFLDIPAMEALETMMREY--PGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-168 |
2.11e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 75.40 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRD-VLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI-------------ERQGTFAYI 69
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadadSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 70 PQL-------------------EEAAVRE-VQDYALMGKL-----GISRV---QAEIMSGGEETRLKIAQALEDNVHGIM 121
Cdd:TIGR02857 402 PQHpflfagtiaenirlarpdaSDAEIREaLERAGLDEFVaalpqGLDTPigeGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 122 ADEPTSHLDRAGIDFLVSRL-KLYTGA-LLIISHDRDLLdRVADKIWEL 168
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALrALAQGRtVLLVTHRLALA-ALADRIVVL 529
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-175 |
2.56e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.00 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEY----MGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIE----------------- 61
Cdd:COG1136 4 LLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 62 RQGTFAYIPQ----------LE-----------EAAVREVQDYALMGKLGIS-RVQAEI--MSGGEETRLKIAQALednV 117
Cdd:COG1136 84 RRRHIGFVFQffnllpeltaLEnvalplllagvSRKERRERARELLERVGLGdRLDHRPsqLSGGQQQRVAIARAL---V 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752069711 118 HG---IMADEPTSHLDRAG----IDFLVSRLKLYTGALLIISHDRDLLDRvADKIWELKDGRITE 175
Cdd:COG1136 161 NRpklILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
300-481 |
2.67e-14 |
|
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: 70.54 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIgYFDQTGYKFTrnqNVMAYMQEGs 379
Cdd:cd03216 6 ITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKIL----SGLYKPDSGEI-LVDGKEVSFA---SPRDARRAG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 380 dysvpdIRAVlssmgftpedvrkelSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYPG---TI 456
Cdd:cd03216 77 ------IAMV---------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAV 135
|
170 180
....*....|....*....|....*
gi 1752069711 457 VFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03216 136 IFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
298-482 |
3.77e-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: 71.40 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---------GVVIA--PKAE--IGYFDQTGYK 364
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpdsgeilidGRDVTgvPPERrnIGMVFQDYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 365 FTrNQNV---MAYMQEGSDYSVPDIRA----VLSSMGFTPEDVRKElSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFL 437
Cdd:cd03259 84 FP-HLTVaenIAFGLKLRGVPKAEIRArvreLLELVGLEGLLNRYP-HELSGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 438 DIPAMEALETMMREYPG----TIVFISHDTRLVERVADQVYVLKKGQLQ 482
Cdd:cd03259 162 DAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
305-481 |
3.82e-14 |
|
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: 70.32 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIAPKAEIGYFDQTGYKftrnQNVMAYMQEGS-- 379
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIlglLRPTSGRVRLDGADISQWDPNELG----DHVGYLPQDDElf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 380 DYSVPDIravlssmgftpedvrkelsMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALET---MMREYPGTI 456
Cdd:cd03246 89 SGSIAEN-------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQaiaALKAAGATR 149
|
170 180
....*....|....*....|....*
gi 1752069711 457 VFISHDTRLVERvADQVYVLKKGQL 481
Cdd:cd03246 150 IVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
286-480 |
3.86e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.83 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 286 VLELHHplpvtgheLCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDreegvVIAPKA-EIGYFdqtGYK 364
Cdd:COG4152 1 MLELKG--------LTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILG-----ILAPDSgEVLWD---GEP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 365 FTR-NQNVMAYMqegsdysvPDIRAVLSSM-------------GFTPEDVRKELSM-----------------LSGGEII 413
Cdd:COG4152 65 LDPeDRRRIGYL--------PEERGLYPKMkvgeqlvylarlkGLSKAEAKRRADEwlerlglgdrankkveeLSKGNQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 414 KLQLARLLLGRYNILLLDEPgnF--LDIPAMEALETMMREY--PG-TIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:COG4152 137 KVQLIAALLHDPELLILDEP--FsgLDPVNVELLKDVIRELaaKGtTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
300-481 |
4.29e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 71.70 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDRE---EGVVIAPKAEIgyfdqTGYK------------ 364
Cdd:cd03219 6 LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrptSGSVLFDGEDI-----TGLPpheiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 365 ---------FTRNQNVM--AYMQEGSDYS-----------VPDIRAVLSSMGFTpeDVRKEL-SMLSGGEIIKLQLARLL 421
Cdd:cd03219 81 fqiprlfpeLTVLENVMvaAQARTGSGLLlararreereaRERAEELLERVGLA--DLADRPaGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 422 LGRYNILLLDEPG---NFLDIPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03219 159 ATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
305-473 |
4.52e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 74.44 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDReegvvIAPKAEIGYFDQTGYKFTRNQNVMAYMQEGSDYSVP 384
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNE-----ISADGGSYTFPGNWQLAWVNQETPALPQPALEYVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 385 DIR-----------------------------------------AVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLG 423
Cdd:PRK10636 87 GDReyrqleaqlhdanerndghaiatihgkldaidawtirsraaSLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALIC 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752069711 424 RYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISHDTRLVERVADQV 473
Cdd:PRK10636 167 RSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
310-476 |
5.16e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 74.25 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVI---APKAE---------IGYFDQTGYKF--TRNQNVM 372
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLlgfVDPTEGSIAvngVPLADadadswrdqIAWVPQHPFLFagTIAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 373 AYMQEGSDysvPDIRAVLSSMGFT------PEDVRKEL----SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAM 442
Cdd:TIGR02857 418 LARPDASD---AEIREALERAGLDefvaalPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 1752069711 443 EALETMMREYPG--TIVFISHDTRLVERvADQVYVL 476
Cdd:TIGR02857 495 AEVLEALRALAQgrTVLLVTHRLALAAL-ADRIVVL 529
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-161 |
6.91e-14 |
|
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: 70.59 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT------------FAYIP 70
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrrrLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 71 Q---------LEE-----AAVREVQD-----YALMGKLGISR---VQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSH 128
Cdd:COG4133 82 HadglkpeltVREnlrfwAALYGLRAdreaiDEALEAVGLAGladLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1752069711 129 LDRAGIDFLVSRLKLYT---GALLIISHDRDLLDRV 161
Cdd:COG4133 162 LDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
302-481 |
9.55e-14 |
|
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: 72.45 E-value: 9.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 302 KQLGDkVILDrVSFQFPLGGKIAITGGNGAGKTTLLNMI------------------RDREEGVVIAP-KAEIGYFDQ-- 360
Cdd:TIGR02142 7 KRLGD-FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIagltrpdegeivlngrtlFDSRKGIFLPPeKRRIGYVFQea 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 361 ---TGYKFTRNQNVMAYMQEGSDYSVPDIRaVLSSMGFTPEdVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFL 437
Cdd:TIGR02142 85 rlfPHLSVRGNLRYGMKRARPSERRISFER-VIELLGIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752069711 438 DIPA----MEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:TIGR02142 163 DDPRkyeiLPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
307-477 |
1.14e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 307 KVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREEGvviapKAEIGYFDQTGYKFTRNQNVMAymQEGSDYSVPDI 386
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG-----TPVAGCVDVPDNQFGREASLID--AIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 387 RAVLSSMGF-TPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIP-AME---ALETMMREYPGTIVFISH 461
Cdd:COG2401 116 VELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtAKRvarNLQKLARRAGITLVVATH 195
|
170
....*....|....*.
gi 1752069711 462 DTRLVERVADQVYVLK 477
Cdd:COG2401 196 HYDVIDDLQPDLLIFV 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-173 |
1.25e-13 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 69.55 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 13 YMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGK---------------------IERQGTFAY--- 68
Cdd:cd03268 10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEitfdgksyqkniealrrigalIEAPGFYPNlta 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 69 ---------IPQLEEAAVREVQDYALMGKLGISRVQAeiMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDF--- 136
Cdd:cd03268 90 renlrllarLLGIRKKRIDEVLDVVGLKDSAKKKVKG--FSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKElre 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1752069711 137 LVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03268 168 LILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
299-481 |
1.38e-13 |
|
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: 69.71 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 299 ELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRD-----------------REEGVViapKAEIGYFDQ- 360
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllkptsgratvaghdvvREPREV---RRRIGIVFQd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 361 -------TGYkftrnQNVmaYMQeGSDYSVPD------IRAVLSSMGFTpeDVRKEL-SMLSGGEIIKLQLARLLLGRYN 426
Cdd:cd03265 82 lsvddelTGW-----ENL--YIH-ARLYGVPGaerrerIDELLDFVGLL--EAADRLvKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 427 ILLLDEPGNFLDIPAM----EALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03265 152 VLFLDEPTIGLDPQTRahvwEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
305-485 |
1.60e-13 |
|
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: 69.84 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---GVVI-----------APKAEIGY---FDQTGYKFTR 367
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRptsGTAYingysirtdrkAARQSLGYcpqFDALFDELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 368 NQNVMAYMQ----EGSDYSVpDIRAVLSSMGFTpeDVRKEL-SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPAM 442
Cdd:cd03263 93 REHLRFYARlkglPKSEIKE-EVELLLRVLGLT--DKANKRaRTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PAS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 443 -----EALETMMREYpgTIVFISHDTRLVERVADQVYVLKKGQL------QRLK 485
Cdd:cd03263 169 rraiwDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLrcigspQELK 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
310-481 |
1.84e-13 |
|
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: 69.54 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVV---------IAP---KAEIGYFDQTGYKF--TRNQNVM 372
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLaglYKPTSGSVlldgtdirqLDPadlRRNIGYVPQDVTLFygTLRDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 373 AYMQEGSDYSVpdIRAV----------LSSMGFTPEdVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAM 442
Cdd:cd03245 100 LGAPLADDERI--LRAAelagvtdfvnKHPNGLDLQ-IGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1752069711 443 EALETMMREYPG--TIVFISHDTRLVErVADQVYVLKKGQL 481
Cdd:cd03245 177 ERLKERLRQLLGdkTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-173 |
1.84e-13 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 70.14 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-FAYIPQLEEAAVREV 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLdDVS-LTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRpLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 81 --QDYAL-----------MGKLGISRVQAEI-----------------------MSGGEETRLKIAQAL------EDNVH 118
Cdd:COG4559 80 lpQHSSLafpftveevvaLGRAPHGSSAAQDrqivrealalvglahlagrsyqtLSGGEQQRVQLARVLaqlwepVDGGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 119 GI-MADEPTSHLD--------RagidfLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:COG4559 160 RWlFLDEPTSALDlahqhavlR-----LARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
284-483 |
1.85e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 69.69 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 284 SEVLELHHplpvtgheLCKQLGDK----VILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI--RDR-EEGVVI------- 349
Cdd:COG1136 2 SPLLELRN--------LTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggLDRpTSGEVLidgqdis 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 350 -APKAE--------IGYFDQTGY---KFTRNQNVM---AYMQEGSDYSVPDIRAVLSSMGFtpEDVRKEL-SMLSGGEii 413
Cdd:COG1136 74 sLSERElarlrrrhIGFVFQFFNllpELTALENVAlplLLAGVSRKERRERARELLERVGL--GDRLDHRpSQLSGGQ-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 414 kLQ---LARLLLGRYNILLLDEP-GNfLD------IpaMEALETMMREYPGTIVFISHDTRLVERvADQVYVLKKGQLQR 483
Cdd:COG1136 150 -QQrvaIARALVNRPKLILADEPtGN-LDsktgeeV--LELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
254-462 |
2.80e-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: 72.01 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 254 HTAARQMQRRIEALDGVSAPEELwsVQFYHSEVLELHHPLPVTGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGK 333
Cdd:TIGR02868 297 LTRVRAAAERIVEVLDAAGPVAE--GSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGK 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 334 TTLLNMI---RDREEGVVI------------APKAEIGYFDQTGYKF--TRNQNVMAYMQEGSDysvPDIRAVLSSMGF- 395
Cdd:TIGR02868 375 STLLATLaglLDPLQGEVTldgvpvssldqdEVRRRVSVCAQDAHLFdtTVRENLRLARPDATD---EELWAALERVGLa 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 396 -----TPEDVRKEL----SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEA-LETMMREYPG-TIVFISHD 462
Cdd:TIGR02868 452 dwlraLPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADElLEDLLAALSGrTVVLITHH 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-175 |
2.90e-13 |
|
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: 71.86 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRD------VLDIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI---------------- 60
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvraVDDVS-LTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklsrrslr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 61 ERQGTFAYIPQ---------------LEEAAV-------REVQD--YALMGKLGISRVQAEI----MSGGEETRLKIAQA 112
Cdd:COG1123 339 ELRRRVQMVFQdpysslnprmtvgdiIAEPLRlhgllsrAERRErvAELLERVGLPPDLADRypheLSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 113 LednVHG---IMADEPTSHLD---RAGI-DFLVS---RLKLytgALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:COG1123 419 L---ALEpklLILDEPTSALDvsvQAQIlNLLRDlqrELGL---TYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
298-483 |
3.73e-13 |
|
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: 68.37 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPlGGKIAITGGNGAGKTTLLNM-----------IRDREEGVVIAPK---AEIGYFDQ--- 360
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRIlatltppssgtIRIDGQDVLKQPQklrRRIGYLPQefg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 361 -----TGYKFTrnqNVMAYMQEGSDYSVPD-IRAVLSSMGFTpeDVRKE-LSMLSGGEIIKLQLARLLLGRYNILLLDEP 433
Cdd:cd03264 83 vypnfTVREFL---DYIAWLKGIPSKEVKArVDEVLELVNLG--DRAKKkIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 434 GNFLDIPAMEALETMMREY-PGTIVFIS-HDTRLVERVADQVYVLKKGQLQR 483
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
306-482 |
6.39e-13 |
|
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: 68.13 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---------RDREEGVViaP-KAEIGYFDQTGYKF-TRNQ----- 369
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILsgllqptsgEVRVAGLV--PwKRRKKFLRRIGVVFgQKTQlwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 370 ------NVMAYMqegsdYSVPDIRAV-----LSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD 438
Cdd:cd03267 111 pvidsfYLLAAI-----YDLPPARFKkrldeLSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752069711 439 IPAMEA----LETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQLQ 482
Cdd:cd03267 186 VVAQENirnfLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-173 |
7.46e-13 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 67.51 E-value: 7.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 19 LDIDRLELYAydrigLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT------------------------FAYIPQL-- 72
Cdd:cd03255 25 LSIEKGEFVA-----IVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhigfvfqsFNLLPDLta 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 73 ------------EEAAVREVQDYALMGKLGIS-----RVQAeiMSGGEETRLKIAQALEDNVHGIMADEPTSHLD----R 131
Cdd:cd03255 100 lenvelplllagVPKKERRERAEELLERVGLGdrlnhYPSE--LSGGQQQRVAIARALANDPKIILADEPTGNLDsetgK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1752069711 132 AGIDFLVSRLKLYTGALLIISHDRDLLDRvADKIWELKDGRI 173
Cdd:cd03255 178 EVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-174 |
7.82e-13 |
|
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: 67.60 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAyDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG------------TFAYIPQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 ----LEEAAVREVQDY-ALMGKLGISRVQAEI-------------------MSGGEETRLKIAQALEDNVHGIMADEPTS 127
Cdd:cd03264 80 efgvYPNFTVREFLDYiAWLKGIPSKEVKARVdevlelvnlgdrakkkigsLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 128 HLD---RAGIDFLVSRLKlyTGALLIIS-HDRDLLDRVADKIWELKDGRIT 174
Cdd:cd03264 160 GLDpeeRIRFRNLLSELG--EDRIVILStHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
313-482 |
1.02e-12 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 67.32 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 313 VSFQFPlGGKIAITGGNGAGKTTLLNMIR------------------DREEGVVIAP-KAEIGYFDQTGYKFTR---NQN 370
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAglekpdggtivlngtvlfDSRKKINLPPqQRKIGLVFQQYALFPHlnvREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 371 VMAYMQEGSDYSVPD-IRAVLSSMGFTPEDVRKeLSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMM 449
Cdd:cd03297 96 LAFGLKRKRNREDRIsVDELLDLLGLDHLLNRY-PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1752069711 450 RE----YPGTIVFISHDTRLVERVADQVYVLKKGQLQ 482
Cdd:cd03297 175 KQikknLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
305-482 |
1.02e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.80 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR--DR-EEGVV-----IAPKAEIG---YFDQTGYkftrnQNVMa 373
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAgiLEpTSGRVevngrVSALLELGagfHPELTGR-----ENIY- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 ymqegsdysvpdIRAVLssMGFTPEDVRK---------ELsmlsgGEIIKLQL--------ARLLLG-----RYNILLLD 431
Cdd:COG1134 111 ------------LNGRL--LGLSRKEIDEkfdeivefaEL-----GDFIDQPVktyssgmrARLAFAvatavDPDILLVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 432 EpgnFL---DIP----AMEALETMMREyPGTIVFISHDTRLVERVADQVYVLKKGQLQ 482
Cdd:COG1134 172 E---VLavgDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
300-482 |
1.09e-12 |
|
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: 67.75 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-------------RDREEGVVIAPKAEIGYFDQTGYKF- 365
Cdd:cd03296 8 VSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIaglerpdsgtilfGGEDATDVPVQERNVGFVFQHYALFr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 366 --TRNQNVMAYMQEGSDYSVPD-------IRAVLSSMGFTPEDVRKElSMLSGGEIIKLQLARLLLGRYNILLLDEPGNF 436
Cdd:cd03296 88 hmTVFDNVAFGLRVKPRSERPPeaeirakVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752069711 437 LDIPAMEALETMMREYPG----TIVFISHDTRLVERVADQVYVLKKGQLQ 482
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-127 |
1.14e-12 |
|
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: 65.36 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 19 LDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-------------FAYIPQLEE----------- 74
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeIGYVFQDPQlfprltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 75 ----------AAVREVQDYALMGKLGIS-------RVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTS 127
Cdd:pfam00005 81 rlglllkglsKREKDARAEEALEKLGLGdladrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
305-481 |
1.18e-12 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 67.17 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreeGVVIAPKaeigyfdqTGyKFTRNQNVMAYMQEGS----D 380
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLL-----AGIYPPD--------SG-TVTVRGRVSSLLGLGGgfnpE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 381 YSVPD-IRAVLSSMGFTPEDVRK---ELSMLSG-GEIIKLQL--------ARLLLG-----RYNILLLDEPG-----NFL 437
Cdd:cd03220 99 LTGREnIYLNGRLLGLSRKEIDEkidEIIEFSElGDFIDLPVktyssgmkARLAFAiatalEPDILLIDEVLavgdaAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752069711 438 DiPAMEALETMMREyPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03220 179 E-KCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
299-481 |
1.21e-12 |
|
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: 66.86 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 299 ELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIGYFDQtgyKFTRNQNVMAYMqeG 378
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII----LGLIKPDSGEITFDGK---SYQKNIEALRRI--G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 379 SDYSVP------------------------DIRAVLSSMGFTPEDVRKeLSMLSGGEIIKLQLARLLLGRYNILLLDEPG 434
Cdd:cd03268 76 ALIEAPgfypnltarenlrllarllgirkkRIDEVLDVVGLKDSAKKK-VKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752069711 435 NFLD---IPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03268 155 NGLDpdgIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
5-165 |
1.37e-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: 69.81 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 5 KAEEIVVEY------MGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYIPQ-LE---E 74
Cdd:COG1245 336 KEEETLVEYpdltksYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQyISpdyD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 75 AAVREVQDYALMGKLGISRVQAEIM----------------SGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGID 135
Cdd:COG1245 416 GTVEEFLRSANTDDFGSSYYKTEIIkplgleklldknvkdlSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVA 495
|
170 180 190
....*....|....*....|....*....|.
gi 1752069711 136 FLVSRLKLYTGA-LLIISHDRDLLDRVADKI 165
Cdd:COG1245 496 KAIRRFAENRGKtAMVVDHDIYLIDYISDRL 526
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
99-480 |
1.37e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 99 MSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRIT 174
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDvsvQAQILQLLRELQQELNmGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 175 EywggysdylaqkeaernrqlaqyqqaeaererleqaisekkvqarrldqksraagknstesggrlahqksQGSKQKKLH 254
Cdd:PRK15134 237 E----------------------------------------------------------------------QNRAATLFS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 255 TAARQMQRRIEALDGVSAPEELWSVQFYHSEVLELHHPLPVTGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGK- 333
Cdd:PRK15134 247 APTHPYTQKLLNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKs 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 334 TTLLNMIRdreegvVIAPKAEIGYFDQTGYKFTRNQ-----------------------NVMAYMQEGSDYSVPDIRA-- 388
Cdd:PRK15134 327 TTGLALLR------LINSQGEIWFDGQPLHNLNRRQllpvrhriqvvfqdpnsslnprlNVLQIIEEGLRVHQPTLSAaq 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 389 -------VLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD--IPA--MEALETMMREYPGTIV 457
Cdd:PRK15134 401 reqqviaVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAqiLALLKSLQQKHQLAYL 480
|
410 420
....*....|....*....|...
gi 1752069711 458 FISHDTRLVERVADQVYVLKKGQ 480
Cdd:PRK15134 481 FISHDLHVVRALCHQVIVLRQGE 503
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
303-480 |
1.46e-12 |
|
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: 67.07 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 303 QLGDKVI--LDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-------------RDREEGVVIAP----------KAEIGY 357
Cdd:COG4778 18 LQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdsgsilvRHDGGWVDLAQaspreilalrRRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 358 FDQtgykFTRnqnvmaymqegsdySVPDIRAV------LSSMGFTPEDVRKE----LSML--------------SGGEII 413
Cdd:COG4778 98 VSQ----FLR--------------VIPRVSALdvvaepLLERGVDREEARARarelLARLnlperlwdlppatfSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 414 KLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYP--GT-IVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKarGTaIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
305-481 |
2.12e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 69.04 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-R--DREEGVV---------IAPKA---EIGYFDQTGYKFTRN- 368
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLlRfyDPTSGRIlidgvdirdLTLESlrrQIGVVPQDTFLFSGTi 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 369 -QNVmAYMQEgsDYSVPDIRAVLSSMGFTpEDVRK-------EL----SMLSGGEIIKLQLARLLLGRYNILLLDEPGNF 436
Cdd:COG1132 431 rENI-RYGRP--DATDEEVEEAAKAAQAH-EFIEAlpdgydtVVgergVNLSGGQRQRIAIARALLKDPPILILDEATSA 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 437 LDiPAME-----ALETMMREYpgTIVFISHdtRL--VERvADQVYVLKKGQL 481
Cdd:COG1132 507 LD-TETEaliqeALERLMKGR--TTIVIAH--RLstIRN-ADRILVLDDGRI 552
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
30-173 |
2.71e-12 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 66.44 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 30 DRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfaYIPQLEEAAVREV--------QDYA-----------LMGKLG 90
Cdd:cd03256 28 EFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--DINKLKGKALRQLrrqigmifQQFNlierlsvlenvLSGRLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 91 -----------------------ISRVQ--------AEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD----RAGID 135
Cdd:cd03256 106 rrstwrslfglfpkeekqralaaLERVGlldkayqrADQLSGGQQQRVAIARALMQQPKLILADEPVASLDpassRQVMD 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1752069711 136 FLVsRLKLYTGALLIIS-HDRDLLDRVADKIWELKDGRI 173
Cdd:cd03256 186 LLK-RINREEGITVIVSlHQVDLAREYADRIVGLKDGRI 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
286-481 |
3.93e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 66.22 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 286 VLELHHplpvtgheLCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGvVIAPKA-EIGYFDQ--TG 362
Cdd:COG0411 4 LLEVRG--------LTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLI----TG-FYRPTSgRILFDGRdiTG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 363 ---YKFTRN------------------QNVMAYMQEGSDYSVPD------------------IRAVLSSMGFtpEDVRKE 403
Cdd:COG0411 71 lppHRIARLgiartfqnprlfpeltvlENVLVAAHARLGRGLLAallrlprarreerearerAEELLERVGL--ADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 404 L-SMLSGGEIIKLQLARLLLGRYNILLLDEPG---NFLDIPAMEALETMMREYPG-TIVFISHDTRLVERVADQVYVLKK 478
Cdd:COG0411 149 PaGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDF 228
|
...
gi 1752069711 479 GQL 481
Cdd:COG0411 229 GRV 231
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-173 |
4.51e-12 |
|
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: 65.76 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT--------------FAYI 69
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithlpmherarlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 70 PQ-----------------LE-----EAAVREVQDYALMGKLGISRVQ---AEIMSGGEETRLKIAQALEDNVHGIMADE 124
Cdd:TIGR04406 82 PQeasifrkltveenimavLEirkdlDRAEREERLEALLEEFQISHLRdnkAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 125 PTshldrAGID--------FLVSRLKLYTGALLIISHD-RDLLDrVADKIWELKDGRI 173
Cdd:TIGR04406 162 PF-----AGVDpiavgdikKIIKHLKERGIGVLITDHNvRETLD-ICDRAYIISDGKV 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
302-480 |
6.88e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.82 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 302 KQLGDKVIldRVSFQFPLGGKIAITGGNGAGKTTLLNMIR------------------DREEGVVIAP-KAEIGYFDQTG 362
Cdd:PRK11144 8 QQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISgltrpqkgrivlngrvlfDAEKGICLPPeKRRIGYVFQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 363 YKFTrNQNVMAYMQEG-SDYSVPDIRAVLSSMGFTPEDVRKELSmLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIP- 440
Cdd:PRK11144 86 RLFP-HYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYPGS-LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPr 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1752069711 441 ---AMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:PRK11144 164 kreLLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
300-481 |
7.99e-12 |
|
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: 64.87 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIgYFDQ---TGYK-FTRNQNVMAYM 375
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMI----VGLVKPDSGKI-LLDGqdiTKLPmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 376 -QEGS---DYSVPD-IRAVLSSMGFTPEDVRKEL-----------------SMLSGGEIIKLQLARLLLGRYNILLLDEP 433
Cdd:cd03218 81 pQEASifrKLTVEEnILAVLEIRGLSKKEREEKLeelleefhithlrkskaSSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 434 GNFLDIPAMEALETMMREYP--GTIVFIS-HDTRLVERVADQVYVLKKGQL 481
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKdrGIGVLITdHNVRETLSITDRAYIIYEGKV 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
305-481 |
8.10e-12 |
|
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: 64.83 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIAPKAEIGYFDQTGYKFTRN------QNVMAYM 375
Cdd:cd03257 16 GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAIlglLKPTSGSIIFDGKDLLKLSRRLRKIRRKeiqmvfQDPMSSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 376 -----------------QEGSDYSVPDIRAVLSSMGFT-PEDVRKEL-SMLSGGEiikLQ---LARLLLGRYNILLLDEP 433
Cdd:cd03257 96 nprmtigeqiaeplrihGKLSKKEARKEAVLLLLVGVGlPEEVLNRYpHELSGGQ---RQrvaIARALALNPKLLIADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 434 GNFLDIPA----MEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03257 173 TSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
305-481 |
8.86e-12 |
|
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: 64.11 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREEGVVIapKAEIGYFDQTGYKFTrnqnvmaymqegsdysvp 384
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV--SGEVLINGRPLDKRS------------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 385 dIRAvlsSMGFTPED--------VRK------ELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPAMEA--LETM 448
Cdd:cd03213 80 -FRK---IIGYVPQDdilhptltVREtlmfaaKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD-SSSALqvMSLL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1752069711 449 MREYPG--TIVFISHDTR-LVERVADQVYVLKKGQL 481
Cdd:cd03213 155 RRLADTgrTIICSIHQPSsEIFELFDKLLLLSQGRV 190
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-173 |
9.09e-12 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 64.70 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT------------FAYIPQ 71
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 ----LEEAAVREVQDYalMGKL-GISRVQAEI---------------------MSGGEETRLKIAQALednVHG---IMA 122
Cdd:COG1131 81 epalYPDLTVRENLRF--FARLyGLPRKEAREridellelfgltdaadrkvgtLSGGMKQRLGLALAL---LHDpelLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 123 DEPTSHLDRAGIDF---LVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:COG1131 156 DEPTSGLDPEARRElweLLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-173 |
1.16e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.79 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLD-IDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-FAYIPQLEEAAVREV 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDdVS-LTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 81 --QDYAL-----------MGK--LGISRVQ-----AEIM----------------SGGEETRLKIAQAL-----EDNVHG 119
Cdd:PRK13548 81 lpQHSSLsfpftveevvaMGRapHGLSRAEddalvAAALaqvdlahlagrdypqlSGGEQQRVQLARVLaqlwePDGPPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 120 I-MADEPTSHLD--------RagidfLVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:PRK13548 161 WlLLDEPTSALDlahqhhvlR-----LARQLAHERGlAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-173 |
1.28e-11 |
|
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: 64.49 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT------------FAYIP 70
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvrkeprearrqIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 71 Q---------LEE-----AAVREVQD-------YALMGKLGISRVQ---AEIMSGGEETRLKIAQALEDNVHGIMADEPT 126
Cdd:COG4555 81 DerglydrltVREniryfAELYGLFDeelkkriEELIELLGLEEFLdrrVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 127 SHLD----RAGIDFLVsRLKLYTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:COG4555 161 NGLDvmarRLLREILR-ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
305-481 |
1.36e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.65 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-RdreegvVIAPKA-EIGYFDQTGYKFTRNQ------------- 369
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFaR------LLTPQSgTVFLGDKPISMLSSRQlarrlallpqhhl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 370 --------NVMAYMQegSDY-------SVPDIRAVLSSMGFTPED--VRKELSMLSGGEIIKLQLARLLLGRYNILLLDE 432
Cdd:PRK11231 87 tpegitvrELVAYGR--SPWlslwgrlSAEDNARVNQAMEQTRINhlADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 433 PGNFLDIPAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
302-479 |
1.63e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.62 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 302 KQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-----RDREEGVVI---------APKAEIGY---FDQTGYK 364
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIlgmtsPDAGKITVLgvpvpararLARARIGVvpqFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 365 FTRNQNVMAYmqegSDY---SVPDIRAVLSS-MGF----TPEDVRkeLSMLSGGEIIKLQLARLLLGRYNILLLDEPGNF 436
Cdd:PRK13536 129 FTVRENLLVF----GRYfgmSTREIEAVIPSlLEFarleSKADAR--VSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752069711 437 LDIPAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKG 479
Cdd:PRK13536 203 LDPHARHLIWERLRSLLArgkTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
308-481 |
1.83e-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: 63.54 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 308 VILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPK--AEIGYFDQTGYKFTRNQNVMAYMQEGSDYSVPD 385
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRML----AGLLEPDAgfATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 386 IRAVLSSMG---------FTP--EDVRKELSM----------LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEA 444
Cdd:cd03266 95 ARENLEYFAglyglkgdeLTArlEELADRLGMeelldrrvggFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1752069711 445 LETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03266 175 LREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
34-248 |
1.94e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.73 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYIPQL-----------------EEAA-----VREVQDYALMGKLGi 91
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQawimnatvrgnilffdeEDAArladaVRVSQLEADLAQLG- 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 92 SRVQAEI------MSGGEETRLKIAQALEDNVHGIMADEPTSHLDrAGIDFLVSRlKLYTGAL-----LIISHDRDLLDR 160
Cdd:PTZ00243 770 GGLETEIgekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD-AHVGERVVE-ECFLGALagktrVLATHQVHVVPR 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 161 vADKIWELKDGRItEYWGGYSDYLAQ------KEAERNRQLAQYQQAEAERERLEQAISEKKVQARRLDQKSRAAG---- 230
Cdd:PTZ00243 848 -ADYVVALGDGRV-EFSGSSADFMRTslyatlAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEggdg 925
|
250 260
....*....|....*....|
gi 1752069711 231 KNSTESGGRL--AHQKSQGS 248
Cdd:PTZ00243 926 AALDAAAGRLmtREEKASGS 945
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-200 |
2.03e-11 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 66.40 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 15 GRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIE---------------RQgtFAYIPQ---LEEAA 76
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpaslrRQ--IGVVLQdvfLFSGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 77 VRE--------VQDYALMGKLGISRVQAEIM-----------------SGGEETRLKIAQALednVHG---IMADEPTSH 128
Cdd:COG2274 565 IREnitlgdpdATDEEIIEAARLAGLHDFIEalpmgydtvvgeggsnlSGGQRQRLAIARAL---LRNpriLILDEATSA 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 129 LDRAGIDFLVSRLKLYTG--ALLIISHDRDLLdRVADKIWELKDGRITEYwGGYSDYLAQKeaERNRQLAQYQQ 200
Cdd:COG2274 642 LDAETEAIILENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRIVED-GTHEELLARK--GLYAELVQQQL 711
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-177 |
2.05e-11 |
|
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: 63.47 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 30 DRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-----------------FAYIPQleEAA------VREVQDYALM 86
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQ--QYAlfphlnVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 87 GKL-GISRVQAEIM-----------------SGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG----IDFLVSRLKLY 144
Cdd:cd03297 102 RKRnREDRISVDELldllgldhllnrypaqlSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNL 181
|
170 180 190
....*....|....*....|....*....|...
gi 1752069711 145 TGALLIISHDRDLLDRVADKIWELKDGRITEYW 177
Cdd:cd03297 182 NIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-173 |
2.16e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.09 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 31 RIGLVGANGAGKSTLLKTLLGRIPLQyGKIERQGT-------------FAYIPQ---------------------LEEAA 76
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRplsdwsaaelarhRAYLSQqqsppfampvfqylalhqpagASSEA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 77 VREV-----QDYALMGKLGISRVQaeiMSGGEETRLKIAQAL-----EDNVHG--IMADEPTSHLD---RAGIDFLVSRL 141
Cdd:COG4138 103 VEQLlaqlaEALGLEDKLSRPLTQ---LSGGEWQRVRLAAVLlqvwpTINPEGqlLLLDEPMNSLDvaqQAALDRLLREL 179
|
170 180 190
....*....|....*....|....*....|..
gi 1752069711 142 KLYTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:COG4138 180 CQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
305-483 |
2.34e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 63.53 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRdREE----GVVI--------APKAEIGYF-------------- 358
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLY-GEErptsGQVLvngqdlsrLKRREIPYLrrrigvvfqdfrll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 359 -DQTGYkftrnQNVMAYMQ-EGSDYSV--PDIRAVLSSMGFtpEDVRKEL-SMLSGGEIIKLQLARLLLGRYNILLLDEP 433
Cdd:COG2884 92 pDRTVY-----ENVALPLRvTGKSRKEirRRVREVLDLVGL--SDKAKALpHELSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752069711 434 -GNfLDiPA-----MEALETMMREypGTIVFI-SHDTRLVERVADQVYVLKKGQLQR 483
Cdd:COG2884 165 tGN-LD-PEtsweiMELLEEINRR--GTTVLIaTHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-172 |
2.62e-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: 63.01 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLL----GRIPLQY----------GKIERQG----TFAYIPQLEEAAVRE--VQDYALMGKLGISR 93
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPNSkggahdpkliREGEVRAqvklAFENANGKKYTITRSlaILENVIFCHQGESN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 94 VQAEIM----SGGEET------RLKIAQALEDNVHGIMADEPTSHLDRAGI-----DFLVSRLKLYTGALLIISHDRDLL 158
Cdd:cd03240 107 WPLLDMrgrcSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeeslaEIIEERKSQKNFQLIVITHDEELV 186
|
170
....*....|....*
gi 1752069711 159 DRvADKIWEL-KDGR 172
Cdd:cd03240 187 DA-ADHIYRVeKDGR 200
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
305-481 |
2.75e-11 |
|
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: 64.06 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRdreeGVVIAPKAEIGYFDQTGYKFTRNQ--------------- 369
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLL----GLEKPAQGTVSFRGQDLYQLDRKQrrafrrdvqlvfqds 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 370 --NVMAYMQEGSDYSVP--------------DIRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEP 433
Cdd:TIGR02769 98 psAVNPRMTVRQIIGEPlrhltsldeseqkaRIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 434 GNFLDI----PAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:TIGR02769 178 VSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-165 |
4.36e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYmGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYIPQLEEAAVRE-VQ 81
Cdd:PRK13409 340 LVEYPDLTKKL-GDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKPDYDGtVE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 82 DYaLM---GKLGISRVQAEIM----------------SGGEETRLKIAQALEDNVHGIMADEPTSHLD---RagidFLVS 139
Cdd:PRK13409 419 DL-LRsitDDLGSSYYKSEIIkplqlerlldknvkdlSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqR----LAVA 493
|
170 180 190
....*....|....*....|....*....|.
gi 1752069711 140 R-LKLYT----GALLIISHDRDLLDRVADKI 165
Cdd:PRK13409 494 KaIRRIAeereATALVVDHDIYMIDYISDRL 524
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-173 |
4.91e-11 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 62.52 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfaYIPQLEEAAVREV-- 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLkGVD-LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE--DISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 81 ------QDYAL----------------MGKLGISRVQAEIM-------------------SGGEETRLKIAQALEDNVHG 119
Cdd:cd03261 78 rmgmlfQSGALfdsltvfenvafplreHTRLSEEEIREIVLekleavglrgaedlypaelSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 120 IMADEPTSHLD--RAG-IDFLVSRLKLYTGA-LLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03261 158 LLYDEPTAGLDpiASGvIDDLIRSLKKELGLtSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
33-173 |
4.99e-11 |
|
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: 62.91 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 33 GLVGANGAGKSTLLKTLLGRIPLQYGKI-------------ERQGTFAYIPQLEEAAVR-EVQDYALMGKL--------- 89
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVdlagvdlhglsrrARARRVALVEQDSDTAVPlTVRDVVALGRIphrslwagd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 90 ----------GISRVQAE--------IMSGGEETRLKIAQALEDNVHGIMADEPTSHLD-RAGIDFL--VSRLKLYTGAL 148
Cdd:TIGR03873 111 sphdaavvdrALARTELShladrdmsTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDvRAQLETLalVRELAATGVTV 190
|
170 180
....*....|....*....|....*
gi 1752069711 149 LIISHDRDLLDRVADKIWELKDGRI 173
Cdd:TIGR03873 191 VAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
300-481 |
7.13e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 62.35 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKViLDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---------RDREEGVVIAP----KAEIGYFDQtGYKFT 366
Cdd:cd03299 6 LSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIagfikpdsgKILLNGKDITNlppeKRDISYVPQ-NYALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 367 RNQNV---MAY-------MQEGSDYSVPDIRAVLssmGFTPEDVRKELSmLSGGEIIKLQLARLLLGRYNILLLDEPGNF 436
Cdd:cd03299 84 PHMTVyknIAYglkkrkvDKKEIERKVLEIAEML---GIDHLLNRKPET-LSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 437 LDIPAMEALETMM----REYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03299 160 LDVRTKEKLREELkkirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-165 |
7.32e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 62.43 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 11 VEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG-TFAYIPQLEEAAVREVQDYALMGKL 89
Cdd:cd03237 7 KKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 90 GI----SRVQAEIM----------------SGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTG 146
Cdd:cd03237 87 KDfythPYFKTEIAkplqieqildrevpelSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|
gi 1752069711 147 A-LLIISHDRDLLDRVADKI 165
Cdd:cd03237 167 KtAFVVEHDIIMIDYLADRL 186
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
312-480 |
8.35e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.08 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 312 RVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIapkaeIGYFDQTGYK---------FTRN---------QN 370
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIagfLPPDSGRIL-----WNGQDLTALPpaerpvsmlFQENnlfphltvaQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 371 VMAYMQEGSDYSVPD---IRAVLSSMGFTPEDVRKElSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPAMEA--- 444
Cdd:COG3840 92 IGLGLRPGLKLTAEQraqVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPILLLDEPFSALD-PALRQeml 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752069711 445 --LETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:COG3840 170 dlVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
311-483 |
9.40e-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: 61.08 E-value: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 311 DRVSFQFpLGGKIAITGGNGAGKTTLL----------------------NMIRDREEGVVIapkaEIGYFDQTG--YKFT 366
Cdd:cd03240 14 ERSEIEF-FSPLTLIVGQNGAGKTTIIealkyaltgelppnskggahdpKLIREGEVRAQV----KLAFENANGkkYTIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 367 RNQNVMAYM----QEGSDYSVPDIRAvlssmgftpedvrkelsMLSGGE------IIKLQLARLLLGRYNILLLDEPGNF 436
Cdd:cd03240 89 RSLAILENVifchQGESNWPLLDMRG-----------------RCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 437 LDIPAME-ALETMMREYPGTIVF----ISHDTRLVERvADQVYVLKKGQLQR 483
Cdd:cd03240 152 LDEENIEeSLAEIIEERKSQKNFqlivITHDEELVDA-ADHIYRVEKDGRQK 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
312-481 |
1.00e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 61.35 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 312 RVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE----GVVI-------APKAE--IGYFDQTGYKF---TRNQNVMAYM 375
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETpqsgRVLIngvdvtaAPPADrpVSMLFQENNLFahlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 376 QEGSDYSVPD---IRAVLSSMGFTPEDVRKElSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPAMEA-----LET 447
Cdd:cd03298 96 SPGLKLTAEDrqaIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALD-PALRAemldlVLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 1752069711 448 MMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
255-483 |
1.18e-10 |
|
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: 63.61 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 255 TAARQMQRRIEALDGVSAPEElwsvqfyhsEVLELhhPLPvTGHELCKQL------GDKVILDRVSFQFPLGGKIAITGG 328
Cdd:COG4618 299 VSARQAYRRLNELLAAVPAEP---------ERMPL--PRP-KGRLSVENLtvvppgSKRPILRGVSFSLEPGEVLGVIGP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 329 NGAGKTTLLNMI---------RDREEGVVIA--PKAE----IGY-------FDqtGykfTRNQNVmAYMQEGSDYSVpdI 386
Cdd:COG4618 367 SGSGKSTLARLLvgvwpptagSVRLDGADLSqwDREElgrhIGYlpqdvelFD--G---TIAENI-ARFGDADPEKV--V 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 387 RA-------------------VLSSMGftpedvrkelSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALET 447
Cdd:COG4618 439 AAaklagvhemilrlpdgydtRIGEGG----------ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA 508
|
250 260 270
....*....|....*....|....*....|....*....
gi 1752069711 448 M---MREYPGTIVFISHDTRLVeRVADQVYVLKKGQLQR 483
Cdd:COG4618 509 AiraLKARGATVVVITHRPSLL-AAVDKLLVLRDGRVQA 546
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
306-476 |
1.21e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIGYFDQT---------------GYKFTRNQN 370
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLI----AGLLNPEKGEILFERQSikkdlctyqkqlcfvGHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 371 VMayMQEGSDYsvpDIRAVLSSMGFTpEDVR---------KELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA 441
Cdd:PRK13540 89 LT--LRENCLY---DIHFSPGAVGIT-ELCRlfslehlidYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752069711 442 MEALETMMREYP---GTIVFISHDTRLVERVADQVYVL 476
Cdd:PRK13540 163 LLTIITKIQEHRakgGAVLLTSHQDLPLNKADYEEYHL 200
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
34-175 |
1.23e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 61.22 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLLGRIPLQYGKIE------RQGTFAYIPQLEeaavREV----QDYALMGKL-------------G 90
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlSRLKRREIPYLR----RRIgvvfQDFRLLPDRtvyenvalplrvtG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 91 ISR--VQAEIM-------------------SGGEETRLKIAQALednVHG---IMADEPTSHLDRAgidflVSR--LKLY 144
Cdd:COG2884 109 KSRkeIRRRVRevldlvglsdkakalphelSGGEQQRVAIARAL---VNRpelLLADEPTGNLDPE-----TSWeiMELL 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1752069711 145 -----TG-ALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:COG2884 181 eeinrRGtTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-173 |
1.47e-10 |
|
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: 61.07 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 14 MGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLL-------GRIPL------QYGKIERQGTFAYIPQ--------- 71
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAglykptsGSVLLdgtdirQLDPADLRRNIGYVPQdvtlfygtl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 ----------------LEEAAVREVQDYALMGKLGISRVQAE---IMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRA 132
Cdd:cd03245 95 rdnitlgapladderiLRAAELAGVTDFVNKHPNGLDLQIGErgrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1752069711 133 GIDFLVSRLKLYTG--ALLIISHDRDLLDrVADKIWELKDGRI 173
Cdd:cd03245 175 SEERLKERLRQLLGdkTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-175 |
1.58e-10 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 60.02 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 18 VLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfayIPQLEEAAVRE----------VQDYALMG 87
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV---PVSDLEKALSSlisvlnqrpyLFDTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 88 KLGISrvqaeiMSGGEETRLKIAQALEDNVHGIMADEPTSHLD----RAGIDFLVSRLKLYTgaLLIISHDRDLLDRVaD 163
Cdd:cd03247 94 NLGRR------FSGGERQRLALARILLQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLKDKT--LIWITHHLTGIEHM-D 164
|
170
....*....|..
gi 1752069711 164 KIWELKDGRITE 175
Cdd:cd03247 165 KILFLENGKIIM 176
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
298-340 |
1.64e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 61.25 E-value: 1.64e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI 340
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMI 47
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
34-173 |
2.06e-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: 60.50 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-----------------------FAYIPQL-----------------E 73
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraipylrrkigvvfqdFRLLPDRnvyenvafalevtgvppR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 74 EAAVREVQDYALMGKLGISRVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTGALLI 150
Cdd:cd03292 112 EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDpdtTWEIMNLLKKINKAGTTVVV 191
|
170 180
....*....|....*....|...
gi 1752069711 151 ISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03292 192 ATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-176 |
2.36e-10 |
|
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: 60.81 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 18 VLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-----------FAYIPQ--------------- 71
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQnyalfphmtvyknia 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 ------LEEAAVREVQDYALMGKLGISRV---QAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLK 142
Cdd:cd03299 94 yglkkrKVDKKEIERKVLEIAEMLGIDHLlnrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752069711 143 ----LYTGALLIISHDRDLLDRVADKIWELKDGRITEY 176
Cdd:cd03299 174 kirkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-191 |
2.59e-10 |
|
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: 60.63 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTF--------------AYI 69
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarlgiGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 70 PQ---------LEE--AAVREVQDY----------ALMGKLGISRVQ---AEIMSGGEETRLKIAQALEDNVHGIMADEP 125
Cdd:cd03218 81 PQeasifrkltVEEniLAVLEIRGLskkereekleELLEEFHITHLRkskASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752069711 126 TshldrAGID--------FLVSRLKLYTGALLIISHD-RDLLDrVADKIWELKDGRITEYwgGYSDYLAQKEAER 191
Cdd:cd03218 161 F-----AGVDpiavqdiqKIIKILKDRGIGVLITDHNvRETLS-ITDRAYIIYEGKVLAE--GTPEEIAANELVR 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
304-481 |
2.77e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.83 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 304 LGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE--GVVIAPKAEIGYFDQTGYKFT----RNQNVMAYMQE 377
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiyDSKIKVDGKVLYFGKDIFQIDaiklRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 378 G---------------SDYSVPDIRAV-------LSSMGFTPE---DVRKELSMLSGGEIIKLQLARLLLGRYNILLLDE 432
Cdd:PRK14246 100 NpfphlsiydniayplKSHGIKEKREIkkiveecLRKVGLWKEvydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 433 PGNFLDIPAMEALETMMREYPG--TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-191 |
3.41e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 1 MLLIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI---------------ERQGt 65
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplharARRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 66 FAYIPQleEAAV------------------------REVQDYALMGKLGISRVQ---AEIMSGGEETRLKIAQALEDNVH 118
Cdd:PRK10895 80 IGYLPQ--EASIfrrlsvydnlmavlqirddlsaeqREDRANELMEEFHIEHLRdsmGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752069711 119 GIMADEPTSHLDRAG---IDFLVSRLKLYTGALLIISHD-RDLLDrVADKIWELKDGRITEYwGGYSDYLAQKEAER 191
Cdd:PRK10895 158 FILLDEPFAGVDPISvidIKRIIEHLRDSGLGVLITDHNvRETLA-VCERAYIVSQGHLIAH-GTPTEILQDEHVKR 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
306-478 |
3.46e-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: 58.70 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRD----REEGVVIAPKAEIGYFDQTGYkftrnqnvmayMQEGSdy 381
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlwpwGSGRIGMPEGEDLLFLPQRPY-----------LPLGT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 382 svpdIRAVLSsmgFTPEDVrkelsmLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISH 461
Cdd:cd03223 80 ----LREQLI---YPWDDV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
170
....*....|....*..
gi 1752069711 462 DTRLvERVADQVYVLKK 478
Cdd:cd03223 147 RPSL-WKFHDRVLDLDG 162
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
306-481 |
3.60e-10 |
|
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: 59.79 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRD---REEGVVIAPKAEIGYFD------------QTGYKFTRN-Q 369
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfyqPQGGQVLLDGKPISQYEhkylhskvslvgQEPVLFARSlQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 370 NVMAY-MQEGSDYSVPDIRAVLSSMGFTPE-------DVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA 441
Cdd:cd03248 106 DNIAYgLQSCSFECVKEAAQKAHAHSFISElasgydtEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1752069711 442 MEALETMMREYPG--TIVFISHDTRLVERvADQVYVLKKGQL 481
Cdd:cd03248 186 EQQVQQALYDWPErrTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
292-479 |
3.73e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.78 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 292 PLPVTGheLCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR---DREEGVVIAPKAEIGYFDQTgykfTRN 368
Cdd:PRK09536 3 MIDVSD--LSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINgtlTPTAGTVLVAGDDVEALSAR----AAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 369 QNVMAYMQEGSDYSVPDIRAVLSsMGFTPEDVR--------------------------KELSMLSGGEIIKLQLARLLL 422
Cdd:PRK09536 77 RRVASVPQDTSLSFEFDVRQVVE-MGRTPHRSRfdtwtetdraaveramertgvaqfadRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 423 GRYNILLLDEPGNFLDIP-AMEALETMMR--EYPGTIVFISHDTRLVERVADQVYVLKKG 479
Cdd:PRK09536 156 QATPVLLLDEPTASLDINhQVRTLELVRRlvDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
300-483 |
4.09e-10 |
|
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: 61.27 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDkVILDrVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIGYFDQTGYKFTRNQNV------MA 373
Cdd:COG4148 7 FRLRRGG-FTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAI----AGLERPDSGRIRLGGEVLQDSARGIFLpphrrrIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 YM-QEGS-----------DYSVPdiRAVLSSMGFTPEDVRKEL----------SMLSGGEiiKlQ---LARLLLGRYNIL 428
Cdd:COG4148 81 YVfQEARlfphlsvrgnlLYGRK--RAPRAERRISFDEVVELLgighlldrrpATLSGGE--R-QrvaIGRALLSSPRLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 429 LLDEPGNFLDIPA----MEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQLQR 483
Cdd:COG4148 156 LMDEPLAALDLARkaeiLPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-197 |
4.81e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.41 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 13 YMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI---------ERQGTFAYIPQL----------- 72
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldySKRGLLALRQQVatvfqdpeqqi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 73 -------------------EEAAVREVQD-YALMGKLGISRVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRA 132
Cdd:PRK13638 91 fytdidsdiafslrnlgvpEAEITRRVDEaLTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 133 GIDFLVSRLKLYTGA---LLIISHDRDLLDRVADKIWELKDGRITEYwGGYSDYLAQKEAERNRQLAQ 197
Cdd:PRK13638 171 GRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQILTH-GAPGEVFACTEAMEQAGLTQ 237
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
388-485 |
5.47e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 388 AVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYPGTIVFISHDTRLVE 467
Cdd:PLN03073 326 SILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLN 405
|
90
....*....|....*...
gi 1752069711 468 RVADQVYVLKKGQLQRLK 485
Cdd:PLN03073 406 TVVTDILHLHGQKLVTYK 423
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
166-275 |
5.77e-10 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 55.66 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 166 WELKDGRITEYWGGYSDYLAQKEAERNRQLAQYQQAEAERERLEQAIsekkvqaRRLdqksraagknstesggrlahqKS 245
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFI-------DRF---------------------RA 52
|
90 100 110
....*....|....*....|....*....|
gi 1752069711 246 QGSKQKKlhtaARQMQRRIEALDGVSAPEE 275
Cdd:pfam12848 53 KASKAKQ----AQSRIKALEKMERIEKPER 78
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
305-484 |
5.94e-10 |
|
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: 59.62 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---------------RDREEGVVIAPKAEIGY-FDQTGY--KFT 366
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrlieptsgeifidgEDIREQDPVELRRKIGYvIQQIGLfpHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 367 RNQNVmAYMQEGSDYSVPDIRA----VLSSMGFTPEDVRKEL-SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA 441
Cdd:cd03295 92 VEENI-ALVPKLLKWPKEKIREradeLLALVGLDPAEFADRYpHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPIT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752069711 442 MEALE----TMMREYPGTIVFISHDTRLVERVADQVYVLKKGQLQRL 484
Cdd:cd03295 171 RDQLQeefkRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQV 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
32-173 |
6.12e-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: 58.72 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQY--------GKIERQGTF----AYIPQ----LEEAAVREvqdyALMgklgisrVQ 95
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGLGvsgevlinGRPLDKRSFrkiiGYVPQddilHPTLTVRE----TLM-------FA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 96 AEI--MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLY--TGALLIIS-HD-RDLLDRVADKIWELK 169
Cdd:cd03213 107 AKLrgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLadTGRTIICSiHQpSSEIFELFDKLLLLS 186
|
....
gi 1752069711 170 DGRI 173
Cdd:cd03213 187 QGRV 190
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-173 |
6.30e-10 |
|
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: 59.61 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfaYIPQLEEAAVREV- 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLdGVS-LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQ--DITGLSEKELYELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 81 -------QDYAL-----------------------------MGKL---GISRVQ----AEImSGGEETRLKIAQALEDNV 117
Cdd:COG1127 82 rrigmlfQGGALfdsltvfenvafplrehtdlseaeirelvLEKLelvGLPGAAdkmpSEL-SGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 118 HGIMADEPTSHLD---RAGIDFLVSRL-KLYTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:COG1127 161 EILLYDEPTAGLDpitSAVIDELIRELrDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-177 |
6.55e-10 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 59.12 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQY-----GKIE---------------- 61
Cdd:cd03260 1 IELRDLNVYYGDKHALkDIS-LDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLldgkdiydldvdvlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 62 --RQGT-F--------------AYIPQL--------EEAAVREVQDYALMGKLGISRVQAEIMSGGEETRLKIAQAL--E 114
Cdd:cd03260 80 rrRVGMvFqkpnpfpgsiydnvAYGLRLhgiklkeeLDERVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALanE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752069711 115 DNVhgIMADEPTSHLDRAG---IDFLVSRLKL-YTgaLLIISHDRDLLDRVADKIWELKDGRITEYW 177
Cdd:cd03260 160 PEV--LLLDEPTSALDPIStakIEELIAELKKeYT--IVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
299-484 |
6.60e-10 |
|
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: 59.17 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 299 ELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---------GVVIAP----KAEIGYFDQTGYKF 365
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETptsgeilldGKDITNlpphKRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 366 ---TRNQNVmAYMQEGSDYSVPDIRA-VLSSMGFT--PEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDI 439
Cdd:cd03300 85 phlTVFENI-AFGLRLKKLPKAEIKErVAEALDLVqlEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 440 PAMEA----LETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQLQRL 484
Cdd:cd03300 164 KLRKDmqleLKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQI 212
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-158 |
6.66e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTF--AYIPQ---LEEAAV 77
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQklyLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 78 REVQDYaLMGKLGI---------SRVQA--------EIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG------- 133
Cdd:PRK09544 84 LTVNRF-LRLRPGTkkedilpalKRVQAghlidapmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGqvalydl 162
|
170 180
....*....|....*....|....*
gi 1752069711 134 IDFLVSRLKLytgALLIISHDRDLL 158
Cdd:PRK09544 163 IDQLRRELDC---AVLMVSHDLHLV 184
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
307-481 |
6.91e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 307 KVILDRVSFQFPLGGKIAITGGNGAGKTTLL---NMIRDREEG------VVIAPKAEIGYFD------QTGYKFTRNQ-- 369
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlNRMNDKVSGyrysgdVLLGGRSIFNYRDvlefrrRVGMLFQRPNpf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 370 ------NVMAYMQEGSDYSVPDIRAV----LSSMGFTpEDVRKELS----MLSGGEIIKLQLARLLLGRYNILLLDEPGN 435
Cdd:PRK14271 114 pmsimdNVLAGVRAHKLVPRKEFRGVaqarLTEVGLW-DAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752069711 436 FLDIPAMEALETMMREYPG--TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-173 |
7.76e-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: 58.31 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 19 LDIDRLELYAydrigLVGANGAGKSTLLKTLLGRiPlQY----GKIERQGtfayipqlEEAAVREVQDYALMGkLGIS-R 93
Cdd:cd03217 21 LTIKKGEVHA-----LMGPNGSGKSTLAKTIMGH-P-KYevteGEILFKG--------EDITDLPPEERARLG-IFLAfQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 94 VQAEI---------------MSGGEETRLKIAQALEDNVHGIMADEPTSHLDragIDFL------VSRLKLYTGALLIIS 152
Cdd:cd03217 85 YPPEIpgvknadflryvnegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD---IDALrlvaevINKLREEGKSVLIIT 161
|
170 180
....*....|....*....|..
gi 1752069711 153 HDRDLLDRV-ADKIWELKDGRI 173
Cdd:cd03217 162 HYQRLLDYIkPDRVHVLYDGRI 183
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-172 |
8.48e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 58.98 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLG---------RIPLQYGKIE------------RQGTFAYIPQL------------------ 72
Cdd:COG4778 40 VALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDGGWVDlaqaspreilalRRRTIGYVSQFlrviprvsaldvvaepll 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 73 -----EEAAVREVQDyaLMGKLGISRVQAEI----MSGGEETRLKIAQALednvhgiMA-------DEPTSHLDRAGIDF 136
Cdd:COG4778 120 ergvdREEARARARE--LLARLNLPERLWDLppatFSGGEQQRVNIARGF-------IAdppllllDEPTASLDAANRAV 190
|
170 180 190
....*....|....*....|....*....|....*....
gi 1752069711 137 LVSRL--KLYTGALLI-ISHDRDLLDRVADKIWELKDGR 172
Cdd:COG4778 191 VVELIeeAKARGTAIIgIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
302-483 |
1.28e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.71 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 302 KQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-----------------------RDREEGVVIAPKA---EI 355
Cdd:PRK10851 10 KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIaglehqtsghirfhgtdvsrlhaRDRKVGFVFQHYAlfrHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 356 GYFDQTGYKFTrnqnVMAYMQEGSDYSVPDIRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGN 435
Cdd:PRK10851 90 TVFDNIAFGLT----VLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 436 FLDIPAMEALETMMR----EYPGTIVFISHDTRLVERVADQVYVLKKGQLQR 483
Cdd:PRK10851 166 ALDAQVRKELRRWLRqlheELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-176 |
1.31e-09 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 58.31 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 20 DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYIPQL-----EEAAVRE-VQDYALMgkLGISR 93
Cdd:cd03220 40 DVS-FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgggfnPELTGREnIYLNGRL--LGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 94 VQ-----------AEI----------MSGGEETRL--KIAQALEDNVhgIMADEPTSHLDRA----GIDFLVSRLKlYTG 146
Cdd:cd03220 117 KEidekideiiefSELgdfidlpvktYSSGMKARLafAIATALEPDI--LLIDEVLAVGDAAfqekCQRRLRELLK-QGK 193
|
170 180 190
....*....|....*....|....*....|
gi 1752069711 147 ALLIISHDRDLLDRVADKIWELKDGRITEY 176
Cdd:cd03220 194 TVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
296-451 |
1.41e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.96 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 296 TGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIGYFDQtGYKFTRNQNVMAYM 375
Cdd:PRK13539 4 EGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLI----AGLLPPAAGTIKLDGG-DIDDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 376 --QEG--SDYSV---------------PDIRAVLSSMGFTP-EDVRkeLSMLSGGEIIKLQLARLLLGRYNILLLDEPGN 435
Cdd:PRK13539 79 ghRNAmkPALTVaenlefwaaflggeeLDIAAALEAVGLAPlAHLP--FGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|....*.
gi 1752069711 436 FLDIPAMEALETMMRE 451
Cdd:PRK13539 157 ALDAAAVALFAELIRA 172
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
305-480 |
1.60e-09 |
|
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: 57.83 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIGYFDQ--TGYK-FTRNQNVMAYmqegsdy 381
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI----MGLLPPRSGSIRFDGRdiTGLPpHERARAGIGY------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 382 sVPDIRAVLSSM-----------GFTPEDVRKELSM------------------LSGGEIIKLQLARLLLGRYNILLLDE 432
Cdd:cd03224 80 -VPEGRRIFPELtveenlllgayARRRAKRKARLERvyelfprlkerrkqlagtLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1752069711 433 PGNFL------DIpaMEALETMMREypG-TIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:cd03224 159 PSEGLapkiveEI--FEAIRELRDE--GvTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
305-478 |
1.80e-09 |
|
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: 57.87 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---------RDREEGVVIA-PKAEIGYFDQTGYKF---TRNQNV 371
Cdd:cd03293 15 GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIaglerptsgEVLVDGEPVTgPGPDRGYVFQQDALLpwlTVLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 372 mAYMQEGSDYSVPDIRAVLSSM-------GFtpedVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDipAM-- 442
Cdd:cd03293 95 -ALGLELQGVPKAEARERAEELlelvglsGF----ENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALD--ALtr 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1752069711 443 ----EALETMMREYPGTIVFISHDtrLVE--RVADQVYVLKK 478
Cdd:cd03293 168 eqlqEELLDIWRETGKTVLLVTHD--IDEavFLADRVVVLSA 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
386-481 |
1.89e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 386 IRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDI---PAMEALETMMREYPGT-IVFISH 461
Cdd:PRK10419 131 ASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGTaCLFITH 210
|
90 100
....*....|....*....|
gi 1752069711 462 DTRLVERVADQVYVLKKGQL 481
Cdd:PRK10419 211 DLRLVERFCQRVMVMDNGQI 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
305-479 |
2.20e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 58.18 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI----RDREEGVVIAPKAEIGYFDQTGYKF---------TRNQNV 371
Cdd:COG1116 22 GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIagleKPTSGEVLVDGKPVTGPGPDRGVVFqepallpwlTVLDNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 372 mAYMQEGSDYSVPDIRA----VLSSMGFtpEDVRKEL-SMLSGGEiiklQ----LARLLLGRYNILLLDEPgnF--LDip 440
Cdd:COG1116 102 -ALGLELRGVPKAERRErareLLELVGL--AGFEDAYpHQLSGGM----RqrvaIARALANDPEVLLMDEP--FgaLD-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752069711 441 AM------EALETMMREYPGTIVFISHDtrlVE---RVADQVYVLKKG 479
Cdd:COG1116 171 ALtrerlqDELLRLWQETGKTVLFVTHD---VDeavFLADRVVVLSAR 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-201 |
2.37e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.47 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 24 LELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQyGKIERQGT-------------FAYI---PQLEEAAVRE-------- 79
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIelreldpeswrkhLSWVgqnPQLPHGTLRDnvllgnpd 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 80 --------------VQDYALMGKLGISRV---QAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLK 142
Cdd:PRK11174 450 asdeqlqqalenawVSEFLPLLPQGLDTPigdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN 529
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 143 LYTGA--LLIISHDRDLLDRVaDKIWELKDGRITEYwGGYSDyLAQKEAERNRQLAQYQQA 201
Cdd:PRK11174 530 AASRRqtTLMVTHQLEDLAQW-DQIWVMQDGQIVQQ-GDYAE-LSQAGGLFATLLAHRQEE 587
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
305-480 |
2.38e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVV------IAPKAE--------IGYfdQTGYK--F 365
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILaglARPDAGEVlwqgepIRRQRDeyhqdllyLGH--QPGIKteL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 366 TRNQNVMAYMQEGSDYSVPDIRAVLSSMG---FtpEDVrkELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAM 442
Cdd:PRK13538 90 TALENLRFYQRLHGPGDDEALWEALAQVGlagF--EDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1752069711 443 EALETMMREYP---GTIVFISHdtRLVERVADQVYVLKKGQ 480
Cdd:PRK13538 166 ARLEALLAQHAeqgGMVILTTH--QDLPVASDKVRKLRLGQ 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
310-476 |
2.92e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.44 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTL---LNMIRDREEG--------VVIAPKAEIGYFDQTGYKFTRN--------QN 370
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIETPTGGelyyqgqdLLKADPEAQKLLRQKIQIVFQNpygslnprKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 371 VMAYMQE----GSDYSVPD----IRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD--IP 440
Cdd:PRK11308 111 VGQILEEplliNTSLSAAErrekALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvsVQ 190
|
170 180 190
....*....|....*....|....*....|....*....
gi 1752069711 441 AmEALETMM---REYPGTIVFISHDTRLVERVADQVYVL 476
Cdd:PRK11308 191 A-QVLNLMMdlqQELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
306-481 |
2.99e-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: 57.24 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-R--DREEGVVI------------APKAEIGYFDQTGYKFtrNQN 370
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfRfyDVSSGSILidgqdirevtldSLRRAIGVVPQDTVLF--NDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 371 VMAYMQEG----SDYSV------PDIRAVLSSMGFTPEDVRKELS-MLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDI 439
Cdd:cd03253 91 IGYNIRYGrpdaTDEEVieaakaAQIHDKIMRFPDGYDTIVGERGlKLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752069711 440 PA-MEALETMMREYPG-TIVFISHdtRLVERV-ADQVYVLKKGQL 481
Cdd:cd03253 171 HTeREIQAALRDVSKGrTTIVIAH--RLSTIVnADKIIVLKDGRI 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-279 |
3.79e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.57 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYIPQ------------------LEEAAVREV-QDYALMGKLGI- 91
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQqawiqndslrenilfgkaLNEKYYQQVlEACALLPDLEIl 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 92 -SRVQAEI------MSGGEETRLKIAQALEDNVHGIMADEPTS----HLDRAGIDFLVSRLKLYTGAL-LIISHDRDLLD 159
Cdd:TIGR00957 747 pSGDRTEIgekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSavdaHVGKHIFEHVIGPEGVLKNKTrILVTHGISYLP 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 160 RVaDKIWELKDGRITEYwGGYSDYLAQKEAERN--RQLAQYQQAEAERERLEQAISEKKVQARRLDQksraaGKNSTESG 237
Cdd:TIGR00957 827 QV-DVIIVMSGGKISEM-GSYQELLQRDGAFAEflRTYAPDEQQGHLEDSWTALVSGEGKEAKLIEN-----GMLVTDVV 899
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1752069711 238 GR-----LAHQKSQGSKQKKLHTAARQMQRriealdgVSAPEELWSV 279
Cdd:TIGR00957 900 GKqlqrqLSASSSDSGDQSRHHGSSAELQK-------AEAKEETWKL 939
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
296-455 |
4.33e-09 |
|
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: 56.21 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 296 TGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIAPKAEIG-----YFDQTGY---- 363
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILaglLRPDSGEVRWNGTPLAeqrdePHENILYlghl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 364 -----KFTRNQNvMAYMQEGSDYSVPDIRAVLSSMGFTP-EDVrkELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFL 437
Cdd:TIGR01189 82 pglkpELSALEN-LHFWAAIHGGAQRTIEDALAAVGLTGfEDL--PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170
....*....|....*...
gi 1752069711 438 DIPAMEALETMMREYPGT 455
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLAR 176
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
305-476 |
4.48e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.05 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTL----LNMIRDREEGVVIAPKAEIGYFDQTGY-KFTRNQNVMAYMQEGS 379
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLvrvvLGLVAPDEGVIKRNGKLRIGYVPQKLYlDTTLPLTVNRFLRLRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 380 DYSVPDIRAVLSSMGfTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEAL----ETMMREYPGT 455
Cdd:PRK09544 95 GTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCA 173
|
170 180
....*....|....*....|.
gi 1752069711 456 IVFISHDTRLVERVADQVYVL 476
Cdd:PRK09544 174 VLMVSHDLHLVMAKTDEVLCL 194
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-174 |
5.57e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.93 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 1 MLLIKAEEIVVEYMGRDVLD-----IDRLELyaydrIGLVGANGAGKSTLLKTLLG------------------------ 51
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDgvdlsVREGSL-----VGLVGPNGAGKTTLLRAINGtltptagtvlvagddvealsaraa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 52 -------------------RIPLQYGKIERQGTFAYIPQLEEAAVREVqdyalMGKLGISRVQAE---IMSGGEETRLKI 109
Cdd:PRK09536 76 srrvasvpqdtslsfefdvRQVVEMGRTPHRSRFDTWTETDRAAVERA-----MERTGVAQFADRpvtSLSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 110 AQALEDNVHGIMADEPTSHLDragIDFLVSRLKLY-----TGALLIIS-HDRDLLDRVADKIWELKDGRIT 174
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD---INHQVRTLELVrrlvdDGKTAVAAiHDLDLAARYCDELVLLADGRVR 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
306-480 |
5.81e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.28 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR---DREEGVVIAPKAEigyfdqtgykftrnqNVM-----AYMQE 377
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwPYGSGRIARPAGA---------------RVLflpqrPYLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 378 GS------------DYSVPDIRAVLSSMGFTP--EDVRKELS---MLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIP 440
Cdd:COG4178 440 GTlreallypataeAFSDAELREALEAVGLGHlaERLDEEADwdqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1752069711 441 AMEALETMMR-EYPG-TIVFISHDTRLvERVADQVYVLKKGQ 480
Cdd:COG4178 520 NEAALYQLLReELPGtTVISVGHRSTL-AAFHDRVLELTGDG 560
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-176 |
6.31e-09 |
|
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: 55.88 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGR--DVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG-------------TFAY 68
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 69 IPQ---LEEAAVR-------EVQDYALMGKLGISRvQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGiDFLV 138
Cdd:cd03369 87 IPQdptLFSGTIRsnldpfdEYSDEEIYGALRVSE-GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-DALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1752069711 139 SRL--KLYTGA-LLIISHD-RDLLDrvADKIWELKDGRITEY 176
Cdd:cd03369 165 QKTirEEFTNStILTIAHRlRTIID--YDKILVMDAGEVKEY 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
304-481 |
6.44e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.04 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 304 LGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---GVVIAPKAEIGYFDQTGYKFTRNQNVMAYMQEG-- 378
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERpsaGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 379 SDYSVPDIRAV-LSSMGFTPEDVRKELS-----------------MLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIP 440
Cdd:PRK10908 92 MDRTVYDNVAIpLIIAGASGDDIRRRVSaaldkvglldkaknfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752069711 441 AMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK10908 172 LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
286-481 |
6.82e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 56.29 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 286 VLELHHplpvtgheLCKQLGDK----VILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR--DR---------------- 343
Cdd:COG4181 8 IIELRG--------LTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAglDRptsgtvrlagqdlfal 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 344 -EEGVVIAPKAEIGYFDQTgykF------TRNQNVMAYMQEGSDysvPDIR----AVLSSMGF------TPedvrkelSM 406
Cdd:COG4181 80 dEDARARLRARHVGFVFQS---FqllptlTALENVMLPLELAGR---RDARararALLERVGLghrldhYP-------AQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 407 LSGGEIIKLQLARLLLGRYNILLLDEP-GNfLDIPA----MEALETMMREYPGTIVFISHDTRLVERvADQVYVLKKGQL 481
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPtGN-LDAATgeqiIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-171 |
6.82e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfAYiPQLEEAAVRE--- 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI-NY-NKLDHKLAAQlgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 80 --------------VQDYALMGKL------GIS-------RVQAEIM-----------------SGGEETRLKIAQALED 115
Cdd:PRK09700 83 giiyqelsvideltVLENLYIGRHltkkvcGVNiidwremRVRAAMMllrvglkvdldekvanlSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 116 NVHGIMADEPTSHLDRAGIDFL---VSRLKLYTGALLIISHDRDLLDRVADKIWELKDG 171
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
305-481 |
7.38e-09 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 55.88 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---------GVVIA--PKAEIGYFDQT-GYKF------- 365
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELptsgtirvnGQDVSdlRGRAIPYLRRKiGVVFqdfrllp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 366 TRN--QNVMAYMqEGSDYSVPDIR----AVLSSMGFtpEDVRKELSM-LSGGEIIKLQLARLLLGRYNILLLDEPGNFLD 438
Cdd:cd03292 92 DRNvyENVAFAL-EVTGVPPREIRkrvpAALELVGL--SHKHRALPAeLSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752069711 439 IPAMEALETMMREYP---GTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03292 169 PDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
305-480 |
7.76e-09 |
|
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: 56.04 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---GVVI---------------APKAEIGYFDQtGYKFT 366
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEptsGSVLidgtdinklkgkalrQLRRQIGMIFQ-QFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 367 RNQNVMAYMQEGSDYSVPDIRAVLSsmGFTPEDVRKEL----------------SMLSGGEIIKLQLARLLLGRYNILLL 430
Cdd:cd03256 91 ERLSVLENVLSGRLGRRSTWRSLFG--LFPKEEKQRALaalervglldkayqraDQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1752069711 431 DEPGNFLDiPA-----MEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:cd03256 169 DEPVASLD-PAssrqvMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
305-476 |
1.06e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 54.93 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI----RDREEGVVIAPKAEIGYFDQTGykftrnqnvmaymqegsd 380
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLagvlRPTSGTVRRAGGARVAYVPQRS------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 381 ySVPD---IRAV-LSSMGF----------TPED----------------VRKELSMLSGGEIIKLQLARLLLGRYNILLL 430
Cdd:NF040873 65 -EVPDslpLTVRdLVAMGRwarrglwrrlTRDDraavddalervgladlAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 431 DEPGNFLDIPAMEALETMMREYPG---TIVFISHDTRLVeRVADQVYVL 476
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELV-RRADPCVLL 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-173 |
1.10e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.95 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 33 GLVGANGAGKSTLLKtLLGR-IPLQYGKIERQGT-------------FAYIPQLEEAA----VRE---VQDYALMGKLGI 91
Cdd:PRK10575 41 GLIGHNGSGKSTLLK-MLGRhQPPSEGEILLDAQpleswsskafarkVAYLPQQLPAAegmtVRElvaIGRYPWHGALGR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 92 ------SRVQAEI---------------MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRA-GIDF--LVSRLKLYTGA 147
Cdd:PRK10575 120 fgaadrEKVEEAIslvglkplahrlvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhQVDVlaLVHRLSQERGL 199
|
170 180
....*....|....*....|....*..
gi 1752069711 148 LLI-ISHDRDLLDRVADKIWELKDGRI 173
Cdd:PRK10575 200 TVIaVLHDINMAARYCDYLVALRGGEM 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-170 |
1.26e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 54.08 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 15 GRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIER--QGTFAYIPQ---LEEAAVREVQDYALMgkl 89
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQrpyLPLGTLREQLIYPWD--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 90 gisrvqaEIMSGGEETRLKIAQALednVHG---IMADEPTSHLDRAGIDFLVSRLKLYTGALLIISHdRDLLDRVADKIW 166
Cdd:cd03223 90 -------DVLSGGEQQRLAFARLL---LHKpkfVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVL 158
|
....
gi 1752069711 167 ELKD 170
Cdd:cd03223 159 DLDG 162
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-172 |
1.34e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIP--------------LQYGKI---ERQGt 65
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiifegeeLQASNIrdtERAG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 66 FAYIPQlEEAAVRE-----------------VQDYALMG----------KLGISrVQAEIM--SGGEETRLKIAQALEDN 116
Cdd:PRK13549 84 IAIIHQ-ELALVKElsvleniflgneitpggIMDYDAMYlraqkllaqlKLDIN-PATPVGnlGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 117 VHGIMADEPTSHLDRAGIDFL---VSRLKLYTGALLIISHDRDLLDRVADKIWELKDGR 172
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLldiIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
305-479 |
1.34e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.84 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREegvviapkaeigyfdqtGYKFTRNQNVMaymqEGSDYS-- 382
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHP-----------------KYEVTEGEILF----KGEDITdl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 383 VPDIRAVLS-SMGF-TPEDVR--KELSML-------SGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALE---TM 448
Cdd:cd03217 70 PPEERARLGiFLAFqYPPEIPgvKNADFLryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAeviNK 149
|
170 180 190
....*....|....*....|....*....|..
gi 1752069711 449 MREYPGTIVFISHDTRLVERV-ADQVYVLKKG 479
Cdd:cd03217 150 LREEGKSVLIITHYQRLLDYIkPDRVHVLYDG 181
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
306-481 |
1.35e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.85 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTL---LNMIRDREEGVVIAPKAEIGYFDQTGYKFtrNQNVMAYMQEGSDY- 381
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKPTSGEVLIKGEPIKYDKKSLLEV--RKTVGIVFQNPDDQl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 382 ---SV-PDIRAVLSSMGFTPEDVR-------KELSM----------LSGGEIIKLQLARLLLGRYNILLLDEPGNFLD-- 438
Cdd:PRK13639 92 fapTVeEDVAFGPLNLGLSKEEVEkrvkealKAVGMegfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpm 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752069711 439 --IPAMEALETMMREypG-TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK13639 172 gaSQIMKLLYDLNKE--GiTIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
20-176 |
1.66e-08 |
|
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: 55.28 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 20 DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGripLQY---GKIERQGTfaYIPQLEEAAVREV--------QDYALMGK 88
Cdd:cd03258 23 DVS-LSVPKGEIFGIIGRSGAGKSTLIRCING---LERptsGSVLVDGT--DLTLLSGKELRKArrrigmifQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 89 ----------LGISRV-QAEI-----------------------MSGGEETRLKIAQALEDNVHGIMADEPTSHLD---- 130
Cdd:cd03258 97 rtvfenvalpLEIAGVpKAEIeervlellelvgledkadaypaqLSGGQKQRVGIARALANNPKVLLCDEATSALDpett 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 131 RAGIDFLVS---RLKLytgALLIISHDRDLLDRVADKIWELKDGRITEY 176
Cdd:cd03258 177 QSILALLRDinrELGL---TIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-481 |
1.67e-08 |
|
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: 56.73 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLG------------------------RIPLQYGK 59
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvalcekcgyvERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 60 --------------------------------IERQGTFAY----------IPQLEEA------AVREVQDYALMGKLG- 90
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklrrrirkriaIMLQRTFALygddtvldnvLEALEEIgyegkeAVGRAVDLIEMVQLSh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 91 -ISRVqAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD--RAGI--DFLVSRLKLYTGALLIISHDRDLLDRVADK- 164
Cdd:TIGR03269 161 rITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqTAKLvhNALEEAVKASGISMVLTSHWPEVIEDLSDKa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 165 IWeLKDGRITEYwgGYSDYLAQKEAERNRQLAQYQQAEAErerlEQAISEKKVQARRLdqksraagknSTESGgrlahqk 244
Cdd:TIGR03269 240 IW-LENGEIKEE--GTPDEVVAVFMEGVSEVEKECEVEVG----EPIIKVRNVSKRYI----------SVDRG------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 245 sqgskqkklhtaarqmqrRIEALDGVSapeelwsVQFYHSEVLelhhplpvtghelckqlgdkvildrvsfqfplggkiA 324
Cdd:TIGR03269 296 ------------------VVKAVDNVS-------LEVKEGEIF------------------------------------G 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 325 ITGGNGAGKTTLLNMI-------------RDREEGVVIA---------PKAEIGYFDQTgYKFTRNQNVMAYMQEGSDYS 382
Cdd:TIGR03269 315 IVGTSGAGKTTLSKIIagvleptsgevnvRVGDEWVDMTkpgpdgrgrAKRYIGILHQE-YDLYPHRTVLDNLTEAIGLE 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 383 VPD----IRAV--LSSMGFTPEDVRKEL----SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD-IPAMEALETMMR- 450
Cdd:TIGR03269 394 LPDelarMKAVitLKMVGFDEEKAEEILdkypDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKa 473
|
570 580 590
....*....|....*....|....*....|...
gi 1752069711 451 --EYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:TIGR03269 474 reEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-190 |
1.84e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 55.44 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 17 DVLDIDRLELYAYDR---------------IGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAY----IPQLEEAAV 77
Cdd:PRK14246 9 DVFNISRLYLYINDKailkditikipnnsiFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 78 RE------------------------VQDYALMGKLGISRVQAEIM--------------------SGGEETRLKIAQAL 113
Cdd:PRK14246 89 RKevgmvfqqpnpfphlsiydniaypLKSHGIKEKREIKKIVEECLrkvglwkevydrlnspasqlSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 114 EDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTgALLIISHDRDLLDRVADKIWELKDGRITEyWGGYSDYLAQKEAE 190
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDivnSQAIEKLITELKNEI-AIVIVSHNPQQVARVADYVAFLYNGELVE-WGSSNEIFTSPKNE 246
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
24-175 |
2.03e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.32 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 24 LELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIE---RQGTFAYIPQLEEAAVRE--------VQDYALMG-KLGI 91
Cdd:PRK11701 27 FDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLRDLYALSEAERRRllrtewgfVHQHPRDGlRMQV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 92 S--------------------RVQA-------EI-----------MSGGEETRLKIAQALEDNVHGIMADEPTSHLD--- 130
Cdd:PRK11701 107 SaggnigerlmavgarhygdiRATAgdwlervEIdaariddlpttFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsv 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 131 RAGI-DF---LVSRLKLytgALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:PRK11701 187 QARLlDLlrgLVRELGL---AVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
302-480 |
2.10e-08 |
|
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: 54.40 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 302 KQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIAPKAeIGYFDQTGYKF--TRNQNVMAymq 376
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgeLEKLSGSVSVPGS-IAYVSQEPWIQngTIRENILF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 377 eGSDYSVPDIRAVLSSMGFTPeDVrKELS------------MLSGGEIIKLQLARLLLGRYNILLLDEP--------GNF 436
Cdd:cd03250 89 -GKPFDEERYEKVIKACALEP-DL-EILPdgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPlsavdahvGRH 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752069711 437 LdipaME-ALETMMREyPGTIVFISHDTRLVERvADQVYVLKKGQ 480
Cdd:cd03250 166 I----FEnCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
306-481 |
2.12e-08 |
|
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: 56.65 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-RDRE--------EGVVIAP------KAEIGYFDQTGYKF--TRN 368
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIpRFYEpdsgqillDGHDLADytlaslRRQVALVSQDVVLFndTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 369 QNVmAYmQEGSDYSVPDIRAVLSS---MGFT---PEDVRKEL----SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD 438
Cdd:TIGR02203 424 NNI-AY-GRTEQADRAEIERALAAayaQDFVdklPLGLDTPIgengVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752069711 439 IPA----MEALETMMREYpgTIVFISHDTRLVERvADQVYVLKKGQL 481
Cdd:TIGR02203 502 NESerlvQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-165 |
2.77e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKI----------------ERQGTFAYI----------PQ-------------- 71
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildefrgsELQNYFTKLlegdvkvivkPQyvdlipkavkgkvg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 --LEEAAVREVQDYaLMGKLGISRV---QAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKL 143
Cdd:cd03236 109 elLKKKDERGKLDE-LVDQLELRHVldrNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqRLNAARLIRELAE 187
|
170 180
....*....|....*....|..
gi 1752069711 144 YTGALLIISHDRDLLDRVADKI 165
Cdd:cd03236 188 DDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
299-482 |
2.79e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.98 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 299 ELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLL---NMIRDREEGVVIAPKAEIGY----------FDQTGYKF 365
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLrciNFLEKPSEGSIVVNGQTINLvrdkdgqlkvADKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 366 TRN------------------QNVM-AYMQE-GSDYSVPDIRAV--LSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLG 423
Cdd:PRK10619 90 LRTrltmvfqhfnlwshmtvlENVMeAPIQVlGLSKQEARERAVkyLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 424 RYNILLLDEPGNFLDiPAM--EALETMMR--EYPGTIVFISHDTRLVERVADQVYVLKKGQLQ 482
Cdd:PRK10619 170 EPEVLLFDEPTSALD-PELvgEVLRIMQQlaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-173 |
2.79e-08 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 54.07 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYIPQLEEAAVRE--- 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLkGID-LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQkvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 80 --VQDY--------------ALMGKLGISRVQAEI---------------------MSGGEETRLKIAQALEDNVHGIMA 122
Cdd:cd03262 80 mvFQQFnlfphltvlenitlAPIKVKGMSKAEAEEralellekvgladkadaypaqLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 123 DEPTSHLDRAGIDFLVSRLK--LYTG-ALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKdlAEEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-173 |
2.89e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 17 DVLDIDRLELYAYDRIGLVGANGAGKSTLLkTLLG----------RIPLQ---------YGKIERQgTFAYIPQ------ 71
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLM-NILGcldkptsgtyRVAGQdvatldadaLAQLRRE-HFGFIFQryhlls 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 -------LEEAAV--------REVQDYALMGKLGIS-RV--QAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD-RA 132
Cdd:PRK10535 100 hltaaqnVEVPAVyaglerkqRLLRAQELLQRLGLEdRVeyQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDsHS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1752069711 133 GIDFL--VSRLKLYTGALLIISHDRDLLDRvADKIWELKDGRI 173
Cdd:PRK10535 180 GEEVMaiLHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-154 |
3.01e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.89 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLLGRIPLQYGKIE----------RQGTFAYIPQLEEAAVR---EVQDYALMGKLG---------- 90
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLASGKISilgqptrqalQKNLVAYVPQSEEVDWSfpvLVEDVVMMGRYGhmgwlrrakk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 91 ---------ISRV--------QAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTGALLI 150
Cdd:PRK15056 118 rdrqivtaaLARVdmvefrhrQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDvktEARIISLLRELRDEGKTMLV 197
|
....
gi 1752069711 151 ISHD 154
Cdd:PRK15056 198 STHN 201
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
310-481 |
3.09e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.46 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRD--REEGVVI--------APKAEI----GYFDQTgykfTRNQNVMA-- 373
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGllPGQGEILlngrplsdWSAAELarhrAYLSQQ----QSPPFAMPvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 -----YMQEGSDYSVPD--IRAVLSSMGFTPEdVRKELSMLSGGEIIKLQLARLLL---------GRYniLLLDEPGNFL 437
Cdd:COG4138 88 qylalHQPAGASSEAVEqlLAQLAEALGLEDK-LSRPLTQLSGGEWQRVRLAAVLLqvwptinpeGQL--LLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752069711 438 DIPAMEALETMMREYP---GTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:COG4138 165 DVAQQAALDRLLRELCqqgITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
307-478 |
3.17e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.13 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 307 KVILDRVSFQFPLGGKIAITGGNGAGKTTllnmirdreegvviapkaeigYFDQTGYKFTRNQNVM-AYMQEGSDYSVPD 385
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKST---------------------ILDAIGLALGGAQSATrRRSGVKAGCIVAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 386 IRAVLSSMgftpedvrkeLSMLSGGEIIKLQLARLL----LGRYNILLLDEPGNFLDIPAMEALETMMREY--PGTIV-F 458
Cdd:cd03227 67 VSAELIFT----------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAQViV 136
|
170 180
....*....|....*....|
gi 1752069711 459 ISHDTRLVERvADQVYVLKK 478
Cdd:cd03227 137 ITHLPELAEL-ADKLIHIKK 155
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-174 |
3.19e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.63 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-------------FAYIP 70
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 71 QL----EEAAVREVQDY------ALMGKLGI---SRVQAEI---------------MSGGEETRLKIAQALEDNVHGIMA 122
Cdd:PRK11231 83 QHhltpEGITVRELVAYgrspwlSLWGRLSAednARVNQAMeqtrinhladrrltdLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1752069711 123 DEPTSHLD---RAGIDFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRIT 174
Cdd:PRK11231 163 DEPTTYLDinhQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
309-481 |
3.49e-08 |
|
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: 53.57 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 309 ILDRVSFQFPLGGKIAITGGNGAGKTTL-LNMIR--DREEGvviapKAEIGYFDQTGYKFTRNQNVMAYMQEGSDYSVPD 385
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRflEAEEG-----KIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 386 IRAVLSSMG-FTPEDVRKELSMLSGGEIIK------LQLARLLLGRYNILLLDEPGNFLDIpAMEAL--ETMMREYPG-T 455
Cdd:cd03369 98 IRSNLDPFDeYSDEEIYGALRVSEGGLNLSqgqrqlLCLARALLKRPRVLVLDEATASIDY-ATDALiqKTIREEFTNsT 176
|
170 180
....*....|....*....|....*.
gi 1752069711 456 IVFISHDTRLVERVaDQVYVLKKGQL 481
Cdd:cd03369 177 ILTIAHRLRTIIDY-DKILVMDAGEV 201
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
310-479 |
3.72e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 54.74 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLL---NMIRDREEGVVIAPKAEIgyfDQTGYKFTRNQnVMAYMQEGSDysvpdi 386
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLlhlNGIYLPQRGRVKVMGREV---NAENEKWVRSK-VGLVFQDPDD------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 387 rAVLSS------------MGFTPEDVR-------KELSM----------LSGGEIIKLQLARLLLGRYNILLLDEPGNFL 437
Cdd:PRK13647 91 -QVFSStvwddvafgpvnMGLDKDEVErrveealKAVRMwdfrdkppyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752069711 438 DIPAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKG 479
Cdd:PRK13647 170 DPRGQETLMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
299-481 |
3.87e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.42 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 299 ELCKQL-GDKVILDRVSFQFPLGGKIAITGGNGAGKTTL---LNMIRDREEGVVI--------APKAEIGYF-------- 358
Cdd:PRK13652 8 DLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLfrhFNGILKPTSGSVLirgepitkENIREVRKFvglvfqnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 359 DQTGYKFTRNQNV------MAYMQEGSDYSVPDiraVLSSMGFtpEDVRKELSM-LSGGEIIKLQLARLLLGRYNILLLD 431
Cdd:PRK13652 88 DDQIFSPTVEQDIafgpinLGLDEETVAHRVSS---ALHMLGL--EELRDRVPHhLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 432 EPGNFLDIPAMEALETMMR----EYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNdlpeTYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
292-481 |
4.84e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.91 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 292 PLPVTGheLCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---GVVIA---PKAEIGyfDQTGYKF 365
Cdd:PRK11247 12 PLLLNA--VSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETpsaGELLAgtaPLAEAR--EDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 366 TRN-----QNVMAYMQEG-SDYSVPDIRAVLSSMGFtpEDVRKEL-SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD 438
Cdd:PRK11247 88 QDArllpwKKVIDNVGLGlKGQWRDAALQALAAVGL--ADRANEWpAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752069711 439 ----IPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK11247 166 altrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
302-448 |
5.36e-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: 53.43 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 302 KQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREEG-------VVIAPKA--------EIGYFDQ------ 360
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqILFNGQPrkpdqfqkCVAYVRQddillp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 361 --TGYKFTRNQNVMAyMQEGSDYSVPDIRAVLSSMG-FTPEDVRKEL-SMLSGGEIIKLQLARLLLGRYNILLLDEPGNF 436
Cdd:cd03234 95 glTVRETLTYTAILR-LPRKSSDAIRKKRVEDVLLRdLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170
....*....|..
gi 1752069711 437 LDipAMEALETM 448
Cdd:cd03234 174 LD--SFTALNLV 183
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-172 |
5.53e-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: 55.22 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIP--------------LQYGKI---ERQGt 65
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiywsgspLKASNIrdtERAG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 66 FAYIPQ----LEEAAVRE-------------VQDYALMG----------KLGISRVQAEIMS--GGEETRLKIAQALEDN 116
Cdd:TIGR02633 80 IVIIHQeltlVPELSVAEniflgneitlpggRMAYNAMYlraknllrelQLDADNVTRPVGDygGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 117 VHGIMADEPTSHLDRAGIDFL---VSRLKLYTGALLIISHDRDLLDRVADKIWELKDGR 172
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILldiIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
32-126 |
5.69e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 53.21 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT--------------FAYIPQ--------------------LEEAAV 77
Cdd:cd03224 29 VALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgrrifpeltveenlllgayaRRRAKR 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 78 REVQD--YALMGKLG-ISRVQAEIMSGGEETRLKIAQALEDNVHGIMADEPT 126
Cdd:cd03224 109 KARLErvYELFPRLKeRRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-174 |
5.79e-08 |
|
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: 54.73 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 19 LDIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-----------------FAYI-------PQLE- 73
Cdd:TIGR02142 14 LDAD-FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflppekrrIGYVfqearlfPHLSv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 74 -----------EAAVREVQDYALMGKLGIS----RVQAEiMSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGID 135
Cdd:TIGR02142 93 rgnlrygmkraRPSERRISFERVIELLGIGhllgRLPGR-LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdprKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1752069711 136 FLVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRIT 174
Cdd:TIGR02142 172 PYLERLHAEFGiPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
295-481 |
6.10e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.74 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 295 VTGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-----RDR------EEGVVIAPKAE-----IGYF 358
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVvgivpRDAgniiidDEDISLLPLHArarrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 359 DQTGYKFTR---NQNVMAYMQEGSDYSVP--DIRAVLSSMGFTPEDVRKELSM-LSGGEIIKLQLARLLLGRYNILLLDE 432
Cdd:PRK10895 84 PQEASIFRRlsvYDNLMAVLQIRDDLSAEqrEDRANELMEEFHIEHLRDSMGQsLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 433 PGNFLD---IPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK10895 164 PFAGVDpisVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-172 |
6.18e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 33 GLVGANGAGKSTLLKTLLGRIPLQYGKI---ERQGTFA------------------YIPQL------------------- 72
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSIlidGQEMRFAsttaalaagvaiiyqelhLVPEMtvaenlylgqlphkggivn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 73 EEAAVREVQDYalMGKLGIS---RVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFL---VSRLKLYTG 146
Cdd:PRK11288 114 RRLLNYEAREQ--LEHLGVDidpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLfrvIRELRAEGR 191
|
170 180
....*....|....*....|....*.
gi 1752069711 147 ALLIISHDRDLLDRVADKIWELKDGR 172
Cdd:PRK11288 192 VILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
286-481 |
6.23e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 286 VLELHHplpvtgheLCKQLGDKVILDRVSFQFPlGGKI-AITGGNGAGKTTLLNM-------------IRDREegVVIA- 350
Cdd:COG3845 5 ALELRG--------ITKRFGGVVANDDVSLTVR-PGEIhALLGENGAGKSTLMKIlyglyqpdsgeilIDGKP--VRIRs 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 351 PKAEIGY-----------FDqtgyKFTRNQNVMAYMqEGSDYSVPD-------IRAVLSSMGFT--PEDVRKELSMlsgG 410
Cdd:COG3845 74 PRDAIALgigmvhqhfmlVP----NLTVAENIVLGL-EPTKGGRLDrkaararIRELSERYGLDvdPDAKVEDLSV---G 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 411 -----EIIKLqlarLLLGRyNILLLDEPGNFLDIPAMEAL-ETM--MREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:COG3845 146 eqqrvEILKA----LYRGA-RILILDEPTAVLTPQEADELfEILrrLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-171 |
7.10e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.81 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 15 GRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIER--QGTFAYIPQ--------------------- 71
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpaGARVLFLPQrpylplgtlreallypataea 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 LEEAAVREVQDYALMGKLgISRVQAE-----IMSGGEETRLKIAQALednVHG---IMADEPTSHLDRAGIDFLVSRLK- 142
Cdd:COG4178 455 FSDAELREALEAVGLGHL-AERLDEEadwdqVLSLGEQQRLAFARLL---LHKpdwLFLDEATSALDEENEAALYQLLRe 530
|
170 180 190
....*....|....*....|....*....|
gi 1752069711 143 -LYTGALLIISHdRDLLDRVADKIWELKDG 171
Cdd:COG4178 531 eLPGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
300-484 |
7.11e-08 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 53.03 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---GVVIapkaeIGYFDQTG-YKFTRN-----QN 370
Cdd:cd03301 6 VTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEptsGRIY-----IGGRDVTDlPPKDRDiamvfQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 371 VMAYmqegSDYSVPD-IRAVLSSMGFTPEDVRKEL-----------------SMLSGGEIIKLQLARLLLGRYNILLLDE 432
Cdd:cd03301 81 YALY----PHMTVYDnIAFGLKLRKVPKDEIDERVrevaellqiehlldrkpKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 433 PGNFLD----IPAMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQLQRL 484
Cdd:cd03301 157 PLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
32-79 |
7.67e-08 |
|
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: 52.47 E-value: 7.67e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYIPQ---LEEAAVRE 79
Cdd:cd03250 34 VAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQepwIQNGTIRE 84
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-176 |
7.80e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.65 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 1 MLLIKAEEIVVEYMG-RDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfayipQLEEAAVRE 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE-----PITKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 80 V---------------------QDYAL----MG---------------KLGISRVQAEI---MSGGEETRLKIAQALEDN 116
Cdd:PRK13652 76 VrkfvglvfqnpddqifsptveQDIAFgpinLGldeetvahrvssalhMLGLEELRDRVphhLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 117 VHGIMADEPTSHLDRAG----IDFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEY 176
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGvkelIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
33-173 |
9.88e-08 |
|
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: 52.51 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 33 GLVGANGAGKSTLLKTLLGRIPLQYGKI------------ERQGTFAYIPQ----LEEAAVRE-VQDYA----------- 84
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdrkAARQSLGYCPQfdalFDELTVREhLRFYArlkglpkseik 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 85 -----LMGKLGISRVQ---AEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTG--ALLIISHD 154
Cdd:cd03263 112 eevelLLRVLGLTDKAnkrARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
170
....*....|....*....
gi 1752069711 155 RDLLDRVADKIWELKDGRI 173
Cdd:cd03263 192 MDEAEALCDRIAIMSDGKL 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
309-481 |
1.03e-07 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 54.36 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 309 ILDRVSFQFPLGGKIAITGGNGAGKTTL----LNMIRDREEGVVIAPKA-----------EIGYFDQTGYKFTRN--QNV 371
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLakllVGFFQARSGEILLNGFSlkdidrhtlrqFINYLPQEPYIFSGSilENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 372 MayMQEGSDYSVPDIRAVLS-----------SMGFTPEdVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD-I 439
Cdd:TIGR01193 569 L--LGAKENVSQDEIWAACEiaeikddienmPLGYQTE-LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDtI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1752069711 440 PAMEALETMMREYPGTIVFISHDTRLVERVaDQVYVLKKGQL 481
Cdd:TIGR01193 646 TEKKIVNNLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKI 686
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
300-433 |
1.09e-07 |
|
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: 52.66 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI-----------RDREEGVVIAPKAE-----IGYFDQTGY 363
Cdd:TIGR04406 7 LIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIvglvrpdagkiLIDGQDITHLPMHErarlgIGYLPQEAS 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 364 ---KFTRNQNVMAYMQEGSDYSVPDIRAVLSSM--GFTPEDVRKELSM-LSGGEIIKLQLARLLLGRYNILLLDEP 433
Cdd:TIGR04406 87 ifrKLTVEENIMAVLEIRKDLDRAEREERLEALleEFQISHLRDNKAMsLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
294-480 |
1.10e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 53.27 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 294 PVTGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI----------------------RDREEGVVIAP 351
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLlglthpdagsislcgepvpsraRHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 352 KaeigyFDQTGYKFTRNQNVMAYmqegSDY---SVPDIRAVLSS-MGFTPEDVRKE--LSMLSGGEIIKLQLARLLLGRY 425
Cdd:PRK13537 87 Q-----FDNLDPDFTVRENLLVF----GRYfglSAAAARALVPPlLEFAKLENKADakVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 426 NILLLDEPGNFLDIPAM----EALETMMREyPGTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARhlmwERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-176 |
1.15e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 52.28 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG---------TFAYIP---- 70
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 71 ---------------QLE----EAAVREVQDYalMGKLGIS---RVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSH 128
Cdd:cd03269 81 lypkmkvidqlvylaQLKglkkEEARRRIDEW--LERLELSeyaNKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 129 LDRAGIDFL---VSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITEY 176
Cdd:cd03269 159 LDPVNVELLkdvIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
310-481 |
1.59e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.91 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIGYFDQTGYKFTRNQNVMAYMQE-GSDYSVPDIR- 387
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHF----NALLKPSSGTITIAGYHITPETGNKNLKKLRKKvSLVFQFPEAQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 388 ---AVLSSMGFTP------EDVRKELSM-------------------LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDI 439
Cdd:PRK13641 99 fenTVLKDVEFGPknfgfsEDEAKEKALkwlkkvglsedliskspfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752069711 440 PAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK13641 179 EGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
377-481 |
1.60e-07 |
|
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: 51.28 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 377 EGSDYSVPDIRAVLSS-MGFTPEDVRKEL--------------SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA 441
Cdd:cd03215 60 DGKPVTRRSPRDAIRAgIAYVPEDRKREGlvldlsvaenialsSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1752069711 442 MEALETMMREYP---GTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03215 140 KAEIYRLIRELAdagKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
305-481 |
1.69e-07 |
|
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: 51.84 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR---DREEGVVI--------APKAE----IGYFDQTGYKFTRnq 369
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMrfyDPQKGQILidgidirdISRKSlrsmIGVVLQDTFLFSG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 370 NVMAYMQEGSDYS-VPDIRAVLSSMGFT------PEDVRKEL----SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD 438
Cdd:cd03254 92 TIMENIRLGRPNAtDEEVIEAAKEAGAHdfimklPNGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 439 iPAME-----ALETMMREYpgTIVFISHdtRL-VERVADQVYVLKKGQL 481
Cdd:cd03254 172 -TETEkliqeALEKLMKGR--TSIIIAH--RLsTIKNADKILVLDDGKI 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-173 |
1.89e-07 |
|
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: 52.05 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 24 LELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIE---------------RQG---TFAyIPQL------------- 72
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglppheiaRLGigrTFQ-IPRLfpeltvlenvmva 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 73 ----------------EEAAVREvQDYALMGKLGISRV---QAEIMSGGEETRLKIAQALEDNVHGIMADEPT---SHLD 130
Cdd:cd03219 100 aqartgsglllararrEEREARE-RAEELLERVGLADLadrPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1752069711 131 RAGIDFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03219 179 TEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
299-461 |
1.99e-07 |
|
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: 51.34 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 299 ELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIAPKAEIGYFD------------QTGY 363
Cdd:cd03231 5 ELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILaglSPPLAGRVLLNGGPLDFQRdsiargllylghAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 364 K--FTRNQNVMAYMQEGSDYSVPDIRAVLSSMGFtpEDVrkELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA 441
Cdd:cd03231 85 KttLSVLENLRFWHADHSDEQVEEALARVGLNGF--EDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|...
gi 1752069711 442 MEALETMMREYP---GTIVFISH 461
Cdd:cd03231 161 VARFAEAMAGHCargGMVVLTTH 183
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
298-433 |
2.15e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.95 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIgYFDQ---TG---YKftRNQNV 371
Cdd:COG1137 7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMI----VGLVKPDSGRI-FLDGediTHlpmHK--RARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 372 MAYM-QEGS---DYSVPD-IRAVLSSMGFTPED----------------VRKELSM-LSGGEIIKLQLARLLLGRYNILL 429
Cdd:COG1137 80 IGYLpQEASifrKLTVEDnILAVLELRKLSKKEreerleelleefgithLRKSKAYsLSGGERRRVEIARALATNPKFIL 159
|
....
gi 1752069711 430 LDEP 433
Cdd:COG1137 160 LDEP 163
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
99-175 |
2.16e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.74 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 99 MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDF---LVSRLKLYTG-ALLIISHDRDLLDRVADKIwELKDGRIT 174
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSifqLLGELNRLQGtAFLVVTHDLQLAKRMSRQL-EMRDGRLT 224
|
.
gi 1752069711 175 E 175
Cdd:PRK11629 225 A 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-154 |
2.41e-07 |
|
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: 53.13 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 18 VLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI----------------ERQGTFAYIPQLEEAAVRE-- 79
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssldqdevrRRVSVCAQDAHLFDTTVREnl 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 80 ------VQDYALMGKLgiSRVQAEI-------------------MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGI 134
Cdd:TIGR02868 430 rlarpdATDEELWAAL--ERVGLADwlralpdgldtvlgeggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
170 180
....*....|....*....|..
gi 1752069711 135 DFLVSRL-KLYTG-ALLIISHD 154
Cdd:TIGR02868 508 DELLEDLlAALSGrTVVLITHH 529
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
313-481 |
2.41e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.86 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 313 VSFQFPLGGKIAITGGNGAGKTTLLNMIRDREEGvviapKAEIgYFDQT--------------GYkFTRNQNVMAYM--- 375
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-----SGSI-QFAGQpleawsaaelarhrAY-LSQQQTPPFAMpvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 376 -----------QEGSDYSVpdIRAVLSSMGFTPEDVRKeLSMLSGGEIIKLQLARLLL---------GRynILLLDEPGN 435
Cdd:PRK03695 88 qyltlhqpdktRTEAVASA--LNEVAEALGLDDKLGRS-VNQLSGGEWQRVRLAAVVLqvwpdinpaGQ--LLLLDEPMN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 436 FLDIPAMEALETMMREYP---GTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCqqgIAVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
269-481 |
2.44e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.31 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 269 GVSAPEELwsVQFYHSEVLELH---------HPLPVTGHELC-KQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLN 338
Cdd:PRK11174 317 AVGAAESL--VTFLETPLAHPQqgekelasnDPVTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 339 MI-----------------RDREEGvviAPKAEIGYFDQTGYKF--TRNQNV-MAymqeGSDYSVPDIRAVLSSMG---F 395
Cdd:PRK11174 395 ALlgflpyqgslkingielRELDPE---SWRKHLSWVGQNPQLPhgTLRDNVlLG----NPDASDEQLQQALENAWvseF 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 396 TPE-------DVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA----MEALETMMREYpgTIVFISHdtR 464
Cdd:PRK11174 468 LPLlpqgldtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSeqlvMQALNAASRRQ--TTLMVTH--Q 543
|
250
....*....|....*...
gi 1752069711 465 LVE-RVADQVYVLKKGQL 481
Cdd:PRK11174 544 LEDlAQWDQIWVMQDGQI 561
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
286-482 |
2.49e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.70 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 286 VLELHHplpvtgheLCKQLGDK----VILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR---DREEGVVIAPKAEIGYF 358
Cdd:PRK10584 6 IVEVHH--------LKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAgldDGSSGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 359 DQTGYKFTRNQNVMAYMQ----------------------EGSDYSVPDIRAVLSSMGFTpEDVRKELSMLSGGEIIKLQ 416
Cdd:PRK10584 78 DEEARAKLRAKHVGFVFQsfmliptlnalenvelpallrgESSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 417 LARLLLGRYNILLLDEPGNFLDIPAMEA----LETMMREYPGTIVFISHDTRLVERvADQVYVLKKGQLQ 482
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKiadlLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-67 |
2.79e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 51.62 E-value: 2.79e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1752069711 20 DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFA 67
Cdd:COG1134 44 DVS-FEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVS 90
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
33-172 |
2.82e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.53 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 33 GLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT------------FAYIPQLE--------------------------E 74
Cdd:PRK13536 71 GLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpararlararIGVVPQFDnldleftvrenllvfgryfgmstreiE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 75 AAVREVQDYALMGKLGISRVQAeiMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLK--LYTG-ALLII 151
Cdd:PRK13536 151 AVIPSLLEFARLESKADARVSD--LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRslLARGkTILLT 228
|
170 180
....*....|....*....|.
gi 1752069711 152 SHDRDLLDRVADKIWELKDGR 172
Cdd:PRK13536 229 THFMEEAERLCDRLCVLEAGR 249
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-340 |
3.14e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 19 LDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGkiERQGTFAYI-----PQLEEAAVREVQdyalmgklgisR 93
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG--ERQSQFSHItrlsfEQLQKLVSDEWQ-----------R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 94 VQAEIMSGGEE-TRLKIAQALEDNVHgimadEPTSHLDRA---GIDFLVSR--LKLYTGA---------------LLIIS 152
Cdd:PRK10938 86 NNTDMLSPGEDdTGRTTAEIIQDEVK-----DPARCEQLAqqfGITALLDRrfKYLSTGEtrktllcqalmsepdLLILD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 153 HDRDLLDRVADKIWelkdgriteywggysdylaqkeAERNRQLAQYQQAEAererleqaisekkVQARRLDQKSRAAGKn 232
Cdd:PRK10938 161 EPFDGLDVASRQQL----------------------AELLASLHQSGITLV-------------LVLNRFDEIPDFVQF- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 233 stesGGRLA--HQKSQGSKQKKLHTAARQMQRRIEALDGVSAPEelwsvqfyhSEVLELHHPLP-----VTGHELCKQLG 305
Cdd:PRK10938 205 ----AGVLAdcTLAETGEREEILQQALVAQLAHSEQLEGVQLPE---------PDEPSARHALPaneprIVLNNGVVSYN 271
|
330 340 350
....*....|....*....|....*....|....*
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI 340
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
307-481 |
3.55e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 307 KVILDRVSFQFPLGGKIAITGGNGAGKTT---LLNMIRDREE---------GVVIAPKAEIGYFDQTGYKFTR--NQNVM 372
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDnpnskitvdGITLTAKTVWDIREKVGIVFQNpdNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 373 AYMQEGSDY-----SVPD------IRAVLSSMGFTpEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPA 441
Cdd:PRK13640 100 ATVGDDVAFglenrAVPRpemikiVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD-PA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752069711 442 -----MEALETMMREYPGTIVFISHDTRLVErVADQVYVLKKGQL 481
Cdd:PRK13640 178 gkeqiLKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-165 |
3.80e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.26 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG-TFAYIPQLEEaavrevqdyalmgklgisrvqaeiMSGGEETRLKIA 110
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQYID------------------------LSGGELQRVAIA 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 111 QALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTG-ALLIISHDRDLLDRVADKI 165
Cdd:cd03222 84 AALLRNATFYLFDEPSAYLDieqRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRI 142
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-173 |
5.15e-07 |
|
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: 50.85 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 1 MLLIKAEEIVVEYMGRDVLD-IDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGK------IERQGT-------- 65
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDdIS-WTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEdvwelrkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 66 --------FAYIPQLEEaaVREV------------QDY---------ALMGKLGISRVQAEI---MSGGEETRLKIAQAL 113
Cdd:COG1119 80 iglvspalQLRFPRDET--VLDVvlsgffdsiglyREPtdeqrerarELLELLGLAHLADRPfgtLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 114 ednVHG----IMaDEPTSHLDRAGIDFLVSRLKLYTG----ALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:COG1119 158 ---VKDpellIL-DEPTAGLDLGARELLLALLDKLAAegapTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-173 |
6.67e-07 |
|
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: 49.83 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG-TFAYIPqleeAAVREV-- 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrDVTGVP----PERRNIgm 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 81 --QDYAL-------------MGKLGISRVQAEI---------------------MSGGEETRLKIAQALEDNVHGIMADE 124
Cdd:cd03259 77 vfQDYALfphltvaeniafgLKLRGVPKAEIRArvrellelvglegllnrypheLSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 125 PTSHLD---RAGIDFLVSRLKLYTGALLI-ISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03259 157 PLSALDaklREELREELKELQRELGITTIyVTHDQEEALALADRIAVMNEGRI 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
306-484 |
6.89e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.03 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTT---LLNMIRDREEGVVIAPKAEIGYFDqtgYKFTRNQnVMAYMQE----- 377
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPTGGQVLLDGVPLVQYD---HHYLHRQ-VALVGQEpvlfs 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 378 GS----------DYSVPDIRAVLSS-------MGFTP---EDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFL 437
Cdd:TIGR00958 569 GSvreniaygltDTPDEEIMAAAKAanahdfiMEFPNgydTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752069711 438 DIPAMEALETMMREYPGTIVFISHDTRLVERvADQVYVLKKGQLQRL 484
Cdd:TIGR00958 649 DAECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEM 694
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
34-159 |
7.46e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.96 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYIPQleEAAVRE--------VQDYALMGKLGISRVQAEI-----MS 100
Cdd:COG2401 61 IVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR--EASLIDaigrkgdfKDAVELLNAVGLSDAVLWLrrfkeLS 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 101 GGEETRLKIAQALEDNVHGIMADEPTSHLDR-------AGIDFLVSRLKlytGALLIISHDRDLLD 159
Cdd:COG2401 139 TGQKFRFRLALLLAERPKLLVIDEFCSHLDRqtakrvaRNLQKLARRAG---ITLVVATHHYDVID 201
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
34-175 |
7.97e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.55 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLLGRIPLQYGKIE--------------------RQGTFAYIP--QLEEAAV-------------- 77
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTvdditithktkdkyirpvrkRIGMVFQFPesQLFEDTVereiifgpknfkmn 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 78 -REVQDYA--LMGKLGISRVQAEI----MSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTG- 146
Cdd:PRK13646 118 lDEVKNYAhrLLMDLGFSRDVMSQspfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqsKRQVMRLLKSLQTDENk 197
|
170 180
....*....|....*....|....*....
gi 1752069711 147 ALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:PRK13646 198 TIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
34-176 |
1.02e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.18 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLLGRIPlQYGKIERQGTFAYIPQLEEAA--------------------VREVQDYALmgklgisR 93
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTE-GNVSVEGDIHYNGIPYKEFAEkypgeiiyvseedvhfptltVRETLDFAL-------R 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 94 VQAEIM----SGGEETRLKIAQALEDNVHGIMADEPTSHLDRA-GIDFlVSRLKLYTGAL---LIIShdrdlLDRVADKI 165
Cdd:cd03233 110 CKGNEFvrgiSGGERKRVSIAEALVSRASVLCWDNSTRGLDSStALEI-LKCIRTMADVLkttTFVS-----LYQASDEI 183
|
170
....*....|....*...
gi 1752069711 166 WE-------LKDGRITEY 176
Cdd:cd03233 184 YDlfdkvlvLYEGRQIYY 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
307-481 |
1.02e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 307 KVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR------DREEGVVI---------------AP-----KAEIGYFDQ 360
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltggGAPRGARVtgdvtlngeplaaidAPrlarlRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 361 TGYKFTRNQNVM----AYMQEGSDYSVPD---IRAVLSSMGFTPEDvRKELSMLSGGEIIKLQLARLLL----------- 422
Cdd:PRK13547 94 PAFAFSAREIVLlgryPHARRAGALTHRDgeiAWQALALAGATALV-GRDVTTLSGGELARVQFARVLAqlwpphdaaqp 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 423 GRYniLLLDEPGNFLDIP----AMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK13547 173 PRY--LLLDEPTAALDLAhqhrLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-175 |
1.03e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.08 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIP----LQYGKIERQG-----------TFAY 68
Cdd:PRK10418 5 IELRNIALQAAQPLVHGVS-LTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGkpvapcalrgrKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 69 IPQLEEAA---VREVQDYAL-----MGKLGISRVQAEI-------------------MSGGEETRLKIAQALEDNVHGIM 121
Cdd:PRK10418 84 IMQNPRSAfnpLHTMHTHARetclaLGKPADDATLTAAleavglenaarvlklypfeMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 122 ADEPTSHLD---RAGI-DFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:PRK10418 164 ADEPTTDLDvvaQARIlDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-165 |
1.05e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-------------FAYIPQLEEAAVREVQ-----DYA--------- 84
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdevlkrfrgtelQNYFKKLYNGEIKVVHkpqyvDLIpkvfkgkvr 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 85 --------------LMGKLGISRV---QAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RagidFLVSRL--K 142
Cdd:PRK13409 182 ellkkvdergkldeVVERLGLENIldrDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqR----LNVARLirE 257
|
170 180
....*....|....*....|....
gi 1752069711 143 LYTG-ALLIISHDRDLLDRVADKI 165
Cdd:PRK13409 258 LAEGkYVLVVEHDLAVLDYLADNV 281
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
389-481 |
1.16e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.16 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 389 VLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD----IPAMEALETMMREYPGTIVFISHDTR 464
Cdd:PRK13646 128 LLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHDMN 207
|
90
....*....|....*..
gi 1752069711 465 LVERVADQVYVLKKGQL 481
Cdd:PRK13646 208 EVARYADEVIVMKEGSI 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
306-481 |
1.21e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.01 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTL---LNMIRDREEGVVIAPKAEIGYfDQTGYKFTRNQnvMAYMQEGSDYS 382
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfmnLSGLLRPQKGAVLWQGKPLDY-SKRGLLALRQQ--VATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 383 V------PDIRAVLSSMGFTPEDVRKE-----------------LSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDI 439
Cdd:PRK13638 90 IfytdidSDIAFSLRNLGVPEAEITRRvdealtlvdaqhfrhqpIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752069711 440 PAMEALETMMREYPGT---IVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-165 |
1.22e-06 |
|
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: 50.44 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRD-----VLDIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQY---GKIERQGT--------- 65
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkaVDGVS-FDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEdllklseke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 66 --------FAYIPQ---------------LEEAAV-------REVQDYA--LMGKLGISRVQAEI------MSGGEETRL 107
Cdd:COG0444 80 lrkirgreIQMIFQdpmtslnpvmtvgdqIAEPLRihgglskAEARERAieLLERVGLPDPERRLdrypheLSGGMRQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 108 KIAQAL--EDNVhgIMADEPTSHLD---RAGIDFLVSRLKLYTG-ALLIISHDRDLLDRVADKI 165
Cdd:COG0444 160 MIARALalEPKL--LIADEPTTALDvtiQAQILNLLKDLQRELGlAILFITHDLGVVAEIADRV 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-187 |
1.23e-06 |
|
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: 49.54 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 15 GRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfaYIPQLEEAAVREV-----QDYALM--- 86
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ--DIREVTLDSLRRAigvvpQDTVLFndt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 87 -------GKLGISRVQ-------AEI---------------------MSGGEETRLKIAQALEDNVHGIMADEPTSHLD- 130
Cdd:cd03253 91 igyniryGRPDATDEEvieaakaAQIhdkimrfpdgydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDt 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 131 ---RAGIDFLVSRLKLYTgaLLIISHD-RDLLDrvADKIWELKDGRITEYwGGYSDYLAQK 187
Cdd:cd03253 171 hteREIQAALRDVSKGRT--TIVIAHRlSTIVN--ADKIIVLKDGRIVER-GTHEELLAKG 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-153 |
1.23e-06 |
|
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: 48.89 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 6 AEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT------------FAYIPQLE 73
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 74 ----EAAVREVQDY----------------ALMGKLGISRVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG 133
Cdd:TIGR01189 83 glkpELSALENLHFwaaihggaqrtiedalAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|...
gi 1752069711 134 IDFLVSRLKLYT---GALLIISH 153
Cdd:TIGR01189 163 VALLAGLLRAHLargGIVLLTTH 185
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
310-479 |
1.29e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.75 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRdreeGVVIAPKAEIGYFDQ--TGYKFTR-------------NQNV--- 371
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMI----GIEKVKSGEIFYNNQaiTDDNFEKlrkhigivfqnpdNQFVgsi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 372 ----MAYMQEgsDYSVP------DIRAVLSSMGFTpEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA 441
Cdd:PRK13648 101 vkydVAFGLE--NHAVPydemhrRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1752069711 442 MEALETMMREYPG----TIVFISHDtrLVERV-ADQVYVLKKG 479
Cdd:PRK13648 178 RQNLLDLVRKVKSehniTIISITHD--LSEAMeADHVIVMNKG 218
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
320-477 |
1.34e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.14 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 320 GGKIAITGGNGAGKTTLLNMIrdreegvviapkaeIGYFDQTGYKFTRNqnvmaymqegsdySVPDIRAVLSSmGFTPED 399
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL--------------ARELGPPGGGVIYI-------------DGEDILEEVLD-QLLLII 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 400 VRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD---------IPAMEALETMMREYPGTIVFISHDTR------ 464
Cdd:smart00382 54 VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDEKdlgpal 133
|
170
....*....|...
gi 1752069711 465 LVERVADQVYVLK 477
Cdd:smart00382 134 LRRRFDRRIVLLL 146
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-203 |
1.34e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 50.93 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 15 GRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI-------------ERQGTFAYIPQ---LEEAAV 77
Cdd:COG1132 352 DRPVLkDIS-LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdltleSLRRQIGVVPQdtfLFSGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 78 RE-VqdyaLMGKLGISRvqAEIM------------------------------SGGEETRLKIAQALEDNVHGIMADEPT 126
Cdd:COG1132 431 REnI----RYGRPDATD--EEVEeaakaaqahefiealpdgydtvvgergvnlSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 127 SHLD-------RAGIDflvsrlKLYTGA-LLIISHdrdlldRV-----ADKIWELKDGRITEYwGGYSDYLAQKeaERNR 193
Cdd:COG1132 505 SALDtetealiQEALE------RLMKGRtTIVIAH------RLstirnADRILVLDDGRIVEQ-GTHEELLARG--GLYA 569
|
250
....*....|
gi 1752069711 194 QLAQYQQAEA 203
Cdd:COG1132 570 RLYRLQFGEE 579
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-173 |
1.39e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.79 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLD-IDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT---------------- 65
Cdd:COG1129 4 LLEMRGISKSFGGVKALDgVS-LELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 66 -----FAYIPQL-------------------EEAAVREVQdyALMGKLGIS---RVQAEIMSGGEETRLKIAQALEDNVH 118
Cdd:COG1129 83 iihqeLNLVPNLsvaeniflgreprrgglidWRAMRRRAR--ELLARLGLDidpDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 119 GIMADEPTSHLDRAGIDFL---VSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:COG1129 161 VLILDEPTASLTEREVERLfriIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-165 |
1.50e-06 |
|
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: 50.55 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTF--------------------------AYIPQ-------------- 71
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWdevlkrfrgtelqdyfkklangeikvAHKPQyvdlipkvfkgtvr 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 --LEEAAVREVQDYaLMGKLGISRV---QAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKL 143
Cdd:COG1245 182 elLEKVDERGKLDE-LAEKLGLENIldrDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqRLNVARLIRELAE 260
|
170 180
....*....|....*....|..
gi 1752069711 144 YTGALLIISHDRDLLDRVADKI 165
Cdd:COG1245 261 EGKYVLVVEHDLAILDYLADYV 282
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-173 |
1.83e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQY--------GKIERQGT--------- 65
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEplaaidapr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 66 ----FAYIPQLEEAA----VREV------------------------QDYALMGKLGISRVQAEIMSGGEETRLKIAQAL 113
Cdd:PRK13547 81 larlRAVLPQAAQPAfafsAREIvllgrypharragalthrdgeiawQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 114 ------EDNVHG---IMADEPTSHLDRAGIDFLVSRLKLYT-----GALLIIsHDRDLLDRVADKIWELKDGRI 173
Cdd:PRK13547 161 aqlwppHDAAQPpryLLLDEPTAALDLAHQHRLLDTVRRLArdwnlGVLAIV-HDPNLAARHADRIAMLADGAI 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
303-476 |
1.88e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.94 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 303 QLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR---DREEGVVIAPKAEIG------YFDQTGYKF-------- 365
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVAsliSPTSGTLLFEGEDIStlkpeiYRQQVSYCAqtptlfgd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 366 TRNQNVMAYMQEGSDYSVPD-IRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD----IP 440
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQPDPAiFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkHN 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1752069711 441 AMEALETMMREYPGTIVFISHDTRLVERvADQVYVL 476
Cdd:PRK10247 176 VNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
300-438 |
2.13e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.05 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE-GVVIAP--------------KAEIGYFDQ---- 360
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkGVKGSGsvllngmpidakemRAISAYVQQddlf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 361 TGYKFTRNQ-NVMAYMQEGSDYS----VPDIRAVLSSMGF---------TPEDVRKelsmLSGGEIIKLQLARLLLGRYN 426
Cdd:TIGR00955 111 IPTLTVREHlMFQAHLRMPRRVTkkekRERVDEVLQALGLrkcantrigVPGRVKG----LSGGERKRLAFASELLTDPP 186
|
170
....*....|..
gi 1752069711 427 ILLLDEPGNFLD 438
Cdd:TIGR00955 187 LLFCDEPTSGLD 198
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-174 |
2.21e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.72 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMG-RDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGtfAYIPQLEEAAV---- 77
Cdd:PRK10908 1 MIRFEHVSKAYLGgRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG--HDITRLKNREVpflr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 78 REV----QDYALMGKLGI-------------------SRVQAEI---------------MSGGEETRLKIAQALEDNVHG 119
Cdd:PRK10908 79 RQIgmifQDHHLLMDRTVydnvaipliiagasgddirRRVSAALdkvglldkaknfpiqLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 120 IMADEPTSHLDRA---GIDFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRIT 174
Cdd:PRK10908 159 LLADEPTGNLDDAlseGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-130 |
2.44e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 48.42 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIP---LQYGKI----------ERQGTFAYIPQ----LEEAAVREVQDYA---------- 84
Cdd:cd03234 36 MAILGSSGSGKTTLLDAISGRVEgggTTSGQIlfngqprkpdQFQKCVAYVRQddilLPGLTVRETLTYTailrlprkss 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 85 -----------LMGKLGISRVQAEIM---SGGEETRLKIAQALEDNVHGIMADEPTSHLD 130
Cdd:cd03234 116 dairkkrvedvLLRDLALTRIGGNLVkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-65 |
2.95e-06 |
|
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: 48.44 E-value: 2.95e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 1 MLLIKAEEIVVEYMGRDVL-DIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT 65
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLhGVS-LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE 65
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-154 |
3.29e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.54 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYIPQLEEAAV----- 77
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVfqneg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 78 ----REVQDYALMG-KL-GISRVQAEI---------------------MSGGEETRLKIAQALEDNVHGIMADEPTSHLD 130
Cdd:PRK11248 81 llpwRNVQDNVAFGlQLaGVEKMQRLEiahqmlkkvglegaekryiwqLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*...
gi 1752069711 131 ---RAGIDFLVSRLKLYTG-ALLIISHD 154
Cdd:PRK11248 161 aftREQMQTLLLKLWQETGkQVLLITHD 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-175 |
3.58e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 49.30 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRD------------VLDIDrLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQyGKIERQGTfaYIP 70
Cdd:COG4172 275 LLEARDLKVWFPIKRglfrrtvghvkaVDGVS-LTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQ--DLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 71 QLEEAAVREV--------QD-YA----------------LMGKLGISRVQ-----AEIM-----------------SGGE 103
Cdd:COG4172 351 GLSRRALRPLrrrmqvvfQDpFGslsprmtvgqiiaeglRVHGPGLSAAErrarvAEALeevgldpaarhryphefSGGQ 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 104 ETRLKIAQA--LEDNVhgIMADEPTSHLDR---AGIDFLVSRL-KLYTGALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:COG4172 431 RQRIAIARAliLEPKL--LVLDEPTSALDVsvqAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-175 |
3.60e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.53 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 1 MLLIKAEEIVVEYMG---------RDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGR------------IPLQYGK 59
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLespsqgnvswrgEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 60 IERQGTF-------------AYIPQ----------------LEEAAvREVQDYALMGKLGI-----SRVQAEiMSGGEET 105
Cdd:PRK10419 81 RAQRKAFrrdiqmvfqdsisAVNPRktvreiireplrhllsLDKAE-RLARASEMLRAVDLddsvlDKRPPQ-LSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 106 RLKIAQALEDNVHGIMADEPTSHLDR---AGIDFLVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQFGtACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-173 |
3.78e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.54 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 30 DRIGLVGANGAGKSTLL------------KTLLGRIPLQYGK---IERQGTFAYIPQ----------------------- 71
Cdd:PRK13639 29 EMVALLGPNGAGKSTLFlhfngilkptsgEVLIKGEPIKYDKkslLEVRKTVGIVFQnpddqlfaptveedvafgplnlg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 --LEEAAVREVQDYALMGKLGISRVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYT--GA 147
Cdd:PRK13639 109 lsKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkeGI 188
|
170 180
....*....|....*....|....*..
gi 1752069711 148 LLIIS-HDRDLLDRVADKIWELKDGRI 173
Cdd:PRK13639 189 TIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-175 |
3.83e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG------------------------TFAYIPQL--------------E 73
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakhvgfvfqSFMLIPTLnalenvelpallrgE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 74 EAAVREVQDYALMGKLGISRVQAEI---MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG----IDFLVSRLKLYTG 146
Cdd:PRK10584 119 SSRQSRNGAKALLEQLGLGKRLDHLpaqLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLFSLNREHGT 198
|
170 180
....*....|....*....|....*....
gi 1752069711 147 ALLIISHDRDLLDRvADKIWELKDGRITE 175
Cdd:PRK10584 199 TLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
310-481 |
3.87e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.47 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTL---LNMIRDREEGVViapkaEIGYF-----------DQTGYKFTR--NQNVMA 373
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLLPEAGTI-----TVGGMvlseetvwdvrRQVGMVFQNpdNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 YMQEG-----------SDYSVPDIRAVLSSMGFTpEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPA- 441
Cdd:PRK13635 98 TVQDDvafglenigvpREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD-PRg 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752069711 442 -MEALET---MMREYPGTIVFISHDTRLVERvADQVYVLKKGQL 481
Cdd:PRK13635 176 rREVLETvrqLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEI 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
323-475 |
3.93e-06 |
|
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: 48.17 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 323 IAITGGNGAGKTTLLNMIRDR---EEGVVIAPKAEIGYFDQtgykftrnqnvmaYMQEGSDYSVPD-IRAVLSSMGFTPE 398
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVlkpDEGDIEIELDTVSYKPQ-------------YIKADYEGTVRDlLSSITKDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 399 ---DVRKELSM----------LSGGEIIKLQLARLLLGRYNILLLDEPGNFLD----IPAMEALETMMREYPGTIVFISH 461
Cdd:cd03237 95 fktEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVEH 174
|
170
....*....|....
gi 1752069711 462 DTRLVERVADQVYV 475
Cdd:cd03237 175 DIIMIDYLADRLIV 188
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-481 |
4.61e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT--------------FAY 68
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 69 IPQ-----------------LEEAAVREVQDYALMGKLGIS---RVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSH 128
Cdd:PRK15439 91 VPQepllfpnlsvkenilfgLPKRQASMQKMKQLLAALGCQldlDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 129 LDRAGIDFLVSRLK--LYTG-ALLIISHDRDLLDRVADKIWELKDGRITeywggysdyLAQKEAERNRqlaqyqqaeaer 205
Cdd:PRK15439 171 LTPAETERLFSRIRelLAQGvGIVFISHKLPEIRQLADRISVMRDGTIA---------LSGKTADLST------------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 206 ERLEQAISeKKVQARRLDQKSraagKNSTESGGrlaHQKSQGSKQKKLhtaarqmqrRIEALDGvsapEELWSVQF--YH 283
Cdd:PRK15439 230 DDIIQAIT-PAAREKSLSASQ----KLWLELPG---NRRQQAAGAPVL---------TVEDLTG----EGFRNISLevRA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 284 SEVLELHHPLPVTGHELCKQLgdkvildrVSFQFPLGGKIAITGGNGAGKTTllnmiRDR-EEGVVIAP---KAEIGYFD 359
Cdd:PRK15439 289 GEILGLAGVVGAGRTELAETL--------YGLRPARGGRIMLNGKEINALST-----AQRlARGLVYLPedrQSSGLYLD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 360 Q----TGYKFTRNQNVMaYMQEGSDysvpdiRAVLS----SMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLD 431
Cdd:PRK15439 356 AplawNVCALTHNRRGF-WIKPARE------NAVLEryrrALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 432 EPGNFLDIPAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAqnvAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-175 |
4.93e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.09 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDID--RLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfayipQLEEAAVRE- 79
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKdvSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM-----VLSEETVWDv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 80 -------------------VQDYALMG--KLGIS------RVQAEI---------------MSGGEETRLKIAQALEDNV 117
Cdd:PRK13635 80 rrqvgmvfqnpdnqfvgatVQDDVAFGleNIGVPreemveRVDQALrqvgmedflnrephrLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 118 HGIMADEPTSHLDRAG-IDFL--VSRLKLYTGALLI-ISHDrdlLDRVA--DKIWELKDGRITE 175
Cdd:PRK13635 160 DIIILDEATSMLDPRGrREVLetVRQLKEQKGITVLsITHD---LDEAAqaDRVIVMNKGEILE 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
306-481 |
5.04e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.86 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDRE---EGVVIAPKAEIGYFDQTGykFTRNqnvMAYM------Q 376
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQppsEGEILLDAQPLESWSSKA--FARK---VAYLpqqlpaA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 377 EG------------------SDYSVPDIRAV---LSSMGFTPEDVRKELSmLSGGEIIKLQLARLLLGRYNILLLDEPGN 435
Cdd:PRK10575 98 EGmtvrelvaigrypwhgalGRFGAADREKVeeaISLVGLKPLAHRLVDS-LSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752069711 436 FLDIP----AMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK10575 177 ALDIAhqvdVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
297-481 |
5.46e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.06 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 297 GHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR------------DREEGVVIAPKA---EIGYFDQT 361
Cdd:PRK10253 10 GEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahghvwlDGEHIQHYASKEvarRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 362 GYKfTRNQNVMAYMQEGSDYSVP--------DIRAVLSSMGFT--PEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLD 431
Cdd:PRK10253 90 ATT-PGDITVQELVARGRYPHQPlftrwrkeDEEAVTKAMQATgiTHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 432 EPGNFLDIP----AMEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK10253 169 EPTTWLDIShqidLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-173 |
5.72e-06 |
|
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: 47.36 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMG----RDV-LDIDRLELYaydriGLVGANGAGKSTLLKTLLGRIPLQYGK------------IERQGTF 66
Cdd:cd03265 1 IEVENLVKKYGDfeavRGVsFRVRRGEIF-----GLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvrepREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 67 AYIPQL------------------------EEAAVREVQDYALMGKLGISRVQAEIMSGGEETRLKIAQALednVHG--- 119
Cdd:cd03265 76 GIVFQDlsvddeltgwenlyiharlygvpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL---VHRpev 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 120 IMADEPTSHLD---RAGIDFLVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03265 153 LFLDEPTIGLDpqtRAHVWEYIEKLKEEFGmTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
308-481 |
5.72e-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: 47.48 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 308 VILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR------------DREEGVVIAP---KAEIGYFDQTGYKFTRN-QNV 371
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQrfyvpengrvlvDGHDLALADPawlRRQVGVVLQENVLFNRSiRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 372 MAYMQEGSDY-------SVPDIRAVLSSMgftPED----VRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIP 440
Cdd:cd03252 96 IALADPGMSMervieaaKLAGAHDFISEL---PEGydtiVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1752069711 441 AMEALETMMREYPG--TIVFISHDTRLVERvADQVYVLKKGQL 481
Cdd:cd03252 173 SEHAIMRNMHDICAgrTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
309-481 |
5.98e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 48.67 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 309 ILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIAPKAEIGYFDQTG------------YKFT---RNQN 370
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtraWDPQQGEILLNGQPIADYSEAAlrqaisvvsqrvHLFSatlRDNL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 371 VMAYMQEGSDysvpDIRAVLSSMGF-TPEDVRKELSM--------LSGGEIIKLQLARLLLGRYNILLLDEPGNFLD--- 438
Cdd:PRK11160 435 LLAAPNASDE----ALIEVLQQVGLeKLLEDDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDaet 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752069711 439 ---IpaMEALETMMREypGTIVFISHDTRLVERVaDQVYVLKKGQL 481
Cdd:PRK11160 511 erqI--LELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
310-481 |
7.77e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.67 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGK--------------IAITGGNGAGKTTL---LNMIRDREEGVVIAPKAEIGyfdqtgyKFTRNQNVM 372
Cdd:PRK13644 4 LENVSYSYPDGTPaleninlvikkgeyIGIIGKNGSGKSTLalhLNGLLRPQKGKVLVSGIDTG-------DFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 373 AYMqeGSDYSVPDI----RAVLSSMGFTPE-------DVRKELSM-----------------LSGGEIIKLQLARLLLGR 424
Cdd:PRK13644 77 KLV--GIVFQNPETqfvgRTVEEDLAFGPEnlclppiEIRKRVDRalaeiglekyrhrspktLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 425 YNILLLDEPGNFLDIPAMEA-LETMMR--EYPGTIVFISHDTRLVErVADQVYVLKKGQL 481
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAvLERIKKlhEKGKTIVYITHNLEELH-DADRIIVMDRGKI 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
305-476 |
8.04e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.45 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreeGVVIAP-KAEIgYFD-----------------------Q 360
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI-----GGQIAPdHGEI-LFDgenipamsrsrlytvrkrmsmlfQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 361 TGYKFTRN---QNVMAYMQEGSDYSVPDIRAVLsSMGFTPEDVR--KEL--SMLSGGEIIKLQLARLLLGRYNILLLDEP 433
Cdd:PRK11831 92 SGALFTDMnvfDNVAYPLREHTQLPAPLLHSTV-MMKLEAVGLRgaAKLmpSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752069711 434 GNFLDIPAMEALETMMREYPG----TIVFISHDTRLVERVADQVYVL 476
Cdd:PRK11831 171 FVGQDPITMGVLVKLISELNSalgvTCVVVSHDVPEVLSIADHAYIV 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
310-481 |
8.20e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.42 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR---DREEGVVIAPKAEIGyfdqtgyKFTRN---QNVMAYMQEGS--DY 381
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQrvfDPQSGRILIDGTDIR-------TVTRAslrRNIAVVFQDAGlfNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 382 SVPD-IRavLSSMGFTPEDVRKEL------------------------SMLSGGEIIKLQLARLLLGRYNILLLDEPGNF 436
Cdd:PRK13657 424 SIEDnIR--VGRPDATDEEMRAAAeraqahdfierkpdgydtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752069711 437 LDIPA----MEALETMMREYpgTIVFISHdtRLVE-RVADQVYVLKKGQL 481
Cdd:PRK13657 502 LDVETeakvKAALDELMKGR--TTFIIAH--RLSTvRNADRILVFDNGRV 547
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
33-168 |
8.42e-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: 46.16 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 33 GLVGANGAGKSTLLKTLLGRiPLQYGKIERQGTFAYIPQLEEAAVREVQDYALmGKLGISRvQAEIMSGGEETRLKIAQA 112
Cdd:cd03238 25 VVTGVSGSGKSTLVNEGLYA-SGKARLISFLPKFSRNKLIFIDQLQFLIDVGL-GYLTLGQ-KLSTLSGGELQRVKLASE 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 113 LEDNVHG--IMADEPTSHLDRAGIDFLVSRLK--LYTG-ALLIISHDRDLLDRvADKIWEL 168
Cdd:cd03238 102 LFSEPPGtlFILDEPSTGLHQQDINQLLEVIKglIDLGnTVILIEHNLDVLSS-ADWIIDF 161
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
312-481 |
8.44e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.88 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 312 RVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIGYFDQTGYK-----------FTRN---------QNV 371
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLI----AGFLTPASGSLTLNGQDHTTtppsrrpvsmlFQENnlfshltvaQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 372 MAYMQEG---SDYSVPDIRAVLSSMGFtpEDVRKEL-SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPAMEA--- 444
Cdd:PRK10771 93 GLGLNPGlklNAAQREKLHAIARQMGI--EDLLARLpGQLSGGQRQRVALARCLVREQPILLLDEPFSALD-PALRQeml 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1752069711 445 --LETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK10771 170 tlVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
397-480 |
1.10e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.41 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 397 PEdVRKELSM----LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA----MEALETMMREYPGTIVFISHDTRLVER 468
Cdd:PRK09473 149 PE-ARKRMKMypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqiMTLLNELKREFNTAIIMITHDLGVVAG 227
|
90
....*....|..
gi 1752069711 469 VADQVYVLKKGQ 480
Cdd:PRK09473 228 ICDKVLVMYAGR 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-173 |
1.15e-05 |
|
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: 45.89 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 5 KAEEIVVEYMGRDVldidRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT--------------FAYIP 70
Cdd:cd03215 6 EVRGLSVKGAVRDV----SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 71 qlEEaavRevQDYALMGKLGISR--VQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYT--- 145
Cdd:cd03215 82 --ED---R--KREGLVLDLSVAEniALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdag 154
|
170 180
....*....|....*....|....*...
gi 1752069711 146 GALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03215 155 KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
306-481 |
1.16e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.62 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKT----TLLNMI---------RDREEGVVIAPKAEIGYFDQTGYKFTRN---- 368
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpagvrqtagRVLLDGKPVAPCALRGRKIATIMQNPRSafnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 369 -QNVMAYMQE-----GSDYSVPDIRAVLSSMGFtpEDVRKELSM----LSGGEIIKLQLARLLLGRYNILLLDEPGNFLD 438
Cdd:PRK10418 95 lHTMHTHAREtclalGKPADDATLTAALEAVGL--ENAARVLKLypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1752069711 439 IPA----MEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK10418 173 VVAqariLDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
305-438 |
1.25e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.02 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVViAPKAEIGYFDQTGY--KFTRNQNVM--AYMQE 377
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALlaeMDKVEGHV-HMKGSVAYVPQQAWiqNDSLRENILfgKALNE 727
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1752069711 378 GSDYSVPDIRAVLSSMGFTPEDVRKELSM----LSGGEIIKLQLARLLLGRYNILLLDEPGNFLD 438
Cdd:TIGR00957 728 KYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-173 |
1.34e-05 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 47.49 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRD---VLDIDRLELYAYDR--IGLVGANGAGKSTLLKTLLGRIPLQYGKIE-RQG------------ 64
Cdd:TIGR03269 279 IIKVRNVSKRYISVDrgvVKAVDNVSLEVKEGeiFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGdewvdmtkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 65 --------------TFAYIPQ------LEEAAVREVQDYALMGK-------LGISRVQAE--------IMSGGEETRLKI 109
Cdd:TIGR03269 359 grgrakryigilhqEYDLYPHrtvldnLTEAIGLELPDELARMKavitlkmVGFDEEKAEeildkypdELSEGERHRVAL 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 110 AQALEDNVHGIMADEPTSHLD-----RAGIDFLVSRLKLyTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDpitkvDVTHSILKAREEM-EQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-173 |
1.35e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 46.65 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 31 RIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfaYIPQLEEAAVRE-----------------VQDYALMGKLGISR 93
Cdd:PRK13647 33 KTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR--EVNAENEKWVRSkvglvfqdpddqvfsstVWDDVAFGPVNMGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 94 VQAEI-----------------------MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVS---RLKLYTGA 147
Cdd:PRK13647 111 DKDEVerrveealkavrmwdfrdkppyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEildRLHNQGKT 190
|
170 180
....*....|....*....|....*.
gi 1752069711 148 LLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:PRK13647 191 VIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
305-481 |
1.37e-05 |
|
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: 46.42 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDRE---EGVVIAPKAEIGYFDQTGYKFTRNQNVMAYMQegsdY 381
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLErptSGSVLVDGTDLTLLSGKELRKARRRIGMIFQH----F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 382 SVPDIRAVL-----------SSMGFTPEDVRKEL-------------SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFL 437
Cdd:cd03258 92 NLLSSRTVFenvalpleiagVPKAEIEERVLELLelvgledkadaypAQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 438 DiPA-----MEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03258 172 D-PEttqsiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-173 |
1.40e-05 |
|
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: 48.09 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 10 VVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKI-------------ERQG------------ 64
Cdd:TIGR01257 937 IFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkdietnldaVRQSlgmcpqhnilfh 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 65 --TFA----YIPQLEEAAVREVQ--DYALMGKLGISRV---QAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD--- 130
Cdd:TIGR01257 1017 hlTVAehilFYAQLKGRSWEEAQleMEAMLEDTGLHHKrneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpys 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752069711 131 -RAGIDFLvsrLKLYTGALLIIS-HDRDLLDRVADKIWELKDGRI 173
Cdd:TIGR01257 1097 rRSIWDLL---LKYRSGRTIIMStHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
309-471 |
1.43e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.57 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 309 ILDRVSFQFPLGGKIAITGGNGAGKTTL---LNMIRDREEGVVIAPKAEigYFDQTGYKFTRNQNVMAyMQEGSDYSVPD 385
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELESEVRVEGRVE--FFNQNIYERRVNLNRLR-RQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 386 IRAV---------LSSMGFTP------------------EDVRKELSM----LSGGEIIKLQLARLLLGRYNILLLDEPG 434
Cdd:PRK14258 99 LFPMsvydnvaygVKIVGWRPkleiddivesalkdadlwDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1752069711 435 NFLDIPAMEALETMMREYP----GTIVFISHDTRLVERVAD 471
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSRLSD 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
298-482 |
1.61e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.35 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGD-KV---ILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---GVVI-----------APKA-----E 354
Cdd:PRK11629 9 DNLCKRYQEgSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTptsGDVIfngqpmsklssAAKAelrnqK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 355 IGYFDQTGY---KFTRNQNV-MAYMQEGSDYSVPDIRA--VLSSMGFTpEDVRKELSMLSGGEIIKLQLARLLLGRYNIL 428
Cdd:PRK11629 89 LGFIYQFHHllpDFTALENVaMPLLIGKKKPAEINSRAleMLAAVGLE-HRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 429 LLDEPGNFLDIPAMEALETMMREY---PGT-IVFISHDTRLVERVADQVYvLKKGQLQ 482
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELnrlQGTaFLVVTHDLQLAKRMSRQLE-MRDGRLT 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-134 |
1.61e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.64 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYIPQLEEAA--------------VREVQDY---------------- 83
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylghrnamkpaltVAENLEFwaaflggeeldiaaal 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1752069711 84 ALMGKLGISRVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGI 134
Cdd:PRK13539 113 EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
295-481 |
1.66e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 46.44 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 295 VTGHELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREEgvvIAPKAEIG---YFD-QTGYKF----- 365
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIE---LYPEARVSgevYLDgQDIFKMdviel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 366 -TRNQNVMAYMQEGSDYSV-------PDIRAVLSSMGFTPEDVRKEL-----------------SMLSGGEIIKLQLARL 420
Cdd:PRK14247 81 rRRVQMVFQIPNPIPNLSIfenvalgLKLNRLVKSKKELQERVRWALekaqlwdevkdrldapaGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 421 LLGRYNILLLDEPGNFLDIPAMEALETMMREYPG--TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
397-481 |
1.72e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 46.54 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 397 PED-VRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA----MEALETMMREYPGTIVFISHDTRLVERVAD 471
Cdd:PRK13645 140 PEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIAD 219
|
90
....*....|
gi 1752069711 472 QVYVLKKGQL 481
Cdd:PRK13645 220 EVIVMHEGKV 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
310-481 |
1.77e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.94 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFpLGGKI-AITGGNGAGKTTLLNMI-----------------------RD-REEGVVI-------APK---AE 354
Cdd:COG1129 20 LDGVSLEL-RPGEVhALLGENGAGKSTLMKILsgvyqpdsgeilldgepvrfrspRDaQAAGIAIihqelnlVPNlsvAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 355 ---IGYFDQTGYKFTRNQnvmayMQEgsdysvpDIRAVLSSMGFtPEDVRKELSMLSGG-----EIiklqlARLLLGRYN 426
Cdd:COG1129 99 nifLGREPRRGGLIDWRA-----MRR-------RARELLARLGL-DIDPDTPVGDLSVAqqqlvEI-----ARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 427 ILLLDEPGNFLDIPAMEALETMMREYPG---TIVFISHdtRL--VERVADQVYVLKKGQL 481
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISH--RLdeVFEIADRVTVLRDGRL 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-153 |
2.22e-05 |
|
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: 45.18 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 6 AEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT------------FAYI---P 70
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiargLLYLghaP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 71 QLEEA-AVRE--------------VQDYALMGKLGISRVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGID 135
Cdd:cd03231 83 GIKTTlSVLEnlrfwhadhsdeqvEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|.
gi 1752069711 136 FLVSRLKLYT---GALLIISH 153
Cdd:cd03231 163 RFAEAMAGHCargGMVVLTTH 183
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
305-480 |
3.06e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 45.36 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIGYFDQ--TGYK-FTRNQNVMAYMQEG--- 378
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI----SGLLPPRSGSIRFDGEdiTGLPpHRIARLGIGYVPEGrri 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 379 -SDYSVPD-------IRAVLSSMGFTPEDV----------RKEL-SMLSGGEiiklQ----LARLLLGRYNILLLDEPGN 435
Cdd:COG0410 90 fPSLTVEEnlllgayARRDRAEVRADLERVyelfprlkerRRQRaGTLSGGE----QqmlaIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 436 FL------DIpaMEALETMMREypG-TIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:COG0410 166 GLapliveEI--FEIIRRLNRE--GvTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
309-480 |
3.11e-05 |
|
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: 45.30 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 309 ILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVI------------APKAEIGYFDQTGYKF--TRNQNV 371
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfYDVDSGRILidghdvrdytlaSLRRQIGLVSQDVFLFndTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 372 MaymqegsdYSVPDIravlssmgfTPEDVRKEL------------------------SMLSGGEIIKLQLARLLLGRYNI 427
Cdd:cd03251 97 A--------YGRPGA---------TREEVEEAAraanahefimelpegydtvigergVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752069711 428 LLLDEPGNFLDIPA----MEALETMMREYpgTIVFISHDTRLVERvADQVYVLKKGQ 480
Cdd:cd03251 160 LILDEATSALDTESerlvQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGK 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
299-481 |
3.15e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 45.51 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 299 ELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR-----------------------DREEGVVIAPKAEI 355
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvgditidtarslSQQKGLIRQLRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 356 GYFDQTGYKF---TRNQNVM----AYMQEGSDYSVPDIRAVLSSMGFTPedvrKELSM---LSGGEIIKLQLARLLLGRY 425
Cdd:PRK11264 88 GFVFQNFNLFphrTVLENIIegpvIVKGEPKEEATARARELLAKVGLAG----KETSYprrLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 426 NILLLDEPGNFLDiPAM--EALETM--MREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK11264 164 EVILFDEPTSALD-PELvgEVLNTIrqLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
33-173 |
3.19e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 45.87 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 33 GLVGANGAGKSTLLKTLLGRI------------PLQYGKIERqgtFAYIPqlEE-------------------------A 75
Cdd:COG4152 31 GLLGPNGAGKTTTIRIILGILapdsgevlwdgePLDPEDRRR---IGYLP--EErglypkmkvgeqlvylarlkglskaE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 76 AVREVQDYalMGKLGIS-----RVQAeiMSGGEETRLKIAQALednVHG----IMaDEPTSHLDRAGIDFLVSRLKLYT- 145
Cdd:COG4152 106 AKRRADEW--LERLGLGdrankKVEE--LSKGNQQKVQLIAAL---LHDpellIL-DEPFSGLDPVNVELLKDVIRELAa 177
|
170 180 190
....*....|....*....|....*....|
gi 1752069711 146 -GALLIIS-HDRDLLDRVADKIWELKDGRI 173
Cdd:COG4152 178 kGTTVIFSsHQMELVEELCDRIVIINKGRK 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-174 |
3.44e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.20 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 24 LELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIE---------------RQGtFAYIPQ--------LE------- 73
Cdd:PRK15439 284 LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMlngkeinalstaqrlARG-LVYLPEdrqssglyLDaplawnv 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 74 ----------------EAAVREVQDYALMGKLGISRVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGI 134
Cdd:PRK15439 363 calthnrrgfwikparENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDvsaRNDI 442
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1752069711 135 DFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRIT 174
Cdd:PRK15439 443 YQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
310-479 |
3.59e-05 |
|
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: 45.15 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---GVVIAPKAEIgyfDQTG---------YKF----TRNQNV-M 372
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQptsGGVILEGKQI---TEPGpdrmvvfqnYSLlpwlTVRENIaL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 373 AYMQEGSDYSVPDIRAV----LSSMGFTpEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEAL-ET 447
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIveehIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLqEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1752069711 448 MMR---EYPGTIVFISHDTRLVERVADQVYVLKKG 479
Cdd:TIGR01184 157 LMQiweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
323-475 |
3.62e-05 |
|
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: 46.32 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 323 IAITGGNGAGKTTLLNMIRDRE---EGVVIaPKAEIGYFDQtgykftrnqnvmaYMQEGSDYSVPD-----IRAVLSSMG 394
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLkpdEGEVD-EDLKISYKPQ-------------YISPDYDGTVEEflrsaNTDDFGSSY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 395 FTPEDVR---------KELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD----IPAMEALETMMREYPGTIVFISH 461
Cdd:COG1245 435 YKTEIIKplgleklldKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDH 514
|
170
....*....|....
gi 1752069711 462 DTRLVERVADQVYV 475
Cdd:COG1245 515 DIYLIDYISDRLMV 528
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-172 |
3.81e-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: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLGRIPLQYGKIERqgtfayipqleeAAVREVQDYALMGKLGISRVQAEIMSGGEET-RLKIA 110
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIY------------IDGEDILEEVLDQLLLIIVGGKKASGSGELRlRLALA 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 111 QALEDNVHGIMADEPTSHLDRAG---------IDFLVSRLKLYTGALLIISH-----DRDLLDRVADKIWELKDGR 172
Cdd:smart00382 73 LARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTTNdekdlGPALLRRRFDRRIVLLLIL 148
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
295-476 |
4.06e-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: 44.10 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 295 VTGHELCKQLGDKVILDRVSfQFPLGGKIAITGGNGAGKTTLLNMIRDREEgvviapkaeigyfdqtgykftrnqnvmay 374
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLI----------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 375 mQEGSDYSVPDIRAVlssmgFTPEDVRkelsmLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIP----AMEALETMMR 450
Cdd:cd03222 51 -PNGDNDEWDGITPV-----YKPQYID-----LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSE 119
|
170 180
....*....|....*....|....*.
gi 1752069711 451 EYPGTIVFISHDTRLVERVADQVYVL 476
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-175 |
4.38e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 25 ELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT----------------FAYIPQLEEAAV--REVQDYALM 86
Cdd:PRK10261 346 DLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgklqalrrdIQFIFQDPYASLdpRQTVGDSIM 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 87 ----------GKLGISRVqAEIM-----------------SGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDF 136
Cdd:PRK10261 426 eplrvhgllpGKAAAARV-AWLLervgllpehawryphefSGGQRQRICIARALALNPKVIIADEAVSALDvsiRGQIIN 504
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1752069711 137 LVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:PRK10261 505 LLLDLQRDFGiAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
310-480 |
4.41e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.22 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTL---LNMIRDREEGVVIAPKAEIGYFDQTGYKFTRNQNVMAYMQEGSDYSVP-- 384
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLfqnLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDPDNQLFSASvy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 385 -DIRAVLSSMGFTPEDVRKELS-----------------MLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA----M 442
Cdd:PRK13636 102 qDVSFGAVNLKLPEDEVRKRVDnalkrtgiehlkdkpthCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGvseiM 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752069711 443 EALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:PRK13636 182 KLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
24-173 |
5.04e-05 |
|
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: 44.64 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 24 LELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIE---------------RQG---TFAyIPQL------------- 72
Cdd:COG0411 25 LEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphriaRLGiarTFQ-NPRLfpeltvlenvlva 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 73 ---------------------EEAAVREvQDYALMGKLGISRV---QAEIMSGGEETRLKIAQALednvhgiMA------ 122
Cdd:COG0411 104 aharlgrgllaallrlprarrEEREARE-RAEELLERVGLADRadePAGNLSYGQQRRLEIARAL-------ATepklll 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 123 -DEPT---SHLDRAGIDFLVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:COG0411 176 lDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-130 |
5.11e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 23 RLELYAYDRIGLVGANGAGKSTLLKTLLGRIP-LQYGKIERQGTFAYIPQLE---EAAVRE----------------VQD 82
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGELShAETSSVVIRGSVAYVPQVSwifNATVREnilfgsdfeserywraIDV 716
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 83 YALMGKLGI--SRVQAEI------MSGGEETRLKIAQALEDNVHGIMADEPTSHLD 130
Cdd:PLN03232 717 TALQHDLDLlpGRDLTEIgergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
310-481 |
5.16e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 44.48 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreegvVIAPKAEIGYFDQTGYKFTRNQNvmAYMQEGSDYSVPDIRAV 389
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTL-------CGDPRATSGRIVFDGKDITDWQT--AKIMREAVAIVPEGRRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 390 LSSMgftpeDVRKELSM----------------------------------LSGGEIIKLQLARLLLGRYNILLLDEPG- 434
Cdd:PRK11614 92 FSRM-----TVEENLAMggffaerdqfqerikwvyelfprlherriqragtMSGGEQQMLAIGRALMSQPRLLLLDEPSl 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1752069711 435 NFLDIPAMEALETM--MREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK11614 167 GLAPIIIQQIFDTIeqLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
387-483 |
5.18e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.01 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 387 RAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPA-----MEALETMMREYPGTIVFISH 461
Cdd:PRK13634 126 REMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD-PKgrkemMEMFYKLHKEKGLTTVLVTH 204
|
90 100
....*....|....*....|..
gi 1752069711 462 DTRLVERVADQVYVLKKGQLQR 483
Cdd:PRK13634 205 SMEDAARYADQIVVMHKGTVFL 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
307-340 |
5.57e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 44.69 E-value: 5.57e-05
10 20 30
....*....|....*....|....*....|....
gi 1752069711 307 KVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI 340
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAI 52
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
306-482 |
5.81e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 44.72 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIrdreEGVVIAPKAEIgYFD--------------QTGYKFTR--NQ 369
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLI----DGLLEAESGQI-IIDgdllteenvwdirhKIGMVFQNpdNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 370 NVMAYMQEgsdysvpDIRAVLSSMGFTPEDVR-----------------KELSMLSGGEIIKLQLARLLLGRYNILLLDE 432
Cdd:PRK13650 94 FVGATVED-------DVAFGLENKGIPHEEMKervnealelvgmqdfkeREPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 433 PGNFLD----IPAMEALETMMREYPGTIVFISHDtrlVERVA--DQVYVLKKGQLQ 482
Cdd:PRK13650 167 ATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVAlsDRVLVMKNGQVE 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
407-481 |
6.09e-05 |
|
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: 44.56 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 407 LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPAM-----EALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALD-PLIrremqDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
407-481 |
6.56e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 44.74 E-value: 6.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 407 LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-481 |
7.20e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.45 E-value: 7.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 405 SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMREYPG--TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK14267 148 SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
35-208 |
7.69e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 35 VGANGAGKSTL--LKTLL-----------GRIPLQYGKIER-----------QGTFAYI-P------QLEE--------- 74
Cdd:PRK11308 47 VGESGCGKSTLarLLTMIetptggelyyqGQDLLKADPEAQkllrqkiqivfQNPYGSLnPrkkvgqILEEpllintsls 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 75 AAVREVQDYALMGKLGISRVQAE----IMSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTG- 146
Cdd:PRK11308 127 AAERREKALAMMAKVGLRPEHYDryphMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvsvQAQVLNLMMDLQQELGl 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752069711 147 ALLIISHDRDLLDRVADKIWELKDGRITEywggysdyLAQKEAERNRQLAQYQQA----------EAERERL 208
Cdd:PRK11308 207 SYVFISHDLSVVEHIADEVMVMYLGRCVE--------KGTKEQIFNNPRHPYTQAllsatprlnpDDRRERI 270
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
293-479 |
8.07e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.21 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 293 LPVTGheLCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLN-------------MIRDRE----EGVVIAPKAEI 355
Cdd:PRK11300 6 LSVSG--LMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNcltgfykptggtiLLRGQHieglPGHQIARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 356 GYFdQTGYKFTR---------------NQNVMAYMQEGSDYSVPDIRAV------LSSMGFTpEDVRKELSMLSGGEIIK 414
Cdd:PRK11300 84 RTF-QHVRLFREmtvienllvaqhqqlKTGLFSGLLKTPAFRRAESEALdraatwLERVGLL-EHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 415 LQLARLLLGRYNILLLDEPGNFLDIPAMEALETMM----REYPGTIVFISHDTRLVERVADQVYVLKKG 479
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
99-175 |
8.24e-05 |
|
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: 45.06 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 99 MSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRIT 174
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvQAQILDLLKDLQRELGmALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
.
gi 1752069711 175 E 175
Cdd:COG4172 237 E 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
300-481 |
8.97e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 44.71 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNM-----------------------IRDREEGVV-----IAP 351
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLvaglekptegqifidgedvthrsIQQRDICMVfqsyaLFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 352 KAEIGyfDQTGYKFtRNQNVMaymQEGSDYSVPDIRAVLSSMGFtpEDvrKELSMLSGGEIIKLQLARLLLGRYNILLLD 431
Cdd:PRK11432 92 HMSLG--ENVGYGL-KMLGVP---KEERKQRVKEALELVDLAGF--ED--RYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 432 EPGNFLDIPAMEALETMMRE----YPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-187 |
9.21e-05 |
|
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: 43.76 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 15 GRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGT-------------FAYIPQ---LEEAAVR 78
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQdvfLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 79 EVQDYalmGKLGISRVQAE-----------IM-----------------SGGEETRLKIAQALEDNVHGIMADEPTSHLD 130
Cdd:cd03251 94 ENIAY---GRPGATREEVEeaaraanahefIMelpegydtvigergvklSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 131 -------RAGIDFLvsrLKLYTGalLIISHdRDLLDRVADKIWELKDGRITEYwGGYSDYLAQK 187
Cdd:cd03251 171 teserlvQAALERL---MKNRTT--FVIAH-RLSTIENADRIVVLEDGKIVER-GTHEELLAQG 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
298-481 |
9.27e-05 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 43.67 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 298 HELCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---------GVVI-APKAEIGYFDQ-TGYKFt 366
Cdd:cd03262 4 KNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiiidGLKLtDDKKNINELRQkVGMVF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 367 RNQNVMAYMqegsdysvpdirAVLSSMGFTPEDVRK-------ELSM------------------LSGGEIIKLQLARLL 421
Cdd:cd03262 83 QQFNLFPHL------------TVLENITLAPIKVKGmskaeaeERALellekvgladkadaypaqLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 422 LGRYNILLLDEPGNFLDiPAM--EALETMMR--EYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:cd03262 151 AMNPKVMLFDEPTSALD-PELvgEVLDVMKDlaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
310-451 |
1.00e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.10 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRdreeGVVIAPKAEIGYFDQTGYKFTRnQNVMAYM--QEGSDYSVPDIR 387
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALM----GFVRLASGKISILGQPTRQALQ-KNLVAYVpqSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 388 AVLSSMGF----------TPEDVR----------------KELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA 441
Cdd:PRK15056 98 EDVVMMGRyghmgwlrraKKRDRQivtaalarvdmvefrhRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170
....*....|
gi 1752069711 442 MEALETMMRE 451
Cdd:PRK15056 178 EARIISLLRE 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
302-480 |
1.01e-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: 44.82 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 302 KQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNM-------------------------IRDREE-GVVI------ 349
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIlsgvyphgtwdgeiywsgsplkasnIRDTERaGIVIihqelt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 350 -APKAEIGYFDQTGYKFTRNQNVMAYmqegsDYSVPDIRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNIL 428
Cdd:TIGR02633 89 lVPELSVAENIFLGNEITLPGGRMAY-----NAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1752069711 429 LLDEPGNFLDIPAMEALETMMREYPG---TIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
9-69 |
1.03e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.04 E-value: 1.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 9 IVVEYMGRDVLDIDRLELYAY--DRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAYI 69
Cdd:PRK13546 28 LIPKHKNKTFFALDDISLKAYegDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI 90
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-175 |
1.17e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.87 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTL------------LGRIP----------LQYGKIE 61
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmnelesevrvEGRVEffnqniyerrVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 62 RQGTFAYI-----------------------PQLE-----EAAVREVQDY-ALMGKLGISRVQaeiMSGGEETRLKIAQA 112
Cdd:PRK14258 88 RQVSMVHPkpnlfpmsvydnvaygvkivgwrPKLEiddivESALKDADLWdEIKHKIHKSALD---LSGGQQQRLCIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 113 LEDNVHGIMADEPTSHLDRAG---IDFLVSRLKLYTG-ALLIISHDRDLLDRVAD--KIWELKDGRITE 175
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRLRSElTMVIVSHNLHQVSRLSDftAFFKGNENRIGQ 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
100-176 |
1.19e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.94 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 100 SGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKL-YTGALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvQAQIMTLLNELKReFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
.
gi 1752069711 176 Y 176
Cdd:PRK09473 243 Y 243
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
306-438 |
1.20e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 306 DKVILDRVSFQFPLGGKIAITGGNGAGKTTLLN-MIRD--REEGVVIAPKAEIGYFDQTGYKFtrNQNVMAYMQEGSDYS 382
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGElsHAETSSVVIRGSVAYVPQVSWIF--NATVRENILFGSDFE 706
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 383 VP------DIRAVLSSMGFTPEDVRKELSM----LSGGEIIKLQLARLLLGRYNILLLDEPGNFLD 438
Cdd:PLN03232 707 SErywraiDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
318-480 |
1.27e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.88 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 318 PLGGKIAITGGNGAGKTTLLNMIRdREEGVVIA-PKAEIgyFDQTGYKftrnqnvmaymqegsdysvpDIRAVLSSMGFT 396
Cdd:PRK13637 59 PTSGKIIIDGVDITDKKVKLSDIR-KKVGLVFQyPEYQL--FEETIEK--------------------DIAFGPINLGLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 397 PEDVRKEL--SM-----------------LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA----MEALETMMREYP 453
Cdd:PRK13637 116 EEEIENRVkrAMnivgldyedykdkspfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeiLNKIKELHKEYN 195
|
170 180
....*....|....*....|....*..
gi 1752069711 454 GTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:PRK13637 196 MTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-129 |
1.32e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG---TFA------------ 67
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkevTFNgpkssqeagigi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 68 ------YIPQLEEAAV----REV----------QDYA----LMGKLGI---SRVQAEIMSGGEETRLKIAQAL--EDNVh 118
Cdd:PRK10762 84 ihqelnLIPQLTIAENiflgREFvnrfgridwkKMYAeadkLLARLNLrfsSDKLVGELSIGEQQMVEIAKVLsfESKV- 162
|
170
....*....|.
gi 1752069711 119 gIMADEPTSHL 129
Cdd:PRK10762 163 -IIMDEPTDAL 172
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-173 |
1.32e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.82 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 19 LDIDRLELYAYD----RIGLVGANGAGKSTL-LKTLLGRiplqyGKIERQGTFAYIPQLEEAAVREVqdyalMGKLGISR 93
Cdd:PRK10253 66 LDGEHIQHYASKevarRIGLLAQNATTPGDItVQELVAR-----GRYPHQPLFTRWRKEDEEAVTKA-----MQATGITH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 94 VQAE---IMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRA-GIDFL-----VSRLKLYTGALLIisHDRDLLDRVADK 164
Cdd:PRK10253 136 LADQsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShQIDLLellseLNREKGYTLAAVL--HDLNQACRYASH 213
|
....*....
gi 1752069711 165 IWELKDGRI 173
Cdd:PRK10253 214 LIALREGKI 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
302-481 |
1.36e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.07 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 302 KQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLN-------------MIRDREEGVVIAPKAEIGYFDQTGYK-FTR 367
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYIGDKKNNHELITNPYSKKIKnFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 368 NQNVMAYMQEGSDYS------------------VPDIRA------VLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLG 423
Cdd:PRK13631 114 LRRRVSMVFQFPEYQlfkdtiekdimfgpvalgVKKSEAkklakfYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 424 RYNILLLDEPGNFLDiPAMEalETMMR------EYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK13631 194 QPEILIFDEPTAGLD-PKGE--HEMMQlildakANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
390-481 |
1.40e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.57 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 390 LSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD----IPAMEALETmMREYPGTIVFISHDTRL 465
Cdd:PRK13643 128 LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFES-IHQSGQTVVLVTHLMDD 206
|
90
....*....|....*.
gi 1752069711 466 VERVADQVYVLKKGQL 481
Cdd:PRK13643 207 VADYADYVYLLEKGHI 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-194 |
1.51e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 43.20 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 1 MLLIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTL-------LGRIplQYGKIERQGTFAYIPQle 73
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTI--RVGDITIDTARSLSQQ-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 74 EAAVREVQDY----------------------------------------ALMGKLGISRVQAEI---MSGGEETRLKIA 110
Cdd:PRK11264 77 KGLIRQLRQHvgfvfqnfnlfphrtvleniiegpvivkgepkeeatararELLAKVGLAGKETSYprrLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 111 QALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTG---ALLIISHDRDLLDRVADKIWELKDGRITEYwGGYSDYLAQK 187
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQekrTMVIVTHEMSFARDVADRAIFMDQGRIVEQ-GPAKALFADP 235
|
....*..
gi 1752069711 188 EAERNRQ 194
Cdd:PRK11264 236 QQPRTRQ 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
99-178 |
1.55e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 43.36 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 99 MSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKlYTGALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDpenTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
...
gi 1752069711 176 yWG 178
Cdd:PRK14247 226 -WG 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
32-174 |
1.58e-04 |
|
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: 43.09 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLLG-------------------------RIPLQYGK----------IERQGTFAYIPQLEEAA 76
Cdd:cd03267 50 VGFIGPNGAGKTTTLKILSGllqptsgevrvaglvpwkrrkkflrRIGVVFGQktqlwwdlpvIDSFYLLAAIYDLPPAR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 77 VRE-VQDYALMGKLG-ISRVQAEIMSGGEETRLKIAQALEDNVHGIMADEPTSHLD----RAGIDFLVSRLKLYTGALLI 150
Cdd:cd03267 130 FKKrLDELSELLDLEeLLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvvaqENIRNFLKEYNRERGTTVLL 209
|
170 180
....*....|....*....|....
gi 1752069711 151 ISHDRDLLDRVADKIWELKDGRIT 174
Cdd:cd03267 210 TSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
300-482 |
1.61e-04 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 43.93 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---RDREEGVVIapkaeIGYFDQTG---YKftRNQNVMa 373
Cdd:COG3842 11 VSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagfETPDSGRIL-----LDGRDVTGlppEK--RNVGMV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 374 yMQegsDY------SVPD-IRAVLSSMGFTPEDVRK------EL-----------SMLSGGEiiklQ----LARLLLGRY 425
Cdd:COG3842 83 -FQ---DYalfphlTVAEnVAFGLRMRGVPKAEIRArvaellELvglegladrypHQLSGGQ----QqrvaLARALAPEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 426 NILLLDEP-GNfLDIPAMEALET----MMREYPGTIVFISHDtrLVE--RVADQVYVLKKGQLQ 482
Cdd:COG3842 155 RVLLLDEPlSA-LDAKLREEMREelrrLQRELGITFIYVTHD--QEEalALADRIAVMNDGRIE 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
407-481 |
1.88e-04 |
|
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: 43.90 E-value: 1.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 407 LSGGEIIKLQLARLLLGRYNILLLDEPGNFLD--IPA--MEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDvtVQAqiLDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
300-340 |
1.93e-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: 1.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1752069711 300 LCKQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMI 340
Cdd:COG3839 9 VSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI 49
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
310-481 |
1.94e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.23 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 310 LDRVSFQFPLGGKIAITGGNGAGKTTLLNMI---------------RDREEGvVIAPKAEIGYFDQTGYKF---TRNQNV 371
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILtgllpptsgtvlvggKDIETN-LDAVRQSLGMCPQHNILFhhlTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 372 MAYMQ---EGSDYSVPDIRAVLSSMGFTPEDvRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETM 448
Cdd:TIGR01257 1025 LFYAQlkgRSWEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190
....*....|....*....|....*....|....*
gi 1752069711 449 MREYPG--TIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:TIGR01257 1104 LLKYRSgrTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
324-480 |
2.04e-04 |
|
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: 42.64 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 324 AITGGNGAGKTTLLNMI------------RDREEGVVIAP---KAEIG-YFDQTG--YKFTRnqnvmaymQEGSDYsvpD 385
Cdd:cd03279 32 LICGPTGAGKSTILDAItyalygktprygRQENLRSVFAPgedTAEVSfTFQLGGkkYRVER--------SRGLDY---D 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 386 --IRAVLSSMGFTPEDVRKELSMLSGGEI------IKLQLARLLLGRYNI----LLLDEPGNFLDIPAMEALETMMREYP 453
Cdd:cd03279 101 qfTRIVLLPQGEFDRFLARPVSTLSGGETflaslsLALALSEVLQNRGGArleaLFIDEGFGTLDPEALEAVATALELIR 180
|
170 180 190
....*....|....*....|....*....|
gi 1752069711 454 GT---IVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:cd03279 181 TEnrmVGVISHVEELKERIPQRLEVIKTPG 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
54-173 |
2.17e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.07 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 54 PLQYGKiERQGTFAYIPQLEEAaVREVQDYAlmgklgiSRVQAEiMSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG 133
Cdd:PRK13645 116 PVNLGE-NKQEAYKKVPELLKL-VQLPEDYV-------KRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1752069711 134 -IDF--LVSRL-KLYTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:PRK13645 186 eEDFinLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-130 |
2.18e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 42.23 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLLGR-----------IPLQYGKIERQGTFAYIPQL----EEAAVREVQDY-ALMGKLGISrvqae 97
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGRktagvitgeilINGRPLDKNFQRSTGYVEQQdvhsPNLTVREALRFsALLRGLSVE----- 112
|
90 100 110
....*....|....*....|....*....|...
gi 1752069711 98 imsggEETRLKIAQALEDNVHGIMADEPTSHLD 130
Cdd:cd03232 113 -----QRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-61 |
2.29e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 42.77 E-value: 2.29e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1752069711 24 LELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIE 61
Cdd:COG1101 27 LTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-173 |
2.32e-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: 43.02 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 16 RDV-LDIDRLELYAydrigLVGANGAGKSTLLKTLLGRIPLQYGKIERQGTfaYIPQLEEAAVREV---------QDYAL 85
Cdd:cd03294 41 NDVsLDVREGEIFV-----IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ--DIAAMSRKELRELrrkkismvfQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 86 MGKL-------------GISRVQ-----AEIM----------------SGGEETRLKIAQALEDNVHGIMADEPTSHLD- 130
Cdd:cd03294 114 LPHRtvlenvafglevqGVPRAEreeraAEALelvglegwehkypdelSGGMQQRVGLARALAVDPDILLMDEAFSALDp 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752069711 131 --RAGIDFLVSRLKLYTGALLI-ISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03294 194 liRREMQDELLRLQAELQKTIVfITHDLDEALRLGDRIAIMKDGRL 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-175 |
4.26e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.77 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 32 IGLVGANGAGKSTLLKTLL------GRI-----PLQ------------------------------YGKIERQGTFAYIP 70
Cdd:PRK15134 315 LGLVGESGSGKSTTGLALLrlinsqGEIwfdgqPLHnlnrrqllpvrhriqvvfqdpnsslnprlnVLQIIEEGLRVHQP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 71 QLEeAAVREVQDYALMGKLGIS-----RVQAEiMSGGEETRLKIAQALEDNVHGIMADEPTSHLDR---AGIDFLVSRLK 142
Cdd:PRK15134 395 TLS-AAQREQQVIAVMEEVGLDpetrhRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLDKtvqAQILALLKSLQ 472
|
170 180 190
....*....|....*....|....*....|....
gi 1752069711 143 -LYTGALLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:PRK15134 473 qKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
309-480 |
4.69e-04 |
|
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: 41.76 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 309 ILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIR---DREEGVV---------IAPK---AEIGYFDQTGYKF--TRNQNV 371
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfyDPTSGEIlldgvdirdLNLRwlrSQIGLVSQEPVLFdgTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 372 mAYMQEGSDySVPDIRAVLSS------MGFtPEDVRKEL----SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLD--- 438
Cdd:cd03249 98 -RYGKPDAT-DEEVEEAAKKAnihdfiMSL-PDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDaes 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752069711 439 -IPAMEALETMMREYpgTIVFISHdtRLVE-RVADQVYVLKKGQ 480
Cdd:cd03249 175 eKLVQEALDRAMKGR--TTIVIAH--RLSTiRNADLIAVLQNGQ 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
405-481 |
4.86e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.10 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 405 SMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPA-----MEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKG 479
Cdd:PRK11153 139 AQLSGGQKQRVAIARALASNPKVLLCDEATSALD-PAttrsiLELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAG 217
|
..
gi 1752069711 480 QL 481
Cdd:PRK11153 218 RL 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-199 |
5.23e-04 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 41.70 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 15 GRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG-------------TFAYIPQ---------- 71
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQenvlfnrsir 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 72 ---------------LEEAAVREVQDYALMGKLGISRVQAEI---MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG 133
Cdd:cd03252 94 dnialadpgmsmervIEAAKLAGAHDFISELPEGYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 134 IDFLVSRLK--LYTGALLIISHdRDLLDRVADKIWELKDGRITEywGGYSDYLAQKEAeRNRQLAQYQ 199
Cdd:cd03252 174 EHAIMRNMHdiCAGRTVIIIAH-RLSTVKNADRIIVMEKGRIVE--QGSHDELLAENG-LYAYLYQLQ 237
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-473 |
6.26e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 403 ELSMLSGGEIIKLQLA-RL-----LLGRYNILLLDEPGNFLDIPAMEALETMMREY----PGTIVfISHDTRLVErVADQ 472
Cdd:PRK03918 785 PLTFLSGGERIALGLAfRLalslyLAGNIPLLILDEPTPFLDEERRRKLVDIMERYlrkiPQVII-VSHDEELKD-AADY 862
|
.
gi 1752069711 473 V 473
Cdd:PRK03918 863 V 863
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
34-169 |
6.65e-04 |
|
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: 40.42 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTLLGRIPLQYGKIERQGTFAyiPQLEEAAVrevqDYALMgklgISRVQaeiMSGGEETRLKIAQAL 113
Cdd:cd03227 26 ITGPNGSGKSTILDAIGLALGGAQSATRRRSGVK--AGCIVAAV----SAELI----FTRLQ---LSGGEKELSALALIL 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752069711 114 EDNVHG----IMADEPTSHLD---RAGIDFLVSRLKLYTGALLIISHDRDLLDRvADKIWELK 169
Cdd:cd03227 93 ALASLKprplYILDEIDRGLDprdGQALAEAILEHLVKGAQVIVITHLPELAEL-ADKLIHIK 154
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-173 |
7.11e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 41.57 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 4 IKAEEIVVEYM-----GRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTLLGRIPLQYGKIERQG-------------- 64
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 65 -----TFAYiP--QLEEAAVRevQDYALMGK-LGIS------RVQAEI-----------------MSGGEETRLKIAQAL 113
Cdd:PRK13637 83 kkvglVFQY-PeyQLFEETIE--KDIAFGPInLGLSeeeienRVKRAMnivgldyedykdkspfeLSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752069711 114 EDNVHGIMADEPTSHLDRAGIDFLVSRLKL----YTGALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-176 |
7.17e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.30 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 3 LIKAEEIVVEYMGRDVLDIDRLELYAYDRIGLVGANGAGKSTLLKTL-----LGRIPLQYGKIERQGTFAYIPQLEEAAV 77
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 78 RE----------------------------VQDYALMGK-LGISRVQAEI--------------MSGGEETRLKIAQALE 114
Cdd:PRK14239 85 RKeigmvfqqpnpfpmsiyenvvyglrlkgIKDKQVLDEaVEKSLKGASIwdevkdrlhdsalgLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752069711 115 DNVHGIMADEPTSHLD--RAGI--DFLVSRLKLYTgaLLIISHDRDLLDRVADKIWELKDGRITEY 176
Cdd:PRK14239 165 TSPKIILLDEPTSALDpiSAGKieETLLGLKDDYT--MLLVTRSMQQASRISDRTGFFLDGDLIEY 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
320-481 |
7.76e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 41.94 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 320 GGKIAITGGNGAGKTT---LLNMIRDREEGVVIAPKAEIGYFDQTGYKFTRNQNVMAYMQEGS---DYSVPDIRAVLSSM 393
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTmvrLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFAlmpHMTVLDNTAFGMEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 394 GFTPEDVRKELSM------------------LSGGEIIKLQLARLLLGRYNILLLDEPGNFLD----IPAMEALETMMRE 451
Cdd:PRK10070 134 AGINAEERREKALdalrqvglenyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAK 213
|
170 180 190
....*....|....*....|....*....|
gi 1752069711 452 YPGTIVFISHDTRLVERVADQVYVLKKGQL 481
Cdd:PRK10070 214 HQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
386-479 |
9.24e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 41.23 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 386 IRAVLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIpAMEA-----LETMMREYPGTIVFIS 460
Cdd:PRK15079 141 VKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV-SIQAqvvnlLQQLQREMGLSLIFIA 219
|
90
....*....|....*....
gi 1752069711 461 HDTRLVERVADQVYVLKKG 479
Cdd:PRK15079 220 HDLAVVKHISDRVLVMYLG 238
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
186-268 |
1.00e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 40.06 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 186 QKEAERNRQLAQYQQAEAERERLEQAISEKKVQARRLDQKSRAAGKNSTESGGRLAHQKSQGSKQKKLHTAARQMQRRIE 265
Cdd:pfam11600 19 EKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQE 98
|
...
gi 1752069711 266 ALD 268
Cdd:pfam11600 99 ALE 101
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
407-471 |
1.12e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.92 E-value: 1.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 407 LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPAMEALETMMRE----YpgTIVFISHDTRLVERVAD 471
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHElkeqY--TIIIVTHNMQQAARVSD 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
99-175 |
1.28e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.88 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 99 MSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGI-DFLVSRLKLYTGALLIISHDRDLLDRVADKIWELKDGRIT 174
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiQAQIiELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
.
gi 1752069711 175 E 175
Cdd:PRK11022 234 E 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
19-173 |
1.59e-03 |
|
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: 39.91 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 19 LDIDRLELYAydrigLVGANGAGKSTLLKTLLGRIPLQYGKIERQG-TFAYIPqleeAAVREV----QDYAL-------- 85
Cdd:cd03300 21 LDIKEGEFFT-----LLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLP----PHKRPVntvfQNYALfphltvfe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 86 -------MGKLGISRVQAEI-------------------MSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDF 136
Cdd:cd03300 92 niafglrLKKLPKAEIKERVaealdlvqlegyanrkpsqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDlklRKDMQL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752069711 137 LVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRI 173
Cdd:cd03300 172 ELKRLQKELGiTFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
311-337 |
1.67e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 1.67e-03
10 20
....*....|....*....|....*..
gi 1752069711 311 DRVSFQFPLGGKIAITGGNGAGKTTLL 337
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
99-196 |
1.82e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.08 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 99 MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAGIDFLVSRLKLYTGAL--LIISHDRDLLDRVADKIWELKDGRITEY 176
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLtvIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
90 100
....*....|....*....|
gi 1752069711 177 WGGYSDYLAQKEAERNRQLA 196
Cdd:PRK14271 244 GPTEQLFSSPKHAETARYVA 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
407-480 |
1.91e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.61 E-value: 1.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752069711 407 LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA----MEALETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIqaqiLQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
305-349 |
2.04e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 2.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREEGVVI 349
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVI 818
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
34-61 |
2.35e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 39.68 E-value: 2.35e-03
10 20
....*....|....*....|....*....
gi 1752069711 34 LVGANGAGKSTLLkTLLGR-IPLQYGKIE 61
Cdd:COG4604 32 LIGPNGAGKSTLL-SMISRlLPPDSGEVL 59
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
305-336 |
2.69e-03 |
|
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: 40.19 E-value: 2.69e-03
10 20 30
....*....|....*....|....*....|..
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTL 336
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTL 400
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
389-481 |
2.85e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.22 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 389 VLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDIPA----MEALETMMREYPGTIVFISHDTR 464
Cdd:PRK10261 446 LLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIrgqiINLLLDLQRDFGIAYLFISHDMA 525
|
90
....*....|....*..
gi 1752069711 465 LVERVADQVYVLKKGQL 481
Cdd:PRK10261 526 VVERISHRVAVMYLGQI 542
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
31-176 |
3.09e-03 |
|
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: 39.01 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 31 RIGLVGANGAGKSTLLKTLLGRIPLQYGKIE--------------RQgTFAYIPQ---LEEAAVR-------EVQDYALM 86
Cdd:cd03244 32 KVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiglhdlRS-RISIIPQdpvLFSGTIRsnldpfgEYSDEELW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 87 GKLGISRVQAEI--MSGGEETRLK---------------IAQALEDNVHGIMADEPTSHLDRAGiDFLV-----SRLKLY 144
Cdd:cd03244 111 QALERVGLKEFVesLPGGLDTVVEeggenlsvgqrqllcLARALLRKSKILVLDEATASVDPET-DALIqktirEAFKDC 189
|
170 180 190
....*....|....*....|....*....|...
gi 1752069711 145 TgaLLIISHDRD-LLDrvADKIWELKDGRITEY 176
Cdd:cd03244 190 T--VLTIAHRLDtIID--SDRILVLDKGRVVEF 218
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
373-479 |
3.12e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 373 AYMQEGSDYSVPDIRA---VLSSMGFTPEDVRKELSMLSGGEIIKLQLARLLLG---RYNILLLDEPGNFL---DIPAM- 442
Cdd:PRK00635 773 AYEAEKFFLDEPSIHEkihALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALi 852
|
90 100 110
....*....|....*....|....*....|....*...
gi 1752069711 443 EALETMMreYPG-TIVFISHDTRLVeRVADqvYVLKKG 479
Cdd:PRK00635 853 YVLQSLT--HQGhTVVIIEHNMHVV-KVAD--YVLELG 885
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
307-481 |
3.38e-03 |
|
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: 39.01 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 307 KVILDRVSFQFPLGGKIAITGGNGAGKTTLLN----MIrDREEGVVIAPKAEIgyfdqtgykftrnqnvmaymqegSDYS 382
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLalfrLV-ELSSGSILIDGVDI-----------------------SKIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 383 VPDIRavlSSMGFTPED-------VRKEL---SMLSGGEIIK------------------------------------LQ 416
Cdd:cd03244 73 LHDLR---SRISIIPQDpvlfsgtIRSNLdpfGEYSDEELWQalervglkefveslpggldtvveeggenlsvgqrqlLC 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 417 LARLLLGRYNILLLDEPGNFLDIPAMEAL-ETMMREYPG-TIVFISHdtRLvERVA--DQVYVLKKGQL 481
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIqKTIREAFKDcTVLTIAH--RL-DTIIdsDRILVLDKGRV 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
302-482 |
3.64e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 39.55 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 302 KQLGDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREE---GVVI----------APKAEIGYFDQTGYKF--- 365
Cdd:PRK09452 22 KSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETpdsGRIMldgqdithvpAENRHVNTVFQSYALFphm 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 366 TRNQNVmAY---MQEgsdysVP--DIRavlssmgftpEDVRKELSM-------------LSGGEIIKLQLARLLLGRYNI 427
Cdd:PRK09452 102 TVFENV-AFglrMQK-----TPaaEIT----------PRVMEALRMvqleefaqrkphqLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 428 LLLDEPGNFLDIP---AMEA-LETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQLQ 482
Cdd:PRK09452 166 LLLDESLSALDYKlrkQMQNeLKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
305-450 |
4.35e-03 |
|
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: 38.38 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 305 GDKVILDRVSFQFPLGGKIAITGGNGAGKTTLLNMIRDREEGVVIA--------PKAE-----IGYFDQTgYKFTRNQNV 371
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITgeilingrPLDKnfqrsTGYVEQQ-DVHSPNLTV 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 372 maymQEGSDYSvpdirAVLSsmGFTPEDvRKELSmlsggeiIKLQLArlllGRYNILLLDEPGNFLDipaMEALETMMR 450
Cdd:cd03232 97 ----REALRFS-----ALLR--GLSVEQ-RKRLT-------IGVELA----AKPSILFLDEPTSGLD---SQAAYNIVR 149
|
|
| COG3911 |
COG3911 |
Predicted ATPase [General function prediction only]; |
322-343 |
4.37e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443117 Cd Length: 180 Bit Score: 38.26 E-value: 4.37e-03
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
100-197 |
4.47e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 39.42 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 100 SGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG----IDFLVSRLKLYTgaLLIISHDRDLLDRVaDKIWELKDGRITE 175
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQNKT--VLMITHRLTGLEQF-DRICVMDNGQIIE 553
|
90 100
....*....|....*....|..
gi 1752069711 176 YwGGYSDYLAQKeaERNRQLAQ 197
Cdd:PRK11160 554 Q-GTHQELLAQQ--GRYYQLKQ 572
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-51 |
4.57e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 38.91 E-value: 4.57e-03
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
99-175 |
4.72e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.02 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 99 MSGGEETRLKIAQALEDNVHGIMADEPTSHLD---RAGIDFLVSRLKLYTG-ALLIISHDRDLLDRVADKIWELKDGRIT 174
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEpttQAQIFRLLTRLNQNNNtTILLISHDLQMLSQWADKINVLYCGQTV 238
|
.
gi 1752069711 175 E 175
Cdd:PRK15093 239 E 239
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
99-164 |
5.93e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 38.61 E-value: 5.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 99 MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG---IDFLVSRLK-LYTgaLLIISHDRDLLDRVADK 164
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIStlrIEELMHELKeQYT--IIIVTHNMQQAARVSDM 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
330-480 |
6.43e-03 |
|
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: 38.01 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 330 GAGKTTLLNMIRDREEGVViAPKAEIGY----FDQTGYKFTRNqnvMAYMQEgSDYSVPD------IRAVLSSMGftPED 399
Cdd:cd03233 43 GSGCSTLLKALANRTEGNV-SVEGDIHYngipYKEFAEKYPGE---IIYVSE-EDVHFPTltvretLDFALRCKG--NEF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 400 VRKelsmLSGGEIIKLQLARLLLGRYNILLLDEPGNFLDipAMEALETMMReypgtIVFISHDTRLVERVA--------- 470
Cdd:cd03233 116 VRG----ISGGERKRVSIAEALVSRASVLCWDNSTRGLD--SSTALEILKC-----IRTMADVLKTTTFVSlyqasdeiy 184
|
170
....*....|...
gi 1752069711 471 ---DQVYVLKKGQ 480
Cdd:cd03233 185 dlfDKVLVLYEGR 197
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-175 |
6.62e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 38.28 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 34 LVGANGAGKSTLLKTL-----LGRIPLQYGKIERQGTFAYIPQLEEAAVRE-----------------VQDYALMGKL-G 90
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEVRRevgmvfqypnpfphltiYDNVAIGVKLnG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 91 ISRVQAEI---------------------------MSGGEETRLKIAQALEDNVHGIMADEPTSHLDRAG---IDFLVSR 140
Cdd:PRK14267 115 LVKSKKELdervewalkkaalwdevkdrlndypsnLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGtakIEELLFE 194
|
170 180 190
....*....|....*....|....*....|....*.
gi 1752069711 141 LKL-YTgaLLIISHDRDLLDRVADKIWELKDGRITE 175
Cdd:PRK14267 195 LKKeYT--IVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
407-480 |
7.46e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 38.63 E-value: 7.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752069711 407 LSGGEIIKLQLARLLLGRYNILLLDEPGNFLDiPAMEA-----LETMMREYPGTIVFISHDTRLVERVADQVYVLKKGQ 480
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAME-PTTQAqifrlLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
99-169 |
9.02e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.73 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752069711 99 MSGGEET------RLKIAQALEDNVHGIMADEPTSHLD---RAGI-DFLVSRLKLYTG--ALLIISHDRDLLDrVADKIW 166
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDedrRTNLkDIIEYSLKDSSDipQVIMISHHRELLS-VADVAY 880
|
...
gi 1752069711 167 ELK 169
Cdd:PRK01156 881 EVK 883
|
|
| |
