|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
74-685 |
0e+00 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 825.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 74 KKPAPGLNAAFFKQLLELRKILFPKLVTTETGWLCLHSVALISRTFLSIYVAGLDGKIVKSIVEKKPRTFIIKLIKWLMI 153
Cdd:TIGR00954 65 AKKKAHVNGVFLGKLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 154 AIPATFVNSAIRYLECKLALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTEDIMMFSQSVAHLYSNLTKPIL 233
Cdd:TIGR00954 145 APPASFINSAIKYLLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPIL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 234 DVILTSYTLIRTATSRGASPIGPTllaglvVYATAKVLKACSPKFGSLVAEEAHRKGYLRYVHSRIIANVEEIAFYRGHK 313
Cdd:TIGR00954 225 DVILYSFKLLTALGSVGPAGLFAY------LFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNK 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 314 VEMKQLQKCYKALAYQMNLILSKRLWYIMIEQFLMKYVWSSCGLIMVAIPIITATGFADDlEDGPKQAMvsdrtEAFTTA 393
Cdd:TIGR00954 299 VEKETVMSSFYRLVEHLNLIIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFL-EMSEEELM-----QEFYNN 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 394 RNLLASGADAIERIMSSYKEITELAGYTARVYNMFWVFDEVKRGIYKRTVTQEPENHSKRGGNLELplsdtLAIKGTVID 473
Cdd:TIGR00954 373 GRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNL-----VPGRGIVEY 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 474 VDHGIICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMS 553
Cdd:TIGR00954 448 QDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMT 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 554 LGSLRDQVIYPDSADDMREKGYTDQDLERILHSVHLYHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLD 633
Cdd:TIGR00954 528 LGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1313999337 634 ECTSAVSIDVEGKIFQAAIGAGISLLSITHRPSLWKYHTHLLQFDGEGGWRF 685
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGGYQF 659
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
91-365 |
5.19e-127 |
|
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family of ABC transporters and shares sequence similarity with pfam00664. Mutations in this domain in Swiss:P28288 are believed responsible for Zellweger Syndrome-2; mutations in Swiss:P33897 are responsible for recessive X-linked adrenoleukodystrophy. A Saccharomyces cerevisiae homolog is involved in the import of long-chain fatty acids.
Pssm-ID: 399466 Cd Length: 269 Bit Score: 378.49 E-value: 5.19e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 91 LRKILFPKLVTTETGWLCLHSVALISRTFLSIYVAGLDGKIVKSIVEKKPRTFIIKLIKWLMIAIPATFVNSAIRYLECK 170
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 171 LALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTEDIMMFSQSVAHLYSNLTKPILDVILTSYTLIRTATSRG 250
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 251 aspigpTLLAGLVVYATAKVLKACSPKFGSLVAEEAHRKGYLRYVHSRIIANVEEIAFYRGHKVEMKQLQKCYKALAYQM 330
Cdd:pfam06472 161 ------PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHM 234
|
250 260 270
....*....|....*....|....*....|....*
gi 1313999337 331 NLILSKRLWYIMIEQFLMKYVWSSCGLIMVAIPII 365
Cdd:pfam06472 235 RRILRRRLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
134-690 |
3.77e-89 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 290.94 E-value: 3.77e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 134 SIVEKKPRTFIIKLIKWLMIAIPATFVNSAIRYLECKLALAFRTRLVDHAYETYFANQTYYKVINMDGRLANPDQSLTED 213
Cdd:COG4178 54 ALQARDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDNPDQRIAED 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 214 IMMFSQSVAHLYSNLTKPILDVIltSYTLI-------RTATSRGASPIGPTLLA-GLVVYATakvlkacspkFGSLVA-- 283
Cdd:COG4178 134 IRLFTETTLSLSLGLLSSVVTLI--SFIGIlwslsgsLTFTLGGYSITIPGYMVwAALIYAI----------IGTLLThl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 284 ----------EEAHRKGYLRY--VHSRiiANVEEIAFYRGHKVEMKQLQKCYKALAYQMNLILSKRLWYIMIEQFlmkYv 351
Cdd:COG4178 202 igrplirlnfEQQRREADFRFalVRVR--ENAESIALYRGEAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTG---Y- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 352 wsscGLIMVAIPIITATG--FADDLEDGpkqamvsdrteAFTTARNLLASGADAIERIMSSYKEITELAGYTARVYNMFW 429
Cdd:COG4178 276 ----GQLAVIFPILVAAPryFAGEITLG-----------GLMQAASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFEE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 430 VFDEVKRgiykrtvtqEPENHSkrggnlelplsdtlaikGTVIDVDHGIICENVPIITPAGEVVASRLNFKVEEGMHLLI 509
Cdd:COG4178 341 ALEAADA---------LPEAAS-----------------RIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 510 TGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPDSADDmrekgYTDQDLERILHSVHL 589
Cdd:COG4178 395 TGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALLYPATAEA-----FSDAELREALEAVGL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 590 YHIVQReggWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 667
Cdd:COG4178 470 GHLAER---LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLlrEELPGTTVISVGHRSTL 546
|
570 580
....*....|....*....|...
gi 1313999337 668 WKYHTHLLQFDGEGGWRFEQLDT 690
Cdd:COG4178 547 AAFHDRVLELTGDGSWQLLPAEA 569
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
478-683 |
2.83e-82 |
|
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: 258.62 E-value: 2.83e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSL 557
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 558 RDQVIYPdsaddmrekgytdqdlerilhsvhlyhivqreggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECTS 637
Cdd:cd03223 81 REQLIYP----------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1313999337 638 AVSIDVEGKIFQAAIGAGISLLSITHRPSLWKYHTHLLQFDGEGGW 683
Cdd:cd03223 121 ALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
486-663 |
4.46e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.99 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 486 ITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQH---MFYIPQRPYMSL 554
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGeIYLDgkplsamPPPEWrrqVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 555 GSLRDQVIYPDSaddMREKGYTDQDLERILHSVHLYhivqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLD 633
Cdd:COG4619 88 GTVRDNLPFPFQ---LRERKFDRERALELLERLGLP---------PDILDKPvERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190
....*....|....*....|....*....|....
gi 1313999337 634 ECTSAVSID----VEGKIFQAAIGAGISLLSITH 663
Cdd:COG4619 156 EPTSALDPEntrrVEELLREYLAEEGRAVLWVSH 189
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
478-667 |
5.09e-27 |
|
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: 116.40 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPPP--QHMFYI 546
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdLDPASwrRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 547 PQRPYMSLGSLRDQViypdsadDMREKGYTDQDLERILHSVHLYHIVQR-EGGWDAVmdwkdV------LSGGEKQRMGM 619
Cdd:COG4988 417 PQNPYLFAGTIRENL-------RLGRPDASDEELEAALEAAGLDEFVAAlPDGLDTP-----LgeggrgLSGGQAQRLAL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1313999337 620 ARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 667
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQAlrRLAKGRTVILITHRLAL 534
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
478-667 |
4.17e-26 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 105.16 E-value: 4.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEV-VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhMFYIPQRPYmSLGS 556
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIL------IDGVDLRDL-DLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 LRDQViypdsaddmrekGYTDQDlerilhsVHLYHivqreggwDAVMDwkDVLSGGEKQRMGMARMFYHKPKYALLDECT 636
Cdd:cd03228 74 LRKNI------------AYVPQD-------PFLFS--------GTIRE--NILSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190
....*....|....*....|....*....|...
gi 1313999337 637 SAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 667
Cdd:cd03228 125 SALDPETEALILEAlrALAKGKTVIVIAHRLST 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
497-667 |
3.08e-23 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 105.30 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY------KPPP----QHMFYIPQRPYMSLGSLRDQVIypd 565
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGrILIdgidlrQIDPaslrRQIGVVLQDVFLFSGTIRENIT--- 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 566 saddMREKGYTDQDLERILHSVHLYHIVQR-EGGWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDV 643
Cdd:COG2274 571 ----LGDPDATDEEIIEAARLAGLHDFIEAlPMGYDTvVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
|
170 180
....*....|....*....|....*.
gi 1313999337 644 EGKIFQA--AIGAGISLLSITHRPSL 667
Cdd:COG2274 647 EAIILENlrRLLKGRTVIIIAHRLST 672
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
478-667 |
3.34e-21 |
|
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: 98.13 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPPQHMF----YI 546
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavngvpLADADADSWRdqiaWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 547 PQRPYMSLGSLRDQVIypdsaddMREKGYTDQDLERILHSVHLYHIVQ-REGGWDAVMDWKDV-LSGGEKQRMGMARMFY 624
Cdd:TIGR02857 402 PQHPFLFAGTIAENIR-------LARPDASDAEIREALERAGLDEFVAaLPQGLDTPIGEGGAgLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1313999337 625 HKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 667
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEAlrALAQGRTVLLVTHRLAL 519
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
478-667 |
3.44e-21 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 91.12 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITP-AGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmfyIPQRPYMSLGS 556
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR---------LDGADISQWDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 --LRDQViypdsaddmrekGYTDQDLEriLHSvhlyhivqreggwDAVMDwkDVLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:cd03246 72 neLGDHV------------GYLPQDDE--LFS-------------GSIAE--NILSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 1313999337 635 CTSavSIDVEG-KIFQAAI----GAGISLLSITHRPSL 667
Cdd:cd03246 123 PNS--HLDVEGeRALNQAIaalkAAGATRIVIAHRPET 158
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
413-666 |
6.05e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.54 E-value: 6.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 413 EITELAGYTARVYNMF----WVFDEVKRGI--YKR--TVTQEPENHSKRGGNLELPlsdtlaikgtviDVDHGIICENVp 484
Cdd:COG1132 279 DLVAFILYLLRLFGPLrqlaNVLNQLQRALasAERifELLDEPPEIPDPPGAVPLP------------PVRGEIEFENV- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 485 iiT---PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VL--------YKPP--PQHMFYIPQRP 550
Cdd:COG1132 346 --SfsyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrILidgvdirdLTLEslRRQIGVVPQDT 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 551 YMSLGSLRDQVIYPDsaddmreKGYTDQDLERILHSVHLYHIVQR-EGGWDAVmdwkdV------LSGGEKQRMGMARMF 623
Cdd:COG1132 424 FLFSGTIRENIRYGR-------PDATDEEVEEAAKAAQAHEFIEAlPDGYDTV-----VgergvnLSGGQRQRIAIARAL 491
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1313999337 624 YHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPS 666
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEAleRLMKGRTTIVIAHRLS 536
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
496-637 |
1.16e-20 |
|
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: 88.86 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 496 RLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY----------KPPPQHMFYIPQRP-YMSLGSLRDQVIY 563
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGtILLdgqdltdderKSLRKEIGYVFQDPqLFPRLTVRENLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1313999337 564 PDSADDMREKGYTDQdLERILHSVHLYHIVQReggwdAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTS 637
Cdd:pfam00005 83 GLLLKGLSKREKDAR-AEEALEKLGLGDLADR-----PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
488-666 |
5.46e-20 |
|
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: 94.45 E-value: 5.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 488 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPP----QHMFYIPQRPYMSLGS 556
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSitlggvdLRDLDEddlrRRIAVVPQRPHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 LRD--QVIYPDSaddmrekgyTDQDLERILHSVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALL 632
Cdd:COG4987 425 LREnlRLARPDA---------TDEELWAALERVGLGDWLAAlPDGLDTWLGEGGRrLSGGERRRLALARALLRDAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 1313999337 633 DECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPS 666
Cdd:COG4987 496 DEPTEGLDAATEQALLADllEALAGRTVLLITHRLA 531
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
492-667 |
1.17e-19 |
|
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: 86.53 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 492 VVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmFYIPQRPYMSLGSLRDQViypdsaddmr 571
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-------IDGKDIAKLPLEELRRRI---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 572 ekGYTDQdlerilhsvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI---F 648
Cdd:cd00267 76 --GYVPQ------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLlelL 123
|
170
....*....|....*....
gi 1313999337 649 QAAIGAGISLLSITHRPSL 667
Cdd:cd00267 124 RELAEEGRTVIIVTHDPEL 142
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
481-667 |
1.23e-19 |
|
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: 88.03 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 481 ENVPIITPAGEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY------KPPP----QHMFYIPQ 548
Cdd:cd03245 6 RNVSFSYPNQEIPALDnVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsVLLdgtdirQLDPadlrRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 549 RPYMSLGSLRDQVIYpdsaddmrekGYTDQDLERILHSVHLYHIVQ-------------REGGwdavmdwkDVLSGGEKQ 615
Cdd:cd03245 86 DVTLFYGTLRDNITL----------GAPLADDERILRAAELAGVTDfvnkhpngldlqiGERG--------RGLSGGQRQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1313999337 616 RMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPSL 667
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERlrQLLGDKTLIIITHRPSL 201
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
490-665 |
6.11e-19 |
|
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: 85.61 E-value: 6.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYK---------PPPQHMFYIPQRP--YMSLgSL 557
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGeVLWNgepirdareDYRRRLAYLGHADglKPEL-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 558 RDQVIYpdsADDMREKGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTS 637
Cdd:COG4133 93 RENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVR---------QLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|...
gi 1313999337 638 AvsIDVEGK-----IFQAAIGAGISLLSITHRP 665
Cdd:COG4133 161 A--LDAAGVallaeLIAAHLARGGAVLLTTHQP 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
478-666 |
4.80e-17 |
|
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: 80.73 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-----------KPPPQHMFYI 546
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdisrKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 547 PQRPYMSLGSLRDQVIYPDSaddmrekGYTDQDLERILHSVHLYHIVQR-EGGWDAVM-DWKDVLSGGEKQRMGMARMFY 624
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRP-------NATDEEVIEAAKEAGAHDFIMKlPNGYDTVLgENGGNLSQGERQLLAIARAML 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1313999337 625 HKPKYALLDECTSavSIDVEG-KIFQAAIGA---GISLLSITHRPS 666
Cdd:cd03254 156 RDPKILILDEATS--NIDTETeKLIQEALEKlmkGRTSIIIAHRLS 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
497-675 |
6.26e-17 |
|
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: 79.82 E-value: 6.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPpqHMFYIPQRPYMSLGSLRDQVIYpdsADDMREKGYT 576
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIQNGTIRENILF---GKPFDEERYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 577 --------DQDLErILHSVHLYHIvqREGGwdaVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIF 648
Cdd:cd03250 99 kvikacalEPDLE-ILPDGDLTEI--GEKG---IN-----LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIF 167
|
170 180 190
....*....|....*....|....*....|..
gi 1313999337 649 QAAIGaGISLLS-----ITHRPSLWKYHTHLL 675
Cdd:cd03250 168 ENCIL-GLLLNNktrilVTHQLQLLPHADQIV 198
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
497-671 |
9.88e-17 |
|
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: 79.43 E-value: 9.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP----------QHMFYIPQRPymslgslRDQVIYPD 565
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGeVLVDGKDltklslkelrRKVGLVFQNP-------DDQFFGPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 566 SADD----MREKGYTDQDLERILHSvhlyhiVQREGGWDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLDECTSavS 640
Cdd:cd03225 93 VEEEvafgLENLGLPEEEIEERVEE------ALELVGLEGLRDRSpFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA--G 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1313999337 641 IDVEG-----KIFQAAIGAGISLLSITHRPSLWKYH 671
Cdd:cd03225 165 LDPAGrrellELLKKLKAEGKTIIIVTHDLDLLLEL 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
497-638 |
2.05e-16 |
|
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: 79.15 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPPQHMFYIP-----------QRPYMSLGSLR 558
Cdd:cd03260 19 ISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegevlLDGKDIYDLDVDVlelrrrvgmvfQKPNPFPGSIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 559 DQVIYPDSADDMREKGYTDQDLERILHSVHLyhivqreggWDAVMDWKDV--LSGGEKQRMGMARMFYHKPKYALLDECT 636
Cdd:cd03260 99 DNVAYGLRLHGIKLKEELDERVEEALRKAAL---------WDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
..
gi 1313999337 637 SA 638
Cdd:cd03260 170 SA 171
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
490-638 |
2.61e-16 |
|
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: 79.32 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KP----PP----QHMFYIPQRPYMSLG-SL 557
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlaslSRrelaRRIAYVPQEPPAPFGlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 558 RDQVI---YP-------DSADDMREkgytdqdLERILHSVHLYHIVQREggWDAvmdwkdvLSGGEKQRMGMARMFYHKP 627
Cdd:COG1120 93 RELVAlgrYPhlglfgrPSAEDREA-------VEEALERTGLEHLADRP--VDE-------LSGGERQRVLIARALAQEP 156
|
170
....*....|.
gi 1313999337 628 KYALLDECTSA 638
Cdd:COG1120 157 PLLLLDEPTSH 167
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
493-679 |
3.69e-16 |
|
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: 78.28 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 493 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPPQ--HMFY------IPQRPYMSLGSLRDQV 561
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQyeHKYLhskvslVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 562 IYpdsaddmrekGYTDQDLERILHSVHLYH----IVQREGGWDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLDECT 636
Cdd:cd03248 109 AY----------GLQSCSFECVKEAAQKAHahsfISELASGYDTEVGEKgSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1313999337 637 SAVSIDVEGKIFQAAIG--AGISLLSITHRPSLWKYHTHLLQFDG 679
Cdd:cd03248 179 SALDAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
490-680 |
4.88e-16 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 77.57 E-value: 4.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPPQ--HMF-YIPQRPYMSLG---SLRDQ 560
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGsirVFGKPLEKerKRIgYVPQRRSIDRDfpiSVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 561 V---IYPDSADDMREKGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTS 637
Cdd:cd03235 91 VlmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIG---------ELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1313999337 638 AVsiDVEGK-----IFQAAIGAGISLLSITH-RPSLWKYHTHLLQFDGE 680
Cdd:cd03235 162 GV--DPKTQediyeLLRELRREGMTILVVTHdLGLVLEYFDRVLLLNRT 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
481-667 |
1.40e-15 |
|
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: 80.56 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 481 ENVPIITP-AGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV-------LYKPPP----QHMFYIPQ 548
Cdd:COG4618 334 ENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSvrldgadLSQWDReelgRHIGYLPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 549 RPymSL--GSLRdQVI--YPDsADDmrekgytdqdlERILH-----SVH-LyhIVQREGGWDAVMDWKD-VLSGGEKQRM 617
Cdd:COG4618 414 DV--ELfdGTIA-ENIarFGD-ADP-----------EKVVAaaklaGVHeM--ILRLPDGYDTRIGEGGaRLSGGQRQRI 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1313999337 618 GMARMFYHKPKYALLDECTSavSIDVEG-KIFQAAIGA----GISLLSITHRPSL 667
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNS--NLDDEGeAALAAAIRAlkarGATVVVITHRPSL 529
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
498-663 |
1.90e-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: 76.77 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 498 NFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-------VLYKPPPQHMF----YIPQRPYMSL---GSLRDQVIY 563
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGevtfdgrPVTRRRRKAFRrrvqMVFQDPYASLhprHTVDRILAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 564 PdsaddMREKGYTDQD--LERILHSVHLYhivqreggwDAVMD-WKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVs 640
Cdd:COG1124 105 P-----LRIHGLPDREerIAELLEQVGLP---------PSFLDrYPHQLSGGQRQRVAIARALILEPELLLLDEPTSAL- 169
|
170 180 190
....*....|....*....|....*....|..
gi 1313999337 641 iDVegkIFQAAI---------GAGISLLSITH 663
Cdd:COG1124 170 -DV---SVQAEIlnllkdlreERGLTYLFVSH 197
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
490-665 |
2.59e-15 |
|
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: 75.22 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHMfyipQRPymslgSLRDQVIYPDSAD 568
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrVLLNGGPLDF----QRD-----SIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 569 DMREKGYTDQDLeRILHSVHlyhivQREGGWDAVMD-----WKDV----LSGGEKQRMGMARMFYHKPKYALLDECTsaV 639
Cdd:cd03231 83 GIKTTLSVLENL-RFWHADH-----SDEQVEEALARvglngFEDRpvaqLSAGQQRRVALARLLLSGRPLWILDEPT--T 154
|
170 180 190
....*....|....*....|....*....|.
gi 1313999337 640 SIDVEG-----KIFQAAIGAGISLLSITHRP 665
Cdd:cd03231 155 ALDKAGvarfaEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
490-665 |
3.88e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHmfyipqrpymsLGSLRDQVIYPDSAD 568
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDID-----------DPDVAEACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 569 DMRE--------------KGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMAR-MFYHKPKYaLLD 633
Cdd:PRK13539 83 AMKPaltvaenlefwaafLGGEELDIAAALEAVGLAPLAHLPFG---------YLSAGQKRRVALARlLVSNRPIW-ILD 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1313999337 634 ECTSAvsIDVEG-KIFQAAI-----GAGISLLSiTHRP 665
Cdd:PRK13539 153 EPTAA--LDAAAvALFAELIrahlaQGGIVIAA-THIP 187
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
488-664 |
4.37e-15 |
|
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: 74.84 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 488 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSS----LFRILsglwPVYEGVLY-------KPPP----QHMFYIPQRPYM 552
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILidgvdisKIGLhdlrSRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 553 SLGSLRDQViypdsadDMREKgYTDQDLERILHSVHLY-HIVQREGGWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYA 630
Cdd:cd03244 90 FSGTIRSNL-------DPFGE-YSDEELWQALERVGLKeFVESLPGGLDTvVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1313999337 631 LLDECTSavSIDVEG-KIFQAAIG---AGISLLSITHR 664
Cdd:cd03244 162 VLDEATA--SVDPETdALIQKTIReafKDCTVLTIAHR 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
490-667 |
6.04e-15 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 73.62 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP----QHMFYIPQrpymSLGSLR 558
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldgkdlaSLSPkelaRKIAYVPQ----ALELLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 559 dqviypdsADDMREKGYTDqdlerilhsvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSA 638
Cdd:cd03214 87 --------LAHLADRPFNE-------------------------------LSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190
....*....|....*....|....*....|...
gi 1313999337 639 V----SIDVEGKIFQAAIGAGISLLSITHRPSL 667
Cdd:cd03214 128 LdiahQIELLELLRRLARERGKTVVMVLHDLNL 160
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
487-634 |
1.10e-14 |
|
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: 73.66 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 487 TPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-----KPPPQHMFYIPQR----PYMslg 555
Cdd:cd03293 12 GGGGAVTAlEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGeVLVdgepvTGPGPDRGYVFQQdallPWL--- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1313999337 556 SLRDQVIYPDSADDMREKGYTDQdLERILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:cd03293 89 TVLDNVALGLELQGVPKAEARER-AEELLELVGLSGFENA---------YPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
487-634 |
1.48e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 74.36 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 487 TPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQHMFYIPQRPymslgSL-- 557
Cdd:COG1116 19 TGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGPDRGVVFQEP-----ALlp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 558 ----RDQVIYPDSADDMReKGYTDQDLERILHSVHLyhivqreggwDAVMD-WKDVLSGGEKQRMGMARMFYHKPKYALL 632
Cdd:COG1116 94 wltvLDNVALGLELRGVP-KAERRERARELLELVGL----------AGFEDaYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
..
gi 1313999337 633 DE 634
Cdd:COG1116 163 DE 164
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
497-663 |
1.62e-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: 73.06 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQH-------MFYIPQRPYMSLG--SLRDQVIYpdS 566
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGsILLNGKPIKakerrksIGYVMQDVDYQLFtdSVREELLL--G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 567 ADDMREKGytdQDLERILHSVHLYhivqreggwdavmDWKDV----LSGGEKQRMGMARMFYHKPKYALLDECTSAV--- 639
Cdd:cd03226 97 LKELDAGN---EQAETVLKDLDLY-------------ALKERhplsLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLdyk 160
|
170 180
....*....|....*....|....
gi 1313999337 640 SIDVEGKIFQAAIGAGISLLSITH 663
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITH 184
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
493-664 |
2.15e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 493 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPP--------QHMFYIPQRPYMSLGSLRD-- 559
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngQPIAdyseaalrQAISVVSQRVHLFSATLRDnl 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 560 QVIYPDSaddmrekgyTDQDLERILHSVHLYHIVQREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSA 638
Cdd:PRK11160 435 LLAAPNA---------SDEALIEVLQQVGLEKLLEDDKGLNAWLgEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180
....*....|....*....|....*...
gi 1313999337 639 VSIDVEGKIFQ--AAIGAGISLLSITHR 664
Cdd:PRK11160 506 LDAETERQILEllAEHAQNKTVLMITHR 533
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
488-665 |
2.46e-14 |
|
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: 76.25 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 488 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHMF----------YIPQRPYMSLGS 556
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGeVTLDGVPVSSLdqdevrrrvsVCAQDAHLFDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 LRDQVIY--PDSaddmrekgyTDQDLERILHSVHLY-HIVQREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALL 632
Cdd:TIGR02868 425 VRENLRLarPDA---------TDEELWAALERVGLAdWLRALPDGLDTVLgEGGARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*
gi 1313999337 633 DECTSAVSIDVEGKIFQ--AAIGAGISLLSITHRP 665
Cdd:TIGR02868 496 DEPTEHLDAETADELLEdlLAALSGRTVVLITHHL 530
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
498-670 |
3.60e-14 |
|
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: 72.14 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 498 NFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP--------QHMFYIPQR----PYMSLgslR 558
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisKLSEkelaafrrRHIGFVFQSfnllPDLTA---L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 559 DQVIYP-----DSADDMREKgytdqdLERILHSVHLYHIVQREGGWdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLD 633
Cdd:cd03255 101 ENVELPlllagVPKKERRER------AEELLERVGLGDRLNHYPSE---------LSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1313999337 634 ECTSAV----SIDVEGKIFQAAIGAGISLLSITHRPSLWKY 670
Cdd:cd03255 166 EPTGNLdsetGKEVMELLRELNKEAGTTIVVVTHDPELAEY 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
498-634 |
4.93e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.49 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 498 NFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLG-SLRDQVI--YPDSADDMREK- 573
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDlTVLDTVLdgDAELRALEAELe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 574 ------GYTDQDLERIlhsVHLYHIVQREGGWDA------VM--------DW-KDV--LSGGEKQRMGMARMFYHKPKYA 630
Cdd:COG0488 98 eleaklAEPDEDLERL---AELQEEFEALGGWEAearaeeILsglgfpeeDLdRPVseLSGGWRRRVALARALLSEPDLL 174
|
....
gi 1313999337 631 LLDE 634
Cdd:COG0488 175 LLDE 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
478-666 |
5.01e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 72.26 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQHMF-----YI 546
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdiREVTLDSLrraigVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 547 PQrpymslgslrDQVIYPDS-ADDMRekgY-----TDQDLERILHSVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMG 618
Cdd:cd03253 81 PQ----------DTVLFNDTiGYNIR---YgrpdaTDEEVIEAAKAAQIHDKIMRfPDGYDTIVGERGLkLSGGEKQRVA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1313999337 619 MARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPS 666
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAAlrDVSKGRTTIVIAHRLS 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
490-663 |
1.09e-13 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 71.27 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPPQHMF---YIPQRPYMSLGslrdqviY 563
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtvrLFGKPPRRARRrigYVPQRAEVDWD-------F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 564 PDSADDM------REKG----YTDQDLERI---LHSVHLYHIVQR---EggwdavmdwkdvLSGGEKQRMGMARMFYHKP 627
Cdd:COG1121 91 PITVRDVvlmgryGRRGlfrrPSRADREAVdeaLERVGLEDLADRpigE------------LSGGQQQRVLLARALAQDP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1313999337 628 KYALLDECTSAVsiDVEGkifQAAI--------GAGISLLSITH 663
Cdd:COG1121 159 DLLLLDEPFAGV--DAAT---EEALyellrelrREGKTILVVTH 197
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
488-666 |
1.14e-13 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 71.36 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 488 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VL-------------YKpppQHMFYIPQRPYMS 553
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrVLvdghdlaladpawLR---RQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 554 LGSLRDQVIYPDSADDMREKGYTDQdleriLHSVHLYhIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALL 632
Cdd:cd03252 89 NRSIRDNIALADPGMSMERVIEAAK-----LAGAHDF-ISELPEGYDTIVGEQGAgLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1313999337 633 DECTSAVSIDVEGKIFQ--AAIGAGISLLSITHRPS 666
Cdd:cd03252 163 DEATSALDYESEHAIMRnmHDICAGRTVIIIAHRLS 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
478-668 |
1.32e-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: 73.78 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWP---------VYEGV-LYKPPPQ----H 542
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDgVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggrisgevLLDGRdLLELSEAlrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 543 MFYIPQRPYMSLGSLR--DQVIYP-----DSADDMREKgytdqdLERILHSVHLYHIVQReggwdavmdWKDVLSGGEKQ 615
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgDQIAEAlenlgLSRAEARAR------VLELLEAVGLERRLDR---------YPHQLSGGQRQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1313999337 616 RMGMARMFYHKPKYALLDECTSA----VSIDVEGKIFQAAIGAGISLLSITHRPSLW 668
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
497-667 |
1.38e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPPQ--HMFY------IPQRPYMSLGSLRDQVIYpd 565
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgVPLVQydHHYLhrqvalVGQEPVLFSGSVRENIAY-- 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 566 saddmrekGYTDQDLERILHSVHLYH----IVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVS 640
Cdd:TIGR00958 578 --------GLTDTPDEEIMAAAKAANahdfIMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180
....*....|....*....|....*..
gi 1313999337 641 IDVEGKIFQAAIGAGISLLSITHRPSL 667
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAHRLST 676
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
486-663 |
2.06e-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: 73.40 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 486 ITPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-------------KPPPQHMFYIPQRP 550
Cdd:COG1123 272 VRGKGGVRAvDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGsILFdgkdltklsrrslRELRRRVQMVFQDP 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 551 YMSL---GSLRDQVIYPDSADDMREKGYTDQDLERILHSVHLYhivqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHK 626
Cdd:COG1123 352 YSSLnprMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP---------PDLADRYpHELSGGQRQRVAIARALALE 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1313999337 627 PKYALLDECTSA--VSIdvegkifQAAIGA---------GISLLSITH 663
Cdd:COG1123 423 PKLLILDEPTSAldVSV-------QAQILNllrdlqrelGLTYLFISH 463
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
445-664 |
5.69e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.18 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 445 QEPENHSKRGGNlELPLSDTLAIKGtvidvdhgiicENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRIL 524
Cdd:PRK11174 329 ETPLAHPQQGEK-ELASNDPVTIEA-----------EDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 525 SGLWPvYEGVL--------------YKpppQHMFYIPQRPYMSLGSLRDQVIypdsaddMREKGYTDQDLERILHSVHLY 590
Cdd:PRK11174 397 LGFLP-YQGSLkingielreldpesWR---KHLSWVGQNPQLPHGTLRDNVL-------LGNPDASDEQLQQALENAWVS 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1313999337 591 HIVQR-EGGWD-AVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHR 664
Cdd:PRK11174 466 EFLPLlPQGLDtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAlnAASRRQTTLMVTHQ 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
478-667 |
6.03e-13 |
|
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: 68.90 E-value: 6.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-------KPPP---QHMFYI 546
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGeVLVdgkditkKNLRelrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 547 PQRPymslgslRDQVIYPDSADD----MREKGYTDQDLER----ILHSVHLYHIVQReggwdAVMDwkdvLSGGEKQRMG 618
Cdd:COG1122 81 FQNP-------DDQLFAPTVEEDvafgPENLGLPREEIRErveeALELVGLEHLADR-----PPHE----LSGGQKQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1313999337 619 MARMFYHKPKYALLDECTSavSIDVEGK-----IFQAAIGAGISLLSITHRPSL 667
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTA--GLDPRGRrelleLLKRLNKEGKTVIIVTHDLDL 196
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
490-645 |
6.86e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 68.94 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPP-------QHMFYIPQRP--YMSLgS 556
Cdd:COG1131 11 GDKTAlDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGevrVLGEDVArdpaevrRRIGYVPQEPalYPDL-T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 LRDQV-----IYPDSADDMREKgytdqdLERILHSVHLyhivqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYA 630
Cdd:COG1131 90 VRENLrffarLYGLPRKEARER------IDELLELFGL----------TDAADRKvGTLSGGMKQRLGLALALLHDPELL 153
|
170
....*....|....*
gi 1313999337 631 LLDECTSAVsiDVEG 645
Cdd:COG1131 154 ILDEPTSGL--DPEA 166
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
489-663 |
7.87e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.59 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 489 AGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPPP--QHMFYIPQRPYMSLGSL 557
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegedistLKPEIyrQQVSYCAQTPTLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 558 RDQVIYPDSaddMREKGYTDQDLERILHSVHL-YHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLDECT 636
Cdd:PRK10247 98 YDNLIFPWQ---IRNQQPDPAIFLDDLERFALpDTILTKN---------IAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190
....*....|....*....|....*....|.
gi 1313999337 637 SAVS----IDVEGKIFQAAIGAGISLLSITH 663
Cdd:PRK10247 166 SALDesnkHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
488-663 |
1.09e-12 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 67.06 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 488 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSG-LWPVYEGVLYKPPP------------QHMFYIPQRPymsl 554
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQSGAVLIDGEPldysrkgllerrQRVGLVFQDP---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 555 gslRDQVIYPDSADDM----REKGYTDQDLERI----LHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHK 626
Cdd:TIGR01166 78 ---DDQLFAADVDQDVafgpLNLGLSEAEVERRvreaLTAVGASGLRERP---------THCLSGGEKKRVAIAGAVAMR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1313999337 627 PKYALLDECTSAVsiDVEGKIFQAAI-----GAGISLLSITH 663
Cdd:TIGR01166 146 PDVLLLDEPTAGL--DPAGREQMLAIlrrlrAEGMTVVISTH 185
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
497-666 |
1.13e-12 |
|
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: 68.34 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPP--PQHMFYIPQRPYMSLGSLRDQVIY-- 563
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdLNLRwlRSQIGLVSQEPVLFDGTIAENIRYgk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 564 PDSADDMREKGYTDQDLerilHSVhlyhIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVSID 642
Cdd:cd03249 102 PDATDEEVEEAAKKANI----HDF----IMSLPDGYDTLVGERGSqLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180
....*....|....*....|....*..
gi 1313999337 643 VEgKIFQAAIG---AGISLLSITHRPS 666
Cdd:cd03249 174 SE-KLVQEALDramKGRTTIVIAHRLS 199
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
490-665 |
1.39e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 67.00 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKP---------PPQHMFYIPQRPYM--SLGSL 557
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGeVRWNGtplaeqrdePHENILYLGHLPGLkpELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 558 RDQVIYpdsADDMrekGYTDQDLERILHSVHLYHIVQREGGWdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTs 637
Cdd:TIGR01189 92 ENLHFW---AAIH---GGAQRTIEDALAAVGLTGFEDLPAAQ---------LSAGQQRRLALARLWLSRRPLWILDEPT- 155
|
170 180 190
....*....|....*....|....*....|...
gi 1313999337 638 aVSIDVEG-----KIFQAAIGAGISLLSITHRP 665
Cdd:TIGR01189 156 -TALDKAGvallaGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
497-663 |
2.60e-12 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 65.50 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEG--MHLLitGPNGCGKSSLFRILSGLWPVYEG---VLYKPPP-------QHMFYIPQRPYmslgslrdqvIYP 564
Cdd:cd03230 19 ISLTVEKGeiYGLL--GPNGAGKTTLIKIILGLLKPDSGeikVLGKDIKkepeevkRRIGYLPEEPS----------LYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 565 DsaddmrekgYTdqdlerilhsvhlyhivqregGWDAVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVE 644
Cdd:cd03230 87 N---------LT---------------------VRENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSG--LDPE 129
|
170 180
....*....|....*....|....
gi 1313999337 645 G-----KIFQAAIGAGISLLSITH 663
Cdd:cd03230 130 SrrefwELLRELKKEGKTILLSSH 153
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
490-647 |
6.09e-12 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 66.21 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY--------KPPPQHMF-YIPQR----PYMSlgs 556
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILlngkditnLPPEKRDIsYVPQNyalfPHMT--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 lrdqvIYPDSADDMREKGYTDQDLER----ILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALL 632
Cdd:cd03299 88 -----VYKNIAYGLKKRKVDKKEIERkvleIAEMLGIDHLLNRKPE---------TLSGGEQQRVAIARALVVNPKILLL 153
|
170
....*....|....*
gi 1313999337 633 DECTSAVSIDVEGKI 647
Cdd:cd03299 154 DEPFSALDVRTKEKL 168
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
497-642 |
1.01e-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: 65.65 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP---QHMFYIPQRPYMSLG-SLRDQV---- 561
Cdd:COG4555 20 VSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrKEPRearRQIGVLPDERGLYDRlTVRENIryfa 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 562 -IYPDSADDMREKgytdqdLERILHSVHLyhivqreggwDAVMD--WKDvLSGGEKQRMGMARMFYHKPKYALLDECTSA 638
Cdd:COG4555 100 eLYGLFDEELKKR------IEELIELLGL----------EEFLDrrVGE-LSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
....
gi 1313999337 639 VSID 642
Cdd:COG4555 163 LDVM 166
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
493-647 |
1.17e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.52 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 493 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQR----PYMSLGSLRDQVIYPdsad 568
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlyldTTLPLTVNRFLRLRP---- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1313999337 569 dmrekGYTDQDLERILHSVHLYHIVqreggwDAVMdwkDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVsiDVEGKI 647
Cdd:PRK09544 95 -----GTKKEDILPALKRVQAGHLI------DAPM---QKLSGGETQRVLLARALLNRPQLLVLDEPTQGV--DVNGQV 157
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
491-667 |
1.18e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.98 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 491 EVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLwpvyegvLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPDSADDM 570
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA-------LKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 571 REkgytdqdlerILHSVHLYhivqreggwDAVMdWK---DVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVE--- 644
Cdd:COG2401 116 VE----------LLNAVGLS---------DAVL-WLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSH--LDRQtak 173
|
170 180
....*....|....*....|....*.
gi 1313999337 645 --GKIFQ-AAIGAGISLLSITHRPSL 667
Cdd:COG2401 174 rvARNLQkLARRAGITLVVATHHYDV 199
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
487-666 |
1.32e-11 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 64.94 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 487 TPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-----------VLYKPPPQHMFYIPQRPYMSLG 555
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGrilidghdvrdYTLASLRRQIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 556 SLRDQVIYPDSaddmrekGYTDQDLERILHSVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLD 633
Cdd:cd03251 91 TVAENIAYGRP-------GATREEVEEAARAANAHEFIMElPEGYDTVIGERGVkLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1313999337 634 ECTSAVSIDVEgKIFQAAIG---AGISLLSITHRPS 666
Cdd:cd03251 164 EATSALDTESE-RLVQAALErlmKNRTTFVIAHRLS 198
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
490-664 |
3.72e-11 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 62.06 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmfyipqrpymslgsLRDQVIYPDSAD 568
Cdd:cd03216 11 GGVKAlDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL--------------------VDGKEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 569 DMREKGytdqdlerilhsvhLYHIVQreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSiDVEGKIF 648
Cdd:cd03216 71 DARRAG--------------IAMVYQ--------------LSVGERQMVEIARALARNARLLILDEPTAALT-PAEVERL 121
|
170 180
....*....|....*....|
gi 1313999337 649 QAAIG----AGISLLSITHR 664
Cdd:cd03216 122 FKVIRrlraQGVAVIFISHR 141
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
497-647 |
4.71e-11 |
|
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: 62.98 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLItGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPP---QHMFYIPQ--RPYMSLgSLRDQVIYP 564
Cdd:cd03264 19 VSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRidgqdvlKQPQklrRRIGYLPQefGVYPNF-TVREFLDYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 565 DSADDMREKGyTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTsaVSIDVE 644
Cdd:cd03264 97 AWLKGIPSKE-VKARVDEVLELVNLGDRAKKKIG---------SLSGGMRRRVGIAQALVGDPSILIVDEPT--AGLDPE 164
|
...
gi 1313999337 645 GKI 647
Cdd:cd03264 165 ERI 167
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
490-664 |
6.81e-11 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 62.84 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVA-SRLNFKVEEG-MHLLItGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQ--HM-----FYIPqRPYM 552
Cdd:cd03219 11 GGLVAlDDVSFSVRPGeIHGLI-GPNGAGKTTLFNLISGFLRPTSGsVLFDgeditglPPHEiaRLgigrtFQIP-RLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 553 SLgSLRDQVI---------YPDSADDMREKGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMF 623
Cdd:cd03219 89 EL-TVLENVMvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAG---------ELSYGQQRRLEIARAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1313999337 624 YHKPKYALLDECTSAVS---IDVEGKIFQAAIGAGISLLSITHR 664
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNpeeTEELAELIRELRERGITVLLVEHD 202
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
490-634 |
1.68e-10 |
|
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: 61.50 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQH----MFYipQR----PYMs 553
Cdd:cd03301 11 GNVTAlDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtDLPPKDrdiaMVF--QNyalyPHM- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 554 lgSLRDQVIYPdsaddMREKGYTDQDLERILHSV-HLYHIvqreggwDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYAL 631
Cdd:cd03301 88 --TVYDNIAFG-----LKLRKVPKDEIDERVREVaELLQI-------EHLLDRKpKQLSGGQRQRVALGRAIVREPKVFL 153
|
...
gi 1313999337 632 LDE 634
Cdd:cd03301 154 MDE 156
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
490-666 |
1.90e-10 |
|
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: 61.38 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQhmfyipQR------------ 549
Cdd:cd03259 11 GSVRAlDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILidgrdvtGVPPE------RRnigmvfqdyalf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 550 PYMslgSLRDQVIYPdsaddMREKGYTDQDLER----ILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYH 625
Cdd:cd03259 85 PHL---TVAENIAFG-----LKLRGVPKAEIRArvreLLELVGLEGLLNR---------YPHELSGGQQQRVALARALAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1313999337 626 KPKYALLDECTSAV------SIDVEGKIFQAAigAGISLLSITHRPS 666
Cdd:cd03259 148 EPSLLLLDEPLSALdaklreELREELKELQRE--LGITTIYVTHDQE 192
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
490-664 |
2.15e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 61.14 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---YKP----PPQHMFYIPQR----PYMslgSL 557
Cdd:cd03269 11 GRVTALDdISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdGKPldiaARNRIGYLPEErglyPKM---KV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 558 RDQVIYPDSADDMReKGYTDQDLERILHSVHLyhivqreggwdavMDWKDV----LSGGEKQRMGMARMFYHKPKYALLD 633
Cdd:cd03269 88 IDQLVYLAQLKGLK-KEEARRRIDEWLERLEL-------------SEYANKrveeLSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190
....*....|....*....|....*....|....
gi 1313999337 634 ECTSA---VSIDVEGKIFQAAIGAGISLLSITHR 664
Cdd:cd03269 154 EPFSGldpVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
509-638 |
2.92e-10 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 60.77 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 509 ITGPNGCGKSSLFRILSGLWPVYEGVLY-------------KPPPQ--HMFYIPQR----PYMSLgslRDQVIYPDSADD 569
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkiNLPPQqrKIGLVFQQyalfPHLNV---RENLAFGLKRKR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 570 MREkgytDQDLER-ILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSA 638
Cdd:cd03297 105 NRE----DRISVDeLLDLLGLDHLLNR---------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
490-634 |
3.73e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKpPPQHMFYIP--QRpymSLGSL-RDQVIYP- 564
Cdd:PRK11000 14 GDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPpaER---GVGMVfQSYALYPh 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1313999337 565 -DSADDMR--------EKGYTDQDLERILHSVHLYHIVQREGgwdavmdwKDvLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:PRK11000 90 lSVAENMSfglklagaKKEEINQRVNQVAEVLQLAHLLDRKP--------KA-LSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
497-663 |
4.12e-10 |
|
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: 60.60 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYK-----PPPQHMF--------YIPQRPYMSLG---SLRD 559
Cdd:cd03257 24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGsIIFDgkdllKLSRRLRkirrkeiqMVFQDPMSSLNprmTIGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 560 QVIYP-----DSADDMREKGYTDQDLERILHSVHLYHIVQREggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:cd03257 104 QIAEPlrihgKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE------------LSGGQRQRVAIARALALNPKLLIADE 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1313999337 635 CTSAVSIDVEGKI------FQAAIgaGISLLSITH 663
Cdd:cd03257 172 PTSALDVSVQAQIldllkkLQEEL--GLTLLFITH 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
497-663 |
4.20e-10 |
|
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: 63.43 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKpppQHMFYIPQRPYMSLGSLRDQVIYPDSADDMREKGY 575
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGhVHMK---GSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 576 TDQ-----DLErILHSVHlyhivQREGGWDAVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA 650
Cdd:TIGR00957 734 LEAcallpDLE-ILPSGD-----RTEIGEKGVN-----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
170
....*....|....*...
gi 1313999337 651 AIG-----AGISLLSITH 663
Cdd:TIGR00957 803 VIGpegvlKNKTRILVTH 820
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
489-638 |
5.00e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 60.90 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 489 AGEVVAsrlnfkveegmhllITGPNGCGKSSLFRILSGLWPVYEG-VLY--KP----PPQH-------MfyiPQRPYMSL 554
Cdd:COG4559 26 PGELTA--------------IIGPNGAGKSTLLKLLTGELTPSSGeVRLngRPlaawSPWElarrravL---PQHSSLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 555 GSLRDQVI----YP---DSADDmrekgytDQDLERILHSVHLYHIVQReggwdavmDWKDvLSGGEKQRMGMAR------ 621
Cdd:COG4559 89 PFTVEEVValgrAPhgsSAAQD-------RQIVREALALVGLAHLAGR--------SYQT-LSGGEQQRVQLARvlaqlw 152
|
170
....*....|....*...
gi 1313999337 622 -MFYHKPKYALLDECTSA 638
Cdd:COG4559 153 ePVDGGPRWLFLDEPTSA 170
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
490-665 |
5.67e-10 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 60.48 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSG-LWPVYEGVLY--------------KPppqHMFYI-P--QRPY 551
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlfgerrggedvwelRK---RIGLVsPalQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 552 MSLGSLRDQVI---YpDSADDMREkgYTDQDLER---ILHSVHLYHIVQREggwdavmdWKDvLSGGEKQRMGMARMFYH 625
Cdd:COG1119 92 PRDETVLDVVLsgfF-DSIGLYRE--PTDEQRERareLLELLGLAHLADRP--------FGT-LSQGEQRRVLIARALVK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1313999337 626 KPKYALLDECTSavSIDVEGK-IFQAAIGA-----GISLLSITHRP 665
Cdd:COG1119 160 DPELLILDEPTA--GLDLGAReLLLALLDKlaaegAPTLVLVTHHV 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
475-652 |
1.19e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 475 DHGIICENVPI-ITPagevVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppQH---MFYIPQRP 550
Cdd:TIGR01271 426 DDGLFFSNFSLyVTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----KHsgrISFSPQTS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 551 YMSLGSLRDQVIYPDSADDMRekgYTD-----QDLERILHSVHLYHIVQREGGWdavmdwkdVLSGGEKQRMGMARMFYH 625
Cdd:TIGR01271 497 WIMPGTIKDNIIFGLSYDEYR---YTSvikacQLEEDIALFPEKDKTVLGEGGI--------TLSGGQRARISLARAVYK 565
|
170 180
....*....|....*....|....*..
gi 1313999337 626 KPKYALLDECTSAVSIDVEGKIFQAAI 652
Cdd:TIGR01271 566 DADLYLLDSPFTHLDVVTEKEIFESCL 592
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
497-659 |
1.76e-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: 58.60 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKP------PPQHMF-----YIPQR----PYMS------L 554
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsIRFDGrditglPPHERAragigYVPEGrrifPELTveenllL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 555 GSLRdqviypdsaddmREKGYTDQDLERILHSV-HLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLD 633
Cdd:cd03224 99 GAYA------------RRRAKRKARLERVYELFpRLKERRKQLAG---------TLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180
....*....|....*....|....*....
gi 1313999337 634 ECTSAVSIDVEGKIFQAAIG---AGISLL 659
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRElrdEGVTIL 186
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
493-634 |
1.85e-09 |
|
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: 58.38 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 493 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL---------YKPPPQHMFYIPQRP--YMSLgSLRDQV 561
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgksyqkNIEALRRIGALIEAPgfYPNL-TARENL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1313999337 562 IYPDsaddmREKGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:cd03268 94 RLLA-----RLLGIRKKRIDEVLDVVGLKDSAKKKVK---------GFSLGMKQRLGIALALLGNPDLLILDE 152
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
490-663 |
2.37e-09 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 58.40 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPPQHMFYIPQR------------PYMSLGs 556
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGeILLDGKDITNLPPHKRpvntvfqnyalfPHLTVF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 lrDQVIYPdsaddMREKGYTDQDL----ERILHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALL 632
Cdd:cd03300 91 --ENIAFG-----LRLKKLPKAEIkervAEALDLVQLEGYANRK---------PSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1313999337 633 DECTSAV------SIDVEGKIFQAAIgaGISLLSITH 663
Cdd:cd03300 155 DEPLGALdlklrkDMQLELKRLQKEL--GITFVFVTH 189
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
497-675 |
2.92e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.15 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEG-MHLlITGPNGCGKSSLFRILSGLwPVYE---G-VLYK-------PPPQH----MFYIPQRP---------- 550
Cdd:COG0396 19 VNLTIKPGeVHA-IMGPNGSGKSTLAKVLMGH-PKYEvtsGsILLDgedilelSPDERaragIFLAFQYPveipgvsvsn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 551 --YMSLGSLRDQVIY-PDSADDMREKGYT---DQD-LERilhSVHlyhivqrEGgwdavmdwkdvLSGGEKQRMGMARMF 623
Cdd:COG0396 97 flRTALNARRGEELSaREFLKLLKEKMKElglDEDfLDR---YVN-------EG-----------FSGGEKKRNEILQML 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1313999337 624 YHKPKYALLDECTSAVSID---VEGKIFQAAIGAGISLLSITHRPSLWKY----HTHLL 675
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDalrIVAEGVNKLRSPDRGILIITHYQRILDYikpdFVHVL 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
497-664 |
3.15e-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: 57.42 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQH-----MFYIPQRPYMSLGSLRDQViypD 565
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidiSTIPLEdlrssLTIIPQDPTLFSGTIRSNL---D 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 566 SADDmrekgYTDQDLERILhSVhlyhivqREGGwdavmdwkDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEG 645
Cdd:cd03369 104 PFDE-----YSDEEIYGAL-RV-------SEGG--------LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180
....*....|....*....|..
gi 1313999337 646 KIfQAAIG---AGISLLSITHR 664
Cdd:cd03369 163 LI-QKTIReefTNSTILTIAHR 183
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
493-652 |
4.80e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 58.33 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 493 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppQH---MFYIPQRPYMSLGSLRDQVIYPDSADD 569
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----KHsgrISFSSQFSWIMPGTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 570 MREKGYTD--QDLERILHSVHLYHIVQREGGWdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI 647
Cdd:cd03291 127 YRYKSVVKacQLEEDITKFPEKDNTVLGEGGI--------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
....*
gi 1313999337 648 FQAAI 652
Cdd:cd03291 199 FESCV 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-665 |
5.60e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.75 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 509 ITGPNGCGKSSLFRILSGLWPVYEG-------VLY-------------KPPPQHMFYIPQrPYMSLgSLRDQVIYPDSAD 568
Cdd:PRK14246 41 IMGPSGSGKSTLLKVLNRLIEIYDSkikvdgkVLYfgkdifqidaiklRKEVGMVFQQPN-PFPHL-SIYDNIAYPLKSH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 569 DMREKGYTDQDLERILHSVHLYHIVqreggWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI----DVE 644
Cdd:PRK14246 119 GIKEKREIKKIVEECLRKVGLWKEV-----YDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsqAIE 193
|
170 180
....*....|....*....|.
gi 1313999337 645 GKIFQaaIGAGISLLSITHRP 665
Cdd:PRK14246 194 KLITE--LKNEIAIVIVSHNP 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
497-663 |
5.77e-09 |
|
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: 56.04 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLwpvyegvlykpppqhmfyipQRPYMSLGSLRDQVIYPDSADDMREK--- 573
Cdd:cd03229 19 VSLNIEAGEIVALLGPSGSGKSTLLRCIAGL--------------------EEPDSGSILIDGEDLTDLEDELPPLRrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 574 GYTDQDLERILH-SVhlyhivqreggWDAVMdwkDVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVEGKI-FQAA 651
Cdd:cd03229 79 GMVFQDFALFPHlTV-----------LENIA---LGLSGGQQQRVALARALAMDPDVLLLDEPTSA--LDPITRReVRAL 142
|
170
....*....|....*..
gi 1313999337 652 I-----GAGISLLSITH 663
Cdd:cd03229 143 LkslqaQLGITVVLVTH 159
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
487-667 |
7.53e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 56.59 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 487 TPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY--------KPPPQ-------HMFYIPQR- 549
Cdd:COG1136 16 TGEGEVTAlRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdissLSERElarlrrrHIGFVFQFf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 550 ---PYMSLgslRDQVIYP-----DSADDMREKgytdqdLERILHSVHLYHIvqreggwdavMDWK-DVLSGGEKQRMGMA 620
Cdd:COG1136 96 nllPELTA---LENVALPlllagVSRKERRER------ARELLERVGLGDR----------LDHRpSQLSGGQQQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1313999337 621 RMFYHKPKYALLDECTSAV----SIDVEGKIFQAAIGAGISLLSITHRPSL 667
Cdd:COG1136 157 RALVNRPKLILADEPTGNLdsktGEEVLELLRELNRELGTTIVMVTHDPEL 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
490-638 |
7.70e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 58.42 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQH-----------MFyipqrPY 551
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMldgqditHVPAENrhvntvfqsyaLF-----PH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 552 MSLgslRDQVIYpdsadDMREKGYTDQDLER----ILHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKP 627
Cdd:PRK09452 101 MTV---FENVAF-----GLRMQKTPAAEITPrvmeALRMVQLEEFAQRK---------PHQLSGGQQQRVAIARAVVNKP 163
|
170
....*....|.
gi 1313999337 628 KYALLDECTSA 638
Cdd:PRK09452 164 KVLLLDESLSA 174
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
478-636 |
9.01e-09 |
|
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: 54.76 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPaGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQrpymslgsl 557
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1313999337 558 rdqviypdsaddmrekgytdqdlerilhsvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECT 636
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
495-665 |
9.87e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 495 SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP---------QHMFYIPQRPymslGslrdqvIYP 564
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGeVLWQGEPirrqrdeyhQDLLYLGHQP----G------IKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 565 D-SAddmrekgytdqdLE--RILHSVHlyHIVQREGGWDA-----VMDWKDV----LSGGEKQRMGMARMFYHKPKYALL 632
Cdd:PRK13538 88 ElTA------------LEnlRFYQRLH--GPGDDEALWEAlaqvgLAGFEDVpvrqLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1313999337 633 DECTSAvsIDVEG-KIFQAAIGA-----GISLLSiTHRP 665
Cdd:PRK13538 154 DEPFTA--IDKQGvARLEALLAQhaeqgGMVILT-THQD 189
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
497-670 |
2.06e-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: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLwPVYE----GVLYKP------PPQH-----MFYIPQRPymslgslrdqv 561
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvtegEILFKGeditdlPPEErarlgIFLAFQYP----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 562 iypdsaddMREKGYTDQDLERILHsvhlyhivqrEGgwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI 641
Cdd:cd03217 87 --------PEIPGVKNADFLRYVN----------EG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190
....*....|....*....|....*....|..
gi 1313999337 642 D---VEGKIFQAAIGAGISLLSITHRPSLWKY 670
Cdd:cd03217 138 DalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
490-634 |
3.14e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.38 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG--VL----------YKPPPQHMFyipQR----PYMS 553
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGqiMLdgvdlshvppYQRPINMMF---QSyalfPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 554 LgslrDQVIYPDSADDMREKGYTDQDLERILHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLD 633
Cdd:PRK11607 108 V----EQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRK---------PHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
.
gi 1313999337 634 E 634
Cdd:PRK11607 175 E 175
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
489-675 |
3.60e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 54.16 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 489 AGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQR-------PY-----MSLGS 556
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRsevpdslPLtvrdlVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 LRDQVIY-PDSADDMREkgyTDQDLERilhsVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLDEC 635
Cdd:NF040873 83 WARRGLWrRLTRDDRAA---VDDALER----VGLADLAGRQ---------LGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1313999337 636 TSAVSIDVEGKIFQ---AAIGAGISLLSITHRPSLWKYHTHLL 675
Cdd:NF040873 147 TTGLDAESRERIIAllaEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
491-664 |
6.20e-08 |
|
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: 53.09 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 491 EVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPP-------QHMFYIPQRPYMSLGSLRDQ 560
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITldgVPVSdlekalsSLISVLNQRPYLFDTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 561 VIYPdsaddmrekgytdqdlerilhsvhlyhivqreggwdavmdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTsaVS 640
Cdd:cd03247 95 LGRR--------------------------------------------FSGGERQRLALARILLQDAPIVLLDEPT--VG 128
|
170 180 190
....*....|....*....|....*....|
gi 1313999337 641 IDVEGK------IFQAAigAGISLLSITHR 664
Cdd:cd03247 129 LDPITErqllslIFEVL--KDKTLIWITHH 156
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
495-683 |
9.54e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 53.49 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 495 SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPPPQHMF------------YIPQRPYMSLGSLRD 559
Cdd:cd03290 18 SNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnKNESEPSFeatrsrnrysvaYAAQKPWLLNATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 560 QVIYPDSADDMREKGYTDQ-----DLERILHSVhlyhivQREGGWDAVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:cd03290 98 NITFGSPFNKQRYKAVTDAcslqpDIDLLPFGD------QTEIGERGIN-----LSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1313999337 635 CTSAVSIDVEGKIFQAAIgagISLLSITHRPSLWKyhTHLLQFDGEGGW 683
Cdd:cd03290 167 PFSALDIHLSDHLMQEGI---LKFLQDDKRTLVLV--THKLQYLPHADW 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
511-647 |
9.65e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.01 E-value: 9.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 511 GPNGCGKSSLFRIL---SGLWP---VYEGVLYKpppQHMFYIP---------------QRPYMSLGSLRDQVIYPDSADD 569
Cdd:PRK14239 38 GPSGSGKSTLLRSInrmNDLNPevtITGSIVYN---GHNIYSPrtdtvdlrkeigmvfQQPNPFPMSIYENVVYGLRLKG 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1313999337 570 MREKGYTDQDLERILHSVHLYHIVQreggwDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKI 647
Cdd:PRK14239 115 IKDKQVLDEAVEKSLKGASIWDEVK-----DRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI 187
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
497-663 |
1.01e-07 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 53.62 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGL-WPVYEGVLYK------PPPQHMFYIPQRPYMSLGSLRDQV-IYPDSAD 568
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLaQPTSGGVILEgkqitePGPDRMVVFQNYSLLPWLTVRENIaLAVDRVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 569 DMREKGYTDQDLERILHSVHLYHivqreggwdAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI----DVE 644
Cdd:TIGR01184 84 PDLSKSERRAIVEEHIALVGLTE---------AADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNLQ 154
|
170
....*....|....*....
gi 1313999337 645 GKIFQAAIGAGISLLSITH 663
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTH 173
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
488-666 |
1.05e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 55.11 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 488 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG--VLYKPPPQHMfyipqrpymSLGSLRDQV---- 561
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGqiLLDGHDLADY---------TLASLRRQValvs 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 562 ----IYPDS-ADDM---REKGYTDQDLERILHSVHLYHIVQR-EGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYAL 631
Cdd:TIGR02203 413 qdvvLFNDTiANNIaygRTEQADRAEIERALAAAYAQDFVDKlPLGLDTPIGENGVlLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 1313999337 632 LDECTSAVSIDVEGKIfQAAIGA---GISLLSITHRPS 666
Cdd:TIGR02203 493 LDEATSALDNESERLV-QAALERlmqGRTTLVIAHRLS 529
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
492-680 |
1.06e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 492 VVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQRPYMSLGSLRDQVIYPD--SADD 569
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdiTVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 570 MREKG-YTDQDL---ERILHSVHLYHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAV----SI 641
Cdd:PRK10253 101 LVARGrYPHQPLftrWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLdishQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1313999337 642 DVEGKIFQAAIGAGISLLSITHR-PSLWKYHTHLLQF-DGE 680
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALrEGK 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
490-634 |
1.48e-07 |
|
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: 53.12 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVA-SRLNFKVEEG-MHLLItGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQ--HM-----FYIPQ---- 548
Cdd:COG0411 15 GGLVAvDDVSLEVERGeIVGLI-GPNGAGKTTLFNLITGFYRPTSGrILFDgrditglPPHRiaRLgiartFQNPRlfpe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 549 --------------RPYMSLGSLRDQVIYPDSADDMREKGytdqdlERILHSVHLYHIVQREGGwdavmdwkdVLSGGEK 614
Cdd:COG0411 94 ltvlenvlvaaharLGRGLLAALLRLPRARREEREARERA------EELLERVGLADRADEPAG---------NLSYGQQ 158
|
170 180
....*....|....*....|
gi 1313999337 615 QRMGMARMFYHKPKYALLDE 634
Cdd:COG0411 159 RRLEIARALATEPKLLLLDE 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
490-634 |
1.97e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.30 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQ-RPYMSLG-SLRDQVIypDSA 567
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQhQEELDPDkTVLDELR--DGA 404
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1313999337 568 DDMREK---GYtdqdLERILHSvhlyhivqregGWDAvmdWK--DVLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:COG0488 405 PGGTEQevrGY----LGRFLFS-----------GDDA---FKpvGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
465-634 |
2.17e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.76 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 465 LAIKGTVIDVDHGIICENVPIITPAGEVVAsrlnfkveegmhllITGPNGCGKSSLFRILSGLWPVYEGVLykpppqhmf 544
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVA--------------VVGRSGCGKSTLLRLLAGLETPSAGEL--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 545 yipqrpymslgsLRDQVIYPDSADDMREKgYTDQDL---ERILHSVHLyhivQREGGW--------DAV------MDWKD 607
Cdd:PRK11247 70 ------------LAGTAPLAEAREDTRLM-FQDARLlpwKKVIDNVGL----GLKGQWrdaalqalAAVgladraNEWPA 132
|
170 180
....*....|....*....|....*..
gi 1313999337 608 VLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDE 159
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
490-664 |
3.03e-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: 53.98 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP----------QHMFYIPQRPYMSLGSLR 558
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeILLNGFSlkdidrhtlrQFINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 559 DQVIYPDsaddmrEKGYTDQDLERILHSVHLY-HIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECT 636
Cdd:TIGR01193 566 ENLLLGA------KENVSQDEIWAACEIAEIKdDIENMPLGYQTELSEEGSsISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180
....*....|....*....|....*...
gi 1313999337 637 SAVSIDVEGKIFQaaigagiSLLSITHR 664
Cdd:TIGR01193 640 SNLDTITEKKIVN-------NLLNLQDK 660
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
478-636 |
3.25e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 51.59 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhMF-----YIPQR--P 550
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL------VNgqdlsRLKRReiP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 551 YM--SLG------------SLRDQVIYPdsaddMREKGYTDQDLER----ILHSVHLYHivqreggwdavmdwK-----D 607
Cdd:COG2884 76 YLrrRIGvvfqdfrllpdrTVYENVALP-----LRVTGKSRKEIRRrvreVLDLVGLSD--------------KakalpH 136
|
170 180
....*....|....*....|....*....
gi 1313999337 608 VLSGGEKQRMGMARMFYHKPKYALLDECT 636
Cdd:COG2884 137 ELSGGEQQRVAIARALVNRPELLLADEPT 165
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
479-638 |
3.31e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 52.08 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 479 ICENVPIITPAGEVVAsrlnfkveegmhllITGPNGCGKSSLFRILSGLWPVYEG-VLY--KP----PPQHMFYI----P 547
Cdd:PRK13548 17 LLDDVSLTLRPGEVVA--------------ILGPNGAGKSTLLRALSGELSPDSGeVRLngRPladwSPAELARRravlP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 548 QRPYMSLGSLRDQVI----YPDSaddmREKGYTDQDLERILHSVHLYHIVQReggwdavmdwkDV--LSGGEKQRMGMAR 621
Cdd:PRK13548 83 QHSSLSFPFTVEEVVamgrAPHG----LSRAEDDALVAAALAQVDLAHLAGR-----------DYpqLSGGEQQRVQLAR 147
|
170 180
....*....|....*....|...
gi 1313999337 622 MF------YHKPKYALLDECTSA 638
Cdd:PRK13548 148 VLaqlwepDGPPRWLLLDEPTSA 170
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
478-666 |
4.29e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.48 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhMFYIPQRPYmSLGS 556
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRnINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIL------LDGHDLRDY-TLAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 LRDQV--------IYPDS-ADDM---REKGYTDQDLERILHSVH-LYHIVQREGGWDAVMDWKDV-LSGGEKQRMGMARM 622
Cdd:PRK11176 415 LRNQValvsqnvhLFNDTiANNIayaRTEQYSREQIEEAARMAYaMDFINKMDNGLDTVIGENGVlLSGGQRQRIAIARA 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1313999337 623 FYHKPKYALLDECTSAVSIDVEGKIfQAAIGA---GISLLSITHRPS 666
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAI-QAALDElqkNRTSLVIAHRLS 540
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
486-663 |
5.22e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 50.94 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 486 ITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSG-LWPV--YEGVLY--------KPPPQ-HMFYIPQR---- 549
Cdd:COG4136 9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLlngrrltaLPAEQrRIGILFQDdllf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 550 PYMSLG-------------SLRDQVIypdsaddmrekgytdqdlERILHSVHLYHIVQReggwdavmdwkDV--LSGGEK 614
Cdd:COG4136 89 PHLSVGenlafalpptigrAQRRARV------------------EQALEEAGLAGFADR-----------DPatLSGGQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1313999337 615 QRMGMARMFYHKPKYALLDECTS----AVSIDVEGKIFQAAIGAGISLLSITH 663
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSkldaALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
497-666 |
6.07e-07 |
|
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: 52.90 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGlwpvyegvlykpppqhmFYIPQ-----------RPYmSLGSLRDQV-IYP 564
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFR-----------------FYDVTsgrilidgqdiRDV-TQASLRAAIgIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 565 -DSA---DDMREK-GY-----TDQDLERILHSVHLYHIVQR-EGGWDAVmdwkdV------LSGGEKQRMGMARMFYHKP 627
Cdd:COG5265 439 qDTVlfnDTIAYNiAYgrpdaSEEEVEAAARAAQIHDFIESlPDGYDTR-----VgerglkLSGGEKQRVAIARTLLKNP 513
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1313999337 628 KYALLDECTSAVSIDVEGKIfQAA---IGAGISLLSITHRPS 666
Cdd:COG5265 514 PILIFDEATSALDSRTERAI-QAAlreVARGRTTLVIAHRLS 554
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
492-663 |
6.82e-07 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 50.90 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 492 VVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY----------KPPPQHMFYipqrpymslgsLRDQ 560
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsILVrhdggwvdlaQASPREILA-----------LRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 561 VIypdsaddmrekGYTDQDLeRILHSVHLYHIVQ---REGGWD---AVMDWKDVL-----------------SGGEKQRM 617
Cdd:COG4778 94 TI-----------GYVSQFL-RVIPRVSALDVVAeplLERGVDreeARARARELLarlnlperlwdlppatfSGGEQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1313999337 618 GMARMFYHKPKYALLDECTSavSIDVEGK-----IFQAAIGAGISLLSITH 663
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTA--SLDAANRavvveLIEEAKARGTAIIGIFH 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
497-663 |
7.17e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 51.55 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppqhmfyipqrpymslgSLRDQVIYPDSADDMREK--- 573
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI--------------------TVGGMVLSEETVWDVRRQvgm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 574 ----------GYTDQD----------------LERI---LHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFY 624
Cdd:PRK13635 86 vfqnpdnqfvGATVQDdvafglenigvpreemVERVdqaLRQVGMEDFLNRE---------PHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1313999337 625 HKPKYALLDECTSAVS----IDVEGKIFQAAIGAGISLLSITH 663
Cdd:PRK13635 157 LQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITH 199
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
497-663 |
7.22e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.63 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY----KPPPQHMFYIPQRPYMSLGSLRDQVIYPDSADD--- 569
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgeLLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 570 -MREKGYTDQDL----ERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVE 644
Cdd:PRK13642 106 gMENQGIPREEMikrvDEALLAVNMLDFKTREPA---------RLSGGQKQRVAVAGIIALRPEIIILDESTSM--LDPT 174
|
170 180
....*....|....*....|....*
gi 1313999337 645 GK------IFQAAIGAGISLLSITH 663
Cdd:PRK13642 175 GRqeimrvIHEIKEKYQLTVLSITH 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
490-663 |
9.59e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 50.66 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV------------LYKPPPQHMFYIPQRPYMslgsL 557
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGYLPQEASI----F 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 558 RDQVIYPD--SADDMREKGYTDQDLER---ILHSVHLYHIVQREGgwdavmdwkDVLSGGEKQRMGMARMFYHKPKYALL 632
Cdd:PRK10895 91 RRLSVYDNlmAVLQIRDDLSAEQREDRaneLMEEFHIEHLRDSMG---------QSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1313999337 633 DECTSAVS----IDVEgKIFQAAIGAGISLLSITH 663
Cdd:PRK10895 162 DEPFAGVDpisvIDIK-RIIEHLRDSGLGVLITDH 195
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
497-663 |
1.05e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.89 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY----KPPPQHMFYIPQRPYMSLGSLRDQVIYPDSADD--- 569
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdLLTEENVWDIRHKIGMVFQNPDNQFVGATVEDDvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 570 -MREKGYTDQDL-ERILHSVHLYhivqreggwdAVMDWKDV----LSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDV 643
Cdd:PRK13650 106 gLENKGIPHEEMkERVNEALELV----------GMQDFKEReparLSGGQKQRVAIAGAVAMRPKIIILDEATSM--LDP 173
|
170 180
....*....|....*....|....*...
gi 1313999337 644 EGKifQAAIGA--------GISLLSITH 663
Cdd:PRK13650 174 EGR--LELIKTikgirddyQMTVISITH 199
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
462-666 |
1.36e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 51.64 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 462 SDTLAIKGTVIDVDhgiiceNVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppq 541
Cdd:PRK10790 331 NDDRPLQSGRIDID------NVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR----- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 542 hmfyIPQRPYMSL--GSLR--------DQVIYPDS--ADDMREKGYTDQDLERILHSVHLYHIVQR--EGGWDAVMDWKD 607
Cdd:PRK10790 400 ----LDGRPLSSLshSVLRqgvamvqqDPVVLADTflANVTLGRDISEEQVWQALETVQLAELARSlpDGLYTPLGEQGN 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1313999337 608 VLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA--AIGAGISLLSITHRPS 666
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAlaAVREHTTLVVIAHRLS 536
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
489-634 |
1.63e-06 |
|
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: 49.85 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 489 AGEVVAsrlnfkveegmhLLitGPNGCGKSSLFRILSGLWPVYEGVLY-------KPPPQH-----MFYIPQRP--YMSL 554
Cdd:cd03218 25 QGEIVG------------LL--GPNGAGKTTTFYMIVGLVKPDSGKILldgqditKLPMHKrarlgIGYLPQEAsiFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 555 gSLRDQVIypdSADDMREKGYTDQD--LERILHSVHLYHIVQREGgwdavmdwkDVLSGGEKQRMGMARMFYHKPKYALL 632
Cdd:cd03218 91 -TVEENIL---AVLEIRGLSKKEREekLEELLEEFHITHLRKSKA---------SSLSGGERRRVEIARALATNPKFLLL 157
|
..
gi 1313999337 633 DE 634
Cdd:cd03218 158 DE 159
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
491-678 |
1.69e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.87 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 491 EVVASRLNFKVEEGMHLLITGPNGCGKSS----LFRILSGLWP--VYEGVLYKPPPQH-----MFYIPQRPYMSLGSLRD 559
Cdd:TIGR00957 1299 DLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRINESAEGeiIIDGLNIAKIGLHdlrfkITIIPQDPVLFSGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 560 QvIYPDSAddmrekgYTDQDLERILHSVHLYHIVQR----------EGGwdavmdwkDVLSGGEKQRMGMARMFYHKPKY 629
Cdd:TIGR00957 1379 N-LDPFSQ-------YSDEEVWWALELAHLKTFVSAlpdkldhecaEGG--------ENLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1313999337 630 ALLDECTSAVSIDVEGKIfQAAIGAGI---SLLSITHRPSLWKYHTHLLQFD 678
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLI-QSTIRTQFedcTVLTIAHRLNTIMDYTRVIVLD 1493
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
493-663 |
2.18e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.18 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 493 VASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGL-----------------------WPVYE--GVLYKPPPQHMfyip 547
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnskitvdgitltaktvWDIREkvGIVFQNPDNQF---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 548 qrpymsLGSlrdqVIYPDSADDMREKGYTDQDLERILHSVhlyhiVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKP 627
Cdd:PRK13640 98 ------VGA----TVGDDVAFGLENRAVPRPEMIKIVRDV-----LADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1313999337 628 KYALLDECTSAvsIDVEGK------IFQAAIGAGISLLSITH 663
Cdd:PRK13640 163 KIIILDESTSM--LDPAGKeqilklIRKLKKKNNLTVISITH 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
478-639 |
2.52e-06 |
|
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: 49.49 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 478 IICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYkpppqhmFY---IPQRPYMSL 554
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVL-------IDgtdINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 555 GSLRDQViypdsaddmrekGYTDQD---------LERILHS-----------VHLYHIVQREGGWDAV----MDWK---- 606
Cdd:cd03256 74 RQLRRQI------------GMIFQQfnlierlsvLENVLSGrlgrrstwrslFGLFPKEEKQRALAALervgLLDKayqr 141
|
170 180 190
....*....|....*....|....*....|....
gi 1313999337 607 -DVLSGGEKQRMGMARMFYHKPKYALLDECTSAV 639
Cdd:cd03256 142 aDQLSGGQQQRVAIARALMQQPKLILADEPVASL 175
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
497-679 |
3.08e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY---KPP-----PQHMFYIPQrpymsLGSLRdqviypdsad 568
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQidgKTAtrgdrSRFMAYLGH-----LPGLK---------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 569 dmrekgytdQDLERI--LH---SVHLYHIVQREGGWDAVM---DWKDV----LSGGEKQRMGMARMFYHKPKYALLDEct 636
Cdd:PRK13543 95 ---------ADLSTLenLHflcGLHGRRAKQMPGSALAIVglaGYEDTlvrqLSAGQKKRLALARLWLSPAPLWLLDE-- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1313999337 637 SAVSIDVEG-----KIFQAAIGAGISLLSITH--RPSLwKYHTHLLQFDG 679
Cdd:PRK13543 164 PYANLDLEGitlvnRMISAHLRGGGAALVTTHgaYAAP-PVRTRMLTLEA 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
497-678 |
4.90e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.96 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILsglwpvyegvlykpppqHMFYIPQRPY----------MSLGSLRDQ--VIYP 564
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLL-----------------QRVFDPQSGRilidgtdirtVTRASLRRNiaVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 565 DS-------ADDMR--EKGYTDQDLERILHSVH-LYHIVQREGGWDAVMDWK-DVLSGGEKQRMGMARMFYHKPKYALLD 633
Cdd:PRK13657 417 DAglfnrsiEDNIRvgRPDATDEEMRAAAERAQaHDFIERKPDGYDTVVGERgRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1313999337 634 ECTSAVSIDVEGKIfQAAIGA---GISLLSITHRPSLWKYHTHLLQFD 678
Cdd:PRK13657 497 EATSALDVETEAKV-KAALDElmkGRTTFIIAHRLSTVRNADRILVFD 543
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
495-656 |
6.94e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 495 SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYE--GVLYKpppQHMFYIPQRPYMSLGSLRDQVIYpdSADDMRE 572
Cdd:PLN03232 634 SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtsSVVIR---GSVAYVPQVSWIFNATVRENILF--GSDFESE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 573 KGYTDQDLERILHSVHLYHIVQR-EGGWDAVMdwkdvLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQAA 651
Cdd:PLN03232 709 RYWRAIDVTALQHDLDLLPGRDLtEIGERGVN-----ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC 783
|
....*
gi 1313999337 652 IGAGI 656
Cdd:PLN03232 784 MKDEL 788
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
497-667 |
8.30e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.56 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGlwpvyegvLYKPPPQHMFY-------IPQR--PYM--SLGS-------LR 558
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICG--------IERPSAGKIWFsghditrLKNRevPFLrrQIGMifqdhhlLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 559 DQVIYPDSADDMREKGYTDQDLERILHSVhlyhiVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECT-- 636
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAA-----LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTgn 167
|
170 180 190
....*....|....*....|....*....|...
gi 1313999337 637 --SAVSIDVEgKIFQAAIGAGISLLSITHRPSL 667
Cdd:PRK10908 168 ldDALSEGIL-RLFEEFNRVGVTVLMATHDIGL 199
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
488-634 |
8.45e-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: 47.67 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 488 PAGEVVAsrlnfkveegmhlLItGPNGCGKSSLFRILSGLWPVYEG-VLYK-------PPPQ----HMFYIPQR----PY 551
Cdd:COG0410 27 EEGEIVA-------------LL-GRNGAGKTTLLKAISGLLPPRSGsIRFDgeditglPPHRiarlGIGYVPEGrrifPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 552 MS------LGSLRdqviypdsaddMREKGYTDQDLERILHSV-HLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFY 624
Cdd:COG0410 93 LTveenllLGAYA-----------RRDRAEVRADLERVYELFpRLKERRRQRAG---------TLSGGEQQMLAIGRALM 152
|
170
....*....|
gi 1313999337 625 HKPKYALLDE 634
Cdd:COG0410 153 SRPKLLLLDE 162
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
476-666 |
9.63e-06 |
|
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: 46.78 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 476 HGIICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGL--WPVYEG-VLYKPPPQHMFyipqrpym 552
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGeVLINGRPLDKR-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 553 slgSLRDQViypdsaddmrekGYTDQDLerILHS---VH--LYHIVQREGgwdavmdwkdvLSGGEKQRMGMARMFYHKP 627
Cdd:cd03213 79 ---SFRKII------------GYVPQDD--ILHPtltVRetLMFAAKLRG-----------LSGGERKRVSIALELVSNP 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1313999337 628 KYALLDECTS------AVSIdveGKIFQAAIGAGISLLSITHRPS 666
Cdd:cd03213 131 SLLFLDEPTSgldsssALQV---MSLLRRLADTGRTIICSIHQPS 172
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
496-685 |
1.05e-05 |
|
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: 48.78 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 496 RLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPPPQHMFYIPQrpymSLGSLRD-----QVIyPDSADDM 570
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ----SRDALDPnktvwEEI-SGGLDII 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 571 REKGY---------------TDQdlerilhsvhlyhivQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDEC 635
Cdd:TIGR03719 415 KLGKReipsrayvgrfnfkgSDQ---------------QKKVG---------QLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1313999337 636 TSavSIDVEG-KIFQAAIG--AGISLLsITH-RPSLWKYHTHLLQFDGEGGWRF 685
Cdd:TIGR03719 471 TN--DLDVETlRALEEALLnfAGCAVV-ISHdRWFLDRIATHILAFEGDSHVEW 521
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
497-664 |
1.07e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL-----------YKPPPQHMFYIPQRPYMSLGSLRDQViypd 565
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRImiddcdvakfgLTDLRRVLSIIPQSPVLFSGTVRFNI---- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 566 saDDMREkgYTDQDLERILHSVHLYHIVQREG-GWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDV 643
Cdd:PLN03232 1331 --DPFSE--HNDADLWEALERAHIKDVIDRNPfGLDAeVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180
....*....|....*....|....
gi 1313999337 644 EGKIfQAAIGA---GISLLSITHR 664
Cdd:PLN03232 1407 DSLI-QRTIREefkSCTMLVIAHR 1429
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
487-638 |
1.32e-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: 47.19 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 487 TPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLY-------------KPPPQHMFYIPQRpY 551
Cdd:cd03258 13 DTGGKVTAlKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGsVLVdgtdltllsgkelRKARRRIGMIFQH-F 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 552 MSLGSL--RDQVIYPDSADDMrEKGYTDQDLERILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKY 629
Cdd:cd03258 92 NLLSSRtvFENVALPLEIAGV-PKAEIEERVLELLELVGLEDKADA---------YPAQLSGGQKQRVGIARALANNPKV 161
|
....*....
gi 1313999337 630 ALLDECTSA 638
Cdd:cd03258 162 LLCDEATSA 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
487-637 |
1.96e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.37 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 487 TPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLF----RILSGLWPV------YEGVLYKPPPQHMFYIPQRPYMSLGS 556
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTEGEIqidgvsWNSVTLQTWRKAFGVIPQKVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 LRDQViypdsadDMREKgYTDQDLERILHSVHLYHIV-QREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:TIGR01271 1308 FRKNL-------DPYEQ-WSDEEIWKVAEEVGLKSVIeQFPDKLDFVLvDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
...
gi 1313999337 635 CTS 637
Cdd:TIGR01271 1380 PSA 1382
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
491-636 |
2.06e-05 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 46.56 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 491 EVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-------VLYKPPPQHMFYIP----QR--------P 550
Cdd:cd03267 33 EVEALKgISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGevrvaglVPWKRRKKFLRRIGvvfgQKtqlwwdlpV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 551 YMSLGSLRDqvIY--PDSADDMREKGYTDQ-DLERILHSVhlyhiVQReggwdavmdwkdvLSGGEKQRMGMARMFYHKP 627
Cdd:cd03267 113 IDSFYLLAA--IYdlPPARFKKRLDELSELlDLEELLDTP-----VRQ-------------LSLGQRMRAEIAAALLHEP 172
|
....*....
gi 1313999337 628 KYALLDECT 636
Cdd:cd03267 173 EILFLDEPT 181
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
497-638 |
2.48e-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: 45.98 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-------VLYKPPP------QHMFYIPQR----PYMSLgsLRD 559
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglKLTDDKKninelrQKVGMVFQQfnlfPHLTV--LEN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1313999337 560 QVIYPdsaddMREKGYTDQDLERILhsvhlYHIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSA 638
Cdd:cd03262 97 ITLAP-----IKVKGMSKAEAEERA-----LELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
509-652 |
4.32e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.77 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 509 ITGPNGCGKSSLFRILSGLW-PVYEGVLYKPPP-----QHMFYIPQRPYMSLGSLRDQVIYPDSADD----MREKGYTDQ 578
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLrPQKGAVLWQGKPldyskRGLLALRQQVATVFQDPEQQIFYTDIDSDiafsLRNLGVPEA 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1313999337 579 DLER----ILHSVHLYHIVQREggwdavmdwKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAvsIDVEGKIFQAAI 652
Cdd:PRK13638 112 EITRrvdeALTLVDAQHFRHQP---------IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG--LDPAGRTQMIAI 178
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
450-526 |
4.99e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 4.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1313999337 450 HSKRGGNLELPLSDTLAIKGTVIDVDHGIICENVpIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSG 526
Cdd:PRK10938 233 HSEQLEGVQLPEPDEPSARHALPANEPRIVLNNG-VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
487-634 |
5.00e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 45.62 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 487 TPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLF----RILSGLWPV-YEGVLYKPPPQHMF-----YIPQRPYMSLGS 556
Cdd:cd03289 13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLNTEGDIqIDGVSWNSVPLQKWrkafgVIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 LRDQViypdsadDMREKgYTDQDLERILHSVHLYHIV-QREGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:cd03289 93 FRKNL-------DPYGK-WSDEEIWKVAEEVGLKSVIeQFPGQLDFVLvDGGCVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
487-527 |
7.12e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.07 E-value: 7.12e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1313999337 487 TPAGEVVA-SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGL 527
Cdd:COG1134 34 TRREEFWAlKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI 75
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
477-647 |
7.28e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 45.26 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 477 GIICENVPIITPAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG---VLYKPPPQHM-----FYIPQ 548
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisILGQPTRQALqknlvAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 549 RPYM--SLGSLRDQVIYPDSADDM----REKGYTDQDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARM 622
Cdd:PRK15056 86 SEEVdwSFPVLVEDVVMMGRYGHMgwlrRAKKRDRQIVTAALARVDMVEFRHRQIG---------ELSGGQKKRVFLARA 156
|
170 180
....*....|....*....|....*
gi 1313999337 623 FYHKPKYALLDECTSAVSIDVEGKI 647
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARI 181
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
496-646 |
7.52e-05 |
|
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: 44.80 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 496 RLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY----------KPPPQHMFYIPQrpymslgslrDQVIYPD 565
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdrKAARQSLGYCPQ----------FDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 566 -SADDM-----REKGYT----DQDLERILHSVHLYhivqreggwdavmDWKDV----LSGGEKQRMGMARMFYHKPKYAL 631
Cdd:cd03263 90 lTVREHlrfyaRLKGLPkseiKEEVELLLRVLGLT-------------DKANKrartLSGGMKRKLSLAIALIGGPSVLL 156
|
170
....*....|....*
gi 1313999337 632 LDECTSavSIDVEGK 646
Cdd:cd03263 157 LDEPTS--GLDPASR 169
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
493-533 |
8.11e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 44.83 E-value: 8.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1313999337 493 VASRL---NFKVEEGMHLLITGPNGCGKSSLFRILSGLWPvYEG 533
Cdd:COG4138 8 VAGRLgpiSAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQG 50
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
490-636 |
8.33e-05 |
|
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: 44.67 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 490 GEVVASR-LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLykpppqHMFyipqrpymSLGSLRDqviypdsAD 568
Cdd:cd03265 11 GDFEAVRgVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRA------TVA--------GHDVVRE-------PR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 569 DMREK-GYTDQDL---------ERILHSVHLYHIVQREggWD----------AVMDWKDVL----SGGEKQRMGMARMFY 624
Cdd:cd03265 70 EVRRRiGIVFQDLsvddeltgwENLYIHARLYGVPGAE--RReridelldfvGLLEAADRLvktySGGMRRRLEIARSLV 147
|
170
....*....|..
gi 1313999337 625 HKPKYALLDECT 636
Cdd:cd03265 148 HRPEVLFLDEPT 159
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
488-637 |
8.37e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.07 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 488 PAGEVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG-VLYKPPP------------QHMFYIPQRPymsl 554
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGeVLIKGEPikydkksllevrKTVGIVFQNP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 555 gslRDQVIYPDSADD-----MREKGYTDQDLERILHSVHLyhiVQREGGWDAVmdwKDVLSGGEKQRMGMARMFYHKPKY 629
Cdd:PRK13639 88 ---DDQLFAPTVEEDvafgpLNLGLSKEEVEKRVKEALKA---VGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPEI 158
|
....*...
gi 1313999337 630 ALLDECTS 637
Cdd:PRK13639 159 IVLDEPTS 166
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
497-666 |
1.03e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.45 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGV------------LYKPPPQ---------HMFYIPQrPYMSLG 555
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEArvegevrlfgrnIYSPDVDpievrrevgMVFQYPN-PFPHLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 556 SLRDQVIYPDSADDMREKGYTDQDLERILHSVHLYHIVQreggwDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDEC 635
Cdd:PRK14267 102 IYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVK-----DRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1313999337 636 TSAV----SIDVEGKIFQAAIGAGISLlsITHRPS 666
Cdd:PRK14267 177 TANIdpvgTAKIEELLFELKKEYTIVL--VTHSPA 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
497-663 |
1.06e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 44.62 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPppQHMFYIPQRPYMSLG-SLRDQV--------IYPDSA 567
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIA--GNHFDFSKTPSDKAIrELRRNVgmvfqqynLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 568 -------DDMREKGYT-DQDLER---ILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECT 636
Cdd:PRK11124 99 vqqnlieAPCRVLGLSkDQALARaekLLERLRLKPYADR---------FPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190
....*....|....*....|....*....|
gi 1313999337 637 SAVSIDVEG---KIFQAAIGAGISLLSITH 663
Cdd:PRK11124 170 AALDPEITAqivSIIRELAETGITQVIVTH 199
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
497-533 |
1.18e-04 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 44.06 E-value: 1.18e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG 533
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG 77
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
609-664 |
1.33e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 1.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1313999337 609 LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEgKIFQAAI-----GAGISLLSITHR 664
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE-KLIEKTIvdikdKADKTIITIAHR 1418
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
497-652 |
1.87e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.15 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLYKPppQHMFYIPQRPYMSLGSLRDQVIYPDSADDMREkgyt 576
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--RSIAYVPQQAWIMNATVRGNILFFDEEDAARL---- 752
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1313999337 577 dQDLERIlhSVHLYHIVQREGGWDAVMDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQAAI 652
Cdd:PTZ00243 753 -ADAVRV--SQLEADLAQLGGGLETEIGEKGVnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF 826
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
498-638 |
1.93e-04 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 43.44 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 498 NFKVEEGMHLLITGPNGCGKSSLFRILSGLWP------VYEGVLYKPPPQHMFYIPQR-----------PYMSLgslRDQ 560
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiTVDGEDLTDSKKDINKLRRKvgmvfqqfnlfPHLTV---LEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 561 VIYP------DSADDMREKGytdqdlERILHSVHLYhivqreggwdavmDWKDV----LSGGEKQRMGMAR---MfyhKP 627
Cdd:COG1126 98 VTLApikvkkMSKAEAEERA------MELLERVGLA-------------DKADAypaqLSGGQQQRVAIARalaM---EP 155
|
170
....*....|.
gi 1313999337 628 KYALLDECTSA 638
Cdd:COG1126 156 KVMLFDEPTSA 166
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
492-663 |
3.03e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 43.16 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 492 VVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY------KPPPQHMFYIPQRPYM---------SLGS 556
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdglkvNDPKVDERLIRQEAGMvfqqfylfpHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 LRDQVIYPdsaddMREKGYTDQDLERILHSvhlyhIVQREGGWDAVMDWKDVLSGGEKQRMGMARMFYHKPKYALLDECT 636
Cdd:PRK09493 95 LENVMFGP-----LRVRGASKEEAEKQARE-----LLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190
....*....|....*....|....*....|..
gi 1313999337 637 SAvsIDVE-----GKIFQAAIGAGISLLSITH 663
Cdd:PRK09493 165 SA--LDPElrhevLKVMQDLAEEGMTMVIVTH 194
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
465-675 |
3.28e-04 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 43.02 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 465 LAIKGTVIDVDHGIICENVPIITPAGEVVAsrlnfkveegmhllITGPNGCGKSSLFRILSGlWPVYEgvlykpppqhmf 544
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHA--------------IMGPNGSGKSTLSKTIAG-HPSYE------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 545 yipqrpyMSLGS--LRDQVIYPDSADDMREKG--YTDQDLERI--------LHSVhlYHIVQREGGWDA--VMDWKDVL- 609
Cdd:TIGR01978 54 -------VTSGTilFKGQDLLELEPDERARAGlfLAFQYPEEIpgvsnlefLRSA--LNARRSARGEEPldLLDFEKLLk 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 610 ---------------------SGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEgKIFQAAIGA----GISLLSITHR 664
Cdd:TIGR01978 125 eklalldmdeeflnrsvnegfSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDAL-KIVAEGINRlrepDRSFLIITHY 203
|
250
....*....|....*
gi 1313999337 665 PSLWKY----HTHLL 675
Cdd:TIGR01978 204 QRLLNYikpdYVHVL 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
496-663 |
5.42e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.31 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 496 RLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVL--------------YKPPPQHMFYIPQRPYMSLGSlRDQV 561
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqridtlspgkLQALRRDIQFIFQDPYASLDP-RQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 562 IYpDSADDMREKGYTDQDLER-----ILHSVHLyhivQREGGWDavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECT 636
Cdd:PRK10261 421 GD-SIMEPLRVHGLLPGKAAAarvawLLERVGL----LPEHAWR----YPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190
....*....|....*....|....*....|.
gi 1313999337 637 SAVSIDVEGKIFQAAIGA----GISLLSITH 663
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLqrdfGIAYLFISH 522
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
609-638 |
8.00e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.48 E-value: 8.00e-04
10 20 30
....*....|....*....|....*....|
gi 1313999337 609 LSGGEKQRMGMARMFYHKPKYALLDECTSA 638
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSA 170
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
479-641 |
8.80e-04 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 41.92 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 479 ICENVPIITPAGEVVAsrlnfkveegmhlLItGPNGCGKSSLFRILSG-LWPVYEGVLYKPPP----------QHMFYIP 547
Cdd:PRK11231 17 ILNDLSLSLPTGKITA-------------LI-GPNGCGKSTLLKCFARlLTPQSGTVFLGDKPismlssrqlaRRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 548 QRPYMSLG-SLRDQVIYPDS----------ADDmrekgytDQDLERILHSVHLYHIVQReggwdAVMDwkdvLSGGEKQR 616
Cdd:PRK11231 83 QHHLTPEGiTVRELVAYGRSpwlslwgrlsAED-------NARVNQAMEQTRINHLADR-----RLTD----LSGGQRQR 146
|
170 180
....*....|....*....|....*
gi 1313999337 617 MGMARMFYHKPKYALLDECTSAVSI 641
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
511-663 |
1.51e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.93 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 511 GPNGCGKSSLFRILSGLWPVYEG-VLYKPPP----------QHMFYIPQR-PYMSLGSLRDQVI---YPDSADDMREKGY 575
Cdd:PRK10575 44 GHNGSGKSTLLKMLGRHQPPSEGeILLDAQPleswsskafaRKVAYLPQQlPAAEGMTVRELVAigrYPWHGALGRFGAA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 576 TDQDLERILHSVHLYHIVQReggwdavmdWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSAVSI----DVEGKIFQAA 651
Cdd:PRK10575 124 DREKVEEAISLVGLKPLAHR---------LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIahqvDVLALVHRLS 194
|
170
....*....|..
gi 1313999337 652 IGAGISLLSITH 663
Cdd:PRK10575 195 QERGLTVIAVLH 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
609-663 |
1.92e-03 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 40.72 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1313999337 609 LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEG---KIFQAAIGAGISLLSITH 663
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGevlRIMQQLAEEGKTMVVVTH 210
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
493-666 |
2.00e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.66 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 493 VASRLNFKVEEGMHLLITGPNGCGKSSL----FR---ILSGLWpVYEGVLYKPPPQHMF-----YIPQRPYMSLGSLRDQ 560
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRmvdIFDGKI-VIDGIDISKLPLHTLrsrlsIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 561 ViypDSaddmrEKGYTDQDLERILHSVHLYHIVQR-EGGWDAVM-DWKDVLSGGEKQRMGMARMFYHKPKYALLDECTSA 638
Cdd:cd03288 115 L---DP-----ECKCTDDRLWEALEIAQLKNMVKSlPGGLDAVVtEGGENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190
....*....|....*....|....*....|.
gi 1313999337 639 VSIDVEG---KIFQAAIgAGISLLSITHRPS 666
Cdd:cd03288 187 IDMATENilqKVVMTAF-ADRTVVTIAHRVS 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
609-638 |
2.07e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 40.83 E-value: 2.07e-03
10 20 30
....*....|....*....|....*....|
gi 1313999337 609 LSGGEKQRMGMARMFYHKPKYALLDECTSA 638
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
495-652 |
2.28e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 495 SRLNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEG--VLYKpppQHMFYIPQRPYMSLGSLRDQVIYPDSADDMRe 572
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasVVIR---GTVAYVPQVSWIFNATVRDNILFGSPFDPER- 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 573 kgytdqdLERILHSVHLYHIVQREGGWDAV-MDWKDV-LSGGEKQRMGMARMFYHKPKYALLDECTSAVSIDVEGKIFQA 650
Cdd:PLN03130 710 -------YERAIDVTALQHDLDLLPGGDLTeIGERGVnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDK 782
|
..
gi 1313999337 651 AI 652
Cdd:PLN03130 783 CI 784
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
497-664 |
2.61e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSS----LFRILS----------------GLWPvyegvLYKpppqHMFYIPQRPYMSLGS 556
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSmlnaLFRIVElergrilidgcdiskfGLMD-----LRK----VLGIIPQAPVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 557 LRDQViypdsaDDMREkgYTDQDLERILHSVHLYHIVQREG-GWDA-VMDWKDVLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:PLN03130 1329 VRFNL------DPFNE--HNDADLWESLERAHLKDVIRRNSlGLDAeVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190
....*....|....*....|....*....|...
gi 1313999337 635 CTSAVSIDVEGKIfQAAIGA---GISLLSITHR 664
Cdd:PLN03130 1401 ATAAVDVRTDALI-QKTIREefkSCTMLIIAHR 1432
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
493-663 |
2.91e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.84 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 493 VASRLNFKVEEGMHLLITGPNGCGKS----SLFRILSGLWPVY---------EGVLYKPPPQ-------HMFYIPQRPYM 552
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYpsgdirfhgESLLHASEQTlrgvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 553 SLG---SLRDQVIYPDSAD-DMREKGYTDQDLeRILHSVHLYHIVQReggwdaVMDWKDVLSGGEKQRMGMARMFYHKPK 628
Cdd:PRK15134 104 SLNplhTLEKQLYEVLSLHrGMRREAARGEIL-NCLDRVGIRQAAKR------LTDYPHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1313999337 629 YALLDECTSAVSIDVEGKIFQ----AAIGAGISLLSITH 663
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQllreLQQELNMGLLFITH 215
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
495-533 |
3.05e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 3.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1313999337 495 SRLNFKVEEG-MHLLItGPNGCGKSSLFRILSGLWP--VYEG 533
Cdd:NF040905 18 DDVNLSVREGeIHALC-GENGAGKSTLMKVLSGVYPhgSYEG 58
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
497-536 |
3.50e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.21 E-value: 3.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1313999337 497 LNFKVEEGMHLLITGPNGCGKSSLFRILSGLWPVYEGVLY 536
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW 62
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
491-634 |
4.46e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.16 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1313999337 491 EVVASRLNFKVEEGMHLLITGPNGCGKSSLFRILSGlwpvyegvLYKPPPQHMFYIPQRPYMSLGSLRDQV--------I 562
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG--------LLNPEKGEILFERQSIKKDLCTYQKQLcfvghrsgI 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1313999337 563 YPDSAddMREKGYTD-------QDLERILHSVHLYHIVQREGGwdavmdwkdVLSGGEKQRMGMARMFYHKPKYALLDE 634
Cdd:PRK13540 86 NPYLT--LRENCLYDihfspgaVGITELCRLFSLEHLIDYPCG---------LLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
|
| |
