|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
326-906 |
1.84e-134 |
|
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: 420.31 E-value: 1.84e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 326 RVAAMFKVLVPTVFDKQGAQLLAVAFLVVSRTWISDRIASLNGTTVKYVLEQNKTAFIRLIGVSVLQSGASSFIAPSLRH 405
Cdd:TIGR00954 78 KLDFLLKILIPRVFCKETGLLILIAFLLVSRTYLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKY 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 406 LKARLALGWRIRLTQNLLKNYLRNNAFYQVFHMSSKNIDADQRITHDLEKLTTDLSGLVTGMVKPSVDILWFTWRMQLLT 485
Cdd:TIGR00954 158 LLKELKLRFRVRLTRYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSVVELYSNLTKPILDVILYSFKLLTAL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 486 GRRGVAILYAYMLLGLGFLRTVTPDFGDLTSREQQLEGTFRFMHERLRTHAESVAFFGGGAREKAMVDSRFKELFDHSLL 565
Cdd:TIGR00954 238 GSVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 566 LLKKKWLFDILDDFVTKQLPHNVTWFLSLLYALEHKGDRALVTTQGELAHAL----RFLASVVSqsflAFGDILELHRKF 641
Cdd:TIGR00954 318 IIKFRFSYGFLDNIVAKYTWSAVGLVAVSIPIFDKTHPAFLEMSEEELMQEFynngRLLLKAAD----ALGRLMLAGRDM 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 642 LELSGSINRIFELEELLDAAQSGD---------------LSTDNLLQSQRTALSAKDVISFSEVDIITPAQKLLARQLTC 706
Cdd:TIGR00954 394 TRLAGFTARVDTLLQVLDDVKSGNfkrprveeiesgregGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSF 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 707 DVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPshhfdeetASGGIFYVPQRPYTCLGTLRDQIIYPLSREEAE 786
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP--------AKGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMK 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 787 LRELKlygqgenavdatsilDARLKTILENVRLNYLLEReEGGWDANLNWEDILSLGEQQRLGMARLFFHKPKFGILDEC 866
Cdd:TIGR00954 546 RRGLS---------------DKDLEQILDNVQLTHILER-EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1776568118 867 TNATSVDVEEPLYRLAKDLGIT------RPALIPFHALELRLvDGE 906
Cdd:TIGR00954 610 TSAVSVDVEGYMYRLCREFGITlfsvshRKSLWKYHEYLLYM-DGR 654
|
|
| ABC_membrane_2 |
pfam06472 |
ABC transporter transmembrane region 2; This domain covers the transmembrane of a small family ... |
330-598 |
1.02e-88 |
|
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: 285.27 E-value: 1.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 330 MFKVLVPTVFDKQGAQLLAVAFLVVSRTWISDRIASLNGTTVKYVLEQNKTAFIRLIGVSVLQSGASSFIAPSLRHLKAR 409
Cdd:pfam06472 1 LLKILFPRWFSKEAGLLLALAALLVLRTFLSVLVAQLDGQIVKALVAKNGRGFIRLLLKWALLAVPASFVNSALKYLTQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 410 LALGWRIRLTQNLLKNYLRNNAFYQVFHMSSKNIDADQRITHDLEKLTTDLSGLVTGMVKPSVDILWFTWRMQLLTGRRG 489
Cdd:pfam06472 81 LALRFRTRLTRHLHDEYLKGRTYYKMSNLDGRIDNPDQRITQDVEKFCSSLSDLYSNLLKPILDIILFTFRLWRLSGWRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 490 VAILYAYMLLGLGFLRTVTPDFGDLTSREQQLEGTFRFMHERLRTHAESVAFFGGGAREKAMVDSRFKELFDHSLLLLKK 569
Cdd:pfam06472 161 PAILFLYVLLSAVILRRLSPPFGKLVAEEQKLEGEFRYLHSRLITNAEEIAFYRGEKREKKQLQRSFKSLIDHMRRILRR 240
|
250 260
....*....|....*....|....*....
gi 1776568118 570 KWLFDILDDFVTKQLPHNVTWFLSLLYAL 598
Cdd:pfam06472 241 RLWYGFIEDFVLKYTWSILGYVLVALPIF 269
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
31-239 |
1.21e-78 |
|
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: 254.00 E-value: 1.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGsdlnkEIFYVPQRPYT 110
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----DLLFLPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 111 AFGTLRDQLIYPltadqevepltcsgmvdllknvdldylldryppekevnWGDELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:cd03223 76 PLGTLREQLIYP--------------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1776568118 191 CTSAVTTDMEERFCAKVRAMGTSCITISHRPALVAFHDVVLSLDGEGGW 239
Cdd:cd03223 118 ATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGGW 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
346-907 |
7.96e-77 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 263.21 E-value: 7.96e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 346 LLAVAFLVVSRTWISDRIASLNGTTVKyVLEQ-NKTAFIRLIGVSVLQSGASSFIAPSLRHLKARLALGWRIRLTQNLLK 424
Cdd:COG4178 27 LALLLLLTLASVGLNVLLNFWNRDFYD-ALQArDAAAFWQQLGVFALLAAISILLAVYQTYLRQRLQIRWREWLTERLLD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 425 NYLRNNAFYQVfHMSSKNID-ADQRITHDLEKLTTDLSGLVTGMVKPSVD------ILW-------FTWRMQLLTGRRG- 489
Cdd:COG4178 106 RWLSNRAYYRL-QLSGGEIDnPDQRIAEDIRLFTETTLSLSLGLLSSVVTlisfigILWslsgsltFTLGGYSITIPGYm 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 490 VAILYAYMLLG--LGFLrtvtpdFG----DLTSREQQLEGTFRFMHERLRTHAESVAFFGGGAREKAMVDSRFKELFDhs 563
Cdd:COG4178 185 VWAALIYAIIGtlLTHL------IGrpliRLNFEQQRREADFRFALVRVRENAESIALYRGEAAERRRLRRRFDAVIA-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 564 llllkkkwlfdILDDFVTKQLphNVTWF------LSLLYALehkgdralvttqgeLAHALRFLAS-----VVSQSFLAFG 632
Cdd:COG4178 257 -----------NWRRLIRRQR--NLTFFttgygqLAVIFPI--------------LVAAPRYFAGeitlgGLMQAASAFG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 633 DILE-L------HRKFLELSGSINRIFELEELLDAAQSGDLSTDNLLQSQRTALSAKDVisfsevDIITPAQKLLARQLT 705
Cdd:COG4178 310 QVQGaLswfvdnYQSLAEWRATVDRLAGFEEALEAADALPEAASRIETSEDGALALEDL------TLRTPDGRPLLEDLS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 706 CDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHhfdeetasGGIFYVPQRPYTCLGTLRDQIIYPLsreea 785
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG--------ARVLFLPQRPYLPLGTLREALLYPA----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 786 elrelklygqgenavDATSILDARLKTILENVRLNYLLEReeggWDANLNWEDILSLGEQQRLGMARLFFHKPKFGILDE 865
Cdd:COG4178 451 ---------------TAEAFSDAELREALEAVGLGHLAER----LDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1776568118 866 CTNATSVDVEEPLYRLAKDL--GIT------RPALIPFHALELRLVDGEE 907
Cdd:COG4178 512 ATSALDEENEAALYQLLREElpGTTvisvghRSTLAAFHDRVLELTGDGS 561
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-240 |
4.29e-74 |
|
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: 258.14 E-value: 4.29e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 1 MLISKELSADDKKSSLQSAGSRNYLTEANYVEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGL 80
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 81 WPLVSGHIVKPGVGSdlnkeIFYVPQRPYTAFGTLRDQLIYPLTADQEVEP-LTCSGMVDLLKNVDLDYLLDRYPPEKEV 159
Cdd:TIGR00954 502 WPVYGGRLTKPAKGK-----LFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRgLSDKDLEQILDNVQLTHILEREGGWSAV 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 160 -NWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMGTSCITISHRPALVAFHDVVLSLDGEGG 238
Cdd:TIGR00954 577 qDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDGRGG 656
|
..
gi 1776568118 239 WK 240
Cdd:TIGR00954 657 YQ 658
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
9-242 |
2.13e-63 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 225.46 E-value: 2.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 9 ADDKKSSLQSAGSRNYLTEANYVEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI 88
Cdd:COG4178 341 ALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 89 VKPGvgsdlNKEIFYVPQRPYTAFGTLRDQLIYPLTA----DQEVEpltcsgmvDLLKNVDLDYLLDRYppEKEVNWGDE 164
Cdd:COG4178 421 ARPA-----GARVLFLPQRPYLPLGTLREALLYPATAeafsDAELR--------EALEAVGLGHLAERL--DEEADWDQV 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 165 LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDGEGGWKVH 242
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLELTGDGSWQLL 565
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
685-904 |
4.86e-54 |
|
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: 185.44 E-value: 4.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 685 ISFSEVDIITPAQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHhfdeetasGGIFYVPQR 764
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG--------EDLLFLPQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 765 PYTCLGTLRDQIIYPlsreeaelrelklygqgenavdatsildarlktilenvrlnyllereeggwdanlnWEDILSLGE 844
Cdd:cd03223 73 PYLPLGTLREQLIYP--------------------------------------------------------WDDVLSGGE 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776568118 845 QQRLGMARLFFHKPKFGILDECTNATSVDVEEPLYRLAKDLGIT------RPALIPFHALELRLVD 904
Cdd:cd03223 97 QQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITvisvghRPSLWKFHDRVLDLDG 162
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
31-235 |
5.13e-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: 105.54 E-value: 5.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLV-KDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV------GSDLNKEIFY 103
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 104 VPQRPYTAFGTLRDqliypltadqevepltcsgmvdllkNVdldylldryppekevnwgdeLSLGEQQRLGMARLFYHKP 183
Cdd:cd03228 81 VPQDPFLFSGTIRE-------------------------NI--------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1776568118 184 KFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDD 169
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
39-225 |
1.61e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 105.28 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 39 VTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYVPQRPYTAF 112
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkpLSAMPPPEWRRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 113 GTLRDQLIYPLTADQEvePLTCSGMVDLLKNVDLD-YLLDryppeKEVnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:COG4619 88 GTVRDNLPFPFQLRER--KFDRERALELLERLGLPpDILD-----KPV---ERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1776568118 192 TSAVTTDMEERFCAKVRAM----GTSCITISHRPALVA 225
Cdd:COG4619 158 TSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIE 195
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
31-235 |
3.91e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 111.39 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV------GSDLNKEIFYV 104
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 PQRPYTAFGTLRDQL-IYPLTADQEVepltcsgMVDLLKNVDLDYLLDRYP--PEKEVnwGDE---LSLGEQQRLGMARL 178
Cdd:COG4988 417 PQNPYLFAGTIRENLrLGRPDASDEE-------LEAALEAAGLDEFVAALPdgLDTPL--GEGgrgLSGGQAQRLALARA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 179 FYHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDD 546
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
31-235 |
1.54e-23 |
|
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: 99.97 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTP-TGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 103
Cdd:cd03245 3 IEFRNVSFSYPnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqldpADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 104 VPQRPYTAFGTLRDQLI--YPLTADQEV-EPLTCSGMVDLLKNVDLDYllDRYPPEKevnwGDELSLGEQQRLGMARLFY 180
Cdd:cd03245 83 VPQDVTLFYGTLRDNITlgAPLADDERIlRAAELAGVTDFVNKHPNGL--DLQIGER----GRGLSGGQRQAVALARALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 181 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLDLVDRIIVMDS 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
32-233 |
9.04e-22 |
|
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: 93.43 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 32 EFSGVKVVTP-TGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKeifyvpqrpyT 110
Cdd:cd03246 2 EVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA--DISQ----------W 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 111 AFGTLRDQLIYPLtadQEVEPLTCSgmvdLLKNVdldylldryppekevnwgdeLSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:cd03246 70 DPNELGDHVGYLP---QDDELFSGS----IAENI--------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1776568118 191 CTSAVTTDMEERFCAKVRAM---GTSCITISHRPALVAFHDVVLSL 233
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkaaGATRIVIAHRPETLASADRILVL 168
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
43-230 |
1.80e-21 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 93.70 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG-----VGSDLNKEIFYVPQRP--YTAFgTL 115
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdAREDYRRRLAYLGHADglKPEL-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 116 RDQL-----IYPLTADQEvepltcsGMVDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:COG4133 93 RENLrfwaaLYGLRADRE-------AIDEALEAVGLAGLADLPV--------RQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1776568118 191 CTSAVTTDMEERFCAKVRAM---GTSCITISHRPALVAFHDVV 230
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
31-236 |
3.77e-21 |
|
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: 92.94 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLV---KDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV----------GSDL 97
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 98 NKEIFYVPQRPYtafgtlrdqLIYPLTADQEVE-PLTCSGMV---------DLLKNVDLDYLLDRYPpekevnwgDELSL 167
Cdd:cd03255 81 RRHIGFVFQSFN---------LLPDLTALENVElPLLLAGVPkkerreraeELLERVGLGDRLNHYP--------SELSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776568118 168 GEQQRLGMARLFYHKPKFAILDECTSAVTTDMEER----FCAKVRAMGTSCITISHRPALVAFHDVVLSL-DGE 236
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEvmelLRELNKEAGTTIVVVTHDPELAEYADRIIELrDGK 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
47-193 |
5.92e-21 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 90.40 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYVPQRP-----YTAFGTL 115
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdLTDDERKSLRKEIGYVFQDPqlfprLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 116 RD----QLIYPLTADQEVEpltcsgmvDLLKNVDLDYLLDRYPPEKevnwGDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:pfam00005 81 RLglllKGLSKREKDARAE--------EALEKLGLGDLADRPVGER----PGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 1776568118 192 TS 193
Cdd:pfam00005 149 TA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
41-235 |
5.97e-21 |
|
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: 98.75 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 41 PTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---------VKPgvgSDLNKEIFYVPQRPYTA 111
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqIDP---ASLRRQIGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 112 FGTLRDQLIY--PLTADQEVepltcsgmVDLLKNVDLDYLLDRYP-------PEKevnwGDELSLGEQQRLGMARLFYHK 182
Cdd:COG2274 562 SGTIRENITLgdPDATDEEI--------IEAARLAGLHDFIEALPmgydtvvGEG----GSNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776568118 183 PKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDK 684
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
31-235 |
6.48e-21 |
|
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: 92.67 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV-GSDLNKE-----IFYV 104
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdIRDISRKslrsmIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 PQRPYTAFGTLRDQLIY-PLTADQEVEpltcsgmVDLLKNVDLDYLLDRYPP--EKEVN-WGDELSLGEQQRLGMARLFY 180
Cdd:cd03254 83 LQDTFLFSGTIMENIRLgRPNATDEEV-------IEAAKEAGAHDFIMKLPNgyDTVLGeNGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 181 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLSTIKNADKILVLDD 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-233 |
3.28e-20 |
|
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: 95.43 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYV 104
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadaDSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 PQRPYTAFGTLRD--QLIYPLTADQEVEpltcsgmvDLLKNVDLDYLLDRYPPEKEVNWGD---ELSLGEQQRLGMARLF 179
Cdd:TIGR02857 402 PQHPFLFAGTIAEniRLARPDASDAEIR--------EALERAGLDEFVAALPQGLDTPIGEggaGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1776568118 180 YHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSL 233
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
31-226 |
4.59e-20 |
|
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: 90.26 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGN---VLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI-VKPGVGSDLN-------- 98
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIiFDGKDLLKLSrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 99 KEIFYVPQRPYTAFG---TLRDQLIypltadqevEPLTCSGMVD-----------LLKNVDLD-YLLDRYPpekevnwgD 163
Cdd:cd03257 82 KEIQMVFQDPMSSLNprmTIGEQIA---------EPLRIHGKLSkkearkeavllLLVGVGLPeEVLNRYP--------H 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776568118 164 ELSLGEQQRLGMARLFYHKPKFAILDECTSA--VTT---------DMEERFcakvramGTSCITISHRPALVAF 226
Cdd:cd03257 145 ELSGGQRQRVAIARALALNPKLLIADEPTSAldVSVqaqildllkKLQEEL-------GLTLLFITHDLGVVAK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
32-234 |
1.30e-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: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 32 EFSGVKVVTPTGNVLvKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYVP 105
Cdd:cd00267 1 EIENLSFRYGGRTAL-DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlidgkdIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 106 QrpytafgtlrdqliypltadqevepltcsgmvdllknvdldylldryppekevnwgdeLSLGEQQRLGMARLFYHKPKF 185
Cdd:cd00267 80 Q----------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1776568118 186 AILDECTSAVTTDMEERFCAKVRAM---GTSCITISHRPALVAFH-DVVLSLD 234
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAaDRVIVLK 154
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
653-912 |
3.60e-19 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 92.51 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 653 ELEELLDAAQSGDLStdnllQSQRTALSAKDVISFSEVDIITPAQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLR 732
Cdd:COG4988 310 KIFALLDAPEPAAPA-----GTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 733 GLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPYTCLGTLRDQIiyplsreeaelrelKLYgqgenAVDATsilDAR 809
Cdd:COG4988 385 GFLPPYSGSILingVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL--------------RLG-----RPDAS---DEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 810 LKTILENVRLNYLLEREEGGWDANL-----NwediLSLGEQQRLGMARLFFHKPKFGILDECTnaTSVDVE------EPL 878
Cdd:COG4988 443 LEAALEAAGLDEFVAALPDGLDTPLgeggrG----LSGGQAQRLALARALLRDAPLLLLDEPT--AHLDAEteaeilQAL 516
|
250 260 270
....*....|....*....|....*....|....*...
gi 1776568118 879 YRLAKD---LGIT-RPALIPFHALELRLVDGEEPECGA 912
Cdd:COG4988 517 RRLAKGrtvILIThRLALLAQADRILVLDDGRIVEQGT 554
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
43-236 |
4.32e-19 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 86.82 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEIFYVPQRpytaFGTLRDqliY 121
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlEKERKRIGYVPQR----RSIDRD---F 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 122 PLTadqeVEPLTCSGMV------------------DLLKNVDLDYLLDRyppekevNWGdELSLGEQQRLGMARLFYHKP 183
Cdd:cd03235 84 PIS----VRDVVLMGLYghkglfrrlskadkakvdEALERVGLSELADR-------QIG-ELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 184 KFAILDECTSAVTTDMEERF---CAKVRAMGTSCITISHRPALV-AFHDVVLSLDGE 236
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIyelLRELRREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
31-225 |
5.08e-19 |
|
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: 91.89 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNV-LVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWP---LVSGHIVKPGV------GSDLNKE 100
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRdllelsEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 101 IFYVPQRPYTAFGtlrdqliyPLT-ADQEVEPLTCSGM---------VDLLKNVDLDYLLDRYPpekevnwgDELSLGEQ 170
Cdd:COG1123 85 IGMVFQDPMTQLN--------PVTvGDQIAEALENLGLsraeararvLELLEAVGLERRLDRYP--------HQLSGGQR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 171 QRLGMARLFYHKPKFAILDECTSA--VTTDME--ERFCAKVRAMGTSCITISHRPALVA 225
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTAldVTTQAEilDLLRELQRERGTTVLLITHDLGVVA 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
43-225 |
1.18e-18 |
|
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: 85.39 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---KPGVGSDLNKEIFYVPQRPYTAFG--TLRD 117
Cdd:cd03226 12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngKPIKAKERRKSIGYVMQDVDYQLFtdSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 118 QLIY--PLTAD--QEVEpltcsgmvDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:cd03226 92 ELLLglKELDAgnEQAE--------TVLKDLDLYALKERHP--------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1776568118 194 AVTTDMEERFCAKVR---AMGTSCITISHRPALVA 225
Cdd:cd03226 156 GLDYKNMERVGELIRelaAQGKAVIVITHDYEFLA 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
32-225 |
1.51e-18 |
|
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: 85.21 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 32 EFSGVKVVTPTGNVLV-KDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYV 104
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 PQRPytafgtlRDQLIYPlTADQEV----EPLTCSG------MVDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLG 174
Cdd:cd03225 81 FQNP-------DDQFFGP-TVEEEVafglENLGLPEeeieerVEEALELVGLEGLRDRSP--------FTLSGGQKQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776568118 175 MARLFYHKPKFAILDECTSAV----TTDMEERFcAKVRAMGTSCITISHRPALVA 225
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLdpagRRELLELL-KKLKAEGKTIIIVTHDLDLLL 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
31-230 |
3.06e-17 |
|
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: 86.11 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVV----TPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---------VKPGVGSDL 97
Cdd:COG1123 261 LEVRNLSKRypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 98 NKEIFYVPQRPYTAF---GTLRDQLIYPLTADQEVEPLTCSGMV-DLLKNVDLDY-LLDRYPpekevnwgDELSLGEQQR 172
Cdd:COG1123 341 RRRVQMVFQDPYSSLnprMTVGDIIAEPLRLHGLLSRAERRERVaELLERVGLPPdLADRYP--------HELSGGQRQR 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776568118 173 LGMARLFYHKPKFAILDECTSA----VTTDMEERFCAKVRAMGTSCITISHRPALVAF--HDVV 230
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSAldvsVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiaDRVA 476
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
31-225 |
5.68e-17 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 81.22 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYV 104
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkdITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 PQRPytafgtlRDQLIYPlTADQEVE-PLTCSGM--------VD-LLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLG 174
Cdd:COG1122 81 FQNP-------DDQLFAP-TVEEDVAfGPENLGLpreeirerVEeALELVGLEHLADRPP--------HELSGGQKQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776568118 175 MARLFYHKPKFAILDECTSAV----TTDMEERFcAKVRAMGTSCITISHRPALVA 225
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLdprgRRELLELL-KRLNKEGKTVIIVTHDLDLVA 198
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
43-225 |
1.88e-16 |
|
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: 78.25 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYVPQrpytafgtlr 116
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdLASLSPKELARKIAYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 117 dqliypltadqevepltcsgmvdLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVt 196
Cdd:cd03214 81 -----------------------ALELLGLAHLADRPF--------NELSGGERQRVLLARALAQEPPILLLDEPTSHL- 128
|
170 180 190
....*....|....*....|....*....|....*
gi 1776568118 197 tDME------ERFCAKVRAMGTSCITISHRPALVA 225
Cdd:cd03214 129 -DIAhqiellELLRRLARERGKTVVMVLHDLNLAA 162
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
31-235 |
1.06e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.40 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVkpgV-GSDLNKeifyVPQR-- 107
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL---VnGQDLSR----LKRRei 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 108 PYtafgtLR--------D-QLIYPLTADQEVE-PLTCSGM---------VDLLKNVDLDYLLDRYPPEkevnwgdeLSLG 168
Cdd:COG2884 75 PY-----LRrrigvvfqDfRLLPDRTVYENVAlPLRVTGKsrkeirrrvREVLDLVGLSDKAKALPHE--------LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776568118 169 EQQRLGMARLFYHKPKFAILDECTSAVTTDMEER----FcAKVRAMGTSCITISHRPALV-AFHDVVLSLDG 235
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEimelL-EEINRRGTTVLIATHDLELVdRMPKRVLELED 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
43-194 |
1.52e-15 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 77.39 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---KPgVGS----DLNKEIFYVPQRPYTAFG-T 114
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRD-LASlsrrELARRIAYVPQEPPAPFGlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 115 LRD----------QLIYPLTAD--QEVEpltcsgmvDLLKNVDLDYLLDRYppekeVnwgDELSLGEQQRLGMARLFYHK 182
Cdd:COG1120 92 VRElvalgryphlGLFGRPSAEdrEAVE--------EALERTGLEHLADRP-----V---DELSGGERQRVLIARALAQE 155
|
170
....*....|..
gi 1776568118 183 PKFAILDECTSA 194
Cdd:COG1120 156 PPLLLLDEPTSH 167
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
31-235 |
1.55e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 80.98 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---------VKPgvgSDLNKEI 101
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdLTL---ESLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 102 FYVPQRPYTAFGTLRDQLIY--PLTADQEVEpltcsgmvDLLKNVDLDYLLDRYPP-------EKevnwGDELSLGEQQR 172
Cdd:COG1132 417 GVVPQDTFLFSGTIRENIRYgrPDATDEEVE--------EAAKAAQAHEFIEALPDgydtvvgER----GVNLSGGQRQR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 173 LGMARLFYHKPKFAILDECTSAVTTDMEerfcAKV-RAM-----GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETE----ALIqEALerlmkGRTTIVIAHRLSTIRNADRILVLDD 549
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
42-235 |
1.89e-15 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 75.97 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 42 TGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVkpgvgsdLNKEIFYVPQRPYTAFGTLRDQLIY 121
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-------VPGSIAYVSQEPWIQNGTIRENILF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 122 PLTADQE-----VEplTCSgmvdLLKnvDLDYLLDryppekevnwGDE---------LSLGEQQRLGMARLFYHKPKFAI 187
Cdd:cd03250 89 GKPFDEEryekvIK--ACA----LEP--DLEILPD----------GDLteigekginLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1776568118 188 LDECTSAVTTDMEERFCAKV----RAMGTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFENCilglLLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
43-195 |
2.35e-15 |
|
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: 76.82 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSD-----LNKEIFYVPQRPY-TAFGTLR 116
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkepreARRQIGVLPDERGlYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 117 DQL-----IYPLTaDQEVEPLTcsgmVDLLKNVDLDYLLDRyppekevNWGdELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:COG4555 93 ENIryfaeLYGLF-DEELKKRI----EELIELLGLEEFLDR-------RVG-ELSTGMKKKVALARALVHDPKVLLLDEP 159
|
....
gi 1776568118 192 TSAV 195
Cdd:COG4555 160 TNGL 163
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
31-220 |
3.19e-15 |
|
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: 76.42 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPT--GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLN-----KEIF 102
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDiRDLNlrwlrSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 103 YVPQRPYTAFGTLRDQLIY---PLTADQEVEPLTCSGMVDLLKNvdldyLLDRYppEKEV-NWGDELSLGEQQRLGMARL 178
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYgkpDATDEEVEEAAKKANIHDFIMS-----LPDGY--DTLVgERGSQLSGGQKQRIAIARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1776568118 179 FYHKPKFAILDECTSAVTTDMEERFCAKV-RAM-GTSCITISHR 220
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALdRAMkGRTTIVIAHR 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
43-231 |
4.11e-15 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 76.28 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDL-NKEIFYVPQR-------PYTAF-- 112
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRaRRRIGYVPQRaevdwdfPITVRdv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 113 ---GTLRDQ-LIYPLTAD--QEVEpltcsgmvDLLKNVDLDYLLDRYppekeVNwgdELSLGEQQRLGMARLFYHKPKFA 186
Cdd:COG1121 98 vlmGRYGRRgLFRRPSRAdrEAVD--------EALERVGLEDLADRP-----IG---ELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1776568118 187 ILDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPALVA--FHDVVL 231
Cdd:COG1121 162 LLDEPFAGVDAATEEALYEllrELRREGKTILVVTHDLGAVReyFDRVLL 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
716-868 |
4.25e-15 |
|
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: 73.45 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 716 VTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQrpYTCLG---TLRDQIIYPLsreeaELRE 789
Cdd:pfam00005 16 LVGPNGAGKSTLLKLIAGLLSPTEGTILldgQDLTDDERKSLRKEIGYVFQ--DPQLFprlTVRENLRLGL-----LLKG 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 790 LKlygqgenavdaTSILDARLKTILENVRLNYLLEREEGGWDANLnwedilSLGEQQRLGMARLFFHKPKFGILDECTN 868
Cdd:pfam00005 89 LS-----------KREKDARAEEALEKLGLGDLADRPVGERPGTL------SGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
31-234 |
9.06e-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: 74.45 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKV-VTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 103
Cdd:cd03244 3 IEFKNVSLrYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 104 VPQRPYTAFGTLRDQL-IYPLTADQEV-EPLTCSGMVDLLKNvdLDYLLDryppEKEVNWGDELSLGEQQRLGMARLFYH 181
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdPFGEYSDEELwQALERVGLKEFVES--LPGGLD----TVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776568118 182 KPKFAILDECTSAVTTDMEERFCAKVRAMGTSC--ITISHRPALVAFHDVVLSLD 234
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCtvLTIAHRLDTIIDSDRILVLD 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
693-888 |
1.00e-14 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 74.08 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 693 ITPAQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYkpshhFDEETASGG--------IFYVPQR 764
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY-----LDGKPLSAMpppewrrqVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 765 PYTCLGTLRDQIIYPLSreeaeLRELKLygqgenavdatsiLDARLKTILENVRLNyllereeggwDANLNWE-DILSLG 843
Cdd:COG4619 83 PALWGGTVRDNLPFPFQ-----LRERKF-------------DRERALELLERLGLP----------PDILDKPvERLSGG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1776568118 844 EQQRLGMARLFFHKPKFGILDECTNA----TSVDVEEPLYRLAKDLGIT 888
Cdd:COG4619 135 ERQRLALIRALLLQPDVLLLDEPTSAldpeNTRRVEELLREYLAEEGRA 183
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
31-235 |
2.81e-14 |
|
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: 73.67 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKV-VTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 103
Cdd:cd03252 1 ITFEHVRFrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlaladpAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 104 VPQRPYTAFGTLRDQLIYPLTA---DQEVEPLTCSGMVDLLKNVDLDYllDRYPPEKevnwGDELSLGEQQRLGMARLFY 180
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGmsmERVIEAAKLAGAHDFISELPEGY--DTIVGEQ----GAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 181 HKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEK 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-231 |
6.38e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.30 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 11 DKKSSLQSAGSRNYLTEANYVEFSGVKVVTPT-GNVLV-KDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI 88
Cdd:TIGR00958 459 DRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNrPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 89 V---KPGVGSD---LNKEIFYVPQRPYTAFGTLRDQLIYPLTADQEVEPLTCSGMV---DLLKNVDLDYllDRYPPEKev 159
Cdd:TIGR00958 539 LldgVPLVQYDhhyLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAAnahDFIMEFPNGY--DTEVGEK-- 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776568118 160 nwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMGTSCITISHRPALV--AFHDVVL 231
Cdd:TIGR00958 615 --GSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVerADQILVL 686
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
26-190 |
6.92e-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: 72.81 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 26 TEANYVEFSGVKVV--TPTGNVLV-KDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEI 101
Cdd:COG1116 3 AAAPALELRGVSKRfpTGGGGVTAlDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 102 FYVPQRPytafgTLrdqliYP-LTADQEVE-PLTCSGM---------VDLLKNVDLDYLLDRYPpekevnwgDELSLGEQ 170
Cdd:COG1116 83 GVVFQEP-----AL-----LPwLTVLDNVAlGLELRGVpkaerreraRELLELVGLAGFEDAYP--------HQLSGGMR 144
|
170 180
....*....|....*....|
gi 1776568118 171 QRLGMARLFYHKPKFAILDE 190
Cdd:COG1116 145 QRVAIARALANDPEVLLMDE 164
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
31-234 |
9.04e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 71.88 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYV 104
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDirevtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 PQRPYTAFGTLRDQLIY--PLTADQEVEpltcsgmvDLLKNVDLDYLLDRYPPEKEVNWGD---ELSLGEQQRLGMARLF 179
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYgrPDATDEEVI--------EAAKAAQIHDKIMRFPDGYDTIVGErglKLSGGEKQRVAIARAI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 180 YHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLSTIVNADKIIVLK 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
43-209 |
1.92e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNK---EIFYV-PQRPYTAFGTLRDQ 118
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeACHYLgHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 119 LIYPltadQEVEPLTCSGMVDLLKNVDLDYLLDRypPEKevnwgdELSLGEQQRLGMARLF-YHKPKFaILDECTSAVTT 197
Cdd:PRK13539 94 LEFW----AAFLGGEELDIAAALEAVGLAPLAHL--PFG------YLSAGQKRRVALARLLvSNRPIW-ILDEPTAALDA 160
|
170
....*....|..
gi 1776568118 198 DMEERFCAKVRA 209
Cdd:PRK13539 161 AAVALFAELIRA 172
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-202 |
2.45e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 70.30 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLvKDLFLRVESG-SNLLitGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV-----GSDLNKEIFYV 104
Cdd:cd03264 1 LQLENLTKRYGKKRAL-DGVSLTLGPGmYGLL--GPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 PQ--RPYTAFgTLRDQLIYpLTADQEVEPLTCSGMVD-LLKNVDldyLLDRYppEKEVNwgdELSLGEQQRLGMARLFYH 181
Cdd:cd03264 78 PQefGVYPNF-TVREFLDY-IAWLKGIPSKEVKARVDeVLELVN---LGDRA--KKKIG---SLSGGMRRRVGIAQALVG 147
|
170 180
....*....|....*....|.
gi 1776568118 182 KPKFAILDECTsaVTTDMEER 202
Cdd:cd03264 148 DPSILIVDEPT--AGLDPEER 166
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
30-221 |
2.60e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 73.93 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 30 YVEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV------GSDLNKEIFY 103
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVpvssldQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 104 VPQRPYTAFGTLRDQLIY--PLTADQEVEpltcsgmvDLLKNVDLDYLLDRYPPEKEVNWGDE---LSLGEQQRLGMARL 178
Cdd:TIGR02868 414 CAQDAHLFDTTVRENLRLarPDATDEELW--------AALERVGLADWLRALPDGLDTVLGEGgarLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1776568118 179 FYHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRP 221
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
31-235 |
2.66e-13 |
|
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: 70.58 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPT---GNVLvKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---KPGVGSD---LNKEI 101
Cdd:cd03248 12 VKFQNVTFAYPTrpdTLVL-QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQYEhkyLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 102 FYVPQRPYTAFGTLRDQLIYPLTA---DQEVEPLTCSGMVDLLKNVDLDYLLDryPPEKevnwGDELSLGEQQRLGMARL 178
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYGLQScsfECVKEAAQKAHAHSFISELASGYDTE--VGEK----GSQLSGGQKQRVAIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 179 FYHKPKFAILDECTSAVTTDMEERFCAKVRA--MGTSCITISHRPALVAFHDVVLSLDG 235
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQILVLDG 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
718-875 |
4.72e-13 |
|
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: 69.56 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPYTCLGTLRDQIIY--PLSREEAELRELKL 792
Cdd:cd03254 36 GPTGAGKTTLINLLMRFYDPQKGQILidgIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLgrPNATDEEVIEAAKE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 793 ygqgenavdatsildarlktilenVRLNYLLEREEGGWDANLNWE-DILSLGEQQRLGMARLFFHKPKFGILDECTnaTS 871
Cdd:cd03254 116 ------------------------AGAHDFIMKLPNGYDTVLGENgGNLSQGERQLLAIARAMLRDPKILILDEAT--SN 169
|
....
gi 1776568118 872 VDVE 875
Cdd:cd03254 170 IDTE 173
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
43-221 |
4.73e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 69.06 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSD-----LNKEIFYVPQRP--YTAFGTL 115
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfqrdsIARGLLYLGHAPgiKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 116 RD-QLIYPLTADQEVEpltcsgmvDLLKNVDLDYLLDRyppekEVNwgdELSLGEQQRLGMARLFYHKPKFAILDECTSA 194
Cdd:cd03231 92 ENlRFWHADHSDEQVE--------EALARVGLNGFEDR-----PVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|
gi 1776568118 195 VTTDMEERFCAKVR---AMGTSCITISHRP 221
Cdd:cd03231 156 LDKAGVARFAEAMAghcARGGMVVLTTHQD 185
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
44-220 |
4.77e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 72.94 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 44 NVLvKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYVPQRPYTAFGTLRD 117
Cdd:PRK11160 354 PVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadyseAALRQAISVVSQRVHLFSATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 118 QLIY--PLTADQEvepltcsgMVDLLKNVDLDYLLDRYPPEKevNW----GDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:PRK11160 433 NLLLaaPNASDEA--------LIEVLQQVGLEKLLEDDKGLN--AWlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
170 180 190
....*....|....*....|....*....|.
gi 1776568118 192 TSAVTTDMEERFCAKVR--AMGTSCITISHR 220
Cdd:PRK11160 503 TEGLDAETERQILELLAehAQNKTVLMITHR 533
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
43-222 |
6.96e-13 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 68.70 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlnKEIFYVP--QRP-------YTAFG 113
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG------RDVTGVPpeRRNigmvfqdYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 --TLRDQLIYPLTaDQEVEPLTCSGMVD-LLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:cd03259 86 hlTVAENIAFGLK-LRGVPKAEIRARVReLLELVGLEGLLNRYP--------HELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1776568118 191 CTSAVTTDMEERFCAKVRAM----GTSCITISHRPA 222
Cdd:cd03259 157 PLSALDAKLREELREELKELqrelGITTIYVTHDQE 192
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
344-875 |
7.39e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.50 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 344 AQLLAVAFLVVSRTWISDRIASLNGTTVKYVLeqnktafIRLIGVSVLQSGASsfiapslrhlkaRLALGWRIRLTQNLL 423
Cdd:COG1132 33 SALLELLLPLLLGRIIDALLAGGDLSALLLLL-------LLLLGLALLRALLS------------YLQRYLLARLAQRVV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 424 KNyLRNNAFYQVFHMSSKNIDADQ------RITHDLEKLTTDLSGLVTGMVKPSVDI-------LWFTWRMQLLTgrrgV 490
Cdd:COG1132 94 AD-LRRDLFEHLLRLPLSFFDRRRtgdllsRLTNDVDAVEQFLAHGLPQLVRSVVTLigalvvlFVIDWRLALIV----L 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 491 AILYAYMLLGLGFLRTVTPDFGDLTSREQQLegtFRFMHERLRTHAESVAFfGGGAREKAMVDSRFKELFDHSLLLLKKK 570
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAEL---NGRLQESLSGIRVVKAF-GREERELERFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 571 WLFDILDDFVTkqlphNVTWFLSLLYAlehkGDRAL--VTTQGELAhALRFLASVVSQSFLAFGDILELhrkFLELSGSI 648
Cdd:COG1132 245 ALFFPLMELLG-----NLGLALVLLVG----GLLVLsgSLTVGDLV-AFILYLLRLFGPLRQLANVLNQ---LQRALASA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 649 NRIFEL----EELLDAAQSGDLSTDnllqsqRTALSAKDViSFSevdiITPAQKLLaRQLTCDVVPEKSLLVTGPNGSGK 724
Cdd:COG1132 312 ERIFELldepPEIPDPPGAVPLPPV------RGEIEFENV-SFS----YPGDRPVL-KDISLTIPPGETVALVGPSGSGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 725 SSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPYtcL--GTLRDQIiyplsreeaelrelkLYGQGena 799
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILidgVDIRDLTLESLRRQIGVVPQDTF--LfsGTIRENI---------------RYGRP--- 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776568118 800 vDATsilDARLKTILENVRLNYLLEREEGGWDANLNwED--ILSLGEQQRLGMARLFFHKPKFGILDECTNAtsVDVE 875
Cdd:COG1132 440 -DAT---DEEVEEAAKAAQAHEFIEALPDGYDTVVG-ERgvNLSGGQRQRIAIARALLKDPPILILDEATSA--LDTE 510
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
47-219 |
7.44e-13 |
|
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: 67.81 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV-----GSDLNKEIFYVPQRPYtafgtlrdqlIY 121
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkePEEVKRRIGYLPEEPS----------LY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 122 P-LTAdqevepltcsgmvdllknvdLDYLldryppekevnwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVttDME 200
Cdd:cd03230 86 EnLTV--------------------RENL--------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL--DPE 129
|
170 180
....*....|....*....|....
gi 1776568118 201 ER-----FCAKVRAMGTSCITISH 219
Cdd:cd03230 130 SRrefweLLRELKKEGKTILLSSH 153
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
31-190 |
7.88e-13 |
|
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: 68.65 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVK---DLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---KPGVGSdlNKEIFYV 104
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgEPVTGP--GPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 PQRPY----------TAFGtLRDQLIYPLTADQEVEpltcsgmvDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLG 174
Cdd:cd03293 79 FQQDAllpwltvldnVALG-LELQGVPKAEARERAE--------ELLELVGLSGFENAYP--------HQLSGGMRQRVA 141
|
170
....*....|....*.
gi 1776568118 175 MARLFYHKPKFAILDE 190
Cdd:cd03293 142 LARALAVDPDVLLLDE 157
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
43-233 |
8.20e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.03 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlNKEIFYVPQRpytafGTLRDQLiyP 122
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----GARVAYVPQR-----SEVPDSL--P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 123 LTADQEVE-----------PLTCSG---MVDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:NF040873 72 LTVRDLVAmgrwarrglwrRLTRDDraaVDDALERVGLADLAGRQL--------GELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1776568118 189 DECTSAVTTDMEERFCAKVR---AMGTSCITISHRPALVAFHDVVLSL 233
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAeehARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
43-219 |
1.13e-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: 68.90 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKE---IFYVPQRPY--------- 109
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDiTNLPPEkrdISYVPQNYAlfphmtvyk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 110 -TAFGtLRDQLIYPLTADQEVEpltcsgmvDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:cd03299 91 nIAYG-LKKRKVDKKEIERKVL--------EIAEMLGIDHLLNRKP--------ETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1776568118 189 DECTSAVTTDMEERFCAKV----RAMGTSCITISH 219
Cdd:cd03299 154 DEPFSALDVRTKEKLREELkkirKEFGVTVLHVTH 188
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
641-867 |
1.56e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.39 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 641 FLELSGSINRIFELEELLDAAQSGDLSTDNLLQSQRTALSAKDViSFSEVDIITPAQKllarQLTCDVVPEKSLLVTGPN 720
Cdd:PRK11160 301 FQHLGQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNV-SFTYPDQPQPVLK----GLSLQIKAGEKVALLGRT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 721 GSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPYTCLGTLRDQiiyplsreeaelreLKLygqge 797
Cdd:PRK11160 376 GCGKSTLLQLLTRAWDPQQGEILlngQPIADYSEAALRQAISVVSQRVHLFSATLRDN--------------LLL----- 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 798 NAVDATsilDARLKTILENVRLNYLLEREEGgwdanLN-WedI------LSLGEQQRLGMARLFFHKPKFGILDECT 867
Cdd:PRK11160 437 AAPNAS---DEALIEVLQQVGLEKLLEDDKG-----LNaW--LgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
43-209 |
1.58e-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: 67.38 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG-----VGSDLNKEIFYVPQRP-----YTAF 112
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeQRDEPHENILYLGHLPglkpeLSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 113 GTLRDqliypLTADQEVEPLTCSgmvDLLKNVDLDYLLDRypPEKevnwgdELSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:TIGR01189 92 ENLHF-----WAAIHGGAQRTIE---DALAAVGLTGFEDL--PAA------QLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170
....*....|....*..
gi 1776568118 193 SAVTTDMEERFCAKVRA 209
Cdd:TIGR01189 156 TALDKAGVALLAGLLRA 172
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
31-193 |
1.71e-12 |
|
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: 68.57 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTpTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGG-LWPLVSGHIV----KPGVGS--DLNKEIFY 103
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRlfgeRRGGEDvwELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 104 V-P--QRPYTAFGTLRDQLI----------YPLTADQEVEpltcsgMVDLLKNVDLDYLLDRYppekevnWGdELSLGEQ 170
Cdd:COG1119 83 VsPalQLRFPRDETVLDVVLsgffdsiglyREPTDEQRER------ARELLELLGLAHLADRP-------FG-TLSQGEQ 148
|
170 180
....*....|....*....|...
gi 1776568118 171 QRLGMARLFYHKPKFAILDECTS 193
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTA 171
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
46-243 |
2.22e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 46 LVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLwplvsgHIVKPGVGSdlnkeiFYVPQRPYTAFGTLRDQLIYPLTA 125
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA------LKGTPVAGC------VDVPDNQFGREASLIDAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 126 DQEVEPLTCSGMVDLlknvdldYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCA 205
Cdd:COG2401 113 KDAVELLNAVGLSDA-------VLWLRRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1776568118 206 KV----RAMGTSCITISHRPALVAF--HDVVLSLDGEGGWKVHY 243
Cdd:COG2401 178 NLqklaRRAGITLVVATHHYDVIDDlqPDLLIFVGYGGVPEEKR 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
47-195 |
2.28e-12 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 67.78 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSnllIT---GPNGSGKSSLFRVLGGLWPLVSGHIVkpgV-GSDLNKE-------IFYVPQRP--YTAFg 113
Cdd:COG1131 16 LDGVSLTVEPGE---IFgllGPNGAGKTTTIRMLLGLLRPTSGEVR---VlGEDVARDpaevrrrIGYVPQEPalYPDL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 TLRDQL-----IYPL---TADQEVEpltcsgmvDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKF 185
Cdd:COG1131 89 TVRENLrffarLYGLprkEARERID--------ELLELFGLTDAADRKV--------GTLSGGMKQRLGLALALLHDPEL 152
|
170
....*....|
gi 1776568118 186 AILDECTSAV 195
Cdd:COG1131 153 LILDEPTSGL 162
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
672-901 |
3.18e-12 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 70.39 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 672 LQSQRTALSAKD-VISFSEVDIITPAQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSH 747
Cdd:TIGR02857 308 LAGKAPVTAAPAsSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 748 HFDEETASGGIFYVPQRPYTCLGTLRDQIIypLSREEAElrelklygqgenavdatsilDARLKTILENVRLNYLLEREE 827
Cdd:TIGR02857 388 DADADSWRDQIAWVPQHPFLFAGTIAENIR--LARPDAS--------------------DAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 828 GGWDANLNwED--ILSLGEQQRLGMARLFFHKPKFGILDECT----NATSVDVEEPLYRLAKdlgiTRPALIPFHALELR 901
Cdd:TIGR02857 446 QGLDTPIG-EGgaGLSGGQAQRLALARAFLRDAPLLLLDEPTahldAETEAEVLEALRALAQ----GRTVLLVTHRLALA 520
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
47-201 |
3.53e-12 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 67.21 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSG------------HIVKPGVG-SDLNKEIFYVPQRPYTAFG 113
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegevlldgkDIYDLDVDvLELRRRVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 TLRDQLIYPLTA---------DQEVEpltcsgmvDLLKNVDL-DYLLDRYPpekevnwGDELSLGEQQRLGMARLFYHKP 183
Cdd:cd03260 96 SIYDNVAYGLRLhgiklkeelDERVE--------EALRKAALwDEVKDRLH-------ALGLSGGQQQRLCLARALANEP 160
|
170 180
....*....|....*....|..
gi 1776568118 184 KFAILDECTSAV----TTDMEE 201
Cdd:cd03260 161 EVLLLDEPTSALdpisTAKIEE 182
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
31-220 |
3.95e-12 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 67.26 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKV-VTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 103
Cdd:cd03251 1 VEFKNVTFrYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrdytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 104 VPQRPYTAFGTLRDQLIY--PLTADQEVEpltcsgmvDLLKNVDLDYLLDRYPPEKEVNWGD---ELSLGEQQRLGMARL 178
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYgrPGATREEVE--------EAARAANAHEFIMELPEGYDTVIGErgvKLSGGQRQRIAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1776568118 179 FYHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHR 220
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAHR 196
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
47-234 |
8.81e-12 |
|
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: 65.51 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYVPQRPYTAFGTLRDQL- 119
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistiplEDLRSSLTIIPQDPTLFSGTIRSNLd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 120 IYPLTADQEV-EPLTCSGMvdllknvdldylldryppekevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTD 198
Cdd:cd03369 104 PFDEYSDEEIyGALRVSEG------------------------GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1776568118 199 MEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:cd03369 160 TDALIQKTIREEftNSTILTIAHRLRTIIDYDKILVMD 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
56-221 |
9.86e-12 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 65.39 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 56 SGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG-VGSDLNKEIFYVPQR--------PYTAFG--TLRDQLIYPLT 124
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtVLFDSRKKINLPPQQrkiglvfqQYALFPhlNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 125 ADQEVEPLTC-SGMVDLLknvDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERF 203
Cdd:cd03297 102 RKRNREDRISvDELLDLL---GLDHLLNRYP--------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180
....*....|....*....|..
gi 1776568118 204 CAKVRAMGTS----CITISHRP 221
Cdd:cd03297 171 LPELKQIKKNlnipVIFVTHDL 192
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
31-227 |
1.50e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 65.12 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDL-NKEIFYVPQRP 108
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvSDLrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 109 YTAFGTLRdqLIYPLTADQEVE-PLTCSG---------MVDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARL 178
Cdd:cd03292 81 GVVFQDFR--LLPDRNVYENVAfALEVTGvppreirkrVPAALELVGLSHKHRALP--------AELSGGEQQRVAIARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1776568118 179 FYHKPKFAILDECTSAVTTDMEERFC---AKVRAMGTSCITISHRPALVAFH 227
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMnllKKINKAGTTVVVATHAKELVDTT 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
712-884 |
2.38e-11 |
|
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: 63.17 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 712 KSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPYtclgtlrdqiiyplsreeaelr 788
Cdd:cd03228 29 EKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgVDLRDLDLESLRKNIAYVPQDPF---------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 789 elklygqgenavdatsILDArlkTILENvrlnyllereeggwdanlnwedILSLGEQQRLGMARLFFHKPKFGILDECT- 867
Cdd:cd03228 87 ----------------LFSG---TIREN----------------------ILSGGQRQRIAIARALLRDPPILILDEATs 125
|
170 180
....*....|....*....|
gi 1776568118 868 ---NATSVDVEEPLYRLAKD 884
Cdd:cd03228 126 aldPETEALILEALRALAKG 145
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
609-869 |
2.94e-11 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 67.55 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 609 TQGELAhALRFLASVVSQSFLAFGDILElhrKFLELSGSINRIFELEELLDAAQSGDLSTDnlLQSQRTALSAKDViSFS 688
Cdd:COG2274 410 TLGQLI-AFNILSGRFLAPVAQLIGLLQ---RFQDAKIALERLDDILDLPPEREEGRSKLS--LPRLKGDIELENV-SFR 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 689 evdiITPAQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRP 765
Cdd:COG2274 483 ----YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgIDLRQIDPASLRRQIGVVLQDV 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 766 YTCLGTLRDQIIypLSREEAELRELklygqgENAVDATSILD------ARLKTILEnvrlnyllereEGGwdANLnwedi 839
Cdd:COG2274 559 FLFSGTIRENIT--LGDPDATDEEI------IEAARLAGLHDfiealpMGYDTVVG-----------EGG--SNL----- 612
|
250 260 270
....*....|....*....|....*....|
gi 1776568118 840 lSLGEQQRLGMARLFFHKPKFGILDECTNA 869
Cdd:COG2274 613 -SGGQRQRLAIARALLRNPRILILDEATSA 641
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
646-867 |
4.17e-11 |
|
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: 66.62 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 646 GSINRIFELEELLDAAQSGDLSTDNLLQSQRTALSAKDViSFSEvdiitPAQKLLARQLTCDVVPEKSLLVTGPNGSGKS 725
Cdd:TIGR02868 302 AAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDL-SAGY-----PGAPPVLDGVSLDLPPGERVAILGPSGSGKS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 726 SVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPYTCLGTLRDQIIypLSREEAElrelklygqgenavda 802
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTldgVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLR--LARPDAT---------------- 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 803 tsilDARLKTILENVRLNYLLEREEGGWDANLNwED--ILSLGEQQRLGMARLFFHKPKFGILDECT 867
Cdd:TIGR02868 438 ----DEELWAALERVGLADWLRALPDGLDTVLG-EGgaRLSGGERQRLALARALLADAPILLLDEPT 499
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
685-893 |
4.25e-11 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 62.62 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 685 ISFSEVDIITP-AQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFY 760
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 761 VPQrpytclgtlrdqiiyplsreEAELrelkLYGqgenavdatsildarlkTILENvrlnyllereeggwdanlnwedIL 840
Cdd:cd03246 81 LPQ--------------------DDEL----FSG-----------------SIAEN----------------------IL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776568118 841 SLGEQQRLGMARLFFHKPKFGILDECTNATSVDVEEPLYRLAKDL---GIT------RPALI 893
Cdd:cd03246 98 SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALkaaGATriviahRPETL 159
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
43-194 |
4.97e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 63.80 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlnKEIFYVP--QRP-------YTAFG 113
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG------KDITNLPphKRPvntvfqnYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 --TLRDQLIYPLTADQEVEPLTCSGMVDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:cd03300 86 hlTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKP--------SQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
...
gi 1776568118 192 TSA 194
Cdd:cd03300 158 LGA 160
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
710-879 |
5.00e-11 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 63.64 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 710 PEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPYTCLGTLRDQIIYPLSreEAE 786
Cdd:cd03248 39 PGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLldgKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQ--SCS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 787 LRELKLYGQGENAVDATSILDarlktilenvrLNYLLEREEGGwdanlnweDILSLGEQQRLGMARLFFHKPKFGILDEC 866
Cdd:cd03248 117 FECVKEAAQKAHAHSFISELA-----------SGYDTEVGEKG--------SQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170
....*....|....*..
gi 1776568118 867 TNATSVD----VEEPLY 879
Cdd:cd03248 178 TSALDAEseqqVQQALY 194
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-234 |
5.34e-11 |
|
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: 67.28 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 5 KELSADDKKSSLQSAGSR--NYLTEANYVEFSGVKV-VTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSS----LFRVL 77
Cdd:TIGR00957 1257 KEYSETEKEAPWQIQETAppSGWPPRGRVEFRNYCLrYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSltlgLFRIN 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 78 GGlwplVSGHIVKPGVG------SDLNKEIFYVPQRPYTAFGTLRDQLiypltadqevEPLTCSGMVDLLKNVDLDYLLD 151
Cdd:TIGR00957 1337 ES----AEGEIIIDGLNiakiglHDLRFKITIIPQDPVLFSGSLRMNL----------DPFSQYSDEEVWWALELAHLKT 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 152 --RYPPEK---EVNWGDE-LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMGTSC--ITISHRPAL 223
Cdd:TIGR00957 1403 fvSALPDKldhECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCtvLTIAHRLNT 1482
|
250
....*....|.
gi 1776568118 224 VAFHDVVLSLD 234
Cdd:TIGR00957 1483 IMDYTRVIVLD 1493
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
47-224 |
7.20e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.73 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVkpGVGSDL-----------NKEIFYVPQRPYTAFG-- 113
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVA--WLGKDLlgmkddewravRSDIQMIFQDPLASLNpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 -TLRD------QLIYPLTADQEVEPLTCSGM--VDLLKNvdldyLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPK 184
Cdd:PRK15079 115 mTIGEiiaeplRTYHPKLSRQEVKDRVKAMMlkVGLLPN-----LINRYP--------HEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1776568118 185 FAILDECTSAVTTDMEerfcAKV--------RAMGTSCITISHRPALV 224
Cdd:PRK15079 182 LIICDEPVSALDVSIQ----AQVvnllqqlqREMGLSLIFIAHDLAVV 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
31-202 |
8.53e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.19 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGV-KVVTPTgnVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG--------SDLNKEI 101
Cdd:PRK09493 2 IEFKNVsKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndpkvdeRLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 102 FYVPQRPYtafgtlrdqlIYP-LTADQEVE--PLTCSGM---------VDLLKNVDLDYLLDRYPpekevnwgDELSLGE 169
Cdd:PRK09493 80 GMVFQQFY----------LFPhLTALENVMfgPLRVRGAskeeaekqaRELLAKVGLAERAHHYP--------SELSGGQ 141
|
170 180 190
....*....|....*....|....*....|...
gi 1776568118 170 QQRLGMARLFYHKPKFAILDECTSAVttDMEER 202
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSAL--DPELR 172
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
43-194 |
1.07e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.81 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEIF-----YVPQRPyTAFG-TL 115
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDiSTLKPEIYrqqvsYCAQTP-TLFGdTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 116 RDQLIYP-LTADQEVEPltcSGMVDllknvDLDYL-LDRYPPEKEVNwgdELSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:PRK10247 98 YDNLIFPwQIRNQQPDP---AIFLD-----DLERFaLPDTILTKNIA---ELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
.
gi 1776568118 194 A 194
Cdd:PRK10247 167 A 167
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
32-195 |
1.12e-10 |
|
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: 62.97 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 32 EFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKEIFYVPQRPYTA 111
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--DINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 112 FGTLRDQ--LIYPLTADQEV-------EPL--TCSGMV---------DLLKNVDLDylldryppEKEVNWGDELSLGEQQ 171
Cdd:cd03256 80 IGMIFQQfnLIERLSVLENVlsgrlgrRSTwrSLFGLFpkeekqralAALERVGLL--------DKAYQRADQLSGGQQQ 151
|
170 180
....*....|....*....|....
gi 1776568118 172 RLGMARLFYHKPKFAILDECTSAV 195
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASL 175
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
47-190 |
1.45e-10 |
|
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: 61.85 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKEifyvpqrPYTAFGTLRD-QLIYP-LT 124
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-------ALRRIGALIEaPGFYPnLT 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776568118 125 AdqeVEPLTCSGMVDLLKNVDLDYLLDryppekEVNWGDE-------LSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:cd03268 89 A---RENLRLLARLLGIRKKRIDEVLD------VVGLKDSakkkvkgFSLGMKQRLGIALALLGNPDLLILDE 152
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
702-887 |
1.70e-10 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 62.20 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 702 RQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHFDEETASGGIFYVP----------QRPYTCLGT 771
Cdd:cd03260 17 KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLelrrrvgmvfQKPNPFPGS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 772 LRDQIIYPlsreeaelreLKLYGQGENAVdatsiLDARLKTILENVRLnyllereeggWDANLNWEDILSL--GEQQRLG 849
Cdd:cd03260 97 IYDNVAYG----------LRLHGIKLKEE-----LDERVEEALRKAAL----------WDEVKDRLHALGLsgGQQQRLC 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1776568118 850 MARLFFHKPKFGILDECTNA----TSVDVEEPLYRLAKDLGI 887
Cdd:cd03260 152 LARALANEPEVLLLDEPTSAldpiSTAKIEELIAELKKEYTI 193
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
43-194 |
1.79e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.81 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKeifyVP--QRP-------YTAFG 113
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITH----VPaeNRHvntvfqsYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 --TLRDQLIYPL----TADQEVEPLTcsgmVDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAI 187
Cdd:PRK09452 100 hmTVFENVAFGLrmqkTPAAEITPRV----MEALRMVQLEEFAQRKP--------HQLSGGQQQRVAIARAVVNKPKVLL 167
|
....*..
gi 1776568118 188 LDECTSA 194
Cdd:PRK09452 168 LDESLSA 174
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
697-869 |
2.29e-10 |
|
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: 61.34 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 697 QKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY--KPSHHFDEETASGGIFYVPQRP--YTCLgTL 772
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwnGEPIRDAREDYRRRLAYLGHADglKPEL-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 773 RDQIIYplsreeaelrELKLYGQgenAVDATSILDArlktiLENVRLNYLLEREEGgwdanlnwedILSLGEQQRLGMAR 852
Cdd:COG4133 93 RENLRF----------WAALYGL---RADREAIDEA-----LEAVGLAGLADLPVR----------QLSAGQKRRVALAR 144
|
170
....*....|....*..
gi 1776568118 853 LFFHKPKFGILDECTNA 869
Cdd:COG4133 145 LLLSPAPLWLLDEPFTA 161
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
43-190 |
2.37e-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: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNK------EIFYVPQRpYTAFG--T 114
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDlppkdrDIAMVFQN-YALYPhmT 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776568118 115 LRDQLIYPLTADQEVEPLTCSGMVDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:cd03301 89 VYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKP--------KQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-220 |
2.68e-10 |
|
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: 60.13 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 33 FSGVKVVtptgnvlvKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIvkpgvgsdlnkeifYVPQRPYtAF 112
Cdd:cd03216 10 FGGVKAL--------DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI--------------LVDGKEV-SF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 113 GTLRD------QLIYpltadqevepltcsgmvdllknvdldylldryppekevnwgdELSLGEQQRLGMARLFYHKPKFA 186
Cdd:cd03216 67 ASPRDarragiAMVY------------------------------------------QLSVGERQMVEIARALARNARLL 104
|
170 180 190
....*....|....*....|....*....|....*..
gi 1776568118 187 ILDECTSAVTTDMEERFCA---KVRAMGTSCITISHR 220
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKvirRLRAQGVAVIFISHR 141
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
47-224 |
3.94e-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: 60.76 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKE--IFYVPQ-RPYTAFGTLRDQLIY-- 121
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARnrIGYLPEeRGLYPKMKVIDQLVYla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 122 ------PLTADQEVEpltcsgmvDLLKNVDL-DYLldryppEKEVnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSA 194
Cdd:cd03269 96 qlkglkKEEARRRID--------EWLERLELsEYA------NKRV---EELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190
....*....|....*....|....*....|...
gi 1776568118 195 ---VTTDMEERFCAKVRAMGTSCITISHRPALV 224
Cdd:cd03269 159 ldpVNVELLKDVIRELARAGKTVILSTHQMELV 191
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-220 |
4.58e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 63.33 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 27 EANYVEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLvSGHIVKPGVG-SDLN-----KE 100
Cdd:PRK11174 346 DPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIElRELDpeswrKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 101 IFYVPQRPYTAFGTLRDQLIY--PLTADQEVEpltcsgmvDLLKNVDLDYLLDRYP-----PEKEVNWGdeLSLGEQQRL 173
Cdd:PRK11174 425 LSWVGQNPQLPHGTLRDNVLLgnPDASDEQLQ--------QALENAWVSEFLPLLPqgldtPIGDQAAG--LSVGQAQRL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1776568118 174 GMARLFYHKPKFAILDECTSAVTTDMEERFC-AKVRAM-GTSCITISHR 220
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMqALNAASrRQTTLMVTHQ 543
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
47-208 |
5.11e-10 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 60.82 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV-GSDLN---KEIFYVPQRpYTAFG--TLRDQLI 120
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdATDVPvqeRNVGFVFQH-YALFRhmTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 121 YPLTADQEVEPLTCSGM----VDLLKNVDLDYLLDRYPPEkevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAVT 196
Cdd:cd03296 97 FGLRVKPRSERPPEAEIrakvHELLKLVQLDWLADRYPAQ--------LSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170
....*....|..
gi 1776568118 197 tdmeerfcAKVR 208
Cdd:cd03296 169 --------AKVR 172
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
31-195 |
5.27e-10 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 60.78 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV------GSDLNKEIFYV 104
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 PQR----PYTafgTLRDQLIYPLTADQEVEPLTCSGMVDLLKNVDLD--YLLDRYPpekevnwgDELSLGEQQRLGMARL 178
Cdd:cd03295 81 IQQiglfPHM---TVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYP--------HELSGGQQQRVGVARA 149
|
170
....*....|....*..
gi 1776568118 179 FYHKPKFAILDECTSAV 195
Cdd:cd03295 150 LAADPPLLLMDEPFGAL 166
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
709-888 |
5.79e-10 |
|
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: 60.24 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 709 VPEKSLL-VTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHFDEEtaSGGIFYVPQRpytcLGTLRDqiiYPLSREeaEL 787
Cdd:cd03235 22 VKPGEFLaIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--RKRIGYVPQR----RSIDRD---FPISVR--DV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 788 RELKLYGQGENAVDATSILDARLKTILENVRLNYLLEREEGGwdanlnwediLSLGEQQRLGMARLFFHKPKFGILDECT 867
Cdd:cd03235 91 VLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGE----------LSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180
....*....|....*....|....*.
gi 1776568118 868 naTSVDV--EEPLYRLAKDL---GIT 888
Cdd:cd03235 161 --AGVDPktQEDIYELLRELrreGMT 184
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
718-868 |
6.14e-10 |
|
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: 59.92 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRLykpshhfdeeTASGGIFYVPQRPYTCLGTLRD-QIIYP-LSREEAELRELKLYGQ 795
Cdd:cd03268 33 GPNGAGKTTTMKIILGLIKPDSGEI----------TFDGKSYQKNIEALRRIGALIEaPGFYPnLTARENLRLLARLLGI 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776568118 796 GENAVDATsildarlktilenvrLNYLLEREEGGWDANLnwediLSLGEQQRLGMARLFFHKPKFGILDECTN 868
Cdd:cd03268 103 RKKRIDEV---------------LDVVGLKDSAKKKVKG-----FSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
27-194 |
7.17e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 62.04 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 27 EANYVEFSGVkVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV------------KPGVG 94
Cdd:COG3842 2 AMPALELENV-SKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILldgrdvtglppeKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 95 sdlnkeifYVPQR----PYT------AFGtLRDQLIYPLTADQEVEpltcsgmvDLLKNVDLDYLLDRYPpekevnwgDE 164
Cdd:COG3842 81 --------MVFQDyalfPHLtvaenvAFG-LRMRGVPKAEIRARVA--------ELLELVGLEGLADRYP--------HQ 135
|
170 180 190
....*....|....*....|....*....|
gi 1776568118 165 LSLGEQQRLGMARLFYHKPKFAILDECTSA 194
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
39-190 |
7.69e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.47 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 39 VTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLgglwplvSGHivkPGV----------GSDL---------NK 99
Cdd:COG0396 8 VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL-------MGH---PKYevtsgsilldGEDIlelspderaRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 100 EIFYVPQRP------------YTAFGTLRDQLIYPLTADQEVEpltcsgmvDLLKNVDLDY-LLDRYppekeVNWGdeLS 166
Cdd:COG0396 78 GIFLAFQYPveipgvsvsnflRTALNARRGEELSAREFLKLLK--------EKMKELGLDEdFLDRY-----VNEG--FS 142
|
170 180
....*....|....*....|....*..
gi 1776568118 167 LGEQQR---LGMARLfyhKPKFAILDE 190
Cdd:COG0396 143 GGEKKRneiLQMLLL---EPKLAILDE 166
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-234 |
1.02e-09 |
|
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: 62.45 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 14 SSLQSAGSRNYLTEANY-VEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG 92
Cdd:TIGR01193 456 SEFINKKKRTELNNLNGdIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 93 VGSD------LNKEIFYVPQRPYTAFGTLRDQLIY----PLTADQEVEPLTCSGMVDLLKNVDLDYLLDRYPPekevnwG 162
Cdd:TIGR01193 536 FSLKdidrhtLRQFINYLPQEPYIFSGSILENLLLgakeNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEE------G 609
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776568118 163 DELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMG-TSCITISHRPALVAFHDVVLSLD 234
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLD 682
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
43-194 |
1.19e-09 |
|
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: 59.47 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKeifyvpqrpyTAFGTLRDQL--- 119
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK----------KNINELRQKVgmv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 120 -----IYP-LTADQEVE--PLTCSGM---------VDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHK 182
Cdd:cd03262 82 fqqfnLFPhLTVLENITlaPIKVKGMskaeaeeraLELLEKVGLADKADAYP--------AQLSGGQQQRVAIARALAMN 153
|
170
....*....|..
gi 1776568118 183 PKFAILDECTSA 194
Cdd:cd03262 154 PKVMLFDEPTSA 165
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
685-904 |
1.26e-09 |
|
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: 59.53 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 685 ISFSEVDIITPAQKLLA-RQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFY 760
Cdd:cd03245 3 IEFRNVSFSYPNQEIPAlDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 761 VPQRPYTCLGTLRDQII--YPLSREEAELRELKLYGqgenaVDATSILDARlktilenvrlNYLLEREEGGwdanlnweD 838
Cdd:cd03245 83 VPQDVTLFYGTLRDNITlgAPLADDERILRAAELAG-----VTDFVNKHPN----------GLDLQIGERG--------R 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 839 ILSLGEQQRLGMARLFFHKPKFGILDECTNATSVDVEEPLYRLAKDLGITRPALIPFHALE-LRLVD 904
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSlLDLVD 206
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
43-219 |
2.35e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.62 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNkeifYVP--QRPYT---------- 110
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLS----HVPpyQRPINmmfqsyalfp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 111 --------AFGTLRDQLIYPLTADQEVEPLTCSGMVDLLKnvdldylldRYPpekevnwgDELSLGEQQRLGMARLFYHK 182
Cdd:PRK11607 105 hmtveqniAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAK---------RKP--------HQLSGGQRQRVALARSLAKR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1776568118 183 PKFAILDECTSAVTTDMEERFCAKV----RAMGTSCITISH 219
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVvdilERVGVTCVMVTH 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
610-900 |
2.57e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 61.28 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 610 QGELAHALRFLASVvsqsflaFGDILELhrkflelSGSINRIFELeelLD----AAQSGDLSTDNLlqsqrtalsaKDVI 685
Cdd:TIGR00958 427 QEQLGEAVRVLSYV-------YSGMMQA-------VGASEKVFEY---LDrkpnIPLTGTLAPLNL----------EGLI 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 686 SFSEVDIITPAQ--KLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFY 760
Cdd:TIGR00958 480 EFQDVSFSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldgVPLVQYDHHYLHRQVAL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 761 VPQRPYTCLGTLRDQIIYPLSREEAElrELKLYGQGENAVDATSILDarlKTILENVrlnylleREEGGwdanlnwedIL 840
Cdd:TIGR00958 560 VGQEPVLFSGSVRENIAYGLTDTPDE--EIMAAAKAANAHDFIMEFP---NGYDTEV-------GEKGS---------QL 618
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 841 SLGEQQRLGMARLFFHKPKFGILDECTNATSVDVEEPLYRLAKDLGitRPALIPFHALEL 900
Cdd:TIGR00958 619 SGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRAS--RTVLLIAHRLST 676
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
47-235 |
2.91e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVkpgVGS---------DLNKEIFYVPQRPYTAF--GTL 115
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT---VGGmvlseetvwDVRRQVGMVFQNPDNQFvgATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 116 RDQLIYPLTaDQEVEPLTcsgMV----DLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:PRK13635 100 QDDVAFGLE-NIGVPREE---MVervdQALRQVGMEDFLNREP--------HRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1776568118 192 TSAVTTDMEERFCAKVRAM----GTSCITISHRPALVAFHDVVLSLDG 235
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLkeqkGITVLSITHDLDEAAQADRVIVMNK 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
710-868 |
3.19e-09 |
|
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: 57.86 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 710 PEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPytclgtlRDQIIYPLSREEAE 786
Cdd:cd03225 26 KGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgKDLTKLSLKELRRKVGLVFQNP-------DDQFFGPTVEEEVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 787 --LRELKLygqgenavdATSILDARLKTILENVRLNYLLEReeggwdanlnweDI--LSLGEQQRLGMARLFFHKPKFGI 862
Cdd:cd03225 99 fgLENLGL---------PEEEIEERVEEALELVGLEGLRDR------------SPftLSGGQKQRVAIAGVLAMDPDILL 157
|
....*.
gi 1776568118 863 LDECTN 868
Cdd:cd03225 158 LDEPTA 163
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
700-875 |
3.93e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 57.37 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 700 LARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHFDEETASggifyvPQRPYTCLGTlRDQIIYP 779
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE------PHENILYLGH-LPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 780 LSREEaELRELKLYGQGENavdaTSILDArlktiLENVRLNYLlereeggwdanlnwEDI----LSLGEQQRLGMARLFF 855
Cdd:TIGR01189 88 LSALE-NLHFWAAIHGGAQ----RTIEDA-----LAAVGLTGF--------------EDLpaaqLSAGQQRRLALARLWL 143
|
170 180
....*....|....*....|
gi 1776568118 856 HKPKFGILDECTnaTSVDVE 875
Cdd:TIGR01189 144 SRRPLWILDEPT--TALDKA 161
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
46-195 |
3.99e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 46 LVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlNKEIFYVPQR-------PYTA--FGTLR 116
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----KLRIGYVPQKlyldttlPLTVnrFLRLR 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 117 dqliyPLTADQEVEPltcsgmvdLLKNVDLDYLLDrYPPEKevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAV 195
Cdd:PRK09544 94 -----PGTKKEDILP--------ALKRVQAGHLID-APMQK-------LSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
38-219 |
4.23e-09 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 58.81 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 38 VVTPTGNVL-VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLN------------KEIFYV 104
Cdd:cd03294 30 ILKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQ--DIAamsrkelrelrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 -------PQRpytafgTLRDQLIYPLtadqEVepltcSGM---------VDLLKNVDLDYLLDRYPpekevnwgDELSLG 168
Cdd:cd03294 108 fqsfallPHR------TVLENVAFGL----EV-----QGVpraereeraAEALELVGLEGWEHKYP--------DELSGG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776568118 169 EQQRLGMARLFYHKPKFAILDECTSA----VTTDMEERFCAKVRAMGTSCITISH 219
Cdd:cd03294 165 MQQRVGLARALAVDPDILLMDEAFSAldplIRREMQDELLRLQAELQKTIVFITH 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
718-874 |
4.65e-09 |
|
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: 57.95 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHfDEETASGGIFYVPQRPYTCLG-TLRDQI-----IYPLSREEAELr 788
Cdd:COG4555 34 GPNGAGKTTLLRMLAGLLKPDSGSILidgEDVRK-EPREARRQIGVLPDERGLYDRlTVRENIryfaeLYGLFDEELKK- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 789 elklygqgenavdatsildarlktilenvRLNYLLEREEGGWDANLNWEDiLSLGEQQRLGMARLFFHKPKFGILDECTN 868
Cdd:COG4555 112 -----------------------------RIEELIELLGLEEFLDRRVGE-LSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
....*.
gi 1776568118 869 AtsVDV 874
Cdd:COG4555 162 G--LDV 165
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
31-219 |
5.19e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 58.91 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVK---DLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWP---LVSGHIV-KpgvGSDLN----- 98
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILfD---GEDLLklsek 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 99 -------KEIFYVPQRPYTAFG---TLRDQLIYPLT---------ADQEVepltcsgmVDLLKNVDLDY---LLDRYPpe 156
Cdd:COG0444 79 elrkirgREIQMIFQDPMTSLNpvmTVGDQIAEPLRihgglskaeARERA--------IELLERVGLPDperRLDRYP-- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776568118 157 kevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSA--VTT---------DMEERFcakvramGTSCITISH 219
Cdd:COG0444 149 ------HELSGGMRQRVMIARALALEPKLLIADEPTTAldVTIqaqilnllkDLQREL-------GLAILFITH 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
43-219 |
5.28e-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: 56.81 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKEIFYV-PQRPYTAFGTLRDQLIY 121
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE--DLTDLEDELpPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 122 PLTAdqevepltcsgmvdlLKNVdldylldRYPpekevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSA---VTTD 198
Cdd:cd03229 90 HLTV---------------LENI-------ALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSAldpITRR 137
|
170 180
....*....|....*....|..
gi 1776568118 199 MEERFCAKVRAM-GTSCITISH 219
Cdd:cd03229 138 EVRALLKSLQAQlGITVVLVTH 159
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
42-940 |
7.84e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 42 TGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFR-VLGGLWPLVSGHIVKPGvgsdlnkEIFYVPQRPYTAFGTLRDQLI 120
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-------SVAYVPQVSWIFNATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 121 YpltaDQEVEPLTCSGMVDLlknVDLDYLLDRYPPEKEVNWGDE---LSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 197
Cdd:PLN03232 701 F----GSDFESERYWRAIDV---TALQHDLDLLPGRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 198 DMEERF---CAKVRAMGTSCITISHRPALVAFHD-VVLSLDG----EGGWKVHYKSE---NSSVQSEGEIDLTVSETDRQ 266
Cdd:PLN03232 774 HVAHQVfdsCMKDELKGKTRVLVTNQLHFLPLMDrIILVSEGmikeEGTFAELSKSGslfKKLMENAGKMDATQEVNTND 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 267 TDAIAVqraftaakkdsefsSPRTLSYVSEVIAASPSVNHDAKLPIVPQLHKVPRVLPLRVAAMFKVLVPTVFDKQ---G 343
Cdd:PLN03232 854 ENILKL--------------GPTVTIDVSERNLGSTKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGLWVVMillV 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 344 AQLLAVAFLVVSRTWIS---DRIASLNGTTVKYVLEQNKTAFIRligVSVLQSGASSFIAPSLRHLKarlalgwriRLTQ 420
Cdd:PLN03232 920 CYLTTEVLRVSSSTWLSiwtDQSTPKSYSPGFYIVVYALLGFGQ---VAVTFTNSFWLISSSLHAAK---------RLHD 987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 421 NLLKNYLRNNAFYqvFHMSSKNidadqRITHDLEKLTTDLSGLVTGMVKPSVDILWFTWRMQLLTGRRGVAILYAYMLLG 500
Cdd:PLN03232 988 AMLNSILRAPMLF--FHTNPTG-----RVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLL 1060
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 501 LGFLRTVTpdFGDLTSREQQlegtfrfmheRLrthaESVAffgggareKAMVDSRFKELFDhSLLLLKKKWLFDILDDFV 580
Cdd:PLN03232 1061 ILFYAAYL--YYQSTSREVR----------RL----DSVT--------RSPIYAQFGEALN-GLSSIRAYKAYDRMAKIN 1115
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 581 TKQLPHNVTWFLSLLyalehKGDRALVTTQGELAHALRFLasVVSQSFLAFGDIlELHRKF-----LELSGSINRIFELE 655
Cdd:PLN03232 1116 GKSMDNNIRFTLANT-----SSNRWLTIRLETLGGVMIWL--TATFAVLRNGNA-ENQAGFastmgLLLSYTLNITTLLS 1187
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 656 ELLDAAQSGDLSTDNL--------LQSQRTALSAKD----------VISFSEVDI-ITPAQKLLARQLTCDVVPEKSLLV 716
Cdd:PLN03232 1188 GVLRQASKAENSLNSVervgnyidLPSEATAIIENNrpvsgwpsrgSIKFEDVHLrYRPGLPPVLHGLSFFVSPSEKVGV 1267
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 717 TGPNGSGKSSVFRVLRGLWPIVSGRLYKPshhfDEETASGGIF-------YVPQRPYTCLGTLRDQiIYPLSREEaelre 789
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMID----DCDVAKFGLTdlrrvlsIIPQSPVLFSGTVRFN-IDPFSEHN----- 1337
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 790 lklygqgenavdatsilDARLKTILENVRLNYLLEREEGGWDANL-NWEDILSLGEQQRLGMARLFFHKPKFGILDECTn 868
Cdd:PLN03232 1338 -----------------DADLWEALERAHIKDVIDRNPFGLDAEVsEGGENFSVGQRQLLSLARALLRRSKILVLDEAT- 1399
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776568118 869 aTSVDVEeplyrlakdlgitrpalipFHALELRLVDGEEPECGAnlkLTLLFRVDMIMEKDKFLImLRTGQV 940
Cdd:PLN03232 1400 -ASVDVR-------------------TDSLIQRTIREEFKSCTM---LVIAHRLNTIIDCDKILV-LSSGQV 1447
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
43-194 |
8.01e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 57.82 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---------KPGvgsDLNKEIFYVPQRPYTAFg 113
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawSPW---ELARRRAVLPQHSSLAF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 tlrdqliyPLTAdQEV-----EPLTCSGMVDL------LKNVDLDYLLDR-YPpekevnwgdELSLGEQQRLGMARLF-- 179
Cdd:COG4559 89 --------PFTV-EEVvalgrAPHGSSAAQDRqivreaLALVGLAHLAGRsYQ---------TLSGGEQQRVQLARVLaq 150
|
170 180
....*....|....*....|
gi 1776568118 180 -----YHKPKFAILDECTSA 194
Cdd:COG4559 151 lwepvDGGPRWLFLDEPTSA 170
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
32-236 |
8.42e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.35 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 32 EFSGVKVVTPTGN---VLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEIFYVPQR 107
Cdd:PRK10535 6 ELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvATLDADALAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 108 PYTAFGTLRDQLIYPLTADQEVE-PLTCSGMVDLLKNVDLDYLLDRYPPEKEVNWG-DELSLGEQQRLGMARLFYHKPKF 185
Cdd:PRK10535 86 EHFGFIFQRYHLLSHLTAAQNVEvPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQpSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776568118 186 AILDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPALVAFHDVVLSL-DGE 236
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAilhQLRDRGHTVIIVTHDPQVAAQAERVIEIrDGE 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
31-234 |
9.02e-09 |
|
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: 59.34 E-value: 9.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTP-TGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 103
Cdd:TIGR02203 331 VEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDladytlASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 104 VPQRPYTAFGTLRDQLIYPLTAD---QEVEpltcsgmvDLLKNVDLDYLLDRYPPEKEVNWGDE---LSLGEQQRLGMAR 177
Cdd:TIGR02203 411 VSQDVVLFNDTIANNIAYGRTEQadrAEIE--------RALAAAYAQDFVDKLPLGLDTPIGENgvlLSGGQRQRLAIAR 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 178 LFYHKPKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVMD 541
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
699-874 |
9.57e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 56.35 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 699 LLARQLTCD-------------VVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHhfdeetasggifyvpqrp 765
Cdd:cd03231 1 LEADELTCErdgralfsglsftLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 766 ytclgtlrdqiiyPLSREEAELRELKLYGQGENAVDATSildarlkTILENVRLNYLLEREEGGWDA----NLN-WEDI- 839
Cdd:cd03231 63 -------------PLDFQRDSIARGLLYLGHAPGIKTTL-------SVLENLRFWHADHSDEQVEEAlarvGLNgFEDRp 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 1776568118 840 ---LSLGEQQRLGMARLFFHKPKFGILDECTnaTSVDV 874
Cdd:cd03231 123 vaqLSAGQQRRVALARLLLSGRPLWILDEPT--TALDK 158
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
685-916 |
1.49e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 56.73 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 685 ISFSEVDI-ITPAQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHF---DEETASGGIFY 760
Cdd:cd03252 1 ITFEHVRFrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLalaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 761 VPQRPYTCLGTLRDQIiyPLSREEAELRELklygqgenaVDATSILDARlktilenvrlNYLLEREEGgWDANLNWEDI- 839
Cdd:cd03252 81 VLQENVLFNRSIRDNI--ALADPGMSMERV---------IEAAKLAGAH----------DFISELPEG-YDTIVGEQGAg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 840 LSLGEQQRLGMARLFFHKPKFGILDECTNATSVDVEEPLYRLAKDLGITRPALIPFHALE--------LRLVDGEEPECG 911
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLStvknadriIVMEKGRIVEQG 218
|
....*
gi 1776568118 912 ANLKL 916
Cdd:cd03252 219 SHDEL 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
31-224 |
1.72e-08 |
|
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: 56.29 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVtptgnvlvKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV---------KP------GVGs 95
Cdd:cd03219 8 KRFGGLVAL--------DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgeditglPPheiarlGIG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 96 dlnkEIFYVPqRPYTAFgTLRDQLIYPLTADQEVEPLTCSGMV----------DLLKNVDLDYLLDRYPpekevnwgDEL 165
Cdd:cd03219 79 ----RTFQIP-RLFPEL-TVLENVMVAAQARTGSGLLLARARReereareraeELLERVGLADLADRPA--------GEL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776568118 166 SLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPALV 224
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAElirELRERGITVLLVEHDMDVV 206
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
47-190 |
2.00e-08 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 55.90 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSG---------------HIVKPGVGsdlnkeifYVPQ-RPyt 110
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsirfdgrditglpphERARAGIG--------YVPEgRR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 111 AFGTL--RDQL---IYPLTADQEVEpltcsgmvdllknvDLDYLLDRYP--PEKEVNWGDELSLGEQQRLGMARLFYHKP 183
Cdd:cd03224 86 IFPELtvEENLllgAYARRRAKRKA--------------RLERVYELFPrlKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
....*..
gi 1776568118 184 KFAILDE 190
Cdd:cd03224 152 KLLLLDE 158
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-225 |
2.02e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 46 LVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG----VGSD--------LNKEIFYVPQRPyTAFG 113
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyFGKDifqidaikLRKEVGMVFQQP-NPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 TLR--DQLIYPLTA-----DQEVEPLtcsgMVDLLKNVDL-DYLLDRYPPEkevnwGDELSLGEQQRLGMARLFYHKPKF 185
Cdd:PRK14246 104 HLSiyDNIAYPLKShgikeKREIKKI----VEECLRKVGLwKEVYDRLNSP-----ASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1776568118 186 AILDECTSAV----TTDMEERFCAKVRAMgtSCITISHRPALVA 225
Cdd:PRK14246 175 LLMDEPTSMIdivnSQAIEKLITELKNEI--AIVIVSHNPQQVA 216
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
650-867 |
3.29e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.42 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 650 RIFELeelLDAAQSGDLSTDNLLQSQRTALsakDVISFSEVDiitpaQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFR 729
Cdd:PRK10790 317 RVFEL---MDGPRQQYGNDDRPLQSGRIDI---DNVSFAYRD-----DNLVLQNINLSVPSRGFVALVGHTGSGKSTLAS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 730 VLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPYTCLGTLRDQIIypLSREeaelrelklygqgenavdatsIL 806
Cdd:PRK10790 386 LLMGYYPLTEGEIRldgRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVT--LGRD---------------------IS 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776568118 807 DARLKTILENVRLNYLLEREEGGWDANLNWE-DILSLGEQQRLGMARLFFHKPKFGILDECT 867
Cdd:PRK10790 443 EEQVWQALETVQLAELARSLPDGLYTPLGEQgNNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
43-226 |
3.83e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.46 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGL--WPLVSGHIVKPGVG-SDLNKE------IFYVPQRPYtafg 113
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDiTDLPPEerarlgIFLAFQYPP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 tlrdqliypltadqEVEPLTcsgMVDLLKNVDldylldryppekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:cd03217 88 --------------EIPGVK---NADFLRYVN-----------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 1776568118 194 AVTTD---MEERFCAKVRAMGTSCITISHRPALVAF 226
Cdd:cd03217 134 GLDIDalrLVAEVINKLREEGKSVLIITHYQRLLDY 169
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
43-190 |
4.48e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG-----VGSDLNKEIFYVPQRP-----YTAF 112
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrQRDEYHQDLLYLGHQPgikteLTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 113 GTLR--DQLIYPLTADQEVEPLTCSGMV---DLLKNVdldylldryppekevnwgdeLSLGEQQRLGMARLFYHKPKFAI 187
Cdd:PRK13538 93 ENLRfyQRLHGPGDDEALWEALAQVGLAgfeDVPVRQ--------------------LSAGQQRRVALARLWLTRAPLWI 152
|
...
gi 1776568118 188 LDE 190
Cdd:PRK13538 153 LDE 155
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-234 |
4.80e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.58 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 29 NYVEFSGVKVVTP-TGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGG-LWP--------LVSGHIVKPGVGSDLN 98
Cdd:PRK13640 4 NIVEFKHVSFTYPdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPddnpnskiTVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 99 KEIFYVPQRPYTAF--GTLRDQLIYPLTADQEVEPLTCSGMVDLLKNVD-LDYlLDRYPpekevnwgDELSLGEQQRLGM 175
Cdd:PRK13640 84 EKVGIVFQNPDNQFvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGmLDY-IDSEP--------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776568118 176 ARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM----GTSCITISHRPALVAFHDVVLSLD 234
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITHDIDEANMADQVLVLD 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
707-885 |
6.28e-08 |
|
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: 53.02 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 707 DVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQrpytclgtlrdqiiyplsre 783
Cdd:cd00267 21 TLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILidgKDIAKLPLEELRRRIGYVPQ-------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 784 eaelrelklygqgenavdatsildarlktilenvrlnyllereeggwdanlnwediLSLGEQQRLGMARLFFHKPKFGIL 863
Cdd:cd00267 81 --------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180
....*....|....*....|..
gi 1776568118 864 DECTNATSVDVEEPLYRLAKDL 885
Cdd:cd00267 105 DEPTSGLDPASRERLLELLREL 126
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
39-189 |
7.28e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 39 VTPtgnvLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlnkEIFYVPQRPYTAFGTLRDQ 118
Cdd:TIGR01271 438 VTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776568118 119 LIYPLTADQevepltcSGMVDLLKNVDLDYLLDRYPPEKEVNWGD---ELSLGEQQRLGMARLFYHKPKFAILD 189
Cdd:TIGR01271 507 IIFGLSYDE-------YRYTSVIKACQLEEDIALFPEKDKTVLGEggiTLSGGQRARISLARAVYKDADLYLLD 573
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
43-190 |
8.01e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 56.23 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVkpgVGSDLnkEIFYVPQRpytafgtlRDQLiyp 122
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK---LGETV--KIGYFDQH--------QEEL--- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 123 ltadqevepltcsgmvDLLKNVdLDYLLDRYPPEKEVNW----------GDE-------LSLGEQQRLGMARLFYHKPKF 185
Cdd:COG0488 391 ----------------DPDKTV-LDELRDGAPGGTEQEVrgylgrflfsGDDafkpvgvLSGGEKARLALAKLLLSPPNV 453
|
....*
gi 1776568118 186 AILDE 190
Cdd:COG0488 454 LLLDE 458
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-220 |
8.77e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 33 FSGVKVVTPTGnvlvkdlfLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKpgvgsdLNKEI-FYVPQRPYTA 111
Cdd:PRK10762 14 FPGVKALSGAA--------LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY------LGKEVtFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 112 FGTLRDQ---LIYPLTADQEV----EPLTCSGMVDLLK-NVDLDYLLDR----YPPEKEVNwgdELSLGEQQRLGMARLF 179
Cdd:PRK10762 80 GIGIIHQelnLIPQLTIAENIflgrEFVNRFGRIDWKKmYAEADKLLARlnlrFSSDKLVG---ELSIGEQQMVEIAKVL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1776568118 180 YHKPKFAILDECTSAVT-TDMEERFcaKV----RAMGTSCITISHR 220
Cdd:PRK10762 157 SFESKVIIMDEPTDALTdTETESLF--RVirelKSQGRGIVYISHR 200
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
49-190 |
1.00e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.09 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 49 DLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPgvGSDL------NKEIFYVPQRpYTAFG--TLRDQLI 120
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH--GTDVsrlharDRKVGFVFQH-YALFRhmTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 121 YPLTA------------DQEVepltcsgmVDLLKNVDLDYLLDRYPPekevnwgdELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:PRK10851 97 FGLTVlprrerpnaaaiKAKV--------TQLLEMVQLAHLADRYPA--------QLSGGQKQRVALARALAVEPQILLL 160
|
..
gi 1776568118 189 DE 190
Cdd:PRK10851 161 DE 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
43-192 |
1.07e-07 |
|
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: 52.07 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlNKEIFYVPQrpytafgtlrdqliyp 122
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----TVKIGYFEQ---------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 123 ltadqevepltcsgmvdllknvdldylldryppekevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:cd03221 71 ------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
43-190 |
1.14e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.13 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDL-------NKEIFYVPQ-----RPYT 110
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplharaRRGIGYLPQeasifRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 111 AFGTLRD--QLIYPLTADQEVEPltcsgMVDLLKNVDLDYLLDryppekevNWGDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:PRK10895 95 VYDNLMAvlQIRDDLSAEQREDR-----ANELMEEFHIEHLRD--------SMGQSLSGGERRRVEIARALAANPKFILL 161
|
..
gi 1776568118 189 DE 190
Cdd:PRK10895 162 DE 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
634-888 |
1.17e-07 |
|
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: 55.68 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 634 ILELHRKFLELSGSINRIFELEELLDAAQSGDL---STDNLLQSQRTALSAKDV-ISFSevdiITPAQKLLA-RQLTCDV 708
Cdd:COG1123 213 VVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAargRAAPAAAAAEPLLEVRNLsKRYP----VRGKGGVRAvDDVSLTL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 709 VPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEET---ASGGIFYVPQRPYTCL---GTLRDQIIYP 779
Cdd:COG1123 289 RRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgKDLTKLSRRSlreLRRRVQMVFQDPYSSLnprMTVGDIIAEP 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 780 LsreeaelRELKLYGQGEnavdatsiLDARLKTILENVRLNY-LLER---EeggwdanlnwediLSLGEQQRLGMARLFF 855
Cdd:COG1123 369 L-------RLHGLLSRAE--------RRERVAELLERVGLPPdLADRyphE-------------LSGGQRQRVAIARALA 420
|
250 260 270
....*....|....*....|....*....|....*..
gi 1776568118 856 HKPKFGILDECTNA--TSV--DVEEPLYRLAKDLGIT 888
Cdd:COG1123 421 LEPKLLILDEPTSAldVSVqaQILNLLRDLQRELGLT 457
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
45-234 |
1.23e-07 |
|
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: 52.70 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 45 VLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV-----GSDLNKEIFYVPQRPYTAFGTLRDql 119
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlEKALSSLISVLNQRPYLFDTTLRN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 120 iypltadqevepltcsgmvdllknvdldylldryppekevNWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDM 199
Cdd:cd03247 94 ----------------------------------------NLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 1776568118 200 EERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:cd03247 134 ERQLLSLIFEVlkDKTLIWITHHLTGIEHMDKILFLE 170
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
718-865 |
1.30e-07 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 53.59 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRLY--------KPSHhfdeETASGGIFYVPQrpytclgtlRDQIIYPLSREEaelrE 789
Cdd:cd03224 33 GRNGAGKTTLLKTIMGLLPPRSGSIRfdgrditgLPPH----ERARAGIGYVPE---------GRRIFPELTVEE----N 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 790 LKLYGQGENavdatsilDARLKTILENV-----RLNYLLEREEGGwdanlnwediLSLGEQQRLGMARLFFHKPKFGILD 864
Cdd:cd03224 96 LLLGAYARR--------RAKRKARLERVyelfpRLKERRKQLAGT----------LSGGEQQMLAIARALMSRPKLLLLD 157
|
.
gi 1776568118 865 E 865
Cdd:cd03224 158 E 158
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-233 |
1.64e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.11 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 17 QSAGSRNYLTEANYVEFSGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG---- 92
Cdd:PRK10790 327 QQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrpls 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 93 --VGSDLNKEIFYVPQRPYTAFGTLRDQLIYPLTADQEvepltcsGMVDLLKNVDLDYLLDRYPPEKEVNWGDE---LSL 167
Cdd:PRK10790 407 slSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEE-------QVWQALETVQLAELARSLPDGLYTPLGEQgnnLSV 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 168 GEQQRLGMARLFYHKPKFAILDECTSAVTTDMEE---RFCAKVRAMgTSCITISHRPALVAFHDVVLSL 233
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGTEQaiqQALAAVREH-TTLVVIAHRLSTIVEADTILVL 547
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
682-900 |
2.23e-07 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 54.52 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 682 KDVISFSEVDIITPAQKLLA-RQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPI---VSGRLY---KPSHHFDEETA 754
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAvDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLldgRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 755 SGGIFYVPQRPYTCL--GTLRDQIIYPL-----SREEAElrelklygqgenavdatsildARLKTILENVRLNYLLERee 827
Cdd:COG1123 82 GRRIGMVFQDPMTQLnpVTVGDQIAEALenlglSRAEAR---------------------ARVLELLEAVGLERRLDR-- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 828 ggwdanlnWEDILSLGEQQRLGMARLFFHKPKFGILDECTNA----TSVDVEEPLYRLAKDLGITrpALIPFHALEL 900
Cdd:COG1123 139 --------YPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAldvtTQAEILDLLRELQRERGTT--VLLITHDLGV 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
32-220 |
2.62e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.25 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 32 EFSGVKVVtptgnvlvKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlnkeifyvpqRPYTa 111
Cdd:COG1129 13 SFGGVKAL--------DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG--------------EPVR- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 112 FGTLRD------QLIYpltadQEV----------------EPLTcSGMVD----------LLKNVDLDylLDrypPEKEV 159
Cdd:COG1129 70 FRSPRDaqaagiAIIH-----QELnlvpnlsvaeniflgrEPRR-GGLIDwramrrrareLLARLGLD--ID---PDTPV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776568118 160 nwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVR---AMGTSCITISHR 220
Cdd:COG1129 139 ---GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRrlkAQGVAIIYISHR 199
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
43-194 |
3.46e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 52.85 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIvkpgvgsDLNkeifyvpQRPYTAF---------G 113
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV-------RLN-------GRPLADWspaelarrrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 TLRDQ--LIYPLTADQEVE----PLTCSG-----MVD-LLKNVDLDYLLDR-YPpekevnwgdELSLGEQQRLGMARLF- 179
Cdd:PRK13548 80 VLPQHssLSFPFTVEEVVAmgraPHGLSRaeddaLVAaALAQVDLAHLAGRdYP---------QLSGGEQQRVQLARVLa 150
|
170 180
....*....|....*....|
gi 1776568118 180 -----YHKPKFAILDECTSA 194
Cdd:PRK13548 151 qlwepDGPPRWLLLDEPTSA 170
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
47-190 |
3.47e-07 |
|
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: 52.29 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKE---------IFYVPQ--RpytAFGTL 115
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE--DITGLpphriarlgIGYVPEgrR---IFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 116 --RDQLI---YPLTADQEVEPltcsgmvdllknvDLDYLLDRYPP--EKEVNWGDELSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:COG0410 94 tvEENLLlgaYARRDRAEVRA-------------DLERVYELFPRlkERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
..
gi 1776568118 189 DE 190
Cdd:COG0410 161 DE 162
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-189 |
3.63e-07 |
|
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: 52.94 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 17 QSAGSRNYLTEANYVEFSGVKVVtptGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFR-VLGGLWPlVSGHIVKPGvgs 95
Cdd:cd03291 26 QENNDRKHSSDDNNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELEP-SEGKIKHSG--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 96 dlnkEIFYVPQRPYTAFGTLRDQLIYPLTADQevepltcSGMVDLLKNVDLDYLLDRYPPEKEVNWGD---ELSLGEQQR 172
Cdd:cd03291 99 ----RISFSSQFSWIMPGTIKENIIFGVSYDE-------YRYKSVVKACQLEEDITKFPEKDNTVLGEggiTLSGGQRAR 167
|
170
....*....|....*..
gi 1776568118 173 LGMARLFYHKPKFAILD 189
Cdd:cd03291 168 ISLARAVYKDADLYLLD 184
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
62-254 |
4.56e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 62 ITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYVPQRPYTAFGTLRDQlIYPLTADQEvepltcS 135
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDvakfglTDLRRVLSIIPQSPVLFSGTVRFN-IDPFSEHND------A 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 136 GMVDLLKNVDLDYLLDRYP--PEKEVNWGDE-LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAMGT 212
Cdd:PLN03232 1340 DLWEALERAHIKDVIDRNPfgLDAEVSEGGEnFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFK 1419
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1776568118 213 SC--ITISHRPALVAFHDVVLSLdgEGGWKVHYKSENSSVQSEG 254
Cdd:PLN03232 1420 SCtmLVIAHRLNTIIDCDKILVL--SSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
707-888 |
5.70e-07 |
|
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: 51.34 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 707 DVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYkpshhFDEETASGG------------IFYVPQRpYTCLGTL-- 772
Cdd:cd03255 26 SIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVR-----VDGTDISKLsekelaafrrrhIGFVFQS-FNLLPDLta 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 773 RDQIIYPLSREEAELRELKlygqgenavdatsildARLKTILENVRLNYLLER--EEggwdanlnwediLSLGEQQRLGM 850
Cdd:cd03255 100 LENVELPLLLAGVPKKERR----------------ERAEELLERVGLGDRLNHypSE------------LSGGQQQRVAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1776568118 851 ARLFFHKPKFGILDECTNA----TSVDVEEPLYRLAKDLGIT 888
Cdd:cd03255 152 ARALANDPKIILADEPTGNldseTGKEVMELLRELNKEAGTT 193
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
718-888 |
6.24e-07 |
|
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: 50.47 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHF--DEETASGGIFYVPQRPYtclgtlrdqiiyplsreeaelrelkLYGQ 795
Cdd:cd03230 33 GPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkkEPEEVKRRIGYLPEEPS-------------------------LYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 796 genavdatsildarlKTILENVRLnyllereeggwdanlnwedilSLGEQQRLGMARLFFHKPKFGILDECTNA----TS 871
Cdd:cd03230 88 ---------------LTVRENLKL---------------------SGGMKQRLALAQALLHDPELLILDEPTSGldpeSR 131
|
170
....*....|....*..
gi 1776568118 872 VDVEEPLYRLAKDlGIT 888
Cdd:cd03230 132 REFWELLRELKKE-GKT 147
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
718-875 |
7.17e-07 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 51.60 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRL----YKPSHHFDEetASGGIFYVPQRPYTCLG-TLRDQI-----IYPLSREEAEl 787
Cdd:COG1131 33 GPNGAGKTTTIRMLLGLLRPTSGEVrvlgEDVARDPAE--VRRRIGYVPQEPALYPDlTVRENLrffarLYGLPRKEAR- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 788 relklygqgenavdatsildARLKTILENVRLNYLLEREEGGwdanlnwediLSLGEQQRLGMARLFFHKPKFGILDECT 867
Cdd:COG1131 110 --------------------ERIDELLELFGLTDAADRKVGT----------LSGGMKQRLGLALALLHDPELLILDEPT 159
|
....*...
gi 1776568118 868 NAtsVDVE 875
Cdd:COG1131 160 SG--LDPE 165
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
711-867 |
7.94e-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: 53.20 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 711 EKSLLVtGPNGSGKSSVFRVLRGLWPIVSGRL---YKPSHHFDEETASGGIFYVPQRPYTCLGTLRDQIIYPlSREEAEL 787
Cdd:TIGR01193 501 SKTTIV-GMSGSGKSTLAKLLVGFFQARSGEIllnGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQ 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 788 RELKlygqgenavDATSIldARLKTILENVRLNYLLEREEGGWDanlnwediLSLGEQQRLGMARLFFHKPKFGILDECT 867
Cdd:TIGR01193 579 DEIW---------AACEI--AEIKDDIENMPLGYQTELSEEGSS--------ISGGQKQRIALARALLTDSKVLILDEST 639
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
697-888 |
8.26e-07 |
|
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: 51.58 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 697 QKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPytclgtlr 773
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDLASLSRRELARRIAYVPQEP-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 774 dQIIYPLSreeaeLRELKLYG--------QGENAVDATSILDArlktiLENVRLNYLLEREeggWDAnlnwediLSLGEQ 845
Cdd:COG1120 85 -PAPFGLT-----VRELVALGryphlglfGRPSAEDREAVEEA-----LERTGLEHLADRP---VDE-------LSGGER 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1776568118 846 QRLGMARLFFHKPKFGILDECTNA----TSVDVEEPLYRLAKDLGIT 888
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHldlaHQLEVLELLRRLARERGRT 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
714-869 |
1.08e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 50.64 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 714 LLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHFDEETASGGIFYvpqrpytcLGTlRDQIIYPLSREEAELRELKLY 793
Cdd:PRK13539 31 LVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY--------LGH-RNAMKPALTVAENLEFWAAFL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 794 GQGENAVDATsildarlktiLENVRLNYLLEREEGGwdanlnwediLSLGEQQRLGMARLF-FHKPKFgILDECTNA 869
Cdd:PRK13539 102 GGEELDIAAA----------LEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLvSNRPIW-ILDEPTAA 157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
716-867 |
1.10e-06 |
|
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: 50.33 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 716 VTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHFDEETASGGIFYVPQRPYTCLGTlrdqiiyplSREEAELRE-LKLYG 794
Cdd:cd03226 31 LTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDVDYQLFT---------DSVREELLLgLKELD 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776568118 795 QGENAVDatsildarlkTILENVRLNYLLEREEggWDanlnwediLSLGEQQRLGMARLFFHKPKFGILDECT 867
Cdd:cd03226 102 AGNEQAE----------TVLKDLDLYALKERHP--LS--------LSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
47-231 |
1.26e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.27 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGS------DLNKEIFYVPQRPYTAF--GTLRDQ 118
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteenvwDIRHKIGMVFQNPDNQFvgATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 119 LIYPLtadqEVEPLTCSGMVD----LLKNVDLDYLLDRYPPekevnwgdELSLGEQQRLGMARLFYHKPKFAILDECTSA 194
Cdd:PRK13650 103 VAFGL----ENKGIPHEEMKErvneALELVGMQDFKEREPA--------RLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1776568118 195 VTTDMEERFCAKVRAM----GTSCITISHRPALVAFHDVVL 231
Cdd:PRK13650 171 LDPEGRLELIKTIKGIrddyQMTVISITHDLDEVALSDRVL 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
718-888 |
1.29e-06 |
|
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: 49.74 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRLYkpshhfdeetasggifyvpqrpytclgtLRDQIIYPLSREE-AELRelklygqg 796
Cdd:cd03214 32 GPNGAGKSTLLKTLAGLLKPSSGEIL----------------------------LDGKDLASLSPKElARKI-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 797 enavdatsildARLKTILENVRLNYLLEReeggwdanlNWEDiLSLGEQQRLGMARLFFHKPKFGILDECTNA----TSV 872
Cdd:cd03214 76 -----------AYVPQALELLGLAHLADR---------PFNE-LSGGERQRVLLARALAQEPPILLLDEPTSHldiaHQI 134
|
170
....*....|....*.
gi 1776568118 873 DVEEPLYRLAKDLGIT 888
Cdd:cd03214 135 ELLELLRRLARERGKT 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
31-193 |
1.30e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.14 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKV-VTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFY 103
Cdd:PRK13632 8 IKVENVSFsYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenlKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 104 VPQRPYTAF--GTLRDQLIYPLtadqEVEPLTCSGM----VDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMAR 177
Cdd:PRK13632 88 IFQNPDNQFigATVEDDIAFGL----ENKKVPPKKMkdiiDDLAKKVGMEDYLDKEP--------QNLSGGQKQRVAIAS 155
|
170
....*....|....*.
gi 1776568118 178 LFYHKPKFAILDECTS 193
Cdd:PRK13632 156 VLALNPEIIIFDESTS 171
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
707-880 |
1.56e-06 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 49.78 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 707 DVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYkpshhfdeetASGGIFYVPQRPYTCLGTLRDQIIYPLSREEAE 786
Cdd:cd03250 27 EVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS----------VPGSIAYVSQEPWIQNGTIRENILFGKPFDEER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 787 LRElklygqgenAVDA------TSILDARLKTILenvrlnyllerEEGGwdanLNwediLSLGEQQRLGMARLFFHKPKF 860
Cdd:cd03250 97 YEK---------VIKAcalepdLEILPDGDLTEI-----------GEKG----IN----LSGGQKQRISLARAVYSDADI 148
|
170 180
....*....|....*....|
gi 1776568118 861 GILDECTNATSVDVEEPLYR 880
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHIFE 168
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
40-219 |
1.66e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 40 TPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG--------SDLNKEIFYVPQRP-YT 110
Cdd:PRK13637 16 TPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvklSDIRKKVGLVFQYPeYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 111 AFgtlrDQLIYPLTA---------DQEVEPLTCSGMvdllKNVDLDY--LLDRYPpekevnwgDELSLGEQQRLGMARLF 179
Cdd:PRK13637 96 LF----EETIEKDIAfgpinlglsEEEIENRVKRAM----NIVGLDYedYKDKSP--------FELSGGQKRRVAIAGVV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1776568118 180 YHKPKFAILDECTSAVTTDMEERFCAKVRAM----GTSCITISH 219
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSH 203
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
39-198 |
1.68e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 39 VTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGG--LWPLVSGHIVKPGVgSDLNKE--------IFYVPQRP 108
Cdd:CHL00131 15 ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE-SILDLEpeerahlgIFLAFQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 109 YT------------AFGTLRDQLIYPltadqEVEPLTCSGMV-DLLKNVDLD-YLLDRYppekeVNWGdeLSLGEQQR-- 172
Cdd:CHL00131 94 IEipgvsnadflrlAYNSKRKFQGLP-----ELDPLEFLEIInEKLKLVGMDpSFLSRN-----VNEG--FSGGEKKRne 161
|
170 180
....*....|....*....|....*..
gi 1776568118 173 -LGMARLfyhKPKFAILDECTSAVTTD 198
Cdd:CHL00131 162 iLQMALL---DSELAILDETDSGLDID 185
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
715-865 |
1.71e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.01 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 715 LVTGPNGSGKSSVFRVLR-GLWPIVSGRLYKPSHHFDEETASGGI---FYVPQRPYTClgtLRDQ--IIYPLSREEAELR 788
Cdd:COG0419 27 LIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGSEEASVeleFEHGGKRYRI---ERRQgeFAEFLEAKPSERK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 789 EL--KLYG--QGENAVDATSILDARLKTILENVRLNYLLEREEGGWDANLNWEDILSLGEQQRLGMARLFFHKPKFGILD 864
Cdd:COG0419 104 EAlkRLLGleIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLLSLILDFGSLD 183
|
.
gi 1776568118 865 E 865
Cdd:COG0419 184 E 184
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
47-235 |
2.08e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.46 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKE--------IFYVPQRPYTAFG---T 114
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlAKLNRAqrkafrrdIQMVFQDSISAVNprkT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 115 LRDQLIYPL-------TADQEVEPLtcsgmvDLLKNVDLD-YLLDRYPPekevnwgdELSLGEQQRLGMARLFYHKPKFA 186
Cdd:PRK10419 108 VREIIREPLrhllsldKAERLARAS------EMLRAVDLDdSVLDKRPP--------QLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776568118 187 ILDECTS-----------AVTTDMEERFcakvramGTSCITISHRPALVA-FHDVVLSLDG 235
Cdd:PRK10419 174 ILDEAVSnldlvlqagviRLLKKLQQQF-------GTACLFITHDLRLVErFCQRVMVMDN 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
716-868 |
2.09e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.60 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 716 VTGPNGSGKSSVFRVLRGLWPIVSGRLYKPShhfDEETAsggifYVPQRPYTCLG-TLRDQIIY---PLSREEAELREL- 790
Cdd:COG0488 29 LVGRNGAGKSTLLKILAGELEPDSGEVSIPK---GLRIG-----YLPQEPPLDDDlTVLDTVLDgdaELRALEAELEELe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 791 ----------KLYGQGENAVDATSI--LDARLKTILENVRLnyllerEEGGWDANLNwedILSLGEQQRLGMARLFFHKP 858
Cdd:COG0488 101 aklaepdedlERLAELQEEFEALGGweAEARAEEILSGLGF------PEEDLDRPVS---ELSGGWRRRVALARALLSEP 171
|
170
....*....|
gi 1776568118 859 KFGILDECTN 868
Cdd:COG0488 172 DLLLLDEPTN 181
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
41-193 |
2.64e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.08 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 41 PTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDL-NKEIFYVPQRPYTAFGTLRDQL 119
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdKKSLLEVRKTVGIVFQNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 120 IYPlTADQEVE--PLTC--------SGMVDLLKNVDLDYlLDRYPPEkevnwgdELSLGEQQRLGMARLFYHKPKFAILD 189
Cdd:PRK13639 92 FAP-TVEEDVAfgPLNLglskeeveKRVKEALKAVGMEG-FENKPPH-------HLSGGQKKRVAIAGILAMKPEIIVLD 162
|
....
gi 1776568118 190 ECTS 193
Cdd:PRK13639 163 EPTS 166
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
31-219 |
2.86e-06 |
|
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: 50.04 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTptgnvlvkDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---------------VKPGVG- 94
Cdd:COG0411 12 KRFGGLVAVD--------DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrditglpphriARLGIAr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 95 --------SDL----NKEIFYVPQRPYTAFGTLRDQLIYPLT---ADQEVEpltcsgmvDLLKNVDLDYLLDRYPpekev 159
Cdd:COG0411 84 tfqnprlfPELtvleNVLVAAHARLGRGLLAALLRLPRARREereARERAE--------ELLERVGLADRADEPA----- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776568118 160 nwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRA----MGTSCITISH 219
Cdd:COG0411 151 ---GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlrdeRGITILLIEH 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
45-220 |
3.36e-06 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 49.29 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 45 VLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKEIFYVPQRpytaFGTLRDQL-IYP- 122
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF--DVVKEPAEARRR----LGFVSDSTgLYDr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 123 LTADQEVE---------PLTCSGMVD-LLKNVDLDYLLDRYppekevnwGDELSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:cd03266 93 LTARENLEyfaglyglkGDELTARLEeLADRLGMEELLDRR--------VGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
|
170 180 190
....*....|....*....|....*....|.
gi 1776568118 193 SA---VTTDMEERFCAKVRAMGTSCITISHR 220
Cdd:cd03266 165 TGldvMATRALREFIRQLRALGKCILFSTHI 195
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
709-888 |
4.02e-06 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 49.32 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 709 VPEKSLL-VTGPNGSGKSSVFRVLRGLWPIVSGRLykpsHHFDE--ETASGGIFYVPQRP------------------YT 767
Cdd:COG1121 29 IPPGEFVaIVGPNGAGKSTLLKAILGLLPPTSGTV----RLFGKppRRARRRIGYVPQRAevdwdfpitvrdvvlmgrYG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 768 CLGTLRdqiiyPLSREEAElrelklygqgenAVDAtsildarlktILENVRLNYLLEReeggwdanlnweDI--LSLGEQ 845
Cdd:COG1121 105 RRGLFR-----RPSRADRE------------AVDE----------ALERVGLEDLADR------------PIgeLSGGQQ 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1776568118 846 QRLGMARLFFHKPKFGILDECTnaTSVDV--EEPLYRLAKDL---GIT 888
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPF--AGVDAatEEALYELLRELrreGKT 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
680-913 |
4.06e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 49.66 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 680 SAKDVISFSEVDIITPAQKLLaRQLTCDVvPEKSLL-VTGPNGSGKSSVFRVLRGLWPI------VSGR-LYKPSHHFDE 751
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAIL-KDITIKI-PNNSIFgIMGPSGSGKSTLLKVLNRLIEIydskikVDGKvLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 752 ETAS-----GGIFYVPQrPYTCLgTLRDQIIYPL-SREEAELRELKlygqgenavdatSILDARLKTIlenvrlnyller 825
Cdd:PRK14246 84 DAIKlrkevGMVFQQPN-PFPHL-SIYDNIAYPLkSHGIKEKREIK------------KIVEECLRKV------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 826 eeGGWDA---NLNW-EDILSLGEQQRLGMARLFFHKPKFGILDECTN----ATSVDVEEPLYRLAKDLGITRPALIPFHA 897
Cdd:PRK14246 138 --GLWKEvydRLNSpASQLSGGQQQRLTIARALALKPKVLLMDEPTSmidiVNSQAIEKLITELKNEIAIVIVSHNPQQV 215
|
250 260
....*....|....*....|.
gi 1776568118 898 LELR-----LVDGEEPECGAN 913
Cdd:PRK14246 216 ARVAdyvafLYNGELVEWGSS 236
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
52-238 |
4.56e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.33 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 52 LRVESGS-----NLLITGPNGSGKSSLFRVLGGLwplvsghiVKPGVG---SDLNKeIFYVPQRPYTAFGTLRDQLIYPL 123
Cdd:cd03237 15 LEVEGGSiseseVIGILGPNGIGKTTFIKMLAGV--------LKPDEGdieIELDT-VSYKPQYIKADYEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 124 TADQEVEPLTcsgMVDLLKNVDLDYLLDRyppekEVNwgdELSLGEQQRLGMARLFYHKPKFAILDEcTSAvTTDMEERF 203
Cdd:cd03237 86 TKDFYTHPYF---KTEIAKPLQIEQILDR-----EVP---ELSGGELQRVAIAACLSKDADIYLLDE-PSA-YLDVEQRL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1776568118 204 cakvraMGTSCIT--ISH--RPALVAFHDV---------VLSLDGEGG 238
Cdd:cd03237 153 ------MASKVIRrfAENneKTAFVVEHDIimidyladrLIVFEGEPS 194
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
702-875 |
4.57e-06 |
|
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: 48.64 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 702 RQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLY---KPSHHFDEETASGGIFYVPQRPYTCLGTLRDQIIy 778
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 779 PLSREEaelrelklygqgenavdatsilDARLKTILENVRLNYLLEREEGGWDANL-NWEDILSLGEQQRLGMARLFFHK 857
Cdd:cd03244 100 PFGEYS----------------------DEELWQALERVGLKEFVESLPGGLDTVVeEGGENLSVGQRQLLCLARALLRK 157
|
170
....*....|....*...
gi 1776568118 858 PKFGILDECTnaTSVDVE 875
Cdd:cd03244 158 SKILVLDEAT--ASVDPE 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-195 |
4.70e-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: 51.10 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 2 LISKELSADDKKSSLQSAGSRNYLTEANyVEFSGVKVVTPTGNVLVkdlfLRVESGSNLLITGPNGSGKSSLFRVLGGLW 81
Cdd:TIGR00957 614 LSHEELEPDSIERRTIKPGEGNSITVHN-ATFTWARDLPPTLNGIT----FSIPEGALVAVVGQVGCGKSSLLSALLAEM 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 82 PLVSGHIVKPGvgsdlnkEIFYVPQRPYTAFGTLRDQLIY--PLTADQEVEPL-TCSGMVDL--LKNVDLDYLldrypPE 156
Cdd:TIGR00957 689 DKVEGHVHMKG-------SVAYVPQQAWIQNDSLRENILFgkALNEKYYQQVLeACALLPDLeiLPSGDRTEI-----GE 756
|
170 180 190
....*....|....*....|....*....|....*....
gi 1776568118 157 KEVNwgdeLSLGEQQRLGMARLFYHKPKFAILDECTSAV 195
Cdd:TIGR00957 757 KGVN----LSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
46-220 |
5.04e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 46 LVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV--KPGVGSDL---NKEIFYVPQR----PYTafgTLR 116
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILfeRQSIKKDLctyQKQLCFVGHRsginPYL---TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 117 DQLIYPLTADQeveplTCSGMVDLLKNVDLDYLLDrYPpekevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVT 196
Cdd:PRK13540 93 ENCLYDIHFSP-----GAVGITELCRLFSLEHLID-YP-------CGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*..
gi 1776568118 197 TDMEERFCAKV---RAMGTSCITISHR 220
Cdd:PRK13540 160 ELSLLTIITKIqehRAKGGAVLLTSHQ 186
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
48-223 |
5.69e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 48.80 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 48 KDLFLRVESGSNLLITGPNGSGKSSLFRVLGG--LWPLVSGHI-VKpgvGSDLN---------KEIFYVPQRPYTAFGT- 114
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTIlFK---GQDLLelepderarAGLFLAFQYPEEIPGVs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 115 ----LRDQLIYPLTADQEvEPLTCSGMVDLLKNVDLDYLLDRYPPEKEVNWGdeLSLGEQQR---LGMARLfyhKPKFAI 187
Cdd:TIGR01978 94 nlefLRSALNARRSARGE-EPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEG--FSGGEKKRneiLQMALL---EPKLAI 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 1776568118 188 LDECTSAVTTDMEERFCA---KVRAMGTSCITISHRPAL 223
Cdd:TIGR01978 168 LDEIDSGLDIDALKIVAEginRLREPDRSFLIITHYQRL 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
43-192 |
6.20e-06 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 48.52 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWP------LVSGH-IVKPgvGSDLNKEIFYVPQRPytafgTL 115
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKptsgraTVAGHdVVRE--PREVRRRIGIVFQDL-----SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 116 RDQL-----------IYPL---TADQEVEpltcsgmvDLLKNVDL----DYLLDRYppekevnwgdelSLGEQQRLGMAR 177
Cdd:cd03265 85 DDELtgwenlyiharLYGVpgaERRERID--------ELLDFVGLleaaDRLVKTY------------SGGMRRRLEIAR 144
|
170
....*....|....*
gi 1776568118 178 LFYHKPKFAILDECT 192
Cdd:cd03265 145 SLVHRPEVLFLDEPT 159
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
62-234 |
6.44e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 62 ITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYVPQRPYTAFGTLRDQLiypltadqevEPLTCS 135
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDiskfglMDLRKVLGIIPQAPVLFSGTVRFNL----------DPFNEH 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 136 GMVDLLKNVDLDYLLD--RYPP---EKEVNWGDE-LSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRA 209
Cdd:PLN03130 1340 NDADLWESLERAHLKDviRRNSlglDAEVSEAGEnFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE 1419
|
170 180
....*....|....*....|....*..
gi 1776568118 210 MGTSC--ITISHRPALVAFHDVVLSLD 234
Cdd:PLN03130 1420 EFKSCtmLIIAHRLNTIIDCDRILVLD 1446
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
49-225 |
6.59e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.33 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 49 DLFLRveSGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG--VGSDLNKEIFYVPQRPYTAFGT---LRDQLIYpl 123
Cdd:PRK10908 22 TFHMR--PGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdITRLKNREVPFLRRQIGMIFQDhhlLMDRTVY-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 124 taDQEVEPLTCSGMV--DLLKNVD--LDY--LLDryppeKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 197
Cdd:PRK10908 98 --DNVAIPLIIAGASgdDIRRRVSaaLDKvgLLD-----KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190
....*....|....*....|....*....|.
gi 1776568118 198 DMEE---RFCAKVRAMGTSCITISHRPALVA 225
Cdd:PRK10908 171 ALSEgilRLFEEFNRVGVTVLMATHDIGLIS 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
52-236 |
7.64e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.24 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 52 LRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG-SDLNKEifyvpQRpytafGTLRDQ----------LI 120
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlHQMDEE-----AR-----AKLRAKhvgfvfqsfmLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 121 YPLTADQEVE-PLTCSGM---------VDLLKNVDLDYLLDRYPPEkevnwgdeLSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:PRK10584 101 PTLNALENVElPALLRGEssrqsrngaKALLEQLGLGKRLDHLPAQ--------LSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1776568118 191 CTSAVTTDMEERFCAKV----RAMGTSCITISHRPALVAFHDVVLSL-DGE 236
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQLAARCDRRLRLvNGQ 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
31-232 |
9.66e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 49.07 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTptgnvlvkDLFLRVESGSNLLITGPNGSGKSSLFRVLGG-LWP-----LVSGHIVKPGVGSDLNKEIFYV 104
Cdd:PRK09536 11 VEFGDTTVLD--------GVDLSVREGSLVGLVGPNGAGKTTLLRAINGtLTPtagtvLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 105 PQRPYTAFGTLRDQLI----YPLTADQEVEPLTCSGMVD-LLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLF 179
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVemgrTPHRSRFDTWTETDRAAVErAMERTGVAQFADRPV--------TSLSGGERQRVLLARAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1776568118 180 YHKPKFAILDECTSAVTTDMEERFCAKVRAMGTscitiSHRPALVAFHDVVLS 232
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVD-----DGKTAVAAIHDLDLA 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
47-88 |
1.41e-05 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 47.53 E-value: 1.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI 88
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
685-865 |
1.50e-05 |
|
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: 47.33 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 685 ISFSEVDIITPAQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYkpshHFDEETASGGIF----- 759
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL----VDGKDITKKNLRelrrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 760 --YVPQRPytclgtlRDQIIYP--------------LSREEAElrelklygqgenavdatsildARLKTILENVRLNYLL 823
Cdd:COG1122 77 vgLVFQNP-------DDQLFAPtveedvafgpenlgLPREEIR---------------------ERVEEALELVGLEHLA 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1776568118 824 ERE--EggwdanlnwediLSLGEQQRLGMARLFFHKPKFGILDE 865
Cdd:COG1122 129 DRPphE------------LSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
653-867 |
1.76e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 48.69 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 653 ELEELLDAAQSGDLSTDNLLQSQRT-ALSAKDVISFSevdiitPAQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVL 731
Cdd:PRK11174 323 SLVTFLETPLAHPQQGEKELASNDPvTIEAEDLEILS------PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 732 RGLWPivsgrlYKPS--------HHFDEETASGGIFYVPQRPYTCLGTLRDQIIypLSREEAElrelklygqgenavdat 803
Cdd:PRK11174 397 LGFLP------YQGSlkingielRELDPESWRKHLSWVGQNPQLPHGTLRDNVL--LGNPDAS----------------- 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776568118 804 silDARLKTILENVRLNYLLEREEGGWDANLNWEDI-LSLGEQQRLGMARLFFHKPKFGILDECT 867
Cdd:PRK11174 452 ---DEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAgLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
52-194 |
1.87e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 52 LRVESGSNLLITGPNGSGKSSLFR-VLGGLWPLVSGHIVKPGvgsdlnkEIFYVPQRPYTAFGTLRDQLIY--PLTADQE 128
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-------TVAYVPQVSWIFNATVRDNILFgsPFDPERY 710
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 129 VEPLTCSGM---VDLLKNVDLDYLLDRyppekevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTSA 194
Cdd:PLN03130 711 ERAIDVTALqhdLDLLPGGDLTEIGER---------GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
698-865 |
2.00e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.72 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 698 KLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYkpshhfdeetasggifyvpqrpytclgtLRDQii 777
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL----------------------------WQGE-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 778 yPLSREEAELRELKLYGQGENAVDatsildaRLKTILENVRLNYLLE---REEGGWDA----NL-NWEDI----LSLGEQ 845
Cdd:PRK13538 64 -PIRRQRDEYHQDLLYLGHQPGIK-------TELTALENLRFYQRLHgpgDDEALWEAlaqvGLaGFEDVpvrqLSAGQQ 135
|
170 180
....*....|....*....|
gi 1776568118 846 QRLGMARLFFHKPKFGILDE 865
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDE 155
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
31-219 |
2.18e-05 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 47.11 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVkVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG--VGSDLNKEIFYVPQRp 108
Cdd:cd03261 1 IELRGL-TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedISGLSEAELYRLRRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 109 ytaFG------------TLRDQLIYPL---TADQEVEpltCSGMVDL-LKNVDLDYLLDRYPpekevnwgDELSLGEQQR 172
Cdd:cd03261 79 ---MGmlfqsgalfdslTVFENVAFPLrehTRLSEEE---IREIVLEkLEAVGLRGAEDLYP--------AELSGGMKKR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776568118 173 LGMAR--------LFYHKPkFAILDECTSAVTTDMEERFcakVRAMGTSCITISH 219
Cdd:cd03261 145 VALARalaldpelLLYDEP-TAGLDPIASGVIDDLIRSL---KKELGLTSIMVTH 195
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
46-193 |
2.26e-05 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 46.88 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 46 LVKDLFLRVESGSNLLITGPNGSGKSSLF-----RVLGGlwPLVSGHIVKPGVGSD---LNKEIFYVPQRPYTAFG-TLR 116
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQILFNGQPRKpdqFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 117 DQLIYPLT----------ADQEVEPltcsgmVDLLKNVDLDYLLDRYPPekevnwgdELSLGEQQRLGMARLFYHKPKFA 186
Cdd:cd03234 100 ETLTYTAIlrlprkssdaIRKKRVE------DVLLRDLALTRIGGNLVK--------GISGGERRRVSIAVQLLWDPKVL 165
|
....*..
gi 1776568118 187 ILDECTS 193
Cdd:cd03234 166 ILDEPTS 172
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
716-873 |
2.32e-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: 48.39 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 716 VTGPNGSGKSSVFRVLRGLWPIVSGrlykpshhfdEETASGGIF--YVPQRPY-----TCLGTLR-------------DQ 775
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNG----------EARPQPGIKvgYLPQEPQldptkTVRENVEegvaeikdaldrfNE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 776 IIYPLSREEAELRELkLYGQGE--NAVDATSI--LDARLKTILENVRLNyllereegGWDANLNwedILSLGEQQRLGMA 851
Cdd:TIGR03719 106 ISAKYAEPDADFDKL-AAEQAElqEIIDAADAwdLDSQLEIAMDALRCP--------PWDADVT---KLSGGERRRVALC 173
|
170 180
....*....|....*....|....*
gi 1776568118 852 RLFFHKPKFGILDECTN---ATSVD 873
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNhldAESVA 198
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
47-193 |
2.77e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.00 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSDLNKEIFYVPQRPYTAFGTLRDQLIypLTAD 126
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIV--ATIV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776568118 127 QE----------VEPLTCSGMVD-LLKNVDLdYLLDRYPPEKevnwgdeLSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:PRK13633 104 EEdvafgpenlgIPPEEIRERVDeSLKKVGM-YEYRRHAPHL-------LSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
146-264 |
3.20e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 146 LDYLLDRYPPEKEVN---WGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDME---ERFCAKVRAMG-TSCITIS 218
Cdd:PTZ00265 1337 IDEFIESLPNKYDTNvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEkliEKTIVDIKDKAdKTIITIA 1416
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1776568118 219 HRPALVAFHDVVLSLDGEggwkvhyKSENSSVQSEGEIDLTVSETD 264
Cdd:PTZ00265 1417 HRIASIKRSDKIVVFNNP-------DRTGSFVQAHGTHEELLSVQD 1455
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
685-940 |
3.36e-05 |
|
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: 46.45 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 685 ISFSEVDIITPAQKLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHFDEETASG---GIFYV 761
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 762 PQRpyTCL--GTLRDQIIYplSREEAELRELklygqgENAVDAtsildARLKTILENVRLNYLLEREEGGWDanlnwedi 839
Cdd:cd03253 81 PQD--TVLfnDTIGYNIRY--GRPDATDEEV------IEAAKA-----AQIHDKIMRFPDGYDTIVGERGLK-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 840 LSLGEQQRLGMARLFFHKPKFGILDECTNATSVDVEEPLYRLAKDLGITRPALIPFHalelrlvdgeepecganlkltll 919
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAH----------------------- 194
|
250 260
....*....|....*....|.
gi 1776568118 920 fRVDMIMEKDKfLIMLRTGQV 940
Cdd:cd03253 195 -RLSTIVNADK-IIVLKDGRI 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
46-192 |
3.45e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.35 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 46 LVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPgvGSDLNKeifyvpqRPYTAFGTLRDQ---LIYP 122
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN--GQPMSK-------LSSAAKAELRNQklgFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 123 -------LTADQEVE-PLTCSGM---------VDLLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKF 185
Cdd:PRK11629 95 fhhllpdFTALENVAmPLLIGKKkpaeinsraLEMLAAVGLEHRANHRP--------SELSGGERQRVAIARALVNNPRL 166
|
....*..
gi 1776568118 186 AILDECT 192
Cdd:PRK11629 167 VLADEPT 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
43-190 |
3.62e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.75 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGvgsdlNKEIFYVPQRP-YTAFGTLRDQLiy 121
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----GLRIGYLPQEPpLDDDLTVLDTV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 122 pLTADQEVEPLtcsgMVDL----LKNVDLDYLLDRY-------------------------------PPEKEVNwgdELS 166
Cdd:COG0488 83 -LDGDAELRAL----EAELeeleAKLAEPDEDLERLaelqeefealggweaearaeeilsglgfpeeDLDRPVS---ELS 154
|
170 180
....*....|....*....|....
gi 1776568118 167 LGEQQRLGMARLFYHKPKFAILDE 190
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDE 178
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
40-193 |
4.80e-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: 47.60 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 40 TPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLfrvLGGLWPLVS--GHIVKPGVGSD------LNKEIFYVPQRPYTA 111
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTL---LSALLRLLSteGEIQIDGVSWNsvtlqtWRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 112 FGTLRDQL-IYPLTADQEVEPLTcsgmvdllKNVDLDYLLDRYPPEKE---VNWGDELSLGEQQRLGMARLFYHKPKFAI 187
Cdd:TIGR01271 1305 SGTFRKNLdPYEQWSDEEIWKVA--------EEVGLKSVIEQFPDKLDfvlVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
....*.
gi 1776568118 188 LDECTS 193
Cdd:TIGR01271 1377 LDEPSA 1382
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
718-872 |
5.11e-05 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 45.82 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRL----YKPSHHFDEETASGGIFYVPQRPYTCLgTLRDQIIYpLSReeaelrelkLY 793
Cdd:cd03266 38 GPNGAGKTTTLRMLAGLLEPDAGFAtvdgFDVVKEPAEARRRLGFVSDSTGLYDRL-TARENLEY-FAG---------LY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 794 G-QGENavdatsiLDARLKTILENVRLNYLLEREEGGwdanlnwediLSLGEQQRLGMARLFFHKPKFGILDECTNATSV 872
Cdd:cd03266 107 GlKGDE-------LTARLEELADRLGMEELLDRRVGG----------FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-210 |
6.25e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 34 SGVKVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG--VGSDLNKE-IFYVPQRP-- 108
Cdd:PRK15056 10 NDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqpTRQALQKNlVAYVPQSEev 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 109 ----------------YTAFGTLRdqliYPLTADQEVepltcsgMVDLLKNVD-LDYlldRYppeKEVNwgdELSLGEQQ 171
Cdd:PRK15056 90 dwsfpvlvedvvmmgrYGHMGWLR----RAKKRDRQI-------VTAALARVDmVEF---RH---RQIG---ELSGGQKK 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1776568118 172 RLGMARLFYHKPKFAILDECTSAVTTDMEERFCAKVRAM 210
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL 188
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
47-202 |
6.70e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.94 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWP------LVSGHIVKPGVGSDLNKEIFYVPQRPYTAF------GT 114
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEptsgelLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLnprqriSQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 115 LRDqliYPLTADQEVEPLT-CSGMVDLLKNVDLdylldryPPEKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECTS 193
Cdd:PRK15112 109 ILD---FPLRLNTDLEPEQrEKQIIETLRQVGL-------LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
....*....
gi 1776568118 194 AVttDMEER 202
Cdd:PRK15112 179 SL--DMSMR 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
43-192 |
7.07e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRV-LGGLWPlVSGHIvkpGVGSDLnkEIFYVPQrpYTAF----GTLRD 117
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRI---HCGTKL--EVAYFDQ--HRAEldpeKTVMD 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776568118 118 QLiypltAD--QEVepltcsgMVDLLKNVDLDYLLD-RYPPEKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECT 192
Cdd:PRK11147 403 NL-----AEgkQEV-------MVNGRPRHVLGYLQDfLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
57-224 |
8.01e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 57 GSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGSD---------LNKEIFYVPQRPYTAFGTlRDQLIYPLtadq 127
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspgklqaLRRDIQFIFQDPYASLDP-RQTVGDSI---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 128 eVEPLTCSGMVD----------LLKNVDLDylldrypPEKEVNWGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 197
Cdd:PRK10261 425 -MEPLRVHGLLPgkaaaarvawLLERVGLL-------PEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190
....*....|....*....|....*....|.
gi 1776568118 198 DMEERFCAKV----RAMGTSCITISHRPALV 224
Cdd:PRK10261 497 SIRGQIINLLldlqRDFGIAYLFISHDMAVV 527
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
41-234 |
8.41e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 45.75 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 41 PTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVGS-------DLNKEIFYVPQRPYTAF- 112
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqGIRKLVGIVFQNPETQFv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 113 -GTLRDQLIYPlTADQEVEPLTCSGMVDL-LKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:PRK13644 92 gRTVEEDLAFG-PENLCLPPIEIRKRVDRaLAEIGLEKYRHRSP--------KTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1776568118 191 CTSAVTTDMEERFCAKVRAM---GTSCITISHRPALVAFHDVVLSLD 234
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLhekGKTIVYITHNLEELHDADRIIVMD 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
47-190 |
9.38e-05 |
|
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: 44.84 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVgsDLNKE---------IFYVPQRPyTAFG--TL 115
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ--DITKLpmhkrarlgIGYLPQEA-SIFRklTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 116 RDQL-----IYPLTADQEVEPLtcsgmVDLLKNVDLDYLLDRYppekevnwGDELSLGEQQRLGMARLFYHKPKFAILDE 190
Cdd:cd03218 93 EENIlavleIRGLSKKEREEKL-----EELLEEFHITHLRKSK--------ASSLSGGERRRVEIARALATNPKFLLLDE 159
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
37-199 |
1.39e-04 |
|
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: 44.42 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 37 KVVTPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSG--HIVKPGVGSDLNK---EIFYVPQRPyTA 111
Cdd:cd03263 8 KTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtaYINGYSIRTDRKAarqSLGYCPQFD-AL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 112 FGTL--RDQL--------IYPLTADQEVEpltcsgmvDLLKNVDL-DYLldryppEKEVNwgdELSLGEQQRL--GMARL 178
Cdd:cd03263 87 FDELtvREHLrfyarlkgLPKSEIKEEVE--------LLLRVLGLtDKA------NKRAR---TLSGGMKRKLslAIALI 149
|
170 180
....*....|....*....|.
gi 1776568118 179 FYhkPKFAILDEctsaVTTDM 199
Cdd:cd03263 150 GG--PSVLLLDE----PTSGL 164
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-245 |
1.44e-04 |
|
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: 45.70 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 37 KVVTPTGNVLvKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV-KPGVgsdlnkEIFYVPQRPY------ 109
Cdd:TIGR03719 12 KVVPPKKEIL-KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARpQPGI------KVGYLPQEPQldptkt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 110 ------TAFGTLRDQL-----IYPLTA--DQEVEPL-----TCSGMVDLLKNVDLDYLLD------RYPP-EKEVNwgdE 164
Cdd:TIGR03719 85 vrenveEGVAEIKDALdrfneISAKYAepDADFDKLaaeqaELQEIIDAADAWDLDSQLEiamdalRCPPwDADVT---K 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 165 LSLGEQQRLGMARLFYHKPKFAILDECTS---AVTTDMEERFCAKVRamGTsCITISH-RpalvAFHDVV----LSLD-G 235
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNhldAESVAWLERHLQEYP--GT-VVAVTHdR----YFLDNVagwiLELDrG 234
|
250
....*....|.
gi 1776568118 236 EG-GWKVHYKS 245
Cdd:TIGR03719 235 RGiPWEGNYSS 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
47-234 |
1.59e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 45.72 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEIFYVPQRPYTAFGTLRDQLI 120
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDirtvtrASLRRNIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 121 Y--PLTADQEV-EPLTCSGMVDLLKNVDLDYllDRYPPEKevnwGDELSLGEQQRLGMARLFYHKPKFAILDECTSAVTT 197
Cdd:PRK13657 431 VgrPDATDEEMrAAAERAQAHDFIERKPDGY--DTVVGER----GRQLSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180 190
....*....|....*....|....*....|....*....
gi 1776568118 198 DMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:PRK13657 505 ETEAKVKAALDELmkGRTTFIIAHRLSTVRNADRILVFD 543
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
704-884 |
1.61e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.38 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 704 LTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLwpivsGRLyKPshhfdEETASGGIFYvpqrpytclgtlRDQIIYPLSRE 783
Cdd:PRK14239 24 VSLDFYPNEITALIGPSGSGKSTLLRSINRM-----NDL-NP-----EVTITGSIVY------------NGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 784 EAELR-ELKLYGQGEN----AVDATSILDARLKTILENVRLNYLLEREEGGwdANLnWEDI----------LSLGEQQRL 848
Cdd:PRK14239 81 TVDLRkEIGMVFQQPNpfpmSIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASI-WDEVkdrlhdsalgLSGGQQQRV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1776568118 849 GMARLFFHKPKFGILDECTNA----TSVDVEEPLYRLAKD 884
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSAldpiSAGKIEETLLGLKDD 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
702-885 |
1.73e-04 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 43.76 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 702 RQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLykpshhfdEETASGGIFYVPQR---PYTCLGTLRDQIIY 778
Cdd:NF040873 9 HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------RRAGGARVAYVPQRsevPDSLPLTVRDLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 779 PLSREEAELRELklygqgeNAVDATSILDArlktiLENVRLNYLLEREEGGwdanlnwediLSLGEQQRLGMARLFFHKP 858
Cdd:NF040873 81 GRWARRGLWRRL-------TRDDRAAVDDA-----LERVGLADLAGRQLGE----------LSGGQRQRALLAQGLAQEA 138
|
170 180
....*....|....*....|....*..
gi 1776568118 859 KFGILDECTNATSVDVEEPLYRLAKDL 885
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEE 165
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
52-220 |
1.85e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.40 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 52 LRVESGSNLLITGPNGSGKSSLFRVLGGLWP------LVSGHIVKP---------GVGsdlnkeifYVPQRPytafgtlr 116
Cdd:COG3845 26 LTVRPGEIHALLGENGAGKSTLMKILYGLYQpdsgeiLIDGKPVRIrsprdaialGIG--------MVHQHF-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 117 dQLIYPLTADQEV----EPLTcSGMVDLLK-NVDLDYLLDRY----PPEKEVnwgDELSLGEQQRLGMARLFYHKPKFAI 187
Cdd:COG3845 90 -MLVPNLTVAENIvlglEPTK-GGRLDRKAaRARIRELSERYgldvDPDAKV---EDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1776568118 188 LDECTsAVTTDME-ERF---CAKVRAMGTSCITISHR 220
Cdd:COG3845 165 LDEPT-AVLTPQEaDELfeiLRRLAAEGKSIIFITHK 200
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-234 |
1.99e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 14 SSLQSAGSRNylTEANYVEFSGVKVVTPTGNVLV-KDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPG 92
Cdd:PTZ00243 1294 ASPTSAAPHP--VQAGSLVFEGVQMRYREGLPLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 93 --VGS----DLNKEIFYVPQRPYTAFGTLRdqliypltadQEVEPLTCSGMVDLLKNVDLDYLLDRYPPEKE------VN 160
Cdd:PTZ00243 1372 reIGAyglrELRRQFSMIPQDPVLFDGTVR----------QNVDPFLEASSAEVWAALELVGLRERVASESEgidsrvLE 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776568118 161 WGDELSLGEQQRLGMARLFYHK-PKFAILDECTSAVTTDMEERFCAKVRAM--GTSCITISHRPALVAFHDVVLSLD 234
Cdd:PTZ00243 1442 GGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAfsAYTVITIAHRLHTVAQYDKIIVMD 1518
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
50-108 |
2.00e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.68 E-value: 2.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776568118 50 LFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---VKPGVGSDLNKEIFYVPQRP 108
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidGKTATRGDRSRFMAYLGHLP 91
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
43-200 |
2.05e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGhIVKpgvGSDlNKEIFYVPQRPYTAFG---TLRD-- 117
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG-TVK---WSE-NANIGYYAQDHAYDFEndlTLFDwm 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 118 -QLIYPLTADQEVEpltcsGMV--------DLLKNVDLdylldryppekevnwgdeLSLGEQQRLGMARLFYHKPKFAIL 188
Cdd:PRK15064 406 sQWRQEGDDEQAVR-----GTLgrllfsqdDIKKSVKV------------------LSGGEKGRMLFGKLMMQKPNVLVM 462
|
170
....*....|..
gi 1776568118 189 DECTSAVttDME 200
Cdd:PRK15064 463 DEPTNHM--DME 472
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
58-195 |
2.37e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 58 SNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPgvGSDLNKE-IFYVPQRPYTAFGTLRDQLIYPlTADQEVEPLTCSG 136
Cdd:PRK13652 31 SRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR--GEPITKEnIREVRKFVGLVFQNPDDQIFSP-TVEQDIAFGPINL 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 137 MVD----------LLKNVDLDYLLDRYPpekevnwgDELSLGEQQRLGMARLFYHKPKFAILDECTSAV 195
Cdd:PRK13652 108 GLDeetvahrvssALHMLGLEELRDRVP--------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
702-898 |
2.78e-04 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 43.76 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 702 RQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHFDEETASG---GIFYVPQRPYTCLGTLRDQIIY 778
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrrQIGLVSQDVFLFNDTVAENIAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 779 plSREEAELRElklygqgenavdatsILDArlktiLENVRLNYLLEREEGGWDANLNWEDI-LSLGEQQRLGMARLFFHK 857
Cdd:cd03251 99 --GRPGATREE---------------VEEA-----ARAANAHEFIMELPEGYDTVIGERGVkLSGGQRQRIAIARALLKD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1776568118 858 PKFGILDECTNAtsVDVE------EPLYRLAKDlgitRPALIPFHAL 898
Cdd:cd03251 157 PPILILDEATSA--LDTEserlvqAALERLMKN----RTTFVIAHRL 197
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
40-89 |
2.96e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.92 E-value: 2.96e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1776568118 40 TPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIV 89
Cdd:COG1101 15 TVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
718-865 |
3.40e-04 |
|
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: 42.89 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRLYkpshhFDEETASG------GIFYVPQRP--YTCLgTLRDQIIYPLsreeaelrE 789
Cdd:cd03259 33 GPSGCGKTTLLRLIAGLERPDSGEIL-----IDGRDVTGvpperrNIGMVFQDYalFPHL-TVAENIAFGL--------K 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776568118 790 LKLYGQGEnavdatsiLDARLKTILENVRLNYLLEReeggwdanlnWEDILSLGEQQRLGMARLFFHKPKFGILDE 865
Cdd:cd03259 99 LRGVPKAE--------IRARVRELLELVGLEGLLNR----------YPHELSGGQQQRVALARALAREPSLLLLDE 156
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
47-88 |
4.00e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.15 E-value: 4.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI 88
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
33-220 |
4.96e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.89 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 33 FSGVKVVtptgnvlvKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---------VKPGVGSDLNkeIFY 103
Cdd:PRK15439 21 YSGVEVL--------KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpcarLTPAKAHQLG--IYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 104 VPQRPYT-AFGTLRDQLIYPLTADQEVEpltcSGMVDLLK--NVDLDylLDryppekeVNWGdELSLGEQQRLGMARLFY 180
Cdd:PRK15439 91 VPQEPLLfPNLSVKENILFGLPKRQASM----QKMKQLLAalGCQLD--LD-------SSAG-SLEVADRQIVEILRGLM 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1776568118 181 HKPKFAILDECTSAVTTDMEERFCAKVRAM---GTSCITISHR 220
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELlaqGVGIVFISHK 199
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
31-198 |
5.05e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.64 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGN---VLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGV------GSDLNKE- 100
Cdd:PRK11153 2 IELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 101 -----IF----YVPQRpyTAFgtlrDQLIYPLTA--------DQEVEPLtcsgmvdlLKNVDLDYLLDRYPPEkevnwgd 163
Cdd:PRK11153 82 rqigmIFqhfnLLSSR--TVF----DNVALPLELagtpkaeiKARVTEL--------LELVGLSDKADRYPAQ------- 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 1776568118 164 eLSLGEQQRLGMARLFYHKPKFAILDECTSAV---TTD 198
Cdd:PRK11153 141 -LSGGQKQRVAIARALASNPKVLLCDEATSALdpaTTR 177
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
718-865 |
5.18e-04 |
|
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: 42.65 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHFDEETASgGIFYVPQ-RPYTCLGTLRDQIIYplsreEAELRELKlygqg 796
Cdd:cd03269 33 GPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN-RIGYLPEeRGLYPKMKVIDQLVY-----LAQLKGLK----- 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776568118 797 enavdatsildarLKTILENVRlnYLLEREEGGWDANLNWEDiLSLGEQQRLGMARLFFHKPKFGILDE 865
Cdd:cd03269 102 -------------KEEARRRID--EWLERLELSEYANKRVEE-LSKGNQQKVQFIAAVIHDPELLILDE 154
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-231 |
5.41e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 46 LVKDL--F-LRVESGSN-----LLITGPNGSGKSSLFRVLGGlwplvsghIVKPGVGS-DLNKEIFYVPQRPYTAF-GTL 115
Cdd:PRK13409 346 LTKKLgdFsLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAG--------VLKPDEGEvDPELKISYKPQYIKPDYdGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 116 RDqLIYPLTADQEVEPLTcsgmVDLLKNVDLDYLLDRYppekeVNwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAV 195
Cdd:PRK13409 418 ED-LLRSITDDLGSSYYK----SEIIKPLQLERLLDKN-----VK---DLSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
|
170 180 190
....*....|....*....|....*....|....*....
gi 1776568118 196 ttDMEERF-CAKV--RAMGTSCITishrpALVAFHDVVL 231
Cdd:PRK13409 485 --DVEQRLaVAKAirRIAEEREAT-----ALVVDHDIYM 516
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
714-864 |
6.54e-04 |
|
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: 43.75 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 714 LLVTGPNGSGKSSVFRVLRGLWPIVSGRLykpSHhfdeetaSGGIFYVPQRPYTCLGTLRDQIIYPLSREEAELRELKLY 793
Cdd:TIGR01271 455 LAVAGSTGSGKSSLLMMIMGELEPSEGKI---KH-------SGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKA 524
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776568118 794 GQGENAVdatSILDARLKTILenvrlnyllerEEGGWdanlnwedILSLGEQQRLGMARLFFHKPKFGILD 864
Cdd:TIGR01271 525 CQLEEDI---ALFPEKDKTVL-----------GEGGI--------TLSGGQRARISLARAVYKDADLYLLD 573
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
698-876 |
7.03e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 698 KLLARQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYkpshhfdeetASGGIFYVPQRPYTCLGTLRDQII 777
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW----------AERSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 778 YPLSREEAELrelklygqgENAVdATSILDARLKtilenvRLNYLLEREEGGWDANlnwediLSLGEQQRLGMARLFFHK 857
Cdd:PTZ00243 743 FFDEEDAARL---------ADAV-RVSQLEADLA------QLGGGLETEIGEKGVN------LSGGQKARVSLARAVYAN 800
|
170
....*....|....*....
gi 1776568118 858 PKFGILDECTNATSVDVEE 876
Cdd:PTZ00243 801 RDVYLLDDPLSALDAHVGE 819
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
54-205 |
9.86e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 41.97 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 54 VESGSNLLITGPNGSGKSSLFRVLGG-LWPLVSGH--------IVKPGVGSDLNKeifYvpqrpytaFGTLRDQLIYPLT 124
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGkLKPNLGKFddppdwdeILDEFRGSELQN---Y--------FTKLLEGDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 125 ADQEVE--PLTCSGMV-DLLKNVD----LDYLLDRYPPEKEVNWG-DELSLGEQQRLGMARLFYHKPKFAILDECTSAVt 196
Cdd:cd03236 92 KPQYVDliPKAVKGKVgELLKKKDergkLDELVDQLELRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYL- 170
|
....*....
gi 1776568118 197 tDMEERFCA 205
Cdd:cd03236 171 -DIKQRLNA 178
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
62-231 |
1.39e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 41.66 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 62 ITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGSDLNKEIFYVPQRPY-----------TAFGtLRDQLIyPLT 124
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFEKLRKHIGIVFQNPDnqfvgsivkydVAFG-LENHAV-PYD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 125 ADQEVEPltcsgmvDLLKNVDldyLLDRYPPEKEvnwgdELSLGEQQRLGMARLFYHKPKFAILDECTSAVTTDMEERFC 204
Cdd:PRK13648 118 EMHRRVS-------EALKQVD---MLERADYEPN-----ALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190
....*....|....*....|....*....|...
gi 1776568118 205 AKVRAM----GTSCITISH--RPALVAFHDVVL 231
Cdd:PRK13648 183 DLVRKVksehNITIISITHdlSEAMEADHVIVM 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
47-194 |
1.83e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 41.98 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPlVSGHIVKpgVGSDLN-----------KEIFYVPQRPYtafGTL 115
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRF--DGQDLDglsrralrplrRRMQVVFQDPF---GSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 116 --RdqliypLTADQEV-EPLTCSG-----------MVDLLKNVDLD-YLLDRYPpekevnwgDELSLGEQQRLGMARLFY 180
Cdd:COG4172 376 spR------MTVGQIIaEGLRVHGpglsaaerrarVAEALEEVGLDpAARHRYP--------HEFSGGQRQRIAIARALI 441
|
170
....*....|....
gi 1776568118 181 HKPKFAILDECTSA 194
Cdd:COG4172 442 LEPKLLVLDEPTSA 455
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
685-781 |
1.86e-03 |
|
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: 40.37 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 685 ISFSEVDIITPAQKLLARQ-LTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHFD--EETASGGIFYV 761
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKnLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdlEKALSSLISVL 80
|
90 100
....*....|....*....|
gi 1776568118 762 PQRPYTCLGTLRDQIIYPLS 781
Cdd:cd03247 81 NQRPYLFDTTLRNNLGRRFS 100
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
718-865 |
2.12e-03 |
|
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: 40.74 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRLykpshHFD---------EETASGGIFYVPQRpytclgtlRDqiIYPlsreeaelr 788
Cdd:COG0410 36 GRNGAGKTTLLKAISGLLPPRSGSI-----RFDgeditglppHRIARLGIGYVPEG--------RR--IFP--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 789 elklygqgenavdatsildaRLkTILENVRLNYLLEREEGGWDANLnwEDILSL-----------------GEQQRLGMA 851
Cdd:COG0410 92 --------------------SL-TVEENLLLGAYARRDRAEVRADL--ERVYELfprlkerrrqragtlsgGEQQMLAIG 148
|
170
....*....|....
gi 1776568118 852 RLFFHKPKFGILDE 865
Cdd:COG0410 149 RALMSRPKLLLLDE 162
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
40-190 |
2.13e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 41.38 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 40 TPTGNVLVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPlVSGHIVKPGVGSD------LNKEIFYVPQRPYTAFG 113
Cdd:cd03289 13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNsvplqkWRKAFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 114 TLRDQL-IYPLTADQEVEPLTcsgmvdllKNVDLDYLLDRYPPEKE---VNWGDELSLGEQQRLGMARLFYHKPKFAILD 189
Cdd:cd03289 92 TFRKNLdPYGKWSDEEIWKVA--------EEVGLKSVIEQFPGQLDfvlVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
.
gi 1776568118 190 E 190
Cdd:cd03289 164 E 164
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
48-220 |
2.30e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 41.73 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 48 KDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI---------VKPgvgSDLNKEIFYVPQRpyTA-FG-TLR 116
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdVTQ---ASLRAAIGIVPQD--TVlFNdTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 117 DQLIY--PLTADQEVEpltcsgmvDLLKNVDLDYLLDRYPPEKEVNWGD---ELSLGEQQRLGMARLFYHKPKFAILDEC 191
Cdd:COG5265 450 YNIAYgrPDASEEEVE--------AAARAAQIHDFIESLPDGYDTRVGErglKLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
170 180 190
....*....|....*....|....*....|.
gi 1776568118 192 TSAVTTDMEERFCAKVRAM--GTSCITISHR 220
Cdd:COG5265 522 TSALDSRTERAIQAALREVarGRTTLVIAHR 552
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
46-106 |
2.46e-03 |
|
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: 40.23 E-value: 2.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776568118 46 LVKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGL--WPLVSGHIVKPGVGSDLN---KEIFYVPQ 106
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRsfrKIIGYVPQ 89
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
718-865 |
2.61e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.78 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRG--LWPIVSGR-LYKPSHHFD---EETASGGIFYVPQRPYTCLGT-----LRdqIIYPLSREEAE 786
Cdd:CHL00131 40 GPNGSGKSTLSKVIAGhpAYKILEGDiLFKGESILDlepEERAHLGIFLAFQYPIEIPGVsnadfLR--LAYNSKRKFQG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 787 LRELklygqgenavDATSILDArLKTILENVRLN-YLLEReeggwdaNLNweDILSLGEQQR---LGMARLffhKPKFGI 862
Cdd:CHL00131 118 LPEL----------DPLEFLEI-INEKLKLVGMDpSFLSR-------NVN--EGFSGGEKKRneiLQMALL---DSELAI 174
|
...
gi 1776568118 863 LDE 865
Cdd:CHL00131 175 LDE 177
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
43-233 |
2.86e-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: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 43 GNVLVKDLFLRVES---------------GSNLLITGPNGSGKSSLFRVLGGLWPLVSGHIVKPGVG------SDLNKEI 101
Cdd:cd03288 18 GEIKIHDLCVRYENnlkpvlkhvkayikpGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDisklplHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 102 FYVPQRPYTAFGTLRDQLI--YPLTADQEVEPLTCSGMVDLLKNvdLDYLLDRYPPEKevnwGDELSLGEQQRLGMARLF 179
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDpeCKCTDDRLWEALEIAQLKNMVKS--LPGGLDAVVTEG----GENFSVGQRQLFCLARAF 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776568118 180 YHKPKFAILDECTSAVttDM-EERFCAKVRAMG---TSCITISHRPALVAFHDVVLSL 233
Cdd:cd03288 172 VRKSSILIMDEATASI--DMaTENILQKVVMTAfadRTVVTIAHRVSTILDADLVLVL 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-176 |
2.92e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.31 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 21 SRNYLTEANYVEFSGvkvvtptgnvLVKDL--F-LRVESGS-----NLLITGPNGSGKSSLFRVLGGlwplvsghIVKPG 92
Cdd:COG1245 332 PRREKEEETLVEYPD----------LTKSYggFsLEVEGGEiregeVLGIVGPNGIGKTTFAKILAG--------VLKPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 93 VGS-DLNKEIFYVPQRPYTAF-GTLRDQLIYPLTADQEVEPLTcsgmVDLLKNVDLDYLLDryppeKEVnwgDELSLGEQ 170
Cdd:COG1245 394 EGEvDEDLKISYKPQYISPDYdGTVEEFLRSANTDDFGSSYYK----TEIIKPLGLEKLLD-----KNV---KDLSGGEL 461
|
....*.
gi 1776568118 171 QRLGMA 176
Cdd:COG1245 462 QRVAIA 467
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
31-234 |
2.97e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 40.97 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 31 VEFSGVKVVTPTGNVLVK----DLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI------VKPGVGS----D 96
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKkgldNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhITPETGNknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 97 LNKEIFYVPQRPYTAF---GTLRDQLIYPLT---ADQEVEpltcSGMVDLLKNVDL-DYLLDRYPpekevnwgDELSLGE 169
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLfenTVLKDVEFGPKNfgfSEDEAK----EKALKWLKKVGLsEDLISKSP--------FELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 170 QQRLGMARLFYHKPKFAILDECTSAV----TTDMEERFCAKVRAmGTSCITISHRPALVA-FHDVVLSLD 234
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLdpegRKEMMQLFKDYQKA-GHTVILVTHNMDDVAeYADDVLVLE 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
47-88 |
3.78e-03 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 40.49 E-value: 3.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1776568118 47 VKDLFLRVESGSNLLITGPNGSGKSSLFRVLGGLWPLVSGHI 88
Cdd:TIGR04520 18 LKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKV 59
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
44-194 |
4.29e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.84 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 44 NVLVKDLFLRVESGSNLLITGPNGSGKSS----LFRVL---GGLW----PLvsgHIVKPGVGSDLNKEIFYVPQRPYTAF 112
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIWfdgqPL---HNLNRRQLLPVRHRIQVVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 113 GTLRD--QLI-------YP-LTADQEVEPLtcsgmVDLLKNVDLDylldrypPEKEVNWGDELSLGEQQRLGMARLFYHK 182
Cdd:PRK15134 376 NPRLNvlQIIeeglrvhQPtLSAAQREQQV-----IAVMEEVGLD-------PETRHRYPAEFSGGQRQRIAIARALILK 443
|
170
....*....|..
gi 1776568118 183 PKFAILDECTSA 194
Cdd:PRK15134 444 PSLIILDEPTSS 455
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
840-868 |
4.82e-03 |
|
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: 38.58 E-value: 4.82e-03
10 20
....*....|....*....|....*....
gi 1776568118 840 LSLGEQQRLGMARLFFHKPKFGILDECTN 868
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
718-867 |
5.63e-03 |
|
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: 39.66 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776568118 718 GPNGSGKSSVFRVLRGLWPIVSGRLYKPSHHFDEETAS--GGIFYVPQRPytclgTLRDQiiypLSREEAELRELKLYGQ 795
Cdd:cd03265 33 GPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvrRRIGIVFQDL-----SVDDE----LTGWENLYIHARLYGV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776568118 796 GenavdaTSILDARLKTILENVRLnyllereeggWDANLNWEDILSLGEQQRLGMARLFFHKPKFGILDECT 867
Cdd:cd03265 104 P------GAERRERIDELLDFVGL----------LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
702-763 |
6.29e-03 |
|
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: 39.41 E-value: 6.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776568118 702 RQLTCDVVPEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSH--HFDEETASGGIFYVPQ 763
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsiRTDRKAARQSLGYCPQ 82
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
710-748 |
7.26e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.06 E-value: 7.26e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1776568118 710 PEKSLLVTGPNGSGKSSVFRVLRGLWPIVSGRLYKPSHH 748
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT 74
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
52-74 |
7.51e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 7.51e-03
|
| |
