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Conserved domains on  [gi|1831510678|ref|NP_001367852|]
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ABC transporter domain-containing protein [Caenorhabditis elegans]

Protein Classification

ABC transporter G family protein( domain architecture ID 1000947)

ABC transporter G (ABCG) family protein may be involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
3a01204 super family cl36780
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
1-527 0e+00

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


The actual alignment was detected with superfamily member TIGR00955:

Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 546.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLKFMAKLKMGSEYDLNEQERRVKSVMRSLGLEKIADSIIGTRTR-KGISGGEKKRLA 79
Cdd:TIGR00955  97 MRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvKGLSGGERKRLA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  80 FASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAeTRNMTILLTIHQPSSQVFQLFDSIYMMVNGDVAFCGSQSGAE 159
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 160 KMWSEMKLPIPMNFNPSDHYLATMSIrDQAEETLKKNQIGKICTTFKYSELGKSVFKEssGREVDERDRAFSEDwrrryA 239
Cdd:TIGR00955 256 PFFSDLGHPCPENYNPADFYVQVLAV-IPGSENESRERIEKICDSFAVSDIGRDMLVN--TNLWSGKAGGLVKD-----S 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 240 TTFGRPRFGASFFQQIRALTWRASKTVLREPTLLKVQTFQSIIIAILTGLVYTNnSPVDQQKIMNINGSLYQMISNMAFM 319
Cdd:TIGR00955 328 ENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLG-QGLTQKGVQNINGALFLFLTNMTFQ 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 320 FQFSVVHHFCLEMNTFYRETSSRLYRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGLVPIIDSFLIYMLVGILVQNIA 399
Cdd:TIGR00955 407 NVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVA 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 400 ISIGYMFSCIFGTVNLAVAVMPIFVVPMMAFGGFFINQDTLQWYFVPMKYLSYFGYGYEAVAIAQWTHVEEIPGCSSSLA 479
Cdd:TIGR00955 487 TSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIECTSANTT 566
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1831510678 480 H-CSRNGTDVLNSMSFKPSNFWVDISVMAFMIFVFRFLAFMALYVRVKR 527
Cdd:TIGR00955 567 GpCPSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRR 615
 
Name Accession Description Interval E-value
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
1-527 0e+00

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 546.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLKFMAKLKMGSEYDLNEQERRVKSVMRSLGLEKIADSIIGTRTR-KGISGGEKKRLA 79
Cdd:TIGR00955  97 MRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvKGLSGGERKRLA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  80 FASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAeTRNMTILLTIHQPSSQVFQLFDSIYMMVNGDVAFCGSQSGAE 159
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 160 KMWSEMKLPIPMNFNPSDHYLATMSIrDQAEETLKKNQIGKICTTFKYSELGKSVFKEssGREVDERDRAFSEDwrrryA 239
Cdd:TIGR00955 256 PFFSDLGHPCPENYNPADFYVQVLAV-IPGSENESRERIEKICDSFAVSDIGRDMLVN--TNLWSGKAGGLVKD-----S 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 240 TTFGRPRFGASFFQQIRALTWRASKTVLREPTLLKVQTFQSIIIAILTGLVYTNnSPVDQQKIMNINGSLYQMISNMAFM 319
Cdd:TIGR00955 328 ENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLG-QGLTQKGVQNINGALFLFLTNMTFQ 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 320 FQFSVVHHFCLEMNTFYRETSSRLYRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGLVPIIDSFLIYMLVGILVQNIA 399
Cdd:TIGR00955 407 NVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVA 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 400 ISIGYMFSCIFGTVNLAVAVMPIFVVPMMAFGGFFINQDTLQWYFVPMKYLSYFGYGYEAVAIAQWTHVEEIPGCSSSLA 479
Cdd:TIGR00955 487 TSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIECTSANTT 566
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1831510678 480 H-CSRNGTDVLNSMSFKPSNFWVDISVMAFMIFVFRFLAFMALYVRVKR 527
Cdd:TIGR00955 567 GpCPSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRR 615
PLN03211 PLN03211
ABC transporter G-25; Provisional
7-521 2.92e-57

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 202.03  E-value: 2.92e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   7 YVQQDDCFIGSLTVEEHLKFMAKLKMGSEYDLNEQERRVKSVMRSLGLEKIADSIIGTRTRKGISGGEKKRLAFASEILT 86
Cdd:PLN03211  144 FVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLI 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  87 SPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPSSQVFQLFDSIYMMVNGDVAFCGSQSGAEKMWSEMK 166
Cdd:PLN03211  224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVG 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 167 LPIPMNFNPSDHYLAT---------MSIRDQ---------AEETLKKNQIGKICTTFKYSELGKSVFKESSGREVDERDR 228
Cdd:PLN03211  303 FSPSFPMNPADFLLDLangvcqtdgVSEREKpnvkqslvaSYNTLLAPKVKAAIEMSHFPQANARFVGSASTKEHRSSDR 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 229 AFSEDWrrryattfgrprfgasfFQQIRALTWRASKTVLREP-TLLKVqtFQSIIIAILTGLVYTNNSPVDQQKIMninG 307
Cdd:PLN03211  383 ISISTW-----------------FNQFSILLQRSLKERKHESfNTLRV--FQVIAAALLAGLMWWHSDFRDVQDRL---G 440
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 308 SLYQMISNMAFMFQFSVVHHFCLEMNTFYRETSSRLYRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGLVPIIDSFLI 387
Cdd:PLN03211  441 LLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLL 520
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 388 YMLVgiLVQNIAISIGYMFScifgtvnLAVAVM------PIFVVPMMAF---GGFFINQ--DTLQWyfvpMKYLSYFGYG 456
Cdd:PLN03211  521 TLLV--LLGYVLVSQGLGLA-------LGAAIMdakkasTIVTVTMLAFvltGGFYVHKlpSCMAW----IKYISTTFYS 587
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510678 457 YEAVAIAQWTHVEEIP---GCS----SSLAHCSRNGTDVLNSMSfkpsnFWVDISVMAFMIFVFRFLAFMAL 521
Cdd:PLN03211  588 YRLLINVQYGEGKRISsllGCSlphgSDRASCKFVEEDVAGQIS-----PATSVSVLIFMFVGYRLLAYLAL 654
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
1-153 7.70e-52

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: 176.31  E-value: 7.70e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLKFMAKLKMGSEydlNEQERRVKSVmRSLGLEKIADSIIGTRTRKGISGGEKKRLAF 80
Cdd:cd03234    79 FQKCVAYVRQDDILLPGLTVRETLTYTAILRLPRK---SSDAIRKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSI 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAeTRNMTILLTIHQPSSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03234   155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLA-RRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
ABC2_membrane pfam01061
ABC-2 type transporter;
258-460 2.24e-36

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 133.94  E-value: 2.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 258 LTWRASKTVLREPTLLKVQTFQSIIIAILTGLVYTNNSpvDQQKIMNINGSLYQMISNMAFMFQFSVVHHFCLEMNTFYR 337
Cdd:pfam01061   1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG--NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 338 ETSSRLYRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGLVPIIDSFLIYMLVGILVQNIAISIGYMFSCIFGTVNLAV 417
Cdd:pfam01061  79 ELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDAS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1831510678 418 AVMPIFVVPMMAFGGFFINQDTLQWYFVPMKYLSYFGYGYEAV 460
Cdd:pfam01061 159 QLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEAL 201
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
2-154 1.10e-28

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 113.62  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLKFMAKLKmgsEYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFA 81
Cdd:COG1131    72 RRRIGYVPQEPALYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLA 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  82 SEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:COG1131   144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADGT 214
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
16-128 5.30e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 52.43  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  16 GSLTVEEHLKFMAKLkmgseYDL--NEQERRVKSVMRSLGLEKIADSIIGtrtrkGISGGEKKRLAFASEILTSPPILIC 93
Cdd:NF033858  352 GELTVRQNLELHARL-----FHLpaAEIAARVAEMLERFDLADVADALPD-----SLPLGIRQRLSLAVAVIHKPELLIL 421
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1831510678  94 DEPTSGLD-----SFLAYqvvcvLKKLAETRNMTILLTIH 128
Cdd:NF033858  422 DEPTSGVDpvardMFWRL-----LIELSREDGVTIFISTH 456
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
18-101 1.43e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 44.73  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLkmgseYDLNEQER--RVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDE 95
Cdd:NF033858   93 LSVFENLDFFGRL-----FGQDAAERrrRIDELLRATGLAPFAD-----RPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162

                  ....*.
gi 1831510678  96 PTSGLD 101
Cdd:NF033858  163 PTTGVD 168
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
40-130 1.65e-04

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 42.61  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtR 119
Cdd:NF040873   95 DDRAAVDDALERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-R 168
                          90
                  ....*....|.
gi 1831510678 120 NMTILLTIHQP 130
Cdd:NF040873  169 GATVVVVTHDL 179
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
32-101 1.00e-03

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 41.64  E-value: 1.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  32 MGSEYDLNEQERRVKSvmrSLGLEKIADSIIGTRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:NF000106  110 IGR*LDLSRKDARARA---DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
 
Name Accession Description Interval E-value
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
1-527 0e+00

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 546.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLKFMAKLKMGSEYDLNEQERRVKSVMRSLGLEKIADSIIGTRTR-KGISGGEKKRLA 79
Cdd:TIGR00955  97 MRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvKGLSGGERKRLA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  80 FASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAeTRNMTILLTIHQPSSQVFQLFDSIYMMVNGDVAFCGSQSGAE 159
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAV 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 160 KMWSEMKLPIPMNFNPSDHYLATMSIrDQAEETLKKNQIGKICTTFKYSELGKSVFKEssGREVDERDRAFSEDwrrryA 239
Cdd:TIGR00955 256 PFFSDLGHPCPENYNPADFYVQVLAV-IPGSENESRERIEKICDSFAVSDIGRDMLVN--TNLWSGKAGGLVKD-----S 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 240 TTFGRPRFGASFFQQIRALTWRASKTVLREPTLLKVQTFQSIIIAILTGLVYTNnSPVDQQKIMNINGSLYQMISNMAFM 319
Cdd:TIGR00955 328 ENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLG-QGLTQKGVQNINGALFLFLTNMTFQ 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 320 FQFSVVHHFCLEMNTFYRETSSRLYRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGLVPIIDSFLIYMLVGILVQNIA 399
Cdd:TIGR00955 407 NVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVA 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 400 ISIGYMFSCIFGTVNLAVAVMPIFVVPMMAFGGFFINQDTLQWYFVPMKYLSYFGYGYEAVAIAQWTHVEEIPGCSSSLA 479
Cdd:TIGR00955 487 TSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIECTSANTT 566
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1831510678 480 H-CSRNGTDVLNSMSFKPSNFWVDISVMAFMIFVFRFLAFMALYVRVKR 527
Cdd:TIGR00955 567 GpCPSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRR 615
PLN03211 PLN03211
ABC transporter G-25; Provisional
7-521 2.92e-57

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 202.03  E-value: 2.92e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   7 YVQQDDCFIGSLTVEEHLKFMAKLKMGSEYDLNEQERRVKSVMRSLGLEKIADSIIGTRTRKGISGGEKKRLAFASEILT 86
Cdd:PLN03211  144 FVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLI 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  87 SPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPSSQVFQLFDSIYMMVNGDVAFCGSQSGAEKMWSEMK 166
Cdd:PLN03211  224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVG 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 167 LPIPMNFNPSDHYLAT---------MSIRDQ---------AEETLKKNQIGKICTTFKYSELGKSVFKESSGREVDERDR 228
Cdd:PLN03211  303 FSPSFPMNPADFLLDLangvcqtdgVSEREKpnvkqslvaSYNTLLAPKVKAAIEMSHFPQANARFVGSASTKEHRSSDR 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 229 AFSEDWrrryattfgrprfgasfFQQIRALTWRASKTVLREP-TLLKVqtFQSIIIAILTGLVYTNNSPVDQQKIMninG 307
Cdd:PLN03211  383 ISISTW-----------------FNQFSILLQRSLKERKHESfNTLRV--FQVIAAALLAGLMWWHSDFRDVQDRL---G 440
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 308 SLYQMISNMAFMFQFSVVHHFCLEMNTFYRETSSRLYRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGLVPIIDSFLI 387
Cdd:PLN03211  441 LLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLL 520
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 388 YMLVgiLVQNIAISIGYMFScifgtvnLAVAVM------PIFVVPMMAF---GGFFINQ--DTLQWyfvpMKYLSYFGYG 456
Cdd:PLN03211  521 TLLV--LLGYVLVSQGLGLA-------LGAAIMdakkasTIVTVTMLAFvltGGFYVHKlpSCMAW----IKYISTTFYS 587
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510678 457 YEAVAIAQWTHVEEIP---GCS----SSLAHCSRNGTDVLNSMSfkpsnFWVDISVMAFMIFVFRFLAFMAL 521
Cdd:PLN03211  588 YRLLINVQYGEGKRISsllGCSlphgSDRASCKFVEEDVAGQIS-----PATSVSVLIFMFVGYRLLAYLAL 654
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
1-153 7.70e-52

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: 176.31  E-value: 7.70e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLKFMAKLKMGSEydlNEQERRVKSVmRSLGLEKIADSIIGTRTRKGISGGEKKRLAF 80
Cdd:cd03234    79 FQKCVAYVRQDDILLPGLTVRETLTYTAILRLPRK---SSDAIRKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSI 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAeTRNMTILLTIHQPSSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03234   155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLA-RRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
6-513 7.79e-43

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 164.13  E-value: 7.79e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678    6 AYVQQDDCFIGSLTVEEHLKFMAKLKM-GSEYDLNEQERRVKSV----MRSLGLEKIADSIIGTRTRKGISGGEKKRLAF 80
Cdd:TIGR00956  141 VYNAETDVHFPHLTVGETLDFAARCKTpQNRPDGVSREEYAKHIadvyMATYGLSHTRNTKVGNDFVRGVSGGERKRVSI 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSQVFQLFDSIYMMVNGDVAFCGSQSGAEK 160
Cdd:TIGR00956  221 AEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQ 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  161 MWSEMKLPIPMNFNPSDhYLAtmSIRDQAEETLKKNQIGKICTT-------FKYSELGKSVFKESSGREVDERDRAFSED 233
Cdd:TIGR00956  301 YFEKMGFKCPDRQTTAD-FLT--SLTSPAERQIKPGYEKKVPRTpqefetyWRNSPEYAQLMKEIDEYLDRCSESDTKEA 377
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  234 WRRRYA---TTFGRPR--FGASFFQQIRALTWRASKTVLREPTLLKVQTFQSIIIAILTGLVYTNnspvdqqkIMNINGS 308
Cdd:TIGR00956  378 YRESHVakqSKRTRPSspYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYN--------LPKNTSD 449
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  309 LYQMISNMAFMFQFSVVHHFCLEMNTF------YRETSSRLYRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGLVPII 382
Cdd:TIGR00956  450 FYSRGGALFFAILFNAFSSLLEIASMYearpivEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTA 529
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  383 DSFLIYMLVGILVQniaISIGYMFSCIFG---TVNLAVAVMPIFVVPMMAFGGFFINQDTLQWYFVPMKYLSYFGYGYEA 459
Cdd:TIGR00956  530 GRFFFYLLILFICT---LAMSHLFRSIGAvtkTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFES 606
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510678  460 VAIA-----QWTHVEEIP--GCSSSLAHCSR--------------NGTDVL-NSMSFKPSNFWVDISV-MAFMIFVF 513
Cdd:TIGR00956  607 LMVNefhgrRFECSQYVPsgGGYDNLGVTNKvctvvgaepgqdyvDGDDYLkLSFQYYNSHKWRNFGIiIGFTVFFF 683
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
2-153 5.87e-41

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: 146.16  E-value: 5.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLKFMAKLKmgseydlneqerrvksvmrslglekiadsiigtrtrkGISGGEKKRLAFA 81
Cdd:cd03213    81 RKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGERKRVSIA 123
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510678  82 SEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETrNMTILLTIHQPSSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03213   124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
7-455 9.47e-38

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 148.72  E-value: 9.47e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678    7 YVQQDDCFIGSLTVEEHLKFMAKLKMGSEYDLNEQERRVKSVMRSLGLEKIADSIIGTrTRKGISGGEKKRLAFASEILT 86
Cdd:TIGR00956  840 YVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGV-PGEGLNVEQRKRLTIGVELVA 918
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   87 SPPILI-CDEPTSGLDSFLAYQVVCVLKKLAETrNMTILLTIHQPSSQVFQLFDSIYMMVNG-DVAFCG-----SQSGAE 159
Cdd:TIGR00956  919 KPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGdlgenSHTIIN 997
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  160 KMWSEMKLPIPMNFNPSDHYLATMSirdqAEETLKKNQigkicttfKYSElgksVFKESSGR-----EVDERDRAFSEDW 234
Cdd:TIGR00956  998 YFEKHGAPKCPEDANPAEWMLEVIG----AAPGAHANQ--------DYHE----VWRNSSEYqavknELDRLEAELSKAE 1061
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  235 RRRYATTfgRPRFGASFFQQIRALTWRASKTVLREPTLLKVQTFQSIIIAILTGLVYTN--NSPVDQQKIMninGSLYQM 312
Cdd:TIGR00956 1062 DDNDPDA--LSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKvgTSLQGLQNQM---FAVFMA 1136
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  313 ISNMAFMFQFSVVHHFCLEMNTFYRETSSRLYRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGL-------VPIIDSF 385
Cdd:TIGR00956 1137 TVLFNPLIQQYLPPFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFywnasktGQVHERG 1216
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510678  386 LIYMLVGILVQNIAISIGYMfsCIFGTVNLAVA--VMPIFVVPMMAFGGFFINQDTLQWYFVPMKYLSYFGY 455
Cdd:TIGR00956 1217 VLFWLLSTMFFLYFSTLGQM--VISFNPNADNAavLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTY 1286
ABC2_membrane pfam01061
ABC-2 type transporter;
258-460 2.24e-36

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 133.94  E-value: 2.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 258 LTWRASKTVLREPTLLKVQTFQSIIIAILTGLVYTNNSpvDQQKIMNINGSLYQMISNMAFMFQFSVVHHFCLEMNTFYR 337
Cdd:pfam01061   1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG--NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 338 ETSSRLYRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGLVPIIDSFLIYMLVGILVQNIAISIGYMFSCIFGTVNLAV 417
Cdd:pfam01061  79 ELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDAS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1831510678 418 AVMPIFVVPMMAFGGFFINQDTLQWYFVPMKYLSYFGYGYEAV 460
Cdd:pfam01061 159 QLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEAL 201
PLN03140 PLN03140
ABC transporter G family member; Provisional
2-521 1.16e-29

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 124.19  E-value: 1.16e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678    2 RQVCAYVQQDDCFIGSLTVEEHLKFMAKLK-MGSEYD-LNEQERR-----------------------VKS------VMR 50
Cdd:PLN03140   238 RKTSAYISQNDVHVGVMTVKETLDFSARCQgVGTRYDlLSELARRekdagifpeaevdlfmkatamegVKSslitdyTLK 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   51 SLGLEKIADSIIGTRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQP 130
Cdd:PLN03140   318 ILGLDICKDTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQP 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  131 SSQVFQLFDSIYMMVNGDVAFCGSQSGAEKMWSEMKLPIPMNFNPSDHYLATMSIRDQAEETLKKNQIGKICTTFKYSEL 210
Cdd:PLN03140   398 APETFDLFDDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRYISVSEFAER 477
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  211 GKSvFKESSGREvDERDRAFSEDWRRRYATTFGrpRFGASFFQQIRALTWRASKTVLREPTLLKVQTFQSIIIAILTGLV 290
Cdd:PLN03140   478 FKS-FHVGMQLE-NELSVPFDKSQSHKAALVFS--KYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTV 553
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  291 YTN---NSPVDQQKIMNINGSLYQMISNmafMFQ-FSVVHHFCLEMNTFYRETSSRLYRVSAYFISKNLAELPSYIVSAV 366
Cdd:PLN03140   554 FLRtemHTRNEEDGALYIGALLFSMIIN---MFNgFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESV 630
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  367 IFTSILYWMSGLVPIIDSFLIYMLVGILVQNIAISIGYMFSCIFGTVNLAVAVMPIFVVPMMAFGGFFINQDTLQWYFVP 446
Cdd:PLN03140   631 VWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEW 710
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510678  447 MKYLSYFGYGYEAVAIAQWTHVEEIPGCSSSlaHCSRNGTDVLNSMSFKPSNFWVDISVMAFMIF--VFRFLAFMAL 521
Cdd:PLN03140   711 AYWVSPLSYGFNALAVNEMFAPRWMNKMASD--NSTRLGTAVLNIFDVFTDKNWYWIGVGALLGFtiLFNVLFTLAL 785
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
2-154 1.10e-28

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 113.62  E-value: 1.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLKFMAKLKmgsEYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFA 81
Cdd:COG1131    72 RRRIGYVPQEPALYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLA 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  82 SEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:COG1131   144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADGT 214
PLN03140 PLN03140
ABC transporter G family member; Provisional
3-444 1.90e-28

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 120.34  E-value: 1.90e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678    3 QVCAYVQQDDCFIGSLTVEEHLKFMAKLKMGSEYDLNEQERRVKSVMRSLGLEKIADSIIGTRTRKGISGGEKKRLAFAS 82
Cdd:PLN03140   953 RISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAV 1032
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   83 EILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETrNMTILLTIHQPSSQVFQLFDSIYMMV-NGDVAFCG-----SQS 156
Cdd:PLN03140  1033 ELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSGplgrnSHK 1111
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  157 GAEKMWSEMKLP-IPMNFNPSDHYLATMSIrdQAEETLKKNqigkICTTFKYSEL---GKSVFKESSGREVDERDRAFSE 232
Cdd:PLN03140  1112 IIEYFEAIPGVPkIKEKYNPATWMLEVSSL--AAEVKLGID----FAEHYKSSSLyqrNKALVKELSTPPPGASDLYFAT 1185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  233 dwrrryattfgrpRFGASFFQQIRALTWRASKTVLREPTLLKVQTFQSIIIAILTGLVY----TNNSPVdqQKIMNINGS 308
Cdd:PLN03140  1186 -------------QYSQSTWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFwkvgTKRSNA--NDLTMVIGA 1250
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  309 LYQMISNMAFMFQFSVVHHFCLEMNTFYRETSSRLYRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGLVPIIDSFLIY 388
Cdd:PLN03140  1251 MYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWF 1330
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510678  389 MLVGILVQNIAISIGYMFSCIfgTVNLAVAVmpIFVVPMMA----FGGFFINQDTLQ----WYF 444
Cdd:PLN03140  1331 YFISFFSFLYFTYYGMMTVSL--TPNQQVAA--IFAAAFYGlfnlFSGFFIPRPKIPkwwvWYY 1390
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
2-147 7.93e-28

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 110.03  E-value: 7.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLKFMAKLkmgseydlneqerrvksvmRSLGLEkiadsiigtrtrkgisggEKKRLAFA 81
Cdd:cd03232    78 QRSTGYVEQQDVHSPNLTVREALRFSALL-------------------RGLSVE------------------QRKRLTIG 120
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510678  82 SEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETrNMTILLTIHQPSSQVFQLFDSIYMMVNG 147
Cdd:cd03232   121 VELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPSASIFEKFDRLLLLKRG 185
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
6-153 4.92e-21

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 91.17  E-value: 4.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   6 AYVQQDDCFIGSLTVEEHLKFMAKLKmGSEYdlneqerrvksvmrslglekiadsiigtrtRKGISGGEKKRLAFAsEIL 85
Cdd:cd03233    86 IYVSEEDVHFPTLTVRETLDFALRCK-GNEF------------------------------VRGISGGERKRVSIA-EAL 133
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510678  86 TSPPILIC-DEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03233   134 VSRASVLCwDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
2-154 5.47e-21

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: 91.41  E-value: 5.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLKFMAKLKMGSEYDLNEQerrVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFA 81
Cdd:cd03263    74 RQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEE---VELLLRVLGLTDKANKRART-----LSGGMKRKLSLA 145
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  82 SEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:cd03263   146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSM-DEAEALCDRIAIMSDGKLRCIGS 215
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
1-154 6.33e-20

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: 88.54  E-value: 6.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQ--DDCFIGSlTVEEHLKF-MAKLKMGSEydlnEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKR 77
Cdd:COG1122    73 LRRKVGLVFQnpDDQLFAP-TVEEDVAFgPENLGLPRE----EIRERVEEALELVGLEHLADRPPHE-----LSGGQKQR 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510678  78 LAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:COG1122   143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDL-DLVAELADRVIVLDDGRIVADGT 217
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
2-154 6.70e-20

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: 89.33  E-value: 6.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVcAYVQQDDCFIGSLTVEE--------HLKFMAKLkmgSEYDlneqERRVKSVMRSLGLEKIADSIIGTrtrkgISGG 73
Cdd:COG1120    75 RRI-AYVPQEPPAPFGLTVRElvalgrypHLGLFGRP---SAED----REAVEEALERTGLEHLADRPVDE-----LSGG 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  74 EKKRLAFASEILTSPPILICDEPTSGLDsfLAYQ--VVCVLKKLAETRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAF 151
Cdd:COG1120   142 ERQRVLIARALAQEPPLLLLDEPTSHLD--LAHQleVLELLRRLARERGRTVVMVLHDL-NLAARYADRLVLLKDGRIVA 218

                  ...
gi 1831510678 152 CGS 154
Cdd:COG1120   219 QGP 221
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
1-154 9.59e-20

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: 88.33  E-value: 9.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLKFMakLKMGSEYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAF 80
Cdd:cd03261    75 LRRRMGMLFQSGALFDSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVAL 147
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSqVFQLFDSIYMMVNGDVAFCGS 154
Cdd:cd03261   148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDT-AFAIADRIAVLYDGKIVAEGT 220
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
2-147 5.97e-19

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: 5.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQ--DDCFIGSlTVEEHLKF-MAKLKMGSEydlnEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRL 78
Cdd:cd03225    74 RRKVGLVFQnpDDQFFGP-TVEEEVAFgLENLGLPEE----EIEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRV 143
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510678  79 AFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPsSQVFQLFDSIYMMVNG 147
Cdd:cd03225   144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDL-DLLLELADRVIVLEDG 210
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
15-147 9.62e-19

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: 84.85  E-value: 9.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  15 IGSLTVEEHLKfMAKLKMGSEYDlnEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICD 94
Cdd:cd03255    94 LPDLTALENVE-LPLLLAGVPKK--ERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPKIILAD 165
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  95 EPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPssQVFQLFDSIYMMVNG 147
Cdd:cd03255   166 EPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP--ELAEYADRIIELRDG 216
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
70-147 1.50e-18

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: 82.68  E-value: 1.50e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPsSQVFQLFDSIYMMVNG 147
Cdd:cd00267    81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDP-ELAELAADRVIVLKDG 156
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1-157 2.44e-18

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: 84.52  E-value: 2.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVcAYVQQDDCFIGSLTVEEHLKFMAKLkmgseYDLNEQER--RVKSVMRSLGLEKIADsiigTRTrKGISGGEKKRL 78
Cdd:COG4555    73 RRQI-GVLPDERGLYDRLTVRENIRYFAEL-----YGLFDEELkkRIEELIELLGLEEFLD----RRV-GELSTGMKKKV 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510678  79 AFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCGSQSG 157
Cdd:COG4555   142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDE 218
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
48-153 1.48e-17

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: 80.56  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  48 VMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDsfLAYQ--VVCVLKKLAETRNMTILL 125
Cdd:cd03214    81 ALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEPPILLLDEPTSHLD--IAHQieLLELLRRLARERGKTVVM 153
                          90       100
                  ....*....|....*....|....*...
gi 1831510678 126 TIHQPsSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03214   154 VLHDL-NLAARYADRVILLKDGRIVAQG 180
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
1-147 1.96e-17

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: 79.75  E-value: 1.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLKFmaklkmgseydlneqerrvksvmrslglekiadsiigtrtrkgiSGGEKKRLAF 80
Cdd:cd03230    71 VKRRIGYLPEEPSLYENLTVRENLKL--------------------------------------------SGGMKQRLAL 106
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPsSQVFQLFDSIYMMVNG 147
Cdd:cd03230   107 AQALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHIL-EEAERLCDRVAILNNG 171
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
6-98 3.90e-17

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 78.46  E-value: 3.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   6 AYVQQDDCFIGSLTVEEHLKFMAKLKmgsEYDLNEQERRVKSVMRSLGLEKIADSIIGTRTrKGISGGEKKRLAFASEIL 85
Cdd:pfam00005  62 GYVFQDPQLFPRLTVRENLRLGLLLK---GLSKREKDARAEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALL 137
                          90
                  ....*....|...
gi 1831510678  86 TSPPILICDEPTS 98
Cdd:pfam00005 138 TKPKLLLLDEPTA 150
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
2-147 1.02e-16

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 78.70  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVcAYVQQDdCFIGSLTVEEHLKFMAKLKmgseyDLNEQERRVKSVMRSLGLekiADSIIGTRTRKgISGGEKKRLAFA 81
Cdd:COG4619    74 RQV-AYVPQE-PALWGGTVRDNLPFPFQLR-----ERKFDRERALELLERLGL---PPDILDKPVER-LSGGERQRLALI 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510678  82 SEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPsSQVFQLFDSIYMMVNG 147
Cdd:COG4619   143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDP-EQIERVADRVLTLEAG 207
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1-153 1.17e-16

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: 78.77  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLKFMAKLKmgsEYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAF 80
Cdd:cd03264    70 LRRRIGYLPQEFGVYPNFTVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGI 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  81 ASEILTSPPILICDEPTSGLD-----SFLAyqvvcVLKKLAETRnmTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03264   142 AQALVGDPSILIVDEPTAGLDpeeriRFRN-----LLSELGEDR--IVILSTHI-VEDVESLCNQVAVLNKGKLVFEG 211
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
9-159 1.75e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 79.85  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   9 QQDDCFIGSLTVEEHLKFmAKLKMGseydLNEQ--ERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILT 86
Cdd:PRK13652   85 QNPDDQIFSPTVEQDIAF-GPINLG----LDEEtvAHRVSSALHMLGLEELRD-----RVPHHLSGGEKKRVAIAGVIAM 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  87 SPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDvaFCGSQSGAE 159
Cdd:PRK13652  155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQ-LDLVPEMADYIYVMDKGR--IVAYGTVEE 224
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
2-154 4.35e-16

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: 77.41  E-value: 4.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLKFMAKLkmgseYDLNEQER--RVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLA 79
Cdd:cd03265    72 RRRIGIVFQDLSVDDELTGWENLYIHARL-----YGVPGAERreRIDELLDFVGLLEAADRLVKT-----YSGGMRRRLE 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510678  80 FASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:cd03265   142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHY-MEEAEQLCDRVAIIDHGRIIAEGT 215
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
6-154 1.97e-15

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: 78.79  E-value: 1.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   6 AYVQQD-DCFIGSLTVEEHLKFMAKLKMGSEydlNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEI 84
Cdd:COG1123    86 GMVFQDpMTQLNPVTVGDQIAEALENLGLSR---AEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMAL 157
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  85 LTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:COG1123   158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGP 226
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
7-168 1.99e-15

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 77.84  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   7 YVQQDDCFIGSLTVEEHLKFMAKLKMGSEYDLNEQErrvksVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILT 86
Cdd:TIGR02142  79 YVFQEARLFPHLSVRGNLRYGMKRARPSERRISFER-----VIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLS 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  87 SPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAfcgSQSGAEKMWSEMK 166
Cdd:TIGR02142 149 SPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSL-QEVLRLADRVVVLEDGRVA---AAGPIAEVWASPD 224

                  ..
gi 1831510678 167 LP 168
Cdd:TIGR02142 225 LP 226
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
17-154 3.57e-15

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 75.02  E-value: 3.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  17 SLTVEEHLKFmaKLKMGSEYDLNEQERRVKSVMRSLGLEKIAD---SiigtrtrkGISGGEKKRLAFASEILTSPPILIC 93
Cdd:COG1127    96 SLTVFENVAF--PLREHTDLSEAEIRELVLEKLELVGLPGAADkmpS--------ELSGGMRKRVALARALALDPEILLY 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510678  94 DEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSqVFQLFDSIYMMVNGDVAFCGS 154
Cdd:COG1127   166 DEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEGT 225
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
6-153 4.05e-15

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 74.25  E-value: 4.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   6 AYVQQDDCFIGSLTVEEHLKFMAKLKMGseydlNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEIL 85
Cdd:cd03297    78 GLVFQQYALFPHLNVRENLAFGLKRKRN-----REDRISVDELLDLLGLDHLLNRYPAQ-----LSGGEKQRVALARALA 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  86 TSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03297   148 AQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDL-SEAEYLADRIVVMEDGRLQYIG 214
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
69-147 4.10e-15

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 73.38  E-value: 4.10e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510678  69 GISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPsSQVFQLFDSIYMMVNG 147
Cdd:cd03229   100 GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDL-DEAARLADRVVVLRDG 177
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
15-147 1.49e-14

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 73.15  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  15 IGSLTVEEHLKFMAKLkmgSEYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICD 94
Cdd:COG1136    98 LPELTALENVALPLLL---AGVSRKERRERARELLERVGLGDRLDHRPSQ-----LSGGQQQRVAIARALVNRPKLILAD 169
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  95 EPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPssQVFQLFDSIYMMVNG 147
Cdd:COG1136   170 EPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP--ELAARADRVIRLRDG 220
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-154 1.55e-14

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: 76.10  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQD--DCFIGSLTVEEHLKF-MAKLKMGSEydlNEQERRVKSVMRSLGL-EKIADSIIGTrtrkgISGGEKK 76
Cdd:COG1123   340 LRRRVQMVFQDpySSLNPRMTVGDIIAEpLRLHGLLSR---AERRERVAELLERVGLpPDLADRYPHE-----LSGGQRQ 411
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  77 RLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:COG1123   412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHD-LAVVRYIADRVAVMYDGRIVEDGP 488
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1-147 1.65e-14

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 73.30  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDcfIGSL----TVEEHLkfmaklkmgSE----YDLNEQERRVKSVMRSLGLEKiadsiiGTRTRKG--I 70
Cdd:COG1124    77 FRRRVQMVFQDP--YASLhprhTVDRIL---------AEplriHGLPDREERIAELLEQVGLPP------SFLDRYPhqL 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSqVFQLFDSIYMMVNG 147
Cdd:COG1124   140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAV-VAHLCDRVAVMQNG 215
cbiO PRK13637
energy-coupling factor transporter ATPase;
38-154 2.63e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 73.54  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  38 LNEQE--RRVKSVMRSLGL--EKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLK 113
Cdd:PRK13637  114 LSEEEieNRVKRAMNIVGLdyEDYKD-----KSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIK 188
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1831510678 114 KLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:PRK13637  189 ELHKEYNMTIILVSHS-MEDVAKLADRIIVMNKGKCELQGT 228
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
2-130 3.04e-14

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 71.74  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLKFMAKLkmgseYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFA 81
Cdd:COG4133    74 RRRLAYLGHADGLKPELTVRENLRFWAAL-----YGLRADREAIDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALA 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831510678  82 SEILTSPPILICDEPTSGLDSfLAYQVVC-VLKKLAEtRNMTILLTIHQP 130
Cdd:COG4133   144 RLLLSPAPLWLLDEPFTALDA-AGVALLAeLIAAHLA-RGGAVLLTTHQP 191
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
40-154 4.06e-14

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 72.04  E-value: 4.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtR 119
Cdd:COG1121   115 ADREAVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-E 188
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1831510678 120 NMTILLTIHQPsSQVFQLFDSIyMMVNGDVAFCGS 154
Cdd:COG1121   189 GKTILVVTHDL-GAVREYFDRV-LLLNRGLVAHGP 221
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
40-153 8.64e-14

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 71.27  E-value: 8.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETR 119
Cdd:COG1119   118 EQRERARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEG 192
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1831510678 120 NMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:COG1119   193 APTLVLVTHHV-EEIPPGITHVLLLKDGRVVAAG 225
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
1-149 1.19e-13

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: 70.44  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVcAYVQQDDCFIGSLTVEEHLKFMAKLKMgseYDLNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAF 80
Cdd:cd03299    70 KRDI-SYVPQNYALFPHMTVYKNIAYGLKKRK---VDKKEIERKVLEIAEMLGIDHLLN-----RKPETLSGGEQQRVAI 140
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDV 149
Cdd:cd03299   141 ARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD-FEEAWALADKVAIMLNGKL 208
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
40-153 1.24e-13

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: 69.87  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtR 119
Cdd:cd03235   108 ADKAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-E 181
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1831510678 120 NMTILLTIHQPsSQVFQLFDSIyMMVNGDVAFCG 153
Cdd:cd03235   182 GMTILVVTHDL-GLVLEYFDRV-LLLNRTVVASG 213
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
19-149 4.98e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 69.34  E-value: 4.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  19 TVEEHLKFmAKLKMGSEYDlnEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDEPTS 98
Cdd:PRK13639   95 TVEEDVAF-GPLNLGLSKE--EVEKRVKEALKAVGMEGFEN-----KPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831510678  99 GLDSFLAYQVVCVLKKLAEtRNMTILLTIHQpSSQVFQLFDSIYMMVNGDV 149
Cdd:PRK13639  167 GLDPMGASQIMKLLYDLNK-EGITIIISTHD-VDLVPVYADKVYVMSDGKI 215
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
14-147 5.63e-13

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 68.01  E-value: 5.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  14 FIGSLTVEEHLKFMAKLKMGSEydlneqeRRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILIC 93
Cdd:cd03268    83 FYPNLTARENLRLLARLLGIRK-------KRIDEVLDVVGLKDSAK-----KKVKGFSLGMKQRLGIALALLGNPDLLIL 150
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1831510678  94 DEPTSGLDSFLAYQVVCVLKKLAETrNMTILLTIHQpSSQVFQLFDSIYMMVNG 147
Cdd:cd03268   151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHL-LSEIQKVADRIGIINKG 202
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
17-128 7.55e-13

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: 67.92  E-value: 7.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  17 SLTVEEHLKFMAKLKmGSEYDLNEQERRVKSVMRSLGLekiaDSIIGTRTRKGISGGEKKRLAFASEILTSPPILICDEP 96
Cdd:cd03257    98 RMTIGEQIAEPLRIH-GKLSKKEARKEAVLLLLVGVGL----PEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEP 172
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1831510678  97 TSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:cd03257   173 TSALDVSVQAQILDLLKKLQEELGLTLLFITH 204
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
2-128 7.84e-13

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 67.06  E-value: 7.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQD-DCFIGSLTVEEHLKFmAKLKMGSEYDlnEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAF 80
Cdd:TIGR01166  67 RQRVGLVFQDpDDQLFAADVDQDVAF-GPLNLGLSEA--EVERRVREALTAVGASGLRERPTHC-----LSGGEKKRVAI 138
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIH 128
Cdd:TIGR01166 139 AGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRA-EGMTVVISTH 185
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
40-129 1.09e-12

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 67.61  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETR 119
Cdd:cd03258   116 EIEERVLELLELVGLEDKADAYPAQ-----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINREL 190
                          90
                  ....*....|
gi 1831510678 120 NMTILLTIHQ 129
Cdd:cd03258   191 GLTIVLITHE 200
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
2-153 1.24e-12

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 67.13  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFiGSLTVEEHLKfmakLKMGSEYDLNEQER-RVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAF 80
Cdd:cd03298    70 RPVSMLFQENNLF-AHLTVEQNVG----LGLSPGLKLTAEDRqAIEVALARVGLAGLEKRLPGE-----LSGGERQRVAL 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03298   140 ARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQP-EDAKRLAQRVVFLDNGRIAAQG 211
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
7-128 1.64e-12

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 67.00  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   7 YVQQDDCFIGSLTVEEHLKFMAKLkmgSEYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILT 86
Cdd:COG2884    83 VVFQDFRLLPDRTVYENVALPLRV---TGKSRKEIRRRVREVLDLVGLSDKAKALPHE-----LSGGEQQRVAIARALVN 154
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1831510678  87 SPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIH 128
Cdd:COG2884   155 RPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATH 195
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
59-154 2.02e-12

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: 69.40  E-value: 2.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  59 DSIIGTRTRkGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSSQVFqlF 138
Cdd:COG4988   464 DTPLGEGGR-GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ--A 538
                          90
                  ....*....|....*.
gi 1831510678 139 DSIYMMVNGDVAFCGS 154
Cdd:COG4988   539 DRILVLDDGRIVEQGT 554
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
71-154 2.20e-12

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 66.82  E-value: 2.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSqVFQLFDSIYMMVNGDVA 150
Cdd:cd03256   146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDL-AREYADRIVGLKDGRIV 224

                  ....
gi 1831510678 151 FCGS 154
Cdd:cd03256   225 FDGP 228
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
70-147 2.42e-12

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: 65.10  E-value: 2.42e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSSqvFQLFDSIYMMVNG 147
Cdd:cd03228    97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLST--IRDADRIIVLDDG 170
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
6-153 4.09e-12

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: 65.62  E-value: 4.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   6 AYVQQDDCFIGSLTVEEHLKF-MAKLKMGSEydlnEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEI 84
Cdd:cd03259    75 GMVFQDYALFPHLTVAENIAFgLKLRGVPKA----EIRARVRELLELVGLEGLLN-----RYPHELSGGQQQRVALARAL 145
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510678  85 LTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03259   146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQ-EEALALADRIAVMNEGRIVQVG 213
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
2-154 5.01e-12

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 68.25  E-value: 5.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQD-DCFIGslTVEEHLKfMAKLkmgseyDLNEQErrVKSVMRSLGLEKIA-------DSIIGTRTRkGISGG 73
Cdd:COG4987   408 RRRIAVVPQRpHLFDT--TLRENLR-LARP------DATDEE--LWAALERVGLGDWLaalpdglDTWLGEGGR-RLSGG 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  74 EKKRLAFASEILTSPPILICDEPTSGLDSFLAYQvvcVLKKLAE-TRNMTILLTIHQPssQVFQLFDSIYMMVNGDVAFC 152
Cdd:COG4987   476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQA---LLADLLEaLAGRTVLLITHRL--AGLERMDRILVLEDGRIVEQ 550

                  ..
gi 1831510678 153 GS 154
Cdd:COG4987   551 GT 552
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
1-128 5.36e-12

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: 5.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLKFMAKLkmgSEYDLNEQERRVKSVMRSLGLEKIADSIigtrtRKGISGGEKKRLAF 80
Cdd:cd03292    76 LRRKIGVVFQDFRLLPDRNVYENVAFALEV---TGVPPREIRKRVPAALELVGLSHKHRAL-----PAELSGGEQQRVAI 147
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLaETRNMTILLTIH 128
Cdd:cd03292   148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATH 194
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
6-154 6.25e-12

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: 65.15  E-value: 6.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   6 AYVQQDDCFIGSLTVEEHLKfmaklkMGsEYDLNEQERRvksvmrsLGLEKIAD--SIIGTR-TRKG--ISGGEKKRLAF 80
Cdd:cd03224    78 GYVPEGRRIFPELTVEENLL------LG-AYARRRAKRK-------ARLERVYElfPRLKERrKQLAgtLSGGEQQMLAI 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnMTILLtIHQPSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:cd03224   144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEG-VTILL-VEQNARFALEIADRAYVLERGRVVLEGT 215
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
16-149 9.13e-12

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: 65.15  E-value: 9.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  16 GSLTVEEHLKFMAKLKMGSEYDLN-------EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSP 88
Cdd:cd03219    88 PELTVLENVMVAAQARTGSGLLLArarreerEARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDP 162
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510678  89 PILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPSSqVFQLFDSIYMMVNGDV 149
Cdd:cd03219   163 KLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDV-VMSLADRVTVLDQGRV 221
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
2-126 1.05e-11

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: 64.20  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQD-DCFIGSLTVEEHLKFMAKlkmgseyDLNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAF 80
Cdd:cd03226    70 RKSIGYVMQDvDYQLFTDSVREELLLGLK-------ELDAGNEQAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAI 137
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLT 126
Cdd:cd03226   138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVIT 183
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
18-149 1.68e-11

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: 63.81  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLKMGSEydlNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDEPT 97
Cdd:cd03301    87 MTVYDNIAFGLKLRKVPK---DEIDERVREVAELLQIEHLLD-----RKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1831510678  98 SGLDSFLAYQVVCVLKKLAETRNMTILLTIHqpsSQV--FQLFDSIYMMVNGDV 149
Cdd:cd03301   159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTH---DQVeaMTMADRIAVMNDGQI 209
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
2-128 2.14e-11

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 64.72  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLKFMAKLkmgseYDL--NEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLA 79
Cdd:TIGR01188  65 RRSIGIVPQYASVDEDLTGRENLEMMGRL-----YGLpkDEAEERAEELLELFELGEAADRPVGT-----YSGGMRRRLD 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1831510678  80 FASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETrNMTILLTIH 128
Cdd:TIGR01188 135 IAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEE-GVTILLTTH 182
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
18-153 3.34e-11

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 63.16  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLkmgseYDLN--EQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDE 95
Cdd:cd03266    93 LTARENLEYFAGL-----YGLKgdELTARLEELADRLGMEELLD-----RRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  96 PTSGLDSFLAYQVVCVLKKLAETrNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03266   163 PTTGLDVMATRALREFIRQLRAL-GKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
59-164 4.57e-11

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: 63.02  E-value: 4.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  59 DSIIGTRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSSQVFQlf 138
Cdd:cd03253   128 DTIVGERGLK-LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVNA-- 202
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1831510678 139 DSIYMMVNGDVAFCGS------QSGA-EKMWSE 164
Cdd:cd03253   203 DKIIVLKDGRIVERGTheellaKGGLyAEMWKA 235
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
38-147 5.27e-11

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 65.11  E-value: 5.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  38 LNEQERRVKSVMRSLGLEKIADSIIGTRTRKGI--------------SGGEKKRLAFASEILTSPPILICDEPTSGLDSF 103
Cdd:PRK15134  111 LEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaakrltdyphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVS 190
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1831510678 104 LAYQVVCVLKKLAETRNMTILLTIHQPSSqVFQLFDSIYMMVNG 147
Cdd:PRK15134  191 VQAQILQLLRELQQELNMGLLFITHNLSI-VRKLADRVAVMQNG 233
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
2-147 7.95e-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: 64.86  E-value: 7.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDcFIGSLTVEEHLKFMAKlkmgseyDLNEQErrVKSVMRSLGL-EKIA------DSIIGTRTRkGISGGE 74
Cdd:COG2274   548 RRQIGVVLQDV-FLFSGTIRENITLGDP-------DATDEE--IIEAARLAGLhDFIEalpmgyDTVVGEGGS-NLSGGQ 616
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  75 KKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAetRNMTILLTIHQPSsqVFQLFDSIYMMVNG 147
Cdd:COG2274   617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLS--TIRLADRIIVLDKG 685
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
62-153 2.38e-10

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 59.63  E-value: 2.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  62 IGTRtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLkkLAETRNMTILLTIHQPSSqvFQLFDSI 141
Cdd:cd03247    95 LGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTG--IEHMDKI 166
                          90
                  ....*....|..
gi 1831510678 142 YMMVNGDVAFCG 153
Cdd:cd03247   167 LFLENGKIIMQG 178
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
7-154 5.03e-10

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 59.86  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   7 YVQQDDCFIGSLTVEEHLkfMAKLKMgSEYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILT 86
Cdd:cd03218    79 YLPQEASIFRKLTVEENI--LAVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKASS-----LSGGERRRVEIARALAT 150
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  87 SPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:cd03218   151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHN-VRETLSITDRAYIIYEGKVLAEGT 216
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
40-128 5.30e-10

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 61.64  E-value: 5.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKiadsiiGTRTR--KGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAE 117
Cdd:PRK15134  400 QREQQVIAVMEEVGLDP------ETRHRypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQ 473
                          90
                  ....*....|.
gi 1831510678 118 TRNMTILLTIH 128
Cdd:PRK15134  474 KHQLAYLFISH 484
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
1-164 6.36e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 60.25  E-value: 6.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQD-DCFIGSLTVEEHLKFMAkLKMGSEYDlnEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLA 79
Cdd:PRK13636   80 LRESVGMVFQDpDNQLFSASVYQDVSFGA-VNLKLPED--EVRKRVDNALKRTGIEHLKD-----KPTHCLSFGQKKRVA 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  80 FASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHqpSSQVFQLF-DSIYMMVNGDVAFcgsQSGA 158
Cdd:PRK13636  152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATH--DIDIVPLYcDNVFVMKEGRVIL---QGNP 226

                  ....*.
gi 1831510678 159 EKMWSE 164
Cdd:PRK13636  227 KEVFAE 232
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
6-147 2.75e-09

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 57.09  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   6 AYVQQDDcFIGSLTVEEHLKFmaklkmGSEYDlneqERRVKSVMRSLGLEKiaD---------SIIGtrtRKGI--SGGE 74
Cdd:cd03250    69 AYVSQEP-WIQNGTIRENILF------GKPFD----EERYEKVIKACALEP--DleilpdgdlTEIG---EKGInlSGGQ 132
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510678  75 KKRLAFASEILTSPPILICDEPTSGLDSFLAYQVV--CVLKKLAETRnmTILLTIHQPssQVFQLFDSIYMMVNG 147
Cdd:cd03250   133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFenCILGLLLNNK--TRILVTHQL--QLLPHADQIVVLDNG 203
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
40-129 3.10e-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: 57.15  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETr 119
Cdd:cd03262   111 EAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE- 184
                          90
                  ....*....|
gi 1831510678 120 NMTILLTIHQ 129
Cdd:cd03262   185 GMTMVVVTHE 194
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
59-149 4.27e-09

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: 56.86  E-value: 4.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  59 DSIIGTRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSSqvFQLF 138
Cdd:cd03251   129 DTVIGERGVK-LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLST--IENA 203
                          90
                  ....*....|.
gi 1831510678 139 DSIYMMVNGDV 149
Cdd:cd03251   204 DRIVVLEDGKI 214
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
59-132 4.49e-09

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: 58.84  E-value: 4.49e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510678  59 DSIIGTRTRkGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSS 132
Cdd:TIGR02857 449 DTPIGEGGA-GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLAL 519
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
37-153 6.04e-09

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 56.71  E-value: 6.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  37 DLNEQERR--VKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKK 114
Cdd:TIGR01184  85 DLSKSERRaiVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1831510678 115 LAETRNMTILLTIHQPSSQVFqLFDSIYMMVNGDVAFCG 153
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALL-LSDRVVMLTNGPAANIG 197
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
38-130 6.49e-09

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 56.30  E-value: 6.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  38 LNEQER-RVKSVMRSLGLEKIADsiigtrtRK--GISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKK 114
Cdd:COG3840   102 LTAEQRaQVEQALERVGLAGLLD-------RLpgQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
                          90
                  ....*....|....*.
gi 1831510678 115 LAETRNMTILLTIHQP 130
Cdd:COG3840   175 LCRERGLTVLMVTHDP 190
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
18-147 7.24e-09

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: 56.13  E-value: 7.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLKmgseyDLNEQE--RRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDE 95
Cdd:cd03269    85 MKVIDQLVYLAQLK-----GLKKEEarRRIDEWLERLELSEYANKRVEE-----LSKGNQQKVQFIAAVIHDPELLILDE 154
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1831510678  96 PTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQpSSQVFQLFDSIYMMVNG 147
Cdd:cd03269   155 PFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQ-MELVEELCDRVLLLNKG 204
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-149 8.77e-09

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 56.04  E-value: 8.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLK---FMAKLKMGSE-----YDL--NEQERRVKSVmrslglekiadsiiGTrtrkgI 70
Cdd:PRK11614   78 MREAVAIVPEGRRVFSRMTVEENLAmggFFAERDQFQErikwvYELfpRLHERRIQRA--------------GT-----M 138
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLtIHQPSSQVFQLFDSIYMMVNGDV 149
Cdd:PRK11614  139 SGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFL-VEQNANQALKLADRGYVLENGHV 215
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
18-128 9.02e-09

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 56.19  E-value: 9.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLkfMAKLKMgSEYDLNEQERRVKSVMRSLGLEKIADSiigtrtrKGI--SGGEKKRLAFASEILTSPPILICDE 95
Cdd:COG1137    93 LTVEDNI--LAVLEL-RKLSKKEREERLEELLEEFGITHLRKS-------KAYslSGGERRRVEIARALATNPKFILLDE 162
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1831510678  96 PTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIH 128
Cdd:COG1137   163 PFAGVDPIAVADIQKIIRHLKE-RGIGVLITDH 194
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
2-147 9.88e-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: 55.67  E-value: 9.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQD-DCFIGSLTveehlkfmAKLKMGseyDLNEQERRVKSVMRSLGLEKIA-------DSIIGTRTRkGISGG 73
Cdd:cd03245    77 RRNIGYVPQDvTLFYGTLR--------DNITLG---APLADDERILRAAELAGVTDFVnkhpnglDLQIGERGR-GLSGG 144
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510678  74 EKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSsqVFQLFDSIYMMVNG 147
Cdd:cd03245   145 QRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPS--LLDLVDRIIVMDSG 214
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
18-154 1.02e-08

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 56.66  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLKmGseYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPT 97
Cdd:COG4152    86 MKVGEQLVYLARLK-G--LSKAEAKRRADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLILDEPF 157
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510678  98 SGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:COG4152   158 SGLDPVNVELLKDVIRELAA-KGTTVIFSSHQ-MELVEELCDRIVIINKGRKVLSGS 212
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
11-128 1.19e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 56.15  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  11 DDCFIGSlTVEEHLKFMAKLKMgseYDLNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPI 90
Cdd:PRK13632   93 DNQFIGA-TVEDDIAFGLENKK---VPPKKMKDIIDDLAKKVGMEDYLD-----KEPQNLSGGQKQRVAIASVLALNPEI 163
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1831510678  91 LICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:PRK13632  164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITH 201
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
7-163 1.55e-08

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 56.42  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   7 YVQQDDCFIGSLTVEEHLKFMAKLKMGSEYDlneqerrvkSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILT 86
Cdd:PRK11144   80 YVFQDARLFPHYKVRGNLRYGMAKSMVAQFD---------KIVALLGIEPLLDRYPGS-----LSGGEKQRVAIGRALLT 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  87 SPPILICDEPTSGLD-----SFLAYqvvcvLKKLAETRNMTILLTIHqpSSQ-VFQLFDSIYMMVNGDVAfcgSQSGAEK 160
Cdd:PRK11144  146 APELLLMDEPLASLDlprkrELLPY-----LERLAREINIPILYVSH--SLDeILRLADRVVVLEQGKVK---AFGPLEE 215

                  ...
gi 1831510678 161 MWS 163
Cdd:PRK11144  216 VWA 218
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
7-154 1.60e-08

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 55.36  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   7 YVQQDDCFIGSLTVEEHLkfMAKLKMGSEYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILT 86
Cdd:TIGR04406  80 YLPQEASIFRKLTVEENI--MAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMS-----LSGGERRRVEIARALAT 152
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  87 SPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHLKE-RGIGVLITDHN-VRETLDICDRAYIISDGKVLAEGT 218
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
5-144 1.68e-08

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: 55.17  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   5 CAYVQQDDCFIGSLTVEEHLKFMAKLKMGSEydlNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEI 84
Cdd:cd03293    75 RGYVFQQDALLPWLTVLDNVALGLELQGVPK---AEARERAEELLELVGLSGFEN-----AYPHQLSGGMRQRVALARAL 146
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  85 LTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSQVFqLFDSIYMM 144
Cdd:cd03293   147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVF-LADRVVVL 205
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1-101 1.68e-08

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 57.72  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678    1 MRQVCAYVQQDDCFIGSLTVEEHLKFMAKLK-MGSEydlnEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLA 79
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTGREHLYLYARLRgVPAE----EIEKVANWSIQSLGLSLYADRLAGT-----YSGGNKRKLS 2080
                           90       100
                   ....*....|....*....|..
gi 1831510678   80 FASEILTSPPILICDEPTSGLD 101
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMD 2102
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
48-154 1.79e-08

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 57.14  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  48 VMRSLGLEKIADSIIGTRTRKG-----ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAetRNMT 122
Cdd:PRK11160  449 VLQQVGLEKLLEDDKGLNAWLGeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKT 526
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1831510678 123 ILLTIHQPSSqvFQLFDSIYMMVNGDVAFCGS 154
Cdd:PRK11160  527 VLMITHRLTG--LEQFDRICVMDNGQIIEQGT 556
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
59-102 1.81e-08

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 56.89  E-value: 1.81e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1831510678  59 DSIIGTRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDS 102
Cdd:PRK13657  462 DTVVGERGRQ-LSGGERQRLAIARALLKDPPILILDEATSALDV 504
cbiO PRK13646
energy-coupling factor transporter ATPase;
70-154 2.04e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 55.56  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDV 149
Cdd:PRK13646  146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHD-MNEVARYADEVIVMKEGSI 224

                  ....*
gi 1831510678 150 AFCGS 154
Cdd:PRK13646  225 VSQTS 229
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
8-128 2.05e-08

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 55.99  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   8 VQQDDCFIGSLTVEEHLkfmakLKMGSEYDLNEqeRRVKSVMRSL----GLEKIADSIIGTrtrkgISGGEKKRLAFASE 83
Cdd:PRK13536  119 VPQFDNLDLEFTVRENL-----LVFGRYFGMST--REIEAVIPSLlefaRLESKADARVSD-----LSGGMKRRLTLARA 186
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1831510678  84 ILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAeTRNMTILLTIH 128
Cdd:PRK13536  187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTH 230
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
6-154 2.21e-08

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: 54.99  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   6 AYVQQD-DCFiGSLTVEEHLK---FMAKLKMGSEYDLNE--------QERRvksvmRSLGlekiadsiiGTrtrkgISGG 73
Cdd:COG0410    81 GYVPEGrRIF-PSLTVEENLLlgaYARRDRAEVRADLERvyelfprlKERR-----RQRA---------GT-----LSGG 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  74 EKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLtIHQPSSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:COG0410   141 EQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILL-VEQNARFALEIADRAYVLERGRIVLEG 218

                  .
gi 1831510678 154 S 154
Cdd:COG0410   219 T 219
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
71-125 6.41e-08

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: 54.29  E-value: 6.41e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILL 125
Cdd:COG0444   152 SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILF 206
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
59-150 6.93e-08

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 55.17  E-value: 6.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  59 DSIIGTRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLaeTRNMTILLTIHQPSSqvFQLF 138
Cdd:COG1132   467 DTVVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLST--IRNA 541
                          90
                  ....*....|..
gi 1831510678 139 DSIYMMVNGDVA 150
Cdd:COG1132   542 DRILVLDDGRIV 553
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-128 7.27e-08

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 54.04  E-value: 7.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLkfmakLKMGSEYDLNEQE--RRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLA 79
Cdd:PRK13537   79 RQRVGVVPQFDNLDPDFTVRENL-----LVFGRYFGLSAAAarALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLT 148
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1831510678  80 FASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAeTRNMTILLTIH 128
Cdd:PRK13537  149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTH 196
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
18-128 8.90e-08

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: 53.01  E-value: 8.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLKMGSEydlNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDEPT 97
Cdd:cd03300    87 LTVFENIAFGLRLKKLPK---AEIKERVAEALDLVQLEGYAN-----RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1831510678  98 SGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:cd03300   159 GALDLKLRKDMQLELKRLQKELGITFVFVTH 189
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
58-130 9.08e-08

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: 54.67  E-value: 9.08e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  58 ADSIIGTRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLkkLAETRNMTILLTIHQP 130
Cdd:TIGR02868 461 LDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
40-156 9.76e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 53.13  E-value: 9.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVM----RSLGLEKIADSIIGTRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKL 115
Cdd:PRK14246  121 KEKREIKKIVeeclRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL 199
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1831510678 116 aeTRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCGSQS 156
Cdd:PRK14246  200 --KNEIAIVIVSHNP-QQVARVADYVAFLYNGELVEWGSSN 237
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
2-102 1.13e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 52.18  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLKFMAKLkmgseydLNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFA 81
Cdd:PRK13539   72 AEACHYLGHRNAMKPALTVAENLEFWAAF-------LGGEELDIAAALEAVGLAPLAH-----LPFGYLSAGQKRRVALA 139
                          90       100
                  ....*....|....*....|.
gi 1831510678  82 SEILTSPPILICDEPTSGLDS 102
Cdd:PRK13539  140 RLLVSNRPIWILDEPTAALDA 160
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
39-129 1.52e-07

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 53.54  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  39 NEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLD-----SFLAyqvvcVLK 113
Cdd:COG1135   115 AEIRKRVAELLELVGLSDKADAYPSQ-----LSGGQKQRVGIARALANNPKVLLCDEATSALDpettrSILD-----LLK 184
                          90
                  ....*....|....*.
gi 1831510678 114 KLAETRNMTILLTIHQ 129
Cdd:COG1135   185 DINRELGLTIVLITHE 200
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
18-128 2.04e-07

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 51.95  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLkmgseYDLNEQE--RRVKSVMRSLGLEKIADsiigTRTRKgISGGEKKRLAFASEILTSPPILICDE 95
Cdd:cd03267   110 LPVIDSFYLLAAI-----YDLPPARfkKRLDELSELLDLEELLD----TPVRQ-LSLGQRMRAEIAAALLHEPEILFLDE 179
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1831510678  96 PTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:cd03267   180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSH 212
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
18-130 2.46e-07

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 51.99  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLKMGSEYDLNEQERRVKSVMRSLGL-EKIADsiigtrtR---KGISGGEKKRlafaSEILT----SPP 89
Cdd:COG0396    92 VSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLD-------RyvnEGFSGGEKKR----NEILQmlllEPK 160
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1831510678  90 ILICDEPTSGLDsflayqvVCVLKKLAE------TRNMTILLTIHQP 130
Cdd:COG0396   161 LAILDETDSGLD-------IDALRIVAEgvnklrSPDRGILIITHYQ 200
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
68-131 2.52e-07

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 51.67  E-value: 2.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510678  68 KGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPS 131
Cdd:COG4181   145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA 208
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
39-154 2.62e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 52.55  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  39 NEQERRVKSVMRSLGLekiaDSIIGTRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKlAET 118
Cdd:PRK13631  150 SEAKKLAKFYLNKMGL----DDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKA 224
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1831510678 119 RNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:PRK13631  225 NNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTGT 259
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
40-129 2.92e-07

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 51.63  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtR 119
Cdd:PRK09493  112 EAEKQARELLAKVGLAERAHHYPSE-----LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAE-E 185
                          90
                  ....*....|
gi 1831510678 120 NMTILLTIHQ 129
Cdd:PRK09493  186 GMTMVIVTHE 195
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
59-155 2.96e-07

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: 51.72  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  59 DSIIGTRTrKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSSqvFQLF 138
Cdd:cd03252   129 DTIVGEQG-AGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLST--VKNA 203
                          90
                  ....*....|....*..
gi 1831510678 139 DSIYMMVNGDVAFCGSQ 155
Cdd:cd03252   204 DRIIVMEKGRIVEQGSH 220
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
71-102 3.02e-07

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 53.29  E-value: 3.02e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLDS 102
Cdd:COG5265   496 SGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
44-141 3.03e-07

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 52.89  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  44 RVKSVMRSLGLEKIADSI-IGTRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQvvcVLKKLAETRNMT 122
Cdd:COG4178   459 ELREALEAVGLGHLAERLdEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA---LYQLLREELPGT 535
                          90       100
                  ....*....|....*....|
gi 1831510678 123 ILLTI-HQPSsqVFQLFDSI 141
Cdd:COG4178   536 TVISVgHRST--LAAFHDRV 553
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
11-128 3.07e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 51.94  E-value: 3.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  11 DDCFIGSlTVEEHLKFmAKLKMGSEYDlnEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPI 90
Cdd:PRK13635   91 DNQFVGA-TVQDDVAF-GLENIGVPRE--EMVERVDQALRQVGMEDFLN-----REPHRLSGGQKQRVAIAGVLALQPDI 161
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1831510678  91 LICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:PRK13635  162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITH 199
cbiO PRK13645
energy-coupling factor transporter ATPase;
70-196 3.28e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 51.93  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDV 149
Cdd:PRK13645  151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHN-MDQVLRIADEVIVMHEGKV 229
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1831510678 150 AFCGSQSgaeKMWSEMKLPIPMNFNPSDHYLATMSIRDQAEETLKKN 196
Cdd:PRK13645  230 ISIGSPF---EIFSNQELLTKIEIDPPKLYQLMYKLKNKGIDLLNKN 273
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
70-129 3.48e-07

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 52.11  E-value: 3.48e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQ 129
Cdd:PRK11153  141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHE 200
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
40-129 4.18e-07

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 51.12  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETR 119
Cdd:PRK10771  105 AQREKLHAIARQMGIEDLLA-----RLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQER 179
                          90
                  ....*....|
gi 1831510678 120 NMTILLTIHQ 129
Cdd:PRK10771  180 QLTLLMVSHS 189
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
18-153 4.28e-07

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 51.95  E-value: 4.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLkmgSEYDLNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDEPT 97
Cdd:PRK11000   90 LSVAENMSFGLKL---AGAKKEEINQRVNQVAEVLQLAHLLD-----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  98 SGLDSFLAYQVVCVLKKLAETRNMTILLTIHqpsSQV--FQLFDSIYMMVNGDVAFCG 153
Cdd:PRK11000  162 SNLDAALRVQMRIEISRLHKRLGRTMIYVTH---DQVeaMTLADKIVVLDAGRVAQVG 216
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
70-130 4.45e-07

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 52.50  E-value: 4.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQP 130
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
16-128 5.30e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 52.43  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  16 GSLTVEEHLKFMAKLkmgseYDL--NEQERRVKSVMRSLGLEKIADSIIGtrtrkGISGGEKKRLAFASEILTSPPILIC 93
Cdd:NF033858  352 GELTVRQNLELHARL-----FHLpaAEIAARVAEMLERFDLADVADALPD-----SLPLGIRQRLSLAVAVIHKPELLIL 421
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1831510678  94 DEPTSGLD-----SFLAYqvvcvLKKLAETRNMTILLTIH 128
Cdd:NF033858  422 DEPTSGVDpvardMFWRL-----LIELSREDGVTIFISTH 456
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
2-149 6.41e-07

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 50.30  E-value: 6.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDcFIGSLTVeehlkfMAKLKMGseyDLNEQERRVKSVMRSLG-------LEKIADSIIGTRTrKGISGGE 74
Cdd:cd03254    76 RSMIGVVLQDT-FLFSGTI------MENIRLG---RPNATDEEVIEAAKEAGahdfimkLPNGYDTVLGENG-GNLSQGE 144
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510678  75 KKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSSQVFQlfDSIYMMVNGDV 149
Cdd:cd03254   145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKNA--DKILVLDDGKI 215
cbiO PRK13650
energy-coupling factor transporter ATPase;
11-195 6.58e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 50.89  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  11 DDCFIGSlTVEEHLKFmaklkmGSE---YDLNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTS 87
Cdd:PRK13650   91 DNQFVGA-TVEDDVAF------GLEnkgIPHEEMKERVNEALELVGMQDFKE-----REPARLSGGQKQRVAIAGAVAMR 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  88 PPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSqvFQLFDSIYMMVNGDVAfcgSQSGAEKMWS---- 163
Cdd:PRK13650  159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE--VALSDRVLVMKNGQVE---STSTPRELFSrgnd 233
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1831510678 164 --EMKLPIPMN-----------FNPSDHYLATMSIRDQAEETLKK 195
Cdd:PRK13650  234 llQLGLDIPFTtslvqslrqngYDLPEGYLTEKELEEQLWELISK 278
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
40-149 7.11e-07

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: 50.26  E-value: 7.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGL-EKIADSIIGTrtrkGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAet 118
Cdd:cd03260   115 ELDERVEEALRKAALwDEVKDRLHAL----GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELK-- 188
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1831510678 119 RNMTILLTIHQPsSQVFQLFDSIYMMVNGDV 149
Cdd:cd03260   189 KEYTIVIVTHNM-QQAARVADRTAFLLNGRL 218
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
38-118 7.61e-07

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 50.40  E-value: 7.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  38 LNEQE--RRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKL 115
Cdd:PRK11124  113 LSKDQalARAEKLLERLRLKPYAD-----RFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL 187

                  ...
gi 1831510678 116 AET 118
Cdd:PRK11124  188 AET 190
cbiO PRK13643
energy-coupling factor transporter ATPase;
70-156 8.82e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 50.89  E-value: 8.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTihQPSSQVFQLFDSIYMMVNGDV 149
Cdd:PRK13643  145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVT--HLMDDVADYADYVYLLEKGHI 222

                  ....*..
gi 1831510678 150 AFCGSQS 156
Cdd:PRK13643  223 ISCGTPS 229
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
70-132 1.11e-06

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: 49.78  E-value: 1.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSS 132
Cdd:cd03248   151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLST 211
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
40-128 1.18e-06

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 51.22  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKiadsiiGTRTR--KGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAE 117
Cdd:COG4172   400 ERRARVAEALEEVGLDP------AARHRypHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQR 473
                          90
                  ....*....|.
gi 1831510678 118 TRNMTILLTIH 128
Cdd:COG4172   474 EHGLAYLFISH 484
cbiO PRK13640
energy-coupling factor transporter ATPase;
11-128 1.38e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 50.18  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  11 DDCFIGSlTVEEHLKFMAKLKMGSEydlNEQERRVKSVMRSLGLEKIADSiigtrTRKGISGGEKKRLAFASEILTSPPI 90
Cdd:PRK13640   94 DNQFVGA-TVGDDVAFGLENRAVPR---PEMIKIVRDVLADVGMLDYIDS-----EPANLSGGQKQRVAIAGILAVEPKI 164
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1831510678  91 LICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:PRK13640  165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITH 202
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
59-146 1.55e-06

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 51.18  E-value: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   59 DSIIGTRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSqvFQLF 138
Cdd:PTZ00265   570 ETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLST--IRYA 646

                   ....*...
gi 1831510678  139 DSIYMMVN 146
Cdd:PTZ00265   647 NTIFVLSN 654
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
7-128 1.74e-06

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 50.55  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   7 YVQQDdcfiGSLTVEEHLKFMAKLKMGSEYDLNEqerrvksVMRSLGLEKIADSIIgtrtrKGISGGEKKRLAFASEILT 86
Cdd:COG1245   409 YISPD----YDGTVEEFLRSANTDDFGSSYYKTE-------IIKPLGLEKLLDKNV-----KDLSGGELQRVAIAACLSR 472
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1831510678  87 SPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:COG1245   473 DADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH 514
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
69-160 1.76e-06

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: 48.68  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  69 GISGGEKKRLAFASEILTSPPILICDEPTSGLDsFLAYQVVC-VLKKLAEtRNMTILLTIHQPssqvfQLFDSI-----Y 142
Cdd:cd03217   104 GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDALRLVAeVINKLRE-EGKSVLIITHYQ-----RLLDYIkpdrvH 176
                          90
                  ....*....|....*...
gi 1831510678 143 MMVNGDVAFCGSQSGAEK 160
Cdd:cd03217   177 VLYDGRIVKSGDKELALE 194
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
37-153 1.80e-06

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: 49.56  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  37 DLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLA 116
Cdd:cd03294   133 PRAEREERAAEALELVGLEGWEHKYPDE-----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQ 207
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1831510678 117 ETRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03294   208 AELQKTIVFITHDL-DEALRLGDRIAIMKDGRLVQVG 243
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
3-130 1.92e-06

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: 48.64  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   3 QVCAYVQQDDCFIGSLTVEEHLKFMAklkmgseyDLNEQERrVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFAS 82
Cdd:cd03231    73 RGLLYLGHAPGIKTTLSVLENLRFWH--------ADHSDEQ-VEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALAR 138
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1831510678  83 EILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMtILLTIHQP 130
Cdd:cd03231   139 LLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGM-VVLTTHQD 185
YadH COG0842
ABC-type multidrug transport system, permease component [Defense mechanisms];
312-450 2.19e-06

ABC-type multidrug transport system, permease component [Defense mechanisms];


Pssm-ID: 440604 [Multi-domain]  Cd Length: 200  Bit Score: 48.27  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 312 MISNMAFMFQFSVVHHFclEMNTFYRETSSRLyRVSAYFISKNLAELPSYIVSAVIFTSILYWMSGLVPIIDSFLIYMLV 391
Cdd:COG0842    14 LLFTALMLTALSIARER--EQGTLERLLVTPV-SRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLV 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510678 392 GILVQNIAISIGYMFSCIFGTVNLAVAVMPIFVVPMMAFGGFFINQDTL----QW--YFVPMKYL 450
Cdd:COG0842    91 LLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLpgwlQAiaYLNPLTYF 155
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
59-149 2.28e-06

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: 49.08  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  59 DSIIGTRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSSqvFQLF 138
Cdd:cd03249   130 DTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLST--IRNA 204
                          90
                  ....*....|.
gi 1831510678 139 DSIYMMVNGDV 149
Cdd:cd03249   205 DLIAVLQNGQV 215
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
36-128 2.29e-06

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 49.70  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  36 YDLNEQE--RRVKSVMRSLGLEKIADsiigTRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLK 113
Cdd:COG4586   124 YRIPDAEykKRLDELVELLDLGELLD----TPVRQ-LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLK 198
                          90
                  ....*....|....*
gi 1831510678 114 KLAETRNMTILLTIH 128
Cdd:COG4586   199 EYNRERGTTILLTSH 213
cbiO PRK13649
energy-coupling factor transporter ATPase;
41-154 2.41e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 49.36  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  41 QERRVKSVMRSLGLEKIADSIIGtRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETrN 120
Cdd:PRK13649  118 QEEAEALAREKLALVGISESLFE-KNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-G 195
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1831510678 121 MTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:PRK13649  196 MTIVLVTHL-MDDVANYADFVYVLEKGKLVLSGK 228
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
70-169 2.44e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 49.24  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILltihqpSSQ----VFQLFDSIYMMV 145
Cdd:PRK13638  137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVII------SSHdidlIYEISDAVYVLR 210
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1831510678 146 NGDVAFCGS------------QSGAEKMW-----SEMKLPI 169
Cdd:PRK13638  211 QGQILTHGApgevfacteameQAGLTQPWlvklhTQLGLPL 251
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
71-101 2.46e-06

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: 47.06  E-value: 2.46e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:cd03221    72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
71-163 2.52e-06

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 49.71  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPsSQVFQLFDSIYMMVNGDVA 150
Cdd:COG4148   135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSL-DEVARLADHVVLLEQGRVV 213
                          90
                  ....*....|...
gi 1831510678 151 FCGSqsgAEKMWS 163
Cdd:COG4148   214 ASGP---LAEVLS 223
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
40-154 2.66e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 49.25  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLekiaDSIIGTRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETR 119
Cdd:PRK13634  120 DAKQKAREMIELVGL----PEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEK 195
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1831510678 120 NMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:PRK13634  196 GLTTVLVTHS-MEDAARYADQIVVMHKGTVFLQGT 229
cbiO PRK13642
energy-coupling factor transporter ATPase;
11-149 2.89e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 48.94  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  11 DDCFIGSlTVEEHLKFmaklkmGSEYDLNEQERRVKSVMRSLGLEKIADsiIGTRTRKGISGGEKKRLAFASEILTSPPI 90
Cdd:PRK13642   91 DNQFVGA-TVEDDVAF------GMENQGIPREEMIKRVDEALLAVNMLD--FKTREPARLSGGQKQRVAVAGIIALRPEI 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510678  91 LICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSQVFQlfDSIYMMVNGDV 149
Cdd:PRK13642  162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASS--DRILVMKAGEI 218
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
40-180 3.39e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 48.59  E-value: 3.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSiigtrTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETR 119
Cdd:PRK13648  118 EMHRRVSEALKQVDMLERADY-----EPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEH 192
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510678 120 NMTILLTIHQPSSQVfqlfDSIYMMV--NGDVAFCGSQS---GAEKMWSE--MKLPIPMNFNP----SDHYL 180
Cdd:PRK13648  193 NITIISITHDLSEAM----EADHVIVmnKGTVYKEGTPTeifDHAEELTRigLDLPFPIKINQmlghQTSFL 260
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
40-129 3.45e-06

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 48.47  E-value: 3.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETR 119
Cdd:PRK09984  128 EQKQRALQALTRVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQND 202
                          90
                  ....*....|
gi 1831510678 120 NMTILLTIHQ 129
Cdd:PRK09984  203 GITVVVTLHQ 212
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
40-115 3.70e-06

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 48.93  E-value: 3.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510678  40 EQERRVKSVMRSLGLekIADSIigTRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKL 115
Cdd:PRK15079  136 EVKDRVKAMMLKVGL--LPNLI--NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL 207
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
2-173 3.75e-06

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: 48.10  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVcAYVQQDDCFIGSLTVEEHLKFMAKLKMGSEY-DLNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAF 80
Cdd:cd03296    74 RNV-GFVFQHYALFRHMTVFDNVAFGLRVKPRSERpPEAEIRAKVHELLKLVQLDWLAD-----RYPAQLSGGQRQRVAL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGSqsgAEK 160
Cdd:cd03296   148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHD-QEEALEVADRVVVMNKGRIEQVGT---PDE 223
                         170
                  ....*....|...
gi 1831510678 161 MWSEMKLPIPMNF 173
Cdd:cd03296   224 VYDHPASPFVYSF 236
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1-129 4.34e-06

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 49.63  E-value: 4.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678    1 MRQVCAYVQQDDCFIGSLTVEEHLKFMAKLKmGSEYDlnEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAF 80
Cdd:TIGR01257 1001 VRQSLGMCPQHNILFHHLTVAEHILFYAQLK-GRSWE--EAQLEMEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSV 1072
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1831510678   81 ASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQ 129
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHH 1119
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
18-118 5.77e-06

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 47.70  E-value: 5.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLkFMAKLKMgseYDLNEQERRVK--SVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDE 95
Cdd:COG4161    97 LTVMENL-IEAPCKV---LGLSKEQAREKamKLLARLRLTDKAD-----RFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
                          90       100
                  ....*....|....*....|...
gi 1831510678  96 PTSGLDSFLAYQVVCVLKKLAET 118
Cdd:COG4161   168 PTAALDPEITAQVVEIIRELSQT 190
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
70-126 6.48e-06

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 47.66  E-value: 6.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLT 126
Cdd:PRK10619  153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVT 209
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
69-154 6.89e-06

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 47.46  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  69 GISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtrNMTILLTIHQpSSQVFQLFDSIYMMVNGD 148
Cdd:PRK14239  148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRS-MQQASRISDRTGFFLDGD 224

                  ....*.
gi 1831510678 149 VAFCGS 154
Cdd:PRK14239  225 LIEYND 230
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
70-147 7.32e-06

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: 48.56  E-value: 7.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnmTILLTIHQPSSqvFQLFDSIYMMVNG 147
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLST--IEKADRIVVMDDG 543
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
71-147 7.57e-06

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 46.66  E-value: 7.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLD----SFLaYQvvcVLKKLAEtRNMTILLTihqpSS---QVFQLFDSIYM 143
Cdd:cd03215   106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDvgakAEI-YR---LIRELAD-AGKAVLLI----SSeldELLGLCDRILV 176

                  ....
gi 1831510678 144 MVNG 147
Cdd:cd03215   177 MYEG 180
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
7-130 8.43e-06

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 47.08  E-value: 8.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   7 YVQQDDCFIGSLTVEEHLKFMAKLKMGSEydlNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILT 86
Cdd:PRK10584   92 FVFQSFMLIPTLNALENVELPALLRGESS---RQSRNGAKALLEQLGLGKRLDHLPAQ-----LSGGEQQRVALARAFNG 163
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1831510678  87 SPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQP 130
Cdd:PRK10584  164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDL 207
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
19-128 8.45e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 47.77  E-value: 8.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  19 TVEEHLKFMAkLKMGSeyDLNEQERRVKSVMRSLGLekiaDSIIGTRTRKGISGGEKKRLAFASEILTSPPILICDEPTS 98
Cdd:PRK13651  122 TIEKDIIFGP-VSMGV--SKEEAKKRAAKYIELVGL----DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTA 194
                          90       100       110
                  ....*....|....*....|....*....|
gi 1831510678  99 GLDSFLAYQVVCVLKKLAEtRNMTILLTIH 128
Cdd:PRK13651  195 GLDPQGVKEILEIFDNLNK-QGKTIILVTH 223
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
45-130 8.78e-06

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 46.88  E-value: 8.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  45 VKSVMRSLGLEKIADSIIGTRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTIL 124
Cdd:COG2401   112 FKDAVELLNAVGLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLV 191

                  ....*.
gi 1831510678 125 LTIHQP 130
Cdd:COG2401   192 VATHHY 197
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
66-144 1.13e-05

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 45.81  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  66 TRKGISGGEKKR----LAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTiHQPssQVFQLFDSI 141
Cdd:cd03227    74 TRLQLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVIT-HLP--ELAELADKL 150

                  ...
gi 1831510678 142 YMM 144
Cdd:cd03227   151 IHI 153
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
70-128 1.23e-05

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 47.43  E-value: 1.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:PRK11022  154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITH 212
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
70-128 1.23e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 47.00  E-value: 1.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:PRK13633  145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH 203
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
18-154 1.23e-05

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 47.63  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLKMGSEydlNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDEPT 97
Cdd:PRK09452  101 MTVFENVAFGLRMQKTPA---AEITPRVMEALRMVQLEEFAQ-----RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510678  98 SGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:PRK09452  173 SALDYKLRKQMQNELKALQRKLGITFVFVTHD-QEEALTMSDRIVVMRDGRIEQDGT 228
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
71-128 1.24e-05

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 47.76  E-value: 1.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:COG4172   158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH 215
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
70-154 1.42e-05

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 46.62  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDV 149
Cdd:PRK10418  141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHD-MGVVARLADDVAVMSHGRI 219

                  ....*
gi 1831510678 150 AFCGS 154
Cdd:PRK10418  220 VEQGD 224
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
71-131 1.49e-05

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 45.22  E-value: 1.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLaetrnMTILLTI-HQPS 131
Cdd:cd03223    93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL-----GITVISVgHRPS 149
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
1-154 1.58e-05

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: 46.52  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSLTVEEHLKFMAKLKmgsEYDLNEQERRVKSVMRSLGLE--KIADsiigtRTRKGISGGEKKRL 78
Cdd:cd03295    73 LRRKIGYVIQQIGLFPHMTVEENIALVPKLL---KWPKEKIRERADELLALVGLDpaEFAD-----RYPHELSGGQQQRV 144
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510678  79 AFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:cd03295   145 GVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD-IDEAFRLADRIAIMKNGEIVQVGT 219
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
70-124 1.81e-05

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 46.28  E-value: 1.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLA-ETRNMTIL 124
Cdd:PRK11264  145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAqEKRTMVIV 200
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
40-149 1.91e-05

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 47.02  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETR 119
Cdd:PRK11432  112 ERKQRVKEALELVDLAGFED-----RYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQF 186
                          90       100       110
                  ....*....|....*....|....*....|
gi 1831510678 120 NMTILLTIHQpSSQVFQLFDSIYMMVNGDV 149
Cdd:PRK11432  187 NITSLYVTHD-QSEAFAVSDTVIVMNKGKI 215
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
59-154 2.07e-05

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 47.15  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  59 DSIIGTRTRkGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRnMTILLTiHQPSSqvFQLF 138
Cdd:PRK11174  476 DTPIGDQAA-GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ-TTLMVT-HQLED--LAQW 550
                          90
                  ....*....|....*.
gi 1831510678 139 DSIYMMVNGDVAFCGS 154
Cdd:PRK11174  551 DQIWVMQDGQIVQQGD 566
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
34-149 2.12e-05

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: 44.90  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  34 SEYDLNEQERRVKSVMRSLGLEK--IADSIIgtrtrkgiSGGEKKRLAFASEILTSPPILICDEPTSGLDSF---LAYQV 108
Cdd:cd03246    67 SQWDPNELGDHVGYLPQDDELFSgsIAENIL--------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEgerALNQA 138
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1831510678 109 VCVLKKLAETRnmtILLTiHQPSsqVFQLFDSIYMMVNGDV 149
Cdd:cd03246   139 IAALKAAGATR---IVIA-HRPE--TLASADRILVLEDGRV 173
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-101 2.31e-05

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 46.98  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   6 AYVQQDDCFIGSLTVEEH-----------LKFMAKL--KMG-SEYDLNEQ---------------ERRVKSVMRSLGL-E 55
Cdd:COG0488    64 GYLPQEPPLDDDLTVLDTvldgdaelralEAELEELeaKLAePDEDLERLaelqeefealggweaEARAEEILSGLGFpE 143
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1831510678  56 KIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:COG0488   144 EDLDRPVSE-----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
19-128 2.38e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 47.11  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  19 TVEEHLKFMAKlKMGSEYDLNEqerrvksVMRSLGLEKIADSIIgtrtrKGISGGEKKRLAFASEILTSPPILICDEPTS 98
Cdd:PRK13409  416 TVEDLLRSITD-DLGSSYYKSE-------IIKPLQLERLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
                          90       100       110
                  ....*....|....*....|....*....|
gi 1831510678  99 GLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:PRK13409  483 HLDVEQRLAVAKAIRRIAEEREATALVVDH 512
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
42-128 2.39e-05

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 46.76  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  42 ERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETrNM 121
Cdd:PRK09536  117 RAAVERAMERTGVAQFADRPVTS-----LSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GK 190

                  ....*..
gi 1831510678 122 TILLTIH 128
Cdd:PRK09536  191 TAVAAIH 197
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
2-128 3.30e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 45.27  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSLTVEEHLkfMAKLKMGSEYDLNEQERRVKSVMRSLGLEKIADSIigtrtRKGISGGEKKRLAFA 81
Cdd:PRK10895   77 RRGIGYLPQEASIFRRLSVYDNL--MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIA 149
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1831510678  82 SEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIH 128
Cdd:PRK10895  150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDH 195
ABC2_membrane_7 pfam19055
ABC-2 type transporter;
128-521 4.03e-05

ABC-2 type transporter;


Pssm-ID: 465963 [Multi-domain]  Cd Length: 409  Bit Score: 46.05  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 128 HQPSSQVFQLFDS-IYMMVNGDVAFCGSQSGAEKMWSEMKLPIPMNFNPSDHYLatmsirDQAEETLKKNQIgkicTTFK 206
Cdd:pfam19055   1 HQPSYTLFKMFDDlILLAKGGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFI------DILEGIVKPSTS----SGVD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 207 YSEL----------------------------GKSVFKESSGREVDERD---------RAFSEDWRRRYATTFGRP---- 245
Cdd:pfam19055  71 YKQLpvrwmlhngypvppdmlqnadgiaassgENSSNGTNPGVGSEEQSfagelwqdvKSNVELKRDHIRHNFLKSkdls 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 246 -RFGASFFQQIRALTWRASKTVLREPTLLkvqtFQSIIIAILTGLVYTNNSPVDQQKiMNINGSLYQMISnMAFMFQFSV 324
Cdd:pfam19055 151 nRRTPGVFRQYRYFLGRVGKQRLREARIQ----AVDYLILLLAGACLGTLAKVSDET-FGALGYTYTIIA-VSLLCKIAA 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 325 VHHFCLEMNTFYRETSSRLYRVsAYFISKNLAELPSYIVSAVIFTSILYWMSGlvP---IIDSF-----LIYMLVGIlvq 396
Cdd:pfam19055 225 LRSFSLDKLQYWRESASGMSSL-AYFLAKDTIDHFNTVIKPLVYLSMFYFFNN--PrssFADNYivllcLVYCVTGI--- 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 397 niaisiGYMFSCIF--GTVNLAVAVMPIfVVPMMAfggffiNQDTLQWYFVPMKYLSYFGYGYEAVAIA---QWTHVEEI 471
Cdd:pfam19055 299 ------AYALAIFFepGPAQLWSVLLPV-VLTLIA------TQTNDSKFLKVLANLCYPKWALEAFVIAnaeRYSGVWLI 365
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831510678 472 PGCSSSLahcsRNGTDVlnsmsfkpSNFWVDISVMAFMIFVFRFLAFMAL 521
Cdd:pfam19055 366 TRCGALM----KSGYDL--------HDWGLCLVILILYGVLSRIIAFFCM 403
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
70-153 4.14e-05

ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 45.67  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSqVFQLFDSIYMMvngdv 149
Cdd:COG4170   159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLES-ISQWADTITVL----- 232

                  ....
gi 1831510678 150 aFCG 153
Cdd:COG4170   233 -YCG 235
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
41-154 5.30e-05

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 46.00  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  41 QERRVKSVMRSLGLEKIADS-IIGTRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETR 119
Cdd:PRK10261  139 REEAMVEAKRMLDQVRIPEAqTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEM 218
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1831510678 120 NMTILLTIHQpSSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:PRK10261  219 SMGVIFITHD-MGVVAEIADRVLVMYQGEAVETGS 252
ycf16 CHL00131
sulfate ABC transporter protein; Validated
69-161 7.51e-05

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 44.63  E-value: 7.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  69 GISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpssqvfQLFDSI-----YM 143
Cdd:CHL00131  151 GFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ------RLLDYIkpdyvHV 224
                          90
                  ....*....|....*...
gi 1831510678 144 MVNGDVAFCGSQSGAEKM 161
Cdd:CHL00131  225 MQNGKIIKTGDAELAKEL 242
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
68-163 7.83e-05

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 45.79  E-value: 7.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   68 KGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSqvFQLFDSIYMMVNG 147
Cdd:PTZ00265  1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIAS--IKRSDKIVVFNNP 1434
                           90
                   ....*....|....*...
gi 1831510678  148 DV--AFCGSQSGAEKMWS 163
Cdd:PTZ00265  1435 DRtgSFVQAHGTHEELLS 1452
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
70-139 8.05e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 44.64  E-value: 8.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFD 139
Cdd:PRK14258  151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN-LHQVSRLSD 219
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
71-128 8.45e-05

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 44.72  E-value: 8.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:PRK09473  163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH 220
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
70-131 8.74e-05

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 43.47  E-value: 8.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1831510678  70 ISGGEKKRLAFASEILTSPP--ILICDEPTSGLDSFLAYQVVCVLKKLAETRNmTILLTIHQPS 131
Cdd:cd03238    88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLD 150
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
40-149 1.06e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 44.13  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGL-EKIADSIIGTRTRkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLaeT 118
Cdd:PRK14247  118 ELQERVRWALEKAQLwDEVKDRLDAPAGK--LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--K 193
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1831510678 119 RNMTILLTIHQPsSQVFQLFDSIYMMVNGDV 149
Cdd:PRK14247  194 KDMTIVLVTHFP-QQAARISDYVAFLYKGQI 223
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-101 1.34e-04

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 44.67  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   6 AYVQQD-DCFIGSLTVEEHLkfmaklkmgSEYDLNEQERRVKSVMRSLGLEkiadsiiGTRTRKGI---SGGEKKRLAFA 81
Cdd:COG0488   381 GYFDQHqEELDPDKTVLDEL---------RDGAPGGTEQEVRGYLGRFLFS-------GDDAFKPVgvlSGGEKARLALA 444
                          90       100
                  ....*....|....*....|.
gi 1831510678  82 SeILTSPP-ILICDEPTSGLD 101
Cdd:COG0488   445 K-LLLSPPnVLLLDEPTNHLD 464
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
67-150 1.37e-04

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: 42.42  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  67 RKGI------SGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtRNMTILLTIHQPsSQVFQLFDS 140
Cdd:cd03216    74 RAGIamvyqlSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRL-DEVFEIADR 151
                          90
                  ....*....|
gi 1831510678 141 IYMMVNGDVA 150
Cdd:cd03216   152 VTVLRDGRVV 161
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
18-101 1.43e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 44.73  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  18 LTVEEHLKFMAKLkmgseYDLNEQER--RVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDE 95
Cdd:NF033858   93 LSVFENLDFFGRL-----FGQDAAERrrRIDELLRATGLAPFAD-----RPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162

                  ....*.
gi 1831510678  96 PTSGLD 101
Cdd:NF033858  163 PTTGVD 168
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
40-130 1.65e-04

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 42.61  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtR 119
Cdd:NF040873   95 DDRAAVDDALERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-R 168
                          90
                  ....*....|.
gi 1831510678 120 NMTILLTIHQP 130
Cdd:NF040873  169 GATVVVVTHDL 179
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
8-128 1.77e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 43.57  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   8 VQQD-DCFIGSLTVEEHLKFmAKLKMGseYDLNEQERRVKSVMRSLGLEKIADsiigtRTRKGISGGEKKRLAFASEILT 86
Cdd:PRK13647   84 VFQDpDDQVFSSTVWDDVAF-GPVNMG--LDKDEVERRVEEALKAVRMWDFRD-----KPPYHLSYGQKKRVAIAGVLAM 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1831510678  87 SPPILICDEPTSGLDSFLAYQVVCVLKKLaETRNMTILLTIH 128
Cdd:PRK13647  156 DPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATH 196
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
1-134 1.92e-04

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 43.94  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   1 MRQVCAYVQQDDCFIGSltveehlKFMAKLKMGSEYDlneqERRVKSVMRSLGLEKIADSII-GTRTRKG-----ISGGE 74
Cdd:PRK10790  413 LRQGVAMVQQDPVVLAD-------TFLANVTLGRDIS----EEQVWQALETVQLAELARSLPdGLYTPLGeqgnnLSVGQ 481
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  75 KKRLAFASEILTSPPILICDEPTSGLDSFL--AYQvvcvlKKLAETRNMTILLTI-HQPSSQV 134
Cdd:PRK10790  482 KQLLALARVLVQTPQILILDEATANIDSGTeqAIQ-----QALAAVREHTTLVVIaHRLSTIV 539
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
39-171 1.99e-04

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 43.94  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  39 NEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEt 118
Cdd:PRK10535  119 KQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD- 192
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831510678 119 RNMTILLTIHQPssQVFQLFDSIYMMVNGDVAfcgSQSGAEKMWSEMKLPIPM 171
Cdd:PRK10535  193 RGHTVIIVTHDP--QVAAQAERVIEIRDGEIV---RNPPAQEKVNVAGGTEPV 240
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
40-128 2.03e-04

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 43.24  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDsfLAYQ--VVCVLKKLAE 117
Cdd:PRK10575  123 ADREKVEEAISLVGLKPLAHRLVDS-----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--IAHQvdVLALVHRLSQ 195
                          90
                  ....*....|.
gi 1831510678 118 TRNMTILLTIH 128
Cdd:PRK10575  196 ERGLTVIAVLH 206
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
54-102 2.16e-04

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 43.85  E-value: 2.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831510678  54 LEKIADSIIGtrtRKGI--SGGEKKRLAFASEILTSPPILICDEPTSGLDS 102
Cdd:PRK11176  466 MDNGLDTVIG---ENGVllSGGQRQRIAIARALLRDSPILILDEATSALDT 513
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
37-108 2.36e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 43.41  E-value: 2.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510678  37 DLNEQERRVK--SVMRSLGLE-KIADsiigtRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQV 108
Cdd:PRK11308  124 SLSAAERREKalAMMAKVGLRpEHYD-----RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQV 193
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
70-131 2.42e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 42.91  E-value: 2.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtrNMTILLTIHQPS 131
Cdd:PRK14267  150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPA 209
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
70-150 2.61e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 43.56  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPssQVFQLFDSIYMMVNGDV 149
Cdd:PRK10982  392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMP--ELLGITDRILVMSNGLV 469

                  .
gi 1831510678 150 A 150
Cdd:PRK10982  470 A 470
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
1-154 3.08e-04

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: 43.78  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678    1 MRQVCAYVQQDdCFIGSLTVEEHLKFMAKLkmgseydlneQERRVKSVMRSLGLekIADSII---GTRTR---KGI--SG 72
Cdd:TIGR00957  697 MKGSVAYVPQQ-AWIQNDSLRENILFGKAL----------NEKYYQQVLEACAL--LPDLEIlpsGDRTEigeKGVnlSG 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   73 GEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVV-CVLKKLAETRNMTILLTIHQPS--SQVfqlfDSIYMMVNGDV 149
Cdd:TIGR00957  764 GQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISylPQV----DVIIVMSGGKI 839

                   ....*
gi 1831510678  150 AFCGS 154
Cdd:TIGR00957  840 SEMGS 844
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
40-128 3.38e-04

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 42.11  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSiigtRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETR 119
Cdd:PRK11629  121 EINSRALEMLAAVGLEHRANH----RPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQ 195

                  ....*....
gi 1831510678 120 NMTILLTIH 128
Cdd:PRK11629  196 GTAFLVVTH 204
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
43-128 4.68e-04

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 41.78  E-value: 4.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  43 RRVKSVMRSLGLEKIADSIigtrtRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVcvlkKLAETRN-- 120
Cdd:PRK10908  116 RRVSAALDKVGLLDKAKNF-----PIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL----RLFEEFNrv 186

                  ....*....
gi 1831510678 121 -MTILLTIH 128
Cdd:PRK10908  187 gVTVLMATH 195
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
40-128 4.96e-04

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 41.90  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  40 EQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETR 119
Cdd:PRK10253  119 EDEEAVTKAMQATGITHLADQSVDT-----LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREK 193

                  ....*....
gi 1831510678 120 NMTILLTIH 128
Cdd:PRK10253  194 GYTLAAVLH 202
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
2-108 4.99e-04

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 41.70  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVcAYVQQDDCFIGSLTVEEHLKFmaklKMGSEYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFA 81
Cdd:COG4136    76 RRI-GILFQDDLLFPHLSVGENLAF----ALPPTIGRAQRRARVEQALEEAGLAGFADRDPAT-----LSGGQRARVALL 145
                          90       100
                  ....*....|....*....|....*..
gi 1831510678  82 SEILTSPPILICDEPTSGLDSFLAYQV 108
Cdd:COG4136   146 RALLAEPRALLLDEPFSKLDAALRAQF 172
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
53-131 5.01e-04

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 42.79  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  53 GLEKIADSIIGtrtRKG--ISGGEKKRLAFASEILTSPPILICDEPTSGLDSflayQVVCVLKKLAETRNMTILLTIHQP 130
Cdd:TIGR00958 602 EFPNGYDTEVG---EKGsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRL 674

                  .
gi 1831510678 131 S 131
Cdd:TIGR00958 675 S 675
PLN03232 PLN03232
ABC transporter C family member; Provisional
1-119 5.63e-04

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 43.04  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678    1 MRQVCAYVQQDDcFIGSLTVEEHLKFmaklkmGSEYdlnEQERRVKSVmRSLGLEKIADSIIG-TRTRKG-----ISGGE 74
Cdd:PLN03232   677 IRGSVAYVPQVS-WIFNATVRENILF------GSDF---ESERYWRAI-DVTALQHDLDLLPGrDLTEIGergvnISGGQ 745
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1831510678   75 KKRLAFASEILTSPPILICDEPTSGLDSFLAYQVV--CVLKKL-AETR 119
Cdd:PLN03232   746 KQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdsCMKDELkGKTR 793
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
43-128 5.66e-04

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 42.48  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  43 RRVKSVMRSLGL-EKIADSIIGTRTRKgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNM 121
Cdd:TIGR03269 401 MKAVITLKMVGFdEEKAEEILDKYPDE-LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQ 479

                  ....*..
gi 1831510678 122 TILLTIH 128
Cdd:TIGR03269 480 TFIIVSH 486
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
69-149 5.92e-04

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 42.50  E-value: 5.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  69 GISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPssQVFQLFDSIYMMVNGD 148
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELA--EVLGLSDRVLVIGEGK 480

                  .
gi 1831510678 149 V 149
Cdd:TIGR02633 481 L 481
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
48-128 6.60e-04

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: 41.62  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  48 VMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTI 127
Cdd:cd03237    99 IAKPLQIEQILDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVE 173

                  .
gi 1831510678 128 H 128
Cdd:cd03237   174 H 174
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
71-101 7.00e-04

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 41.27  E-value: 7.00e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:COG4778   154 SGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
70-101 7.33e-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: 42.23  E-value: 7.33e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
15-125 8.29e-04

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 41.94  E-value: 8.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  15 IGSLTVEEHLKfmaklkMGSE------YDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLafasEIL--- 85
Cdd:COG3845    92 VPNLTVAENIV------LGLEptkggrLDRKAARARIRELSERYGLDVDPDAKVED-----LSVGEQQRV----EILkal 156
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1831510678  86 -TSPPILICDEPTSGL-----DSFLAyqvvcVLKKLAEtRNMTILL 125
Cdd:COG3845   157 yRGARILILDEPTAVLtpqeaDELFE-----ILRRLAA-EGKSIIF 196
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
30-154 9.06e-04

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 41.31  E-value: 9.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  30 LKMGSEYDLNEQERRVKSVMRSLGLekIADSIigTRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVV 109
Cdd:PRK15112  114 LRLNTDLEPEQREKQIIETLRQVGL--LPDHA--SYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1831510678 110 CVLKKLAETRNMT-ILLTIHQpsSQVFQLFDSIYMMVNGDVAFCGS 154
Cdd:PRK15112  190 NLMLELQEKQGISyIYVTQHL--GMMKHISDQVLVMHQGEVVERGS 233
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
32-101 1.00e-03

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 41.64  E-value: 1.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  32 MGSEYDLNEQERRVKSvmrSLGLEKIADSIIGTRTRKGISGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:NF000106  110 IGR*LDLSRKDARARA---DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
68-101 1.09e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 41.80  E-value: 1.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1831510678  68 KGISGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:PRK15064  437 KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
PLN03130 PLN03130
ABC transporter C family member; Provisional
1-129 1.12e-03

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 42.03  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678    1 MRQVCAYVQQDDcFIGSLTVEEHLKFmaklkmGSEYDLNEQER--RVKSVMRSLGLEKIAD-SIIGTRTRKgISGGEKKR 77
Cdd:PLN03130   677 IRGTVAYVPQVS-WIFNATVRDNILF------GSPFDPERYERaiDVTALQHDLDLLPGGDlTEIGERGVN-ISGGQKQR 748
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1831510678   78 LAFASEILTSPPILICDEPTSGLDSFLAYQVV--CVLKKLaetRNMTILLTIHQ 129
Cdd:PLN03130   749 VSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdkCIKDEL---RGKTRVLVTNQ 799
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
46-153 1.21e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 40.94  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  46 KSVMRSLGLEkiadsiigtrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILL 125
Cdd:PRK15093  149 KDAMRSFPYE--------------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILL 214
                          90       100       110
                  ....*....|....*....|....*....|
gi 1831510678 126 TIH--QPSSqvfQLFDSIymmvngDVAFCG 153
Cdd:PRK15093  215 ISHdlQMLS---QWADKI------NVLYCG 235
PTZ00243 PTZ00243
ABC transporter; Provisional
68-154 1.25e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 41.69  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   68 KGI--SGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVV--CVLKKLA-ETRnmtiLLTIHQpsSQVFQLFDSIY 142
Cdd:PTZ00243   779 KGVnlSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeeCFLGALAgKTR----VLATHQ--VHVVPRADYVV 852
                           90
                   ....*....|..
gi 1831510678  143 MMVNGDVAFCGS 154
Cdd:PTZ00243   853 ALGDGRVEFSGS 864
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
70-164 1.43e-03

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 40.84  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQpSSQVFQLFDSIYMMVNGDV 149
Cdd:PRK10851  137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHD-QEEAMEVADRVVVMSQGNI 215
                          90
                  ....*....|....*.
gi 1831510678 150 afcgSQSGA-EKMWSE 164
Cdd:PRK10851  216 ----EQAGTpDQVWRE 227
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
71-124 1.66e-03

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 40.49  E-value: 1.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLD-SFLAyQVVCVLKKLAETRNMTIL 124
Cdd:COG4608   159 SGGQRQRIGIARALALNPKLIVCDEPVSALDvSIQA-QVLNLLEDLQDELGLTYL 212
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
70-134 2.09e-03

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 40.05  E-value: 2.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIHQPSSQV 134
Cdd:PRK11247  134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAV 198
hmuV PRK13547
heme ABC transporter ATP-binding protein;
58-157 2.11e-03

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 40.20  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  58 ADSIIGtRTRKGISGGEKKRLAFA--------SEILTSPP-ILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:PRK13547  135 ATALVG-RDVTTLSGGELARVQFArvlaqlwpPHDAAQPPrYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVH 213
                          90       100
                  ....*....|....*....|....*....
gi 1831510678 129 QPSSQVfQLFDSIYMMVNGDVAFCGSQSG 157
Cdd:PRK13547  214 DPNLAA-RHADRIAMLADGAIVAHGAPAD 241
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
2-126 2.26e-03

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 39.62  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSlTVEEHLKFmaklkmGSEYdlNEQerRVKSVMRSLGLEKIADSI-IGTRTRKG-----ISGGEK 75
Cdd:cd03290    78 RYSVAYAAQKPWLLNA-TVEENITF------GSPF--NKQ--RYKAVTDACSLQPDIDLLpFGDQTEIGerginLSGGQR 146
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831510678  76 KRLAFASEILTSPPILICDEPTSGLDSFLAYQVV--CVLKKLAETRNMTILLT 126
Cdd:cd03290   147 QRICVARALYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVT 199
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
70-135 2.49e-03

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 39.68  E-value: 2.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKL-AETRNMTILLTiHQPSSQVF 135
Cdd:PRK11248  129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLIT-HDIEEAVF 194
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
59-101 2.59e-03

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 40.37  E-value: 2.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1831510678  59 DSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:PRK10762  390 EQAIGL-----LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
70-134 2.75e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 39.77  E-value: 2.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtrNMTILLTIH--QPSSQV 134
Cdd:PRK14243  152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHnmQQAARV 216
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
70-166 2.82e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 39.69  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAEtrNMTILLTIHQpSSQVFQLFDSIYMMVNGDV 149
Cdd:PRK14271  164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHN-LAQAARISDRAALFFDGRL 240
                          90
                  ....*....|....*..
gi 1831510678 150 AfcgSQSGAEKMWSEMK 166
Cdd:PRK14271  241 V---EEGPTEQLFSSPK 254
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
70-101 4.44e-03

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 38.94  E-value: 4.44e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:PRK09544  121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
21-101 5.12e-03

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 39.55  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  21 EEHLKFMAKLKMGSEY-DLNEQERRVKSVMRSLGLEkiADSIIGTrtrkgISGGEKKRLAFASEILTSPPILICDEPTSG 99
Cdd:PRK11147  114 EKNLNELAKLQEQLDHhNLWQLENRINEVLAQLGLD--PDAALSS-----LSGGWLRKAALGRALVSNPDVLLLDEPTNH 186

                  ..
gi 1831510678 100 LD 101
Cdd:PRK11147  187 LD 188
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
70-101 6.49e-03

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 39.33  E-value: 6.49e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1831510678  70 ISGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:PRK11819  164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
2-128 7.07e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 38.16  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678   2 RQVCAYVQQDDCFIGSlTVEEHLKFmaklkmgsEYDLNEQERRVKSVMRSLGLEKIADSIIgtrtRKGI---SGGEKKRL 78
Cdd:PRK10247   80 RQQVSYCAQTPTLFGD-TVYDNLIF--------PWQIRNQQPDPAIFLDDLERFALPDTIL----TKNIaelSGGEKQRI 146
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831510678  79 AFASEILTSPPILICDEPTSGLDSFLAYQVVCVLKKLAETRNMTILLTIH 128
Cdd:PRK10247  147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTH 196
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
71-101 8.02e-03

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 38.37  E-value: 8.02e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1831510678  71 SGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:PRK11701  153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
14-153 8.27e-03

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: 37.90  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678  14 FIGSLTVEEHLKFMAKLkMGseYDLNEQERRVKSVMRSLGLEKIADSIIGTrtrkgISGGEKKRLAFASEILTSPPILIC 93
Cdd:cd03220    95 FNPELTGRENIYLNGRL-LG--LSRKEIDEKIDEIIEFSELGDFIDLPVKT-----YSSGMKARLAFAIATALEPDILLI 166
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831510678  94 DEPTSGLDSflAYQVVCvLKKLAETRNM--TILLTIHQPSSqVFQLFDSIYMMVNGDVAFCG 153
Cdd:cd03220   167 DEVLAVGDA--AFQEKC-QRRLRELLKQgkTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
69-101 9.11e-03

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 38.09  E-value: 9.11e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1831510678  69 GISGGEKKRLAFASEILTSPPILICDEPTSGLD 101
Cdd:COG1117   154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
279-518 9.45e-03

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 38.53  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 279 QSIIIAILTGLVYTNNSPVDQQKIMNINGSLYQMISNMAFMFQFSVVhhfcleMNTFYRETSSRLY--------RVSAYF 350
Cdd:pfam12698 133 VLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGAAII------AVSIVEEKESRIKerllvsgvSPLQYW 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 351 ISKNLAELPSYIVSAVIFtsILYWMSGLVPIIDSF--LIYMLVGILVqniAISIGYMFSCIFGTVNLAVAVMPIFVVPMM 428
Cdd:pfam12698 207 LGKILGDFLVGLLQLLII--LLLLFGIGIPFGNLGllLLLFLLYGLA---YIALGYLLGSLFKNSEDAQSIIGIVILLLS 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831510678 429 AFGGFFINQDTLQWyfvPMKYLSYFgygyeavaiaqwthveeIPGCSSSLAHCSRNGTDVLnsmsfkpSNFWVDISVMAF 508
Cdd:pfam12698 282 GFFGGLFPLEDPPS---FLQWIFSI-----------------IPFFSPIDGLLRLIYGDSL-------WEIAPSLIILLL 334
                         250
                  ....*....|
gi 1831510678 509 MIFVFRFLAF 518
Cdd:pfam12698 335 FAVVLLLLAL 344
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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