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Conserved domains on  [gi|767915020|ref|XP_011531328|]
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ATP-binding cassette sub-family G member 5 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
50-211 2.43e-67

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd03234:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 226  Bit Score: 217.52  E-value: 2.43e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  50 RVRPWWDITSCRQQW--TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQD 127
Cdd:cd03234    2 RVLPWWDVGLKAKNWnkYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 128 CFSYVLQSDTLLSSLTVRETLHYTALLAIRRGNPGSFQKKVEAVMaelSLSHVADRLIGNYSLGGISTGERRRVSIAAQL 207
Cdd:cd03234   82 CVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDV---LLRDLALTRIGGNLVKGISGGERRRVSIAVQL 158

                 ....
gi 767915020 208 LQDP 211
Cdd:cd03234  159 LWDP 162
3a01204 super family cl36780
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
60-555 8.36e-50

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: 181.78  E-value: 8.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   60 CRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLL 139
Cdd:TIGR00955  32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  140 SSLTVRETLHYTALLAIRRGNPGSfQKK--VEAVMAELSLSHVADRLIGNYS-LGGISTGERRRVSIAAQLLQDPMDL-- 214
Cdd:TIGR00955 112 PTLTVREHLMFQAHLRMPRRVTKK-EKRerVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLfc 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  215 ----TSVDTQS--------------------------------------------------------------------- 221
Cdd:TIGR00955 191 deptSGLDSFMaysvvqvlkglaqkgktiictihqpsselfelfdkiilmaegrvaylgspdqavpffsdlghpcpenyn 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  222 ------------KEREIETSKRVQMIESAYKKSAICHKTLKNIeRMKHLKTLPMV-----PFKTKDSPGVFSKLGVLLRR 284
Cdd:TIGR00955 271 padfyvqvlaviPGSENESRERIEKICDSFAVSDIGRDMLVNT-NLWSGKAGGLVkdsenMEGIGYNASWWTQFYALLKR 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  285 VTRNLVRNKLAVITRLLQNLIMGLF--LLFFVLRVRSnvlKGaIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSDQE 362
Cdd:TIGR00955 350 SWLSVLRDPLLLKVRLIQTMMTAILigLIYLGQGLTQ---KG-VQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRE 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  363 SQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNS 442
Cdd:TIGR00955 426 TRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALT 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  443 VVALLSIAgVLVGSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEFYGL-NFTCGSSNvsvTTNPMCAFTQGIQfieK 521
Cdd:TIGR00955 506 VGPPFVIP-FLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVdNIECTSAN---TTGPCPSSGEVIL---E 578
                         570       580       590
                  ....*....|....*....|....*....|....
gi 767915020  522 TCPGATSRFTMNFLILYSFIPALVILGIVVFKIR 555
Cdd:TIGR00955 579 TLSFRNADLYLDLIGLVILIFFFRLLAYFALRIR 612
 
Name Accession Description Interval E-value
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
50-211 2.43e-67

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: 217.52  E-value: 2.43e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  50 RVRPWWDITSCRQQW--TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQD 127
Cdd:cd03234    2 RVLPWWDVGLKAKNWnkYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 128 CFSYVLQSDTLLSSLTVRETLHYTALLAIRRGNPGSFQKKVEAVMaelSLSHVADRLIGNYSLGGISTGERRRVSIAAQL 207
Cdd:cd03234   82 CVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDV---LLRDLALTRIGGNLVKGISGGERRRVSIAVQL 158

                 ....
gi 767915020 208 LQDP 211
Cdd:cd03234  159 LWDP 162
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
60-555 8.36e-50

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 181.78  E-value: 8.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   60 CRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLL 139
Cdd:TIGR00955  32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  140 SSLTVRETLHYTALLAIRRGNPGSfQKK--VEAVMAELSLSHVADRLIGNYS-LGGISTGERRRVSIAAQLLQDPMDL-- 214
Cdd:TIGR00955 112 PTLTVREHLMFQAHLRMPRRVTKK-EKRerVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLfc 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  215 ----TSVDTQS--------------------------------------------------------------------- 221
Cdd:TIGR00955 191 deptSGLDSFMaysvvqvlkglaqkgktiictihqpsselfelfdkiilmaegrvaylgspdqavpffsdlghpcpenyn 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  222 ------------KEREIETSKRVQMIESAYKKSAICHKTLKNIeRMKHLKTLPMV-----PFKTKDSPGVFSKLGVLLRR 284
Cdd:TIGR00955 271 padfyvqvlaviPGSENESRERIEKICDSFAVSDIGRDMLVNT-NLWSGKAGGLVkdsenMEGIGYNASWWTQFYALLKR 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  285 VTRNLVRNKLAVITRLLQNLIMGLF--LLFFVLRVRSnvlKGaIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSDQE 362
Cdd:TIGR00955 350 SWLSVLRDPLLLKVRLIQTMMTAILigLIYLGQGLTQ---KG-VQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRE 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  363 SQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNS 442
Cdd:TIGR00955 426 TRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALT 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  443 VVALLSIAgVLVGSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEFYGL-NFTCGSSNvsvTTNPMCAFTQGIQfieK 521
Cdd:TIGR00955 506 VGPPFVIP-FLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVdNIECTSAN---TTGPCPSSGEVIL---E 578
                         570       580       590
                  ....*....|....*....|....*....|....
gi 767915020  522 TCPGATSRFTMNFLILYSFIPALVILGIVVFKIR 555
Cdd:TIGR00955 579 TLSFRNADLYLDLIGLVILIFFFRLLAYFALRIR 612
PLN03211 PLN03211
ABC transporter G-25; Provisional
61-514 1.26e-32

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 132.70  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTFLGEVYVNGRALRREQFQDCfSYVLQSDTLLS 140
Cdd:PLN03211  76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI-QGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYP 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SLTVRETLHYTALLAIrrgnPGSFQKKV-----EAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPMDL- 214
Cdd:PLN03211 154 HLTVRETLVFCSLLRL----PKSLTKQEkilvaESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLi 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 215 -----TSVDTQSKEREIET------------------SKRV-QMIESAYKKS-AIC------HKTLKNIERMKHLKTLPM 263
Cdd:PLN03211 230 ldeptSGLDATAAYRLVLTlgslaqkgktivtsmhqpSSRVyQMFDSVLVLSeGRClffgkgSDAMAYFESVGFSPSFPM 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 264 VP----------------FKTKDSPGVFSKL-----------------------------GVLLRRVTRNLVRNKLA--- 295
Cdd:PLN03211 310 NPadflldlangvcqtdgVSEREKPNVKQSLvasyntllapkvkaaiemshfpqanarfvGSASTKEHRSSDRISIStwf 389
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 296 -----VITRLLQNLIMGLFLLFFVLRV-RSNVLKGA---------IQDRVGLLY---QFVGATPYTgmlNAVNLFPVLRA 357
Cdd:PLN03211 390 nqfsiLLQRSLKERKHESFNTLRVFQViAAALLAGLmwwhsdfrdVQDRLGLLFfisIFWGVFPSF---NSVFVFPQERA 466
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 358 VSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNP 437
Cdd:PLN03211 467 IFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDA 546
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 438 NIVNSVVALLSIAGVLVGsGFLrnIQEMPIPFKIISYFTFQKYCSEILvVNEFYG----LNFTCGSSNVSVTTNPMCAFT 513
Cdd:PLN03211 547 KKASTIVTVTMLAFVLTG-GFY--VHKLPSCMAWIKYISTTFYSYRLL-INVQYGegkrISSLLGCSLPHGSDRASCKFV 622

                 .
gi 767915020 514 Q 514
Cdd:PLN03211 623 E 623
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
66-211 4.97e-27

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 109.38  E-value: 4.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLT 143
Cdd:COG1131   13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL-RPTS--GEVRVLGEDVARDpaEVRRRIGYVPQEPALYPDLT 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 144 VRETLHYTALLairRGNPGS-FQKKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDP 211
Cdd:COG1131   90 VRENLRFFARL---YGLPRKeARERIDELLELFGLTDAADRKVGTLSG-----GMKQRLGLALALLHDP 150
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
69-211 1.82e-25

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: 102.34  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---REQFQDCFSYVLQSDTLLSSLTVR 145
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE---GTILLDGQDLTddeRKSLRKEIGYVFQDPQLFPRLTVR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020  146 ETLHYTALLAIRRGNPgsFQKKVEAVMAELSLSHVADRLIGNYSlGGISTGERRRVSIAAQLLQDP 211
Cdd:pfam00005  78 ENLRLGLLLKGLSKRE--KDARAEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKP 140
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
65-218 1.69e-21

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 99.41  E-value: 1.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020    65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRAlRREQFQDCFSYVLQSDTLLSSLTV 144
Cdd:TIGR00956  775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRP-LDSSFQRSIGYVQQQDLHLPTSTV 853
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020   145 RETLHYTALLaiRRGNPGSFQKK---VEAVMAELSLSHVADRLIGnYSLGGISTGERRRVSIAAQLLQDPMDLTSVD 218
Cdd:TIGR00956  854 RESLRFSAYL--RQPKSVSKSEKmeyVEEVIKLLEMESYADAVVG-VPGEGLNVEQRKRLTIGVELVAKPKLLLFLD 927
ABC2_membrane pfam01061
ABC-2 type transporter;
281-488 3.15e-20

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 88.87  E-value: 3.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  281 LLRRVTRNLVRNKLAVITRLLQNLIMGLFL--LFFVLRvrsnvLKGAIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAV 358
Cdd:pfam01061   1 LLKREFLRRWRDPSLGLWRLIQPILMALIFgtLFGNLG-----NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  359 SDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPN 438
Cdd:pfam01061  76 LYRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767915020  439 IVNSVVALLSIAGVLVgSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVN 488
Cdd:pfam01061 156 DASQLGPLVLLPLLLL-SGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
PLN03140 PLN03140
ABC transporter G family member; Provisional
67-211 1.99e-15

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 79.89  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRlgRAGTFL-GEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVR 145
Cdd:PLN03140  894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYIeGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVR 971
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020  146 ETLHYTALLaiRRGNPGSFQKK---VEAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDP 211
Cdd:PLN03140  972 ESLIYSAFL--RLPKEVSKEEKmmfVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANP 1038
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
71-211 2.16e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 47.43  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  71 DVSLYVESGQIMCILGSSGSGKTT-------LLDAMSGR---LGRagtflgEVYVNGRALRREqfqdcFSYVLQSDTLLS 140
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPASEGEawlFGQ------PVDAGDIATRRR-----VGYMSQAFSLYG 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SLTVRE--TLHytALLairrgnpgsFQ-------KKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDP 211
Cdd:NF033858 353 ELTVRQnlELH--ARL---------FHlpaaeiaARVAEMLERFDLADVADALPDSLPL-----GIRQRLSLAVAVIHKP 416
GguA NF040905
sugar ABC transporter ATP-binding protein;
62-121 1.14e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 44.78  E-value: 1.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020  62 QQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLldAMSgRLGRA-GTFL-GEVYVNGRALR 121
Cdd:NF040905 269 LHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL--AMS-VFGRSyGRNIsGTVFKDGKEVD 327
GguA NF040905
sugar ABC transporter ATP-binding protein;
69-121 7.36e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 42.08  E-value: 7.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGrAGTFLGEVYVNGRALR 121
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGSYEGEILFDGEVCR 68
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
78-127 9.18e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.05  E-value: 9.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767915020    78 SGQIMCILGSSGSGKTTLLDAMSGRLGRAGTflGEVYVNGRALRREQFQD 127
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGG--GVIYIDGEDILEEVLDQ 48
 
Name Accession Description Interval E-value
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
50-211 2.43e-67

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: 217.52  E-value: 2.43e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  50 RVRPWWDITSCRQQW--TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQD 127
Cdd:cd03234    2 RVLPWWDVGLKAKNWnkYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 128 CFSYVLQSDTLLSSLTVRETLHYTALLAIRRGNPGSFQKKVEAVMaelSLSHVADRLIGNYSLGGISTGERRRVSIAAQL 207
Cdd:cd03234   82 CVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDV---LLRDLALTRIGGNLVKGISGGERRRVSIAVQL 158

                 ....
gi 767915020 208 LQDP 211
Cdd:cd03234  159 LWDP 162
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
60-555 8.36e-50

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 181.78  E-value: 8.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   60 CRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLL 139
Cdd:TIGR00955  32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  140 SSLTVRETLHYTALLAIRRGNPGSfQKK--VEAVMAELSLSHVADRLIGNYS-LGGISTGERRRVSIAAQLLQDPMDL-- 214
Cdd:TIGR00955 112 PTLTVREHLMFQAHLRMPRRVTKK-EKRerVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLfc 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  215 ----TSVDTQS--------------------------------------------------------------------- 221
Cdd:TIGR00955 191 deptSGLDSFMaysvvqvlkglaqkgktiictihqpsselfelfdkiilmaegrvaylgspdqavpffsdlghpcpenyn 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  222 ------------KEREIETSKRVQMIESAYKKSAICHKTLKNIeRMKHLKTLPMV-----PFKTKDSPGVFSKLGVLLRR 284
Cdd:TIGR00955 271 padfyvqvlaviPGSENESRERIEKICDSFAVSDIGRDMLVNT-NLWSGKAGGLVkdsenMEGIGYNASWWTQFYALLKR 349
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  285 VTRNLVRNKLAVITRLLQNLIMGLF--LLFFVLRVRSnvlKGaIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAVSDQE 362
Cdd:TIGR00955 350 SWLSVLRDPLLLKVRLIQTMMTAILigLIYLGQGLTQ---KG-VQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRE 425
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  363 SQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPNIVNS 442
Cdd:TIGR00955 426 TRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALT 505
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  443 VVALLSIAgVLVGSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEFYGL-NFTCGSSNvsvTTNPMCAFTQGIQfieK 521
Cdd:TIGR00955 506 VGPPFVIP-FLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVdNIECTSAN---TTGPCPSSGEVIL---E 578
                         570       580       590
                  ....*....|....*....|....*....|....
gi 767915020  522 TCPGATSRFTMNFLILYSFIPALVILGIVVFKIR 555
Cdd:TIGR00955 579 TLSFRNADLYLDLIGLVILIFFFRLLAYFALRIR 612
PLN03211 PLN03211
ABC transporter G-25; Provisional
61-514 1.26e-32

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 132.70  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTFLGEVYVNGRALRREQFQDCfSYVLQSDTLLS 140
Cdd:PLN03211  76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI-QGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYP 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SLTVRETLHYTALLAIrrgnPGSFQKKV-----EAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDPMDL- 214
Cdd:PLN03211 154 HLTVRETLVFCSLLRL----PKSLTKQEkilvaESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLi 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 215 -----TSVDTQSKEREIET------------------SKRV-QMIESAYKKS-AIC------HKTLKNIERMKHLKTLPM 263
Cdd:PLN03211 230 ldeptSGLDATAAYRLVLTlgslaqkgktivtsmhqpSSRVyQMFDSVLVLSeGRClffgkgSDAMAYFESVGFSPSFPM 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 264 VP----------------FKTKDSPGVFSKL-----------------------------GVLLRRVTRNLVRNKLA--- 295
Cdd:PLN03211 310 NPadflldlangvcqtdgVSEREKPNVKQSLvasyntllapkvkaaiemshfpqanarfvGSASTKEHRSSDRISIStwf 389
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 296 -----VITRLLQNLIMGLFLLFFVLRV-RSNVLKGA---------IQDRVGLLY---QFVGATPYTgmlNAVNLFPVLRA 357
Cdd:PLN03211 390 nqfsiLLQRSLKERKHESFNTLRVFQViAAALLAGLmwwhsdfrdVQDRLGLLFfisIFWGVFPSF---NSVFVFPQERA 466
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 358 VSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNP 437
Cdd:PLN03211 467 IFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDA 546
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 438 NIVNSVVALLSIAGVLVGsGFLrnIQEMPIPFKIISYFTFQKYCSEILvVNEFYG----LNFTCGSSNVSVTTNPMCAFT 513
Cdd:PLN03211 547 KKASTIVTVTMLAFVLTG-GFY--VHKLPSCMAWIKYISTTFYSYRLL-INVQYGegkrISSLLGCSLPHGSDRASCKFV 622

                 .
gi 767915020 514 Q 514
Cdd:PLN03211 623 E 623
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
50-212 3.63e-32

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: 122.27  E-value: 3.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  50 RVRPWWD-----ITSCRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTfLGEVYVNGRALRREQ 124
Cdd:cd03213    1 GVTLSFRnltvtVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV-SGEVLINGRPLDKRS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 125 FQDCFSYVLQSDTLLSSLTVRETLHYTALLAirrgnpgsfqkkveavmaelslshvadrlignyslgGISTGERRRVSIA 204
Cdd:cd03213   80 FRKIIGYVPQDDILHPTLTVRETLMFAAKLR------------------------------------GLSGGERKRVSIA 123

                 ....*...
gi 767915020 205 AQLLQDPM 212
Cdd:cd03213  124 LELVSNPS 131
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
66-211 4.97e-27

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 109.38  E-value: 4.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLT 143
Cdd:COG1131   13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLL-RPTS--GEVRVLGEDVARDpaEVRRRIGYVPQEPALYPDLT 89
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 144 VRETLHYTALLairRGNPGS-FQKKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDP 211
Cdd:COG1131   90 VRENLRFFARL---YGLPRKeARERIDELLELFGLTDAADRKVGTLSG-----GMKQRLGLALALLHDP 150
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
66-224 1.45e-25

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: 104.48  E-value: 1.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSLT 143
Cdd:COG4133   15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSA---GEVLWNGEPIRdaREDYRRRLAYLGHADGLKPELT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 144 VRETLHYTALLAIRRGNPGSfqkkVEAVMAELSLSHVADRLIGNYslggiSTGERRRVSIAAQLLQDP----MD--LTSV 217
Cdd:COG4133   92 VRENLRFWAALYGLRADREA----IDEALEAVGLAGLADLPVRQL-----SAGQKRRVALARLLLSPAplwlLDepFTAL 162

                 ....*..
gi 767915020 218 DTQSKER 224
Cdd:COG4133  163 DAAGVAL 169
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
69-211 1.82e-25

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: 102.34  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---REQFQDCFSYVLQSDTLLSSLTVR 145
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE---GTILLDGQDLTddeRKSLRKEIGYVFQDPQLFPRLTVR 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020  146 ETLHYTALLAIRRGNPgsFQKKVEAVMAELSLSHVADRLIGNYSlGGISTGERRRVSIAAQLLQDP 211
Cdd:pfam00005  78 ENLRLGLLLKGLSKRE--KDARAEEALEKLGLGDLADRPVGERP-GTLSGGQRQRVAIARALLTKP 140
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
61-550 3.89e-25

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 110.58  E-value: 3.89e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020    61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL-GRAGTFLGEVYVNGRALR--REQFQDCFSYVLQSDT 137
Cdd:TIGR00956   69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdGFHIGVEGVITYDGITPEeiKKHYRGDVVYNAETDV 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   138 LLSSLTVRETLHYTALLAIRRGNPGSFQKKVEA------VMAELSLSHVADRLIGNYSLGGISTGERRRVSIAA------ 205
Cdd:TIGR00956  149 HFPHLTVGETLDFAARCKTPQNRPDGVSREEYAkhiadvYMATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEaslgga 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   206 ------------------------------------------------------------QLLQDPMD------------ 213
Cdd:TIGR00956  229 kiqcwdnatrgldsatalefiralktsanildttplvaiyqcsqdayelfdkvivlyegyQIYFGPADkakqyfekmgfk 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   214 ----------LTSVdTQSKEREI--ETSKRV----QMIESAYKKS-------AICHKTLKNIERMKHLKTLPMVPFKTKD 270
Cdd:TIGR00956  309 cpdrqttadfLTSL-TSPAERQIkpGYEKKVprtpQEFETYWRNSpeyaqlmKEIDEYLDRCSESDTKEAYRESHVAKQS 387
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   271 ------SPGVFSKLGVLLRRVTRNLVR---NKLAVITRLLQNLIMGLFLLFFVLRVRSNVLKGAIqdRVGLLYQFVGATP 341
Cdd:TIGR00956  388 krtrpsSPYTVSFSMQVKYCLARNFLRmkgNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYS--RGGALFFAILFNA 465
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   342 YTGMLNAVNLFPVlRAVSDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGY-----FSAAL 416
Cdd:TIGR00956  466 FSSLLEIASMYEA-RPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFyllilFICTL 544
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   417 LAPHL---IGEFLTLVLLGivqnpnivNSVVALLSIAGVLVgSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVNEFYGL 493
Cdd:TIGR00956  545 AMSHLfrsIGAVTKTLSEA--------MTPAAILLLALSIY-TGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGR 615
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915020   494 NFTC--------GSSNVSVtTNPMCA---------FTQGIQFIEKTCPGATSRFTMNFLILYSFIPALVILGIV 550
Cdd:TIGR00956  616 RFECsqyvpsggGYDNLGV-TNKVCTvvgaepgqdYVDGDDYLKLSFQYYNSHKWRNFGIIIGFTVFFFFVYIL 688
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
66-223 2.34e-23

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: 99.16  E-value: 2.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLT 143
Cdd:COG4555   14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL-KPDS--GSILIDGEDVRKEprEARRQIGVLPDERGLYDRLT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 144 VRETLHYTALLairRGNPGS-FQKKVEAVMAELSLSHVADRLIGNYslggiSTGERRRVSIAAQLLQDP----MD--LTS 216
Cdd:COG4555   91 VRENIRYFAEL---YGLFDEeLKKRIEELIELLGLEEFLDRRVGEL-----STGMKKKVALARALVHDPkvllLDepTNG 162

                 ....*..
gi 767915020 217 VDTQSKE 223
Cdd:COG4555  163 LDVMARR 169
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
66-211 5.07e-23

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: 98.19  E-value: 5.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL----RREQFQdCFSYVLQSDTLLSS 141
Cdd:COG1120   14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSS---GEVLLDGRDLaslsRRELAR-RIAYVPQEPPAPFG 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020 142 LTVRETLhytaLLAiRRGNPGSFQK-------KVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:COG1120   90 LTVRELV----ALG-RYPHLGLFGRpsaedreAVEEALERTGLEHLADRPVDE-----LSGGERQRVLIARALAQEP 156
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
65-211 5.48e-22

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: 93.85  E-value: 5.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRlGRAGTFLGEVYVNGRALrREQFQDCFSYVLQSDTLLSSLTV 144
Cdd:cd03232   19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR-KTAGVITGEILINGRPL-DKNFQRSTGYVEQQDVHSPNLTV 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020 145 RETLHYTALLAirrgnpgsfqkkveavmaelslshvadrlignyslgGISTGERRRVSIAAQLLQDP 211
Cdd:cd03232   97 REALRFSALLR------------------------------------GLSVEQRKRLTIGVELAAKP 127
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
67-233 7.54e-22

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: 93.74  E-value: 7.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRAL------RREqfqdcFSYVLQSDTLLS 140
Cdd:cd03259   14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG-LERPDS--GEILIDGRDVtgvppeRRN-----IGMVFQDYALFP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIgnyslGGISTGERRRVSIAAQLLQDP----MD--L 214
Cdd:cd03259   86 HLTVAENIAFG--LKLRGVPKAEIRARVRELLELVGLEGLLNRYP-----HELSGGQQQRVALARALAREPslllLDepL 158
                        170
                 ....*....|....*....
gi 767915020 215 TSVDTQSKEREIETSKRVQ 233
Cdd:cd03259  159 SALDAKLREELREELKELQ 177
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
65-226 9.82e-22

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: 93.72  E-value: 9.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSL 142
Cdd:cd03263   14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL-RPTS--GTAYINGYSIRtdRKAARQSLGYCPQFDALFDEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 143 TVRETLHYTALLairRGNPGSFQKK-VEAVMAELSLSHVADRLIGNYslggiSTGERRRVSIAAQLLQDP----MD--LT 215
Cdd:cd03263   91 TVREHLRFYARL---KGLPKSEIKEeVELLLRVLGLTDKANKRARTL-----SGGMKRKLSLAIALIGGPsvllLDepTS 162
                        170
                 ....*....|.
gi 767915020 216 SVDTQSKeREI 226
Cdd:cd03263  163 GLDPASR-RAI 172
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
65-218 1.69e-21

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 99.41  E-value: 1.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020    65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRAlRREQFQDCFSYVLQSDTLLSSLTV 144
Cdd:TIGR00956  775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRP-LDSSFQRSIGYVQQQDLHLPTSTV 853
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020   145 RETLHYTALLaiRRGNPGSFQKK---VEAVMAELSLSHVADRLIGnYSLGGISTGERRRVSIAAQLLQDPMDLTSVD 218
Cdd:TIGR00956  854 RESLRFSAYL--RQPKSVSKSEKmeyVEEVIKLLEMESYADAVVG-VPGEGLNVEQRKRLTIGVELVAKPKLLLFLD 927
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
56-233 2.63e-20

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: 89.45  E-value: 2.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  56 DITSCRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCF---SYV 132
Cdd:cd03225    4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTS---GEVLVDGKDLTKLSLKELRrkvGLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 133 LQ-SDTLLSSLTVRETLhytALLAIRRGNPGS-FQKKVEAVMAELSLSHVADRLIgnYSLGGistGERRRVSIAAQLLQD 210
Cdd:cd03225   81 FQnPDDQFFGPTVEEEV---AFGLENLGLPEEeIEERVEEALELVGLEGLRDRSP--FTLSG---GQKQRVAIAGVLAMD 152
                        170       180
                 ....*....|....*....|....*....
gi 767915020 211 P----MD--LTSVDTQSKEREIETSKRVQ 233
Cdd:cd03225  153 PdillLDepTAGLDPAGRRELLELLKKLK 181
ABC2_membrane pfam01061
ABC-2 type transporter;
281-488 3.15e-20

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 88.87  E-value: 3.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  281 LLRRVTRNLVRNKLAVITRLLQNLIMGLFL--LFFVLRvrsnvLKGAIQDRVGLLYQFVGATPYTGMLNAVNLFPVLRAV 358
Cdd:pfam01061   1 LLKREFLRRWRDPSLGLWRLIQPILMALIFgtLFGNLG-----NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  359 SDQESQDGLYQKWQMMLAYALHVLPFSVVATMIFSSVCYWTLGLHPEVARFGYFSAALLAPHLIGEFLTLVLLGIVQNPN 438
Cdd:pfam01061  76 LYRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767915020  439 IVNSVVALLSIAGVLVgSGFLRNIQEMPIPFKIISYFTFQKYCSEILVVN 488
Cdd:pfam01061 156 DASQLGPLVLLPLLLL-SGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
65-211 5.75e-20

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 88.95  E-value: 5.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQfqdcFSYVL 133
Cdd:COG1136   20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-LDRPTS--GEVLIDGQdisslserelaRLRRRH----IGFVF 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 134 QSDTLLSSLTVRETLhytAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:COG1136   93 QFFNLLPELTALENV---ALpLLLAGVSRKERRERARELLERVGLGDRLDHRPSQ-----LSGGQQQRVAIARALVNRP 163
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
65-212 1.62e-19

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: 87.94  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR---ALRREQFQDC---FSYVLQSDTL 138
Cdd:cd03261   12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS---GEVLIDGEdisGLSEAELYRLrrrMGMLFQSGAL 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915020 139 LSSLTVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDPM 212
Cdd:cd03261   89 FDSLTVFENVAF-PLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPE 156
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
65-211 2.28e-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: 86.77  E-value: 2.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQfqdcFSYVL 133
Cdd:cd03255   16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG-LDRPTS--GEVRVDGTdisklsekelaAFRRRH----IGFVF 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 134 QSDTLLSSLTVRETLhytALLAIRRGNPGSFQK-KVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:cd03255   89 QSFNLLPDLTALENV---ELPLLLAGVPKKERReRAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDP 159
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
65-223 8.95e-19

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: 85.22  E-value: 8.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQdcFSYVLQSDTLLSSLTV 144
Cdd:cd03293   16 AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG-LERPTS--GEVLVDGEPVTGPGPD--RGYVFQQDALLPWLTV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 145 RETlhyTAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP----MD--LTSV 217
Cdd:cd03293   91 LDN---VALgLELQGVPKAEARERAEELLELVGLSGFENAYPHQ-----LSGGMRQRVALARALAVDPdvllLDepFSAL 162

                 ....*.
gi 767915020 218 DTQSKE 223
Cdd:cd03293  163 DALTRE 168
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
66-223 1.01e-18

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 84.89  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQdcFSYVLQSDTLLSS--LT 143
Cdd:cd03235   12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTS---GSIRVFGKPLEKERKR--IGYVPQRRSIDRDfpIS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 144 VRETLhytaLLAiRRGNPGSFQ-------KKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP----M 212
Cdd:cd03235   87 VRDVV----LMG-LYGHKGLFRrlskadkAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPdlllL 156
                        170
                 ....*....|...
gi 767915020 213 D--LTSVDTQSKE 223
Cdd:cd03235  157 DepFAGVDPKTQE 169
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
65-224 2.60e-18

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 84.76  E-value: 2.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQfQDCfSYVLQSDTLLSSLTV 144
Cdd:COG1116   23 GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-LEKPTS--GEVLVDGKPVTGPG-PDR-GVVFQEPALLPWLTV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 145 RE--TLHytalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP----MD--LTS 216
Cdd:COG1116   98 LDnvALG----LELRGVPKAERRERARELLELVGLAGFEDAYPHQ-----LSGGMRQRVAIARALANDPevllMDepFGA 168

                 ....*...
gi 767915020 217 VDTQSKER 224
Cdd:COG1116  169 LDALTRER 176
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
66-204 7.08e-18

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: 83.11  E-value: 7.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRREqfqdcFSYVLQ 134
Cdd:COG1127   18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDS---GEILVDGqditglsekelYELRRR-----IGMLFQ 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 135 SDTLLSSLTVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIA 204
Cdd:COG1127   90 GGALFDSLTVFENVAF-PLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSE-----LSGGMRKRVALA 153
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
66-224 8.08e-18

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 83.21  E-value: 8.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQdcFSYVLQSDTLLSS--LT 143
Cdd:COG1121   19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTS---GTVRLFGKPPRRARRR--IGYVPQRAEVDWDfpIT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 144 VRETL---HYTALLAIRRGNPGSFQkKVEAVMAELSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDP----MD--L 214
Cdd:COG1121   94 VRDVVlmgRYGRRGLFRRPSRADRE-AVDEALERVGLEDLADRPIG--ELSG---GQQQRVLLARALAQDPdlllLDepF 167
                        170
                 ....*....|
gi 767915020 215 TSVDTQSKER 224
Cdd:COG1121  168 AGVDAATEEA 177
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
65-211 1.71e-17

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: 81.11  E-value: 1.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGralrrEQFQDCFSYVLQSDTLLSS--- 141
Cdd:cd03268   12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG-LIKPDS--GEITFDG-----KSYQKNIEALRRIGALIEApgf 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915020 142 ---LTVRETLHYTALLAIRRgnpgsfQKKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDP 211
Cdd:cd03268   84 ypnLTARENLRLLARLLGIR------KKRIDEVLDVVGLKDSAKKKVKGFSL-----GMKQRLGIALALLGNP 145
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
71-226 2.89e-17

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: 83.61  E-value: 2.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRAL---RREQF----QDCFSYVLQSDTLLSSLT 143
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAG-LERPDS--GRIRLGGEVLqdsARGIFlpphRRRIGYVFQEARLFPHLS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 144 VRETLHYtallAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP----MD--LTSV 217
Cdd:COG4148   94 VRGNLLY----GRKRAPRAERRISFDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPrlllMDepLAAL 164

                 ....*....
gi 767915020 218 DTQSKeREI 226
Cdd:COG4148  165 DLARK-AEI 172
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
66-211 4.45e-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: 79.02  E-value: 4.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---REQFQDCFSYVLQsdtllssl 142
Cdd:cd03214   12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS---GEILLDGKDLAslsPKELARKIAYVPQ-------- 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 143 tvretlhytallairrgnpgsfqkkveaVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:cd03214   81 ----------------------------ALELLGLAHLADRPFNE-----LSGGERQRVLLARALAQEP 116
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
66-233 8.03e-17

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


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 79.96  E-value: 8.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG---RALRREQFQDCFSYVLQsDTLLSSL 142
Cdd:cd03254   16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQK---GQILIDGidiRDISRKSLRSMIGVVLQ-DTFLFSG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 143 TVRETlhytallaIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNY------SLGGISTGERRRVSIAAQLLQDP----M 212
Cdd:cd03254   92 TIMEN--------IRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYdtvlgeNGGNLSQGERQLLAIARAMLRDPkiliL 163
                        170       180
                 ....*....|....*....|...
gi 767915020 213 D--LTSVDTqskereiETSKRVQ 233
Cdd:cd03254  164 DeaTSNIDT-------ETEKLIQ 179
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
65-211 8.99e-17

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: 79.51  E-value: 8.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLS 140
Cdd:cd03218   12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVG-LVKPDS--GKILLDGQDITKlpmhKRARLGIGYLPQEASIFR 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915020 141 SLTVRETLhyTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDP 211
Cdd:cd03218   89 KLTVEENI--LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSK--ASSLSG---GERRRVEIARALATNP 152
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
56-233 2.03e-16

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 78.92  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  56 DITSCRQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL------RREqfqdcF 129
Cdd:cd03299    2 KVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS---GKILLNGKDItnlppeKRD-----I 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 130 SYVLQSDTLLSSLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQ 209
Cdd:cd03299   74 SYVPQNYALFPHMTVYKNIAYG--LKKRKVDKKEIERKVLEIAEMLGIDHLLNR-----KPETLSGGEQQRVAIARALVV 146
                        170       180       190
                 ....*....|....*....|....*....|
gi 767915020 210 DP----MD--LTSVDTQSKEREIETSKRVQ 233
Cdd:cd03299  147 NPkillLDepFSALDVRTKEKLREELKKIR 176
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
65-211 2.79e-16

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: 81.87  E-value: 2.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDC---FSYVLQS-DTLLS 140
Cdd:COG1123   18 DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRgrrIGMVFQDpMTQLN 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915020 141 SLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:COG1123   98 PVTVGDQIAEA--LENLGLSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALALDP 161
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
68-204 3.20e-16

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: 78.24  E-value: 3.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR-----------ALRREQfqdcFSYVLQSD 136
Cdd:COG4181   27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-LDRPTS--GTVRLAGQdlfaldedaraRLRARH----VGFVFQSF 99
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915020 137 TLLSSLTVREtlhYTALLAIRRGNPGSFQkKVEAVMAELSLSHvadRLiGNYSlGGISTGERRRVSIA 204
Cdd:COG4181  100 QLLPTLTALE---NVMLPLELAGRRDARA-RARALLERVGLGH---RL-DHYP-AQLSGGEQQRVALA 158
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
41-211 5.29e-16

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 77.37  E-value: 5.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  41 LHASYSVsHRVRPWWdITSCRQQWTRQ-----ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYV 115
Cdd:cd03267    6 LSKSYRV-YSKEPGL-IGSLKSLFKRKyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS---GEVRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 116 NGRA--LRREQFQDCFSYVL-QSDTLLSSLTVRETlhYTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSLgg 192
Cdd:cd03267   81 AGLVpwKRRKKFLRRIGVVFgQKTQLWWDLPVIDS--FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL-- 156
                        170
                 ....*....|....*....
gi 767915020 193 istGERRRVSIAAQLLQDP 211
Cdd:cd03267  157 ---GQRMRAEIAAALLHEP 172
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
69-211 6.62e-16

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: 77.09  E-value: 6.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQ------------FQdcfsyVLQsd 136
Cdd:cd03219   16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFL-RPTS--GSVLFDGEDITGLPpheiarlgigrtFQ-----IPR-- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 137 tLLSSLTVRETL--------HYTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLL 208
Cdd:cd03219   86 -LFPELTVLENVmvaaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALA 159

                 ...
gi 767915020 209 QDP 211
Cdd:cd03219  160 TDP 162
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
65-211 7.68e-16

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: 75.51  E-value: 7.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSL 142
Cdd:cd03230   12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLL-KPDS--GEIKVLGKDIKKEpeEVKRRIGYLPEEPSLYENL 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 143 TVRETLHYtallairrgnpgsfqkkveavmaelslshvadrlignyslggiSTGERRRVSIAAQLLQDP 211
Cdd:cd03230   89 TVRENLKL-------------------------------------------SGGMKQRLALAQALLHDP 114
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
66-211 1.73e-15

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: 75.83  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFS---YVLQ-SDTLLSS 141
Cdd:COG1122   14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-LLKPTS--GEVLVDGKDITKKNLRELRRkvgLVFQnPDDQLFA 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915020 142 LTVRETLHYtALLaiRRGNPGSF-QKKVEAVMAELSLSHVADRLIgnYSLggiSTGERRRVSIAAQLLQDP 211
Cdd:COG1122   91 PTVEEDVAF-GPE--NLGLPREEiRERVEEALELVGLEHLADRPP--HEL---SGGQKQRVAIAGVLAMEP 153
PLN03140 PLN03140
ABC transporter G family member; Provisional
67-211 1.99e-15

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 79.89  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRlgRAGTFL-GEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVR 145
Cdd:PLN03140  894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYIeGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVR 971
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020  146 ETLHYTALLaiRRGNPGSFQKK---VEAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQDP 211
Cdd:PLN03140  972 ESLIYSAFL--RLPKEVSKEEKmmfVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANP 1038
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
67-211 2.81e-15

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: 75.16  E-value: 2.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLSSL 142
Cdd:cd03224   14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRS---GSIRFDGRDITGlpphERARAGIGYVPEGRRIFPEL 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 143 TVRETLhytaLLAIRRGNPGSFQKKVEAVMAELS-LSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:cd03224   91 TVEENL----LLGAYARRRAKRKARLERVYELFPrLKERRKQLAGT-----LSGGEQQMLAIARALMSRP 151
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
66-211 3.59e-15

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 75.07  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL------RREQFQdcFSYVLQSDTLL 139
Cdd:COG1137   16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS---GRIFLDGEDIthlpmhKRARLG--IGYLPQEASIF 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020 140 SSLTVRETLhyTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLigNYSLGGistGERRRVSIAAQLLQDP 211
Cdd:COG1137   91 RKLTVEDNI--LAVLELRKLSKKEREERLEELLEEFGITHLRKSK--AYSLSG---GERRRVEIARALATNP 155
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
65-211 5.16e-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: 77.64  E-value: 5.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRRE-Q--FQDCFS 130
Cdd:COG1123  277 GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS---GSILFDGkdltklsrrslRELRRRvQmvFQDPYS 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 131 yvlqsdTLLSSLTVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSLS-HVADRLIgnYSLGGistGERRRVSIAAQLLQ 209
Cdd:COG1123  354 ------SLNPRMTVGDIIAE-PLRLHGLLSRAERRERVAELLERVGLPpDLADRYP--HELSG---GQRQRVAIARALAL 421

                 ..
gi 767915020 210 DP 211
Cdd:COG1123  422 EP 423
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
66-207 9.77e-15

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 74.42  E-value: 9.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRAL----------RREqfqdcfsyVL-Q 134
Cdd:PRK13548  15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGEL-SPDS--GEVRLNGRPLadwspaelarRRA--------VLpQ 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915020 135 SDTLLSSLTVRETLhytAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLignY-SLGGistGERRRVSIA---AQL 207
Cdd:PRK13548  84 HSSLSFPFTVEEVV---AMgRAPHGLSRAEDDALVAAALAQVDLAHLAGRD---YpQLSG---GEQQRVQLArvlAQL 152
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
67-204 1.02e-14

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 75.52  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRAL------RREqfqdcFSYVLQSD 136
Cdd:COG3842   19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG-------FEtpdsGRILLDGRDVtglppeKRN-----VGMVFQDY 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915020 137 TLLSSLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIA 204
Cdd:COG3842   87 ALFPHLTVAENVAFG--LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQ-----LSGGQQQRVALA 147
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
53-208 1.18e-14

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: 72.68  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  53 PWWDITSCRQQ--WTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALR--REQFQDC 128
Cdd:cd03233    5 SWRNISFTTGKgrSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKefAEKYPGE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 129 FSYVLQSDTLLSSLTVRETLHYTAllairrgnpgsfqkkveavmaelslshvadRLIGNYSLGGISTGERRRVSIAAQLL 208
Cdd:cd03233   85 IIYVSEEDVHFPTLTVRETLDFAL------------------------------RCKGNEFVRGISGGERKRVSIAEALV 134
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
66-229 1.42e-14

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 76.36  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNG---RALRREQFQDCFSYVLQsDTL 138
Cdd:COG1132  353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR-------FYdptsGRILIDGvdiRDLTLESLRRQIGVVPQ-DTF 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 139 LSSLTVREtlhytallAIRRGNPGSFQKKVEAVMAELSLSHVADRL-------IGNyslGGI--STGERRRVSIAAQLLQ 209
Cdd:COG1132  425 LFSGTIRE--------NIRYGRPDATDEEVEEAAKAAQAHEFIEALpdgydtvVGE---RGVnlSGGQRQRIAIARALLK 493
                        170       180
                 ....*....|....*....|....*.
gi 767915020 210 DP----MD--LTSVDTQSkEREIETS 229
Cdd:COG1132  494 DPpiliLDeaTSALDTET-EALIQEA 518
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
66-211 1.82e-14

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: 72.61  E-value: 1.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGqIMCILGSSGSGKTTLLDAMSGRL-GRAGTflgeVYVNGRALR--REQFQDCFSYVLQSDTLLSSL 142
Cdd:cd03264   13 KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTpPSSGT----IRIDGQDVLkqPQKLRRRIGYLPQEFGVYPNF 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 143 TVRETLHYTALLaiRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSlGGIstgeRRRVSIAAQLLQDP 211
Cdd:cd03264   88 TVREFLDYIAWL--KGIPSKEVKARVDEVLELVNLGDRAKKKIGSLS-GGM----RRRVGIAQALVGDP 149
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
69-211 4.64e-14

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: 71.63  E-value: 4.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE--QFQDCFSYVLQSDTLLSSLTVRE 146
Cdd:cd03265   16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS---GRATVAGHDVVREprEVRRRIGIVFQDLSVDDELTGWE 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020 147 TLHYTALLAirrGNPGS-FQKKVEAVMAELSLSHVADRLIGNYslggiSTGERRRVSIAAQLLQDP 211
Cdd:cd03265   93 NLYIHARLY---GVPGAeRRERIDELLDFVGLLEAADRLVKTY-----SGGMRRRLEIARSLVHRP 150
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
61-211 5.00e-14

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: 71.38  E-value: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR---ALRREQFQDC---FSYVLQ 134
Cdd:cd03257   13 TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG-LLKPTS--GSIIFDGKdllKLSRRLRKIRrkeIQMVFQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 135 sDTLLS---SLTVRETLhyTALLAIRRGNPGSFQKKvEAVMAELSLSHVADRLIGNY--SLGGistGERRRVSIAAQLLQ 209
Cdd:cd03257   90 -DPMSSlnpRMTIGEQI--AEPLRIHGKLSKKEARK-EAVLLLLVGVGLPEEVLNRYphELSG---GQRQRVAIARALAL 162

                 ..
gi 767915020 210 DP 211
Cdd:cd03257  163 NP 164
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
69-211 5.32e-14

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: 71.46  E-value: 5.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAM-------SGRLGRAGTFLGEvyVNGRALRreQFQDCFSYVLQSDTLLSS 141
Cdd:cd03258   21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInglerptSGSVLVDGTDLTL--LSGKELR--KARRRIGMIFQHFNLLSS 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915020 142 LTVRETLHYTALLAirrGNPGSFQ-KKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:cd03258   97 RTVFENVALPLEIA---GVPKAEIeERVLELLELVGLEDKADAYPAQ-----LSGGQKQRVGIARALANNP 159
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
69-223 8.04e-14

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: 70.79  E-value: 8.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSL---YVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFS-------YVLQSDTL 138
Cdd:cd03297   10 LPDFTLkidFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDG---GTIVLNGTVLFDSRKKINLPpqqrkigLVFQQYAL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 139 LSSLTVRETLHYtallAIRRGNPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDP----MD- 213
Cdd:cd03297   87 FPHLNVRENLAF----GLKRKRNREDRISVDELLDLLGLDHLLNR-----YPAQLSGGEKQRVALARALAAQPelllLDe 157
                        170
                 ....*....|.
gi 767915020 214 -LTSVDTQSKE 223
Cdd:cd03297  158 pFSALDRALRL 168
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
66-204 9.66e-14

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 70.47  E-value: 9.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG--RLGRagtflGEVYVNGR---ALRREQ-----------FQDCf 129
Cdd:COG2884   15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeeRPTS-----GQVLVNGQdlsRLKRREipylrrrigvvFQDF- 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915020 130 syvlqsdTLLSSLTVRETLHYtALLAIRRgNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIA 204
Cdd:COG2884   89 -------RLLPDRTVYENVAL-PLRVTGK-SRKEIRRRVREVLDLVGLSDKAKALPHE-----LSGGEQQRVAIA 149
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
66-229 2.41e-13

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: 68.18  E-value: 2.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRALR---REQFQDCFSYVLQsDTL 138
Cdd:cd03228   15 KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR-------LYdptsGEILIDGVDLRdldLESLRKNIAYVPQ-DPF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 139 LSSLTVRETLhytallairrgnpgsfqkkveavmaelslshvadrlignyslggISTGERRRVSIAAQLLQDP----MD- 213
Cdd:cd03228   87 LFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDPpiliLDe 122
                        170
                 ....*....|....*..
gi 767915020 214 -LTSVDTQSkEREIETS 229
Cdd:cd03228  123 aTSALDPET-EALILEA 138
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
66-211 3.60e-13

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 70.88  E-value: 3.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAM-------SGRLGRAGTFLGEVYVNGRALrreqfqdcfSYVLQSDTL 138
Cdd:PRK10851  15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIaglehqtSGHIRFHGTDVSRLHARDRKV---------GFVFQHYAL 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915020 139 LSSLTVRETLHY--TALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:PRK10851  86 FRHMTVFDNIAFglTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQ-----LSGGQKQRVALARALAVEP 155
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
66-204 4.44e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 68.36  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVR 145
Cdd:PRK13539  15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAA---GTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVA 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 146 ETLHYTAllAIRRGNPGSfqkkVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIA 204
Cdd:PRK13539  92 ENLEFWA--AFLGGEELD----IAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALA 139
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
68-229 5.51e-13

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: 68.80  E-value: 5.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGRLGRAGTFLGEVYVNgrALRREqfqdcFSYVLQsDTLLS 140
Cdd:cd03251   17 VLRDISLDIPAGETVALVGPSGSGKSTLVnliprfyDVDSGRILIDGHDVRDYTLA--SLRRQ-----IGLVSQ-DVFLF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SLTVRETlhytallaIRRGNPGSFQKKVEAVmAELSLSH-VADRLIGNY--SLG--GI--STGERRRVSIAAQLLQDPMD 213
Cdd:cd03251   89 NDTVAEN--------IAYGRPGATREEVEEA-ARAANAHeFIMELPEGYdtVIGerGVklSGGQRQRIAIARALLKDPPI 159
                        170       180
                 ....*....|....*....|..
gi 767915020 214 L-----TS-VDTQSkEREIETS 229
Cdd:cd03251  160 LildeaTSaLDTES-ERLVQAA 180
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
67-234 8.54e-13

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 69.72  E-value: 8.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtfL-----GEVYVNGR------ALRREqfqdcFSYVLQS 135
Cdd:COG3839   17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAG--------LedptsGEILIGGRdvtdlpPKDRN-----IAMVFQS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 136 DTLLSSLTVRETLhytAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNysLGGistGERRRVSIAAQLLQDP--- 211
Cdd:COG3839   84 YALYPHMTVYENI---AFpLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQ--LSG---GQRQRVALGRALVREPkvf 155
                        170       180
                 ....*....|....*....|....*.
gi 767915020 212 -MD--LTSVDTQSkereietskRVQM 234
Cdd:COG3839  156 lLDepLSNLDAKL---------RVEM 172
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
68-218 1.02e-12

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: 67.28  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQD-CFSYVLQSDTLLSSLTVRE 146
Cdd:cd03301   15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTS---GRIYIGGRDVTDLPPKDrDIAMVFQNYALYPHMTVYD 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915020 147 TLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP----MD--LTSVD 218
Cdd:cd03301   92 NIAFG--LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQ-----LSGGQRQRVALGRAIVREPkvflMDepLSNLD 162
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
65-224 1.22e-12

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: 65.73  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR---EQFQDCFSYVLQsdtllss 141
Cdd:cd00267   11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTS---GEILIDGKDIAKlplEELRRRIGYVPQ------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 142 ltvretlhytallairrgnpgsfqkkveavmaelslshvadrlignyslggISTGERRRVSIAAQLLQDP----MD--LT 215
Cdd:cd00267   81 ---------------------------------------------------LSGGQRQRVALARALLLNPdlllLDepTS 109

                 ....*....
gi 767915020 216 SVDTQSKER 224
Cdd:cd00267  110 GLDPASRER 118
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
66-211 1.64e-12

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


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 67.42  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgrAGTFLGEVYVNGRALRREQFQD------CFSYVLQsDTLL 139
Cdd:COG1119   16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDL--PPTYGNDVRLFGERRGGEDVWElrkrigLVSPALQ-LRFP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 140 SSLTVRETL------------HYTALLairrgnpgsfQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQL 207
Cdd:COG1119   93 RDETVLDVVlsgffdsiglyrEPTDEQ----------RERARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARAL 157

                 ....
gi 767915020 208 LQDP 211
Cdd:COG1119  158 VKDP 161
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
59-208 2.93e-12

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 65.84  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   59 SCRQQWtRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL--RREQFQDCFSYVLQSD 136
Cdd:TIGR01189   7 ACSRGE-RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDS---GEVRWNGTPLaeQRDEPHENILYLGHLP 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020  137 TLLSSLTVRETLHYTALLAirrgnpGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLL 208
Cdd:TIGR01189  83 GLKPELSALENLHFWAAIH------GGAQRTIEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWL 143
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
68-226 5.36e-12

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: 68.71  E-value: 5.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRALR---REQFQDCFSYVLQSDTLLS 140
Cdd:COG2274  490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG-------LYeptsGRILIDGIDLRqidPASLRRQIGVVLQDVFLFS 562
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SlTVRETlhytallaIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSL------GGISTGERRRVSIAAQLLQDP--- 211
Cdd:COG2274  563 G-TIREN--------ITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTvvgeggSNLSGGQRQRLAIARALLRNPril 633
                        170
                 ....*....|....*...
gi 767915020 212 -MD--LTSVDTQSkEREI 226
Cdd:COG2274  634 iLDeaTSALDAET-EAII 650
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
66-211 9.42e-12

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: 63.75  E-value: 9.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL-----RREQFQDCFSYVLQSDTLLS 140
Cdd:cd03229   13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDS---GSILIDGEDLtdledELPPLRRRIGMVFQDFALFP 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915020 141 SLTVRETLHYtallairrgnpgsfqkkveavmaelslshvadrlignyslgGISTGERRRVSIAAQLLQDP 211
Cdd:cd03229   90 HLTVLENIAL-----------------------------------------GLSGGQQQRVALARALAMDP 119
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
60-224 1.53e-11

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: 63.67  E-value: 1.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  60 CRQQWtRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL--RREQFQDCFSYVLQSDT 137
Cdd:cd03231    8 CERDG-RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA---GRVLLNGGPLdfQRDSIARGLLYLGHAPG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 138 LLSSLTVRETLHYTALLAIRRGnpgsfqkkVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP----MD 213
Cdd:cd03231   84 IKTTLSVLENLRFWHADHSDEQ--------VEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRplwiLD 150
                        170
                 ....*....|...
gi 767915020 214 --LTSVDTQSKER 224
Cdd:cd03231  151 epTTALDKAGVAR 163
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
66-211 2.22e-11

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 64.14  E-value: 2.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGR-AGTFLGE------VYVNGRALRReqfqdcFSYVLQSDTL 138
Cdd:PRK10895  16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRdAGNIIIDdedislLPLHARARRG------IGYLPQEASI 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915020 139 LSSLTVRETLhyTALLAIRRG-NPGSFQKKVEAVMAELSLSHVADrlignySLG-GISTGERRRVSIAAQLLQDP 211
Cdd:PRK10895  90 FRRLSVYDNL--MAVLQIRDDlSAEQREDRANELMEEFHIEHLRD------SMGqSLSGGERRRVEIARALAANP 156
PLN03140 PLN03140
ABC transporter G family member; Provisional
68-202 2.61e-11

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 66.79  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRET 147
Cdd:PLN03140  180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKET 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  148 LHYTAL-------------LAIRRGNPGSF-QKKVEAVMAELSLSHVADRLIGNYSLG------------------GIST 195
Cdd:PLN03140  260 LDFSARcqgvgtrydllseLARREKDAGIFpEAEVDLFMKATAMEGVKSSLITDYTLKilgldickdtivgdemirGISG 339

                  ....*..
gi 767915020  196 GERRRVS 202
Cdd:PLN03140  340 GQKKRVT 346
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
66-226 4.21e-11

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: 63.27  E-value: 4.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLD-------AMSGRLGRAGTFLGevYVNGRALRREqfqdcFSYVLQSDTL 138
Cdd:cd03252   15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKliqrfyvPENGRVLVDGHDLA--LADPAWLRRQ-----VGVVLQENVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 139 LSSlTVRETlhytallaIRRGNPGSFQKKVEAVmAELSLSHV--------ADRLIGNYSLgGISTGERRRVSIAAQLLQD 210
Cdd:cd03252   88 FNR-SIRDN--------IALADPGMSMERVIEA-AKLAGAHDfiselpegYDTIVGEQGA-GLSGGQRQRIAIARALIHN 156
                        170       180
                 ....*....|....*....|..
gi 767915020 211 PMDL------TSVDTQSkEREI 226
Cdd:cd03252  157 PRILifdeatSALDYES-EHAI 177
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
68-211 5.24e-11

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 62.91  E-value: 5.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL-------RREQFQDCFSYVLQSDTLLS 140
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS---GDVIFNGQPMsklssaaKAELRNQKLGFIYQFHHLLP 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915020 141 SLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVAdrligNYSLGGISTGERRRVSIAAQLLQDP 211
Cdd:PRK11629 101 DFTALENVAMP--LLIGKKKPAEINSRALEMLAAVGLEHRA-----NHRPSELSGGERQRVAIARALVNNP 164
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
67-211 9.10e-11

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 62.00  E-value: 9.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQFQDC--FSYVLQSDTLLSSLTV 144
Cdd:cd03266   19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL-EPDA--GFATVDGFDVVKEPAEARrrLGFVSDSTGLYDRLTA 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915020 145 RETLHYTALLairRG-NPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDP 211
Cdd:cd03266   96 RENLEYFAGL---YGlKGDELTARLEELADRLGMEELLDR-----RVGGFSTGMRQKVAIARALVHDP 155
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
65-204 9.60e-11

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 63.63  E-value: 9.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRalrreqfqDCFS----------YVLQ 134
Cdd:COG1118   14 SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG-LETPDS--GRIVLNGR--------DLFTnlpprerrvgFVFQ 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 135 SDTLLSSLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIA 204
Cdd:COG1118   83 HYALFPHMTVAENIAFG--LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQ-----LSGGQRQRVALA 145
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
73-210 1.01e-10

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 62.08  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  73 SLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRAL-RREQFQDCFSYVLQSDTLLSSLTVRET 147
Cdd:COG3840   19 DLTIAAGERVAILGPSGAGKSTLLNLIAG-------FLppdsGRILWNGQDLtALPPAERPVSMLFQENNLFPHLTVAQN 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915020 148 LhytaLLAIR-RGNPGSFQK-KVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQD 210
Cdd:COG3840   92 I----GLGLRpGLKLTAEQRaQVEQALERVGLAGLLDRLPGQ-----LSGGQRQRVALARCLVRK 147
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
68-146 1.18e-10

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: 60.31  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR---REQFQDCFSYVLQSDTLLSSlTV 144
Cdd:cd03246   17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS---GRVRLDGADISqwdPNELGDHVGYLPQDDELFSG-SI 92

                 ..
gi 767915020 145 RE 146
Cdd:cd03246   93 AE 94
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
69-211 1.82e-10

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 60.88  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrLGRAGTFLGEVYVNGRA---LRREQ---FQDCFSYVLQSDTLLSSL 142
Cdd:cd03292   17 LDGINISISAGEFVFLVGPSGAGKSTLLKLI---YKEELPTSGTIRVNGQDvsdLRGRAipyLRRKIGVVFQDFRLLPDR 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 143 TVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIgnyslGGISTGERRRVSIAAQLLQDP 211
Cdd:cd03292   94 NVYENVAFA--LEVTGVPPREIRKRVPAALELVGLSHKHRALP-----AELSGGEQQRVAIARAIVNSP 155
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
69-213 5.27e-10

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 60.01  E-value: 5.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLdAMSGRLGRAGTflGEVYVNGR--------ALRREqfqdcFSYVLQSDTLLS 140
Cdd:cd03295   17 VNNLNLEIAKGEFLVLIGPSGSGKTTTM-KMINRLIEPTS--GEIFIDGEdireqdpvELRRK-----IGYVIQQIGLFP 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 141 SLTVRETLhyTALLAIRRGNPGSFQKKVEAVMAELSL--SHVADRlignYSlGGISTGERRRVSIAAQLLQDP----MD 213
Cdd:cd03295   89 HMTVEENI--ALVPKLLKWPKEKIRERADELLALVGLdpAEFADR----YP-HELSGGQQQRVGVARALAADPplllMD 160
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
69-211 1.12e-09

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 58.89  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQD-CFSYVLQSDTLLSSLTVRET 147
Cdd:cd03296   18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERPDS--GTILFGGEDATDVPVQErNVGFVFQHYALFRHMTVFDN 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915020 148 LHYTalLAIR----RGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:cd03296   95 VAFG--LRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQ-----LSGGQRQRVALARALAVEP 155
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
66-211 1.39e-09

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 58.73  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG-----------RALRREqfqdcFSYVLQ 134
Cdd:cd03256   14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTS---GSVLIDGtdinklkgkalRQLRRQ-----IGMIFQ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 135 SDTLLSSLTVRET-----LHYTALL-AIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLL 208
Cdd:cd03256   86 QFNLIERLSVLENvlsgrLGRRSTWrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQ-----LSGGQQQRVAIARALM 160

                 ...
gi 767915020 209 QDP 211
Cdd:cd03256  161 QQP 163
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
65-214 1.76e-09

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 60.08  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRaLRreqfqdcFSYVLQSDTLLSSLTV 144
Cdd:COG0488   10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDS---GEVSIPKG-LR-------IGYLPQEPPLDDDLTV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 145 RETL-----------------------------HYTALLA-IRRGNPGSFQKKVEAVMAELSLSHV-ADRLIGNYSlGgi 193
Cdd:COG0488   79 LDTVldgdaelraleaeleeleaklaepdedleRLAELQEeFEALGGWEAEARAEEILSGLGFPEEdLDRPVSELS-G-- 155
                        170       180
                 ....*....|....*....|.
gi 767915020 194 stGERRRVSIAAQLLQDPmDL 214
Cdd:COG0488  156 --GWRRRVALARALLSEP-DL 173
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
65-211 2.20e-09

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 58.97  E-value: 2.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQfQDCFSYVLQSDTLLSSLTV 144
Cdd:COG4152   13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL-APDS--GEVLWDGEPLDPED-RRRIGYLPEERGLYPKMKV 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915020 145 RETLHYtalLAIRRG-NPGSFQKKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDP 211
Cdd:COG4152   89 GEQLVY---LARLKGlSKAEAKRRADEWLERLGLGDRANKKVEELSK-----GNQQKVQLIAALLHDP 148
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
67-211 2.32e-09

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 58.02  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAL------RREqfqdcFSYVLQSDTLLS 140
Cdd:cd03300   14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTS---GEILLDGKDItnlpphKRP-----VNTVFQNYALFP 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915020 141 SLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:cd03300   86 HLTVFENIAFG--LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQ-----LSGGQQQRVAIARALVNEP 149
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
67-208 3.07e-09

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 59.74  E-value: 3.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsGRLGRAGTflGEVYVNGR-----------ALRREQfqdcFSYVLQS 135
Cdd:PRK10535  22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCLDKPTS--GTYRVAGQdvatldadalaQLRREH----FGFIFQR 94
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915020 136 DTLLSSLTVRETLHYTALLAirrGNP-GSFQKKVEAVMAELSLshvADRLigNYSLGGISTGERRRVSIAAQLL 208
Cdd:PRK10535  95 YHLLSHLTAAQNVEVPAVYA---GLErKQRLLRAQELLQRLGL---EDRV--EYQPSQLSGGQQQRVSIARALM 160
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
68-211 3.19e-09

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: 59.30  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG---RALRREQFQDCFSYVLQSDTLLSSlTV 144
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ---GEVTLDGvpvSSLDQDEVRRRVSVCAQDAHLFDT-TV 425
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915020  145 RETLhytallaiRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYS--LGG----ISTGERRRVSIAAQLLQDP 211
Cdd:TIGR02868 426 RENL--------RLARPDATDEELWAALERVGLADWLRALPDGLDtvLGEggarLSGGERQRLALARALLADA 490
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
65-211 5.32e-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: 5.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALR---REQFQDCFSYVLQSDTLLSS 141
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG-FVDPTE--GSIAVNGVPLAdadADSWRDQIAWVPQHPFLFAG 410
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915020  142 lTVRETLhytaLLAIRRGNPGSFQKKVEAV-----MAELSLSHvaDRLIGNYSlGGISTGERRRVSIAAQLLQDP 211
Cdd:TIGR02857 411 -TIAENI----RLARPDASDAEIREALERAgldefVAALPQGL--DTPIGEGG-AGLSGGQAQRLALARAFLRDA 477
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
65-210 5.37e-09

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 57.33  E-value: 5.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRagTFLGEVYVNGRALRR---EQFQDCFSYVLQSDTLLSS 141
Cdd:PRK11231  14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLT--PQSGTVFLGDKPISMlssRQLARRLALLPQHHLTPEG 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020 142 LTVREtlhytaLLAIRRGNPGSF--------QKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQD 210
Cdd:PRK11231  91 ITVRE------LVAYGRSPWLSLwgrlsaedNARVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQD 156
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
68-204 8.72e-09

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 56.33  E-value: 8.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGRLGRAGTFLGEVYVNGRALRREQFqdcFSYVLQSDTLLS 140
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLailagldDGSSGEVSLVGQPLHQMDEEARAKLRAKH---VGFVFQSFMLIP 101
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915020 141 SLTVRETLHYTALLaiRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIA 204
Cdd:PRK10584 102 TLNALENVELPALL--RGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-----LSGGEQQRVALA 158
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
61-146 9.28e-09

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 55.55  E-value: 9.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  61 RQQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRalrreqfqdcFSYVLQSDTLLS 140
Cdd:cd03250   13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLS---GSVSVPGS----------IAYVSQEPWIQN 79

                 ....*.
gi 767915020 141 SlTVRE 146
Cdd:cd03250   80 G-TIRE 84
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
62-211 9.78e-09

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 57.12  E-value: 9.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  62 QQWTRQI--LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNGR--------ALRREQ------F 125
Cdd:PRK11153  12 PQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCIN-LLERPTS--GRVLVDGQdltalsekELRKARrqigmiF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 126 QDcFSyvlqsdtLLSSLTVRETLhytAL-LAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIA 204
Cdd:PRK11153  89 QH-FN-------LLSSRTVFDNV---ALpLELAGTPKAEIKARVTELLELVGLSDKADRYPAQ-----LSGGQKQRVAIA 152

                 ....*..
gi 767915020 205 AQLLQDP 211
Cdd:PRK11153 153 RALASNP 159
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
71-211 1.40e-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: 56.60  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGR---ALRREQFQD----CFSYVLQSDtlLSSL- 142
Cdd:COG0444   23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEdllKLSEKELRKirgrEIQMIFQDP--MTSLn 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915020 143 ---TVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLiGNY--SLGGistGERRRVSIAAQLLQDP 211
Cdd:COG0444  101 pvmTVGDQIAE-PLRIHGGLSKAEARERAIELLERVGLPDPERRL-DRYphELSG---GMRQRVMIARALALEP 169
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
65-211 1.46e-08

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 55.23  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNG----------RALRREqfqdcFSYVLQ 134
Cdd:cd03262   12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN-LLEEPDS--GTIIIDGlkltddkkniNELRQK-----VGMVFQ 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020 135 SDTLLSSLTVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:cd03262   84 QFNLFPHLTVLENITL-APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNP 154
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
66-224 2.44e-08

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 54.42  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALR--REQFQDCFSYVLQSDTLLSSLT 143
Cdd:PRK13538  14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-LARPDA--GEVLWQGEPIRrqRDEYHQDLLYLGHQPGIKTELT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 144 VRETLHYTALLAirrGNPGSFQkkVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP----MD--LTSV 217
Cdd:PRK13538  91 ALENLRFYQRLH---GPGDDEA--LWEALAQVGLAGFEDVPVRQ-----LSAGQQRRVALARLWLTRAplwiLDepFTAI 160

                 ....*..
gi 767915020 218 DTQSKER 224
Cdd:PRK13538 161 DKQGVAR 167
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
67-209 3.18e-08

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 55.02  E-value: 3.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFLGEVYVNGRALRRE--------QFQDCFSYVLQSDTL 138
Cdd:PRK09984  18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREgrlardirKSRANTGYIFQQFNL 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915020 139 LSSLTVRETLHYTAL-------LAIRRGNPGSFQKKVEAvMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQ 209
Cdd:PRK09984  98 VNRLSVLENVLIGALgstpfwrTCFSWFTREQKQRALQA-LTRVGMVHFAHQRVST-----LSGGQQQRVAIARALMQ 169
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
68-232 3.62e-08

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 55.62  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR----REQFQDCFSyVLQSDTLLSSLT 143
Cdd:PRK09536  18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA---GTVLVAGDDVEalsaRAASRRVAS-VPQDTSLSFEFD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 144 VRETL------HYTallaiRRGNPGSFQKK-VEAVMAELSLSHVADRlignySLGGISTGERRRVSIA---AQ-----LL 208
Cdd:PRK09536  94 VRQVVemgrtpHRS-----RFDTWTETDRAaVERAMERTGVAQFADR-----PVTSLSGGERQRVLLAralAQatpvlLL 163
                        170       180
                 ....*....|....*....|....
gi 767915020 209 QDPMdlTSVDTQSKEREIETSKRV 232
Cdd:PRK09536 164 DEPT--ASLDINHQVRTLELVRRL 185
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
65-211 4.91e-08

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: 53.44  E-value: 4.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrlgrAGTFL---GEVYVNGRALRREQFQDcFSYVLQSDTLLSS 141
Cdd:cd03269   12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMI------LGIILpdsGEVLFDGKPLDIAARNR-IGYLPEERGLYPK 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915020 142 LTVRETLHYTALLairRG-NPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDP 211
Cdd:cd03269   85 MKVIDQLVYLAQL---KGlKKEEARRRIDEWLERLELSEYANK-----RVEELSKGNQQKVQFIAAVIHDP 147
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
67-227 6.19e-08

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 53.70  E-value: 6.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLdAMSGRLgrAGTFLGEVYVNGRALRR---EQFQDCFSYVLQSDTLLSSlT 143
Cdd:cd03249   17 PILKGLSLTIPPGKTVALVGSSGCGKSTVV-SLLERF--YDPTSGEILLDGVDIRDlnlRWLRSQIGLVSQEPVLFDG-T 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 144 VRETlhytallaIRRGNPGSFQKKVEAV--MAEL-----SLSHVADRLIGNY--SLGGistGERRRVSIAAQLLQDPMDL 214
Cdd:cd03249   93 IAEN--------IRYGKPDATDEEVEEAakKANIhdfimSLPDGYDTLVGERgsQLSG---GQKQRIAIARALLRNPKIL 161
                        170
                 ....*....|....*....
gi 767915020 215 -----TS-VDTQSkEREIE 227
Cdd:cd03249  162 lldeaTSaLDAES-EKLVQ 179
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
69-146 6.27e-08

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 54.70  E-value: 6.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNG-----------RALRREqfqdcFSYVLQSDT 137
Cdd:COG1135   21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LERPTS--GSVLVDGvdltalserelRAARRK-----IGMIFQHFN 92

                 ....*....
gi 767915020 138 LLSSLTVRE 146
Cdd:COG1135   93 LLSSRTVAE 101
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
66-211 6.84e-08

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 53.94  E-value: 6.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLG-RAGTF-LGEVYVNGRALRReqfqdcfSYVLQSDTLLSSLT 143
Cdd:PRK11248  14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyQHGSItLDGKPVEGPGAER-------GVVFQNEGLLPWRN 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 144 VRETLHYTALLAirrGNPGSFQKKVEAVM-AELSLSHVADRLIgnYSLGGistGERRRVSIAAQLLQDP 211
Cdd:PRK11248  87 VQDNVAFGLQLA---GVEKMQRLEIAHQMlKKVGLEGAEKRYI--WQLSG---GQRQRVGIARALAANP 147
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
66-211 9.64e-08

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: 52.95  E-value: 9.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTFL--GEVYVNGR----------ALRREqfqdcFSYVL 133
Cdd:cd03260   13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPdeGEVLLDGKdiydldvdvlELRRR-----VGMVF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 134 QSDTLLsSLTVRETLHYTalLAIRrgnpGSFQKKVEAVMAELSLS------HVADRLIGnyslGGISTGERRRVSIAAQL 207
Cdd:cd03260   88 QKPNPF-PGSIYDNVAYG--LRLH----GIKLKEELDERVEEALRkaalwdEVKDRLHA----LGLSGGQQQRLCLARAL 156

                 ....
gi 767915020 208 LQDP 211
Cdd:cd03260  157 ANEP 160
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
69-211 1.01e-07

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 54.65  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL----GEVYVNGRALRREQFQDCFSY----VLQSDTLLS 140
Cdd:COG3845   21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYG-------LYqpdsGEILIDGKPVRIRSPRDAIALgigmVHQHFMLVP 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020 141 SLTVRETLhytaLLAIRRGNPGSF-----QKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:COG3845   94 NLTVAENI----VLGLEPTKGGRLdrkaaRARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEILKALYRGA 160
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
67-211 1.34e-07

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 52.71  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAM-------SGRLGRAGT---FLGEVYVN-GRALRREqfqdcFSYVLQS 135
Cdd:PRK11124  16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNhfdFSKTPSDKaIRELRRN-----VGMVFQQ 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020 136 DTLLSSLTVRETLhYTALLAIRRGNPGSFQKKVEAVMAELSLSHVADRlignYSLgGISTGERRRVSIAAQLLQDP 211
Cdd:PRK11124  91 YNLWPHLTVQQNL-IEAPCRVLGLSKDQALARAEKLLERLRLKPYADR----FPL-HLSGGQQQRVAIARALMMEP 160
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
66-210 1.41e-07

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 52.87  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDaMSGRLGRAGTflGEVYVNGRAL---RREQFQDCFSYVLQSDTLLSSL 142
Cdd:PRK10575  24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHQPPSE--GEILLDAQPLeswSSKAFARKVAYLPQQLPAAEGM 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020 143 TVREtlhytaLLAIRR----GNPGSF----QKKVEAVMAELSLSHVADRLIGnySLGGistGERRRVSIAAQLLQD 210
Cdd:PRK10575 101 TVRE------LVAIGRypwhGALGRFgaadREKVEEAISLVGLKPLAHRLVD--SLSG---GERQRAWIAMLVAQD 165
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
71-210 1.45e-07

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: 52.11  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQD-CFSYVLQSDTLLSSLTVRETLH 149
Cdd:cd03298   16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS---GRVLINGVDVTAAPPADrPVSMLFQENNLFAHLTVEQNVG 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020 150 ytalLAIrrgNPG-----SFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQD 210
Cdd:cd03298   93 ----LGL---SPGlkltaEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRD 146
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
72-209 1.52e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 52.63  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  72 VSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgragTFLGEVYVNGRAL----------RReqfqdcfSYVLQSDTLLSS 141
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL----PGSGSIQFAGQPLeawsaaelarHR-------AYLSQQQTPPFA 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915020 142 LTVretLHYTALLAIRRGNPGSFQKKVEAVMAELSLshvADRLigNYSLGGISTGERRRVSIAAQLLQ 209
Cdd:PRK03695  84 MPV---FQYLTLHQPDKTRTEAVASALNEVAEALGL---DDKL--GRSVNQLSGGEWQRVRLAAVVLQ 143
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
66-103 2.05e-07

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 50.52  E-value: 2.05e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL 103
Cdd:cd03221   13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGEL 50
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
69-226 2.20e-07

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 52.58  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG--RLGRagtflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVre 146
Cdd:PRK15056  23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfvRLAS-----GKISILGQPTRQALQKNLVAYVPQSEEVDWSFPV-- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 147 tLHYTALLAIRRGNPGSF-------QKKVEAVMAELSLSHVADRLIGNyslggISTGERRRV----SIAAQ----LLQDP 211
Cdd:PRK15056  96 -LVEDVVMMGRYGHMGWLrrakkrdRQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVflarAIAQQgqviLLDEP 169
                        170
                 ....*....|....*
gi 767915020 212 mdLTSVDTQSKEREI 226
Cdd:PRK15056 170 --FTGVDVKTEARII 182
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
65-122 2.46e-07

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 52.24  E-value: 2.46e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL----------GRAGTFLgEVYVNGRALRR 122
Cdd:PRK11701  18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLapdagevhyrMRDGQLR-DLYALSEAERR 84
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
69-249 3.24e-07

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: 51.44  E-value: 3.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNG--------RALRREqfqdcFSYVLQSDTLLS 140
Cdd:cd03245   20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAG-LYKPTS--GSVLLDGtdirqldpADLRRN-----IGYVPQDVTLFY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SlTVRETLHYTALLAirrgnpgsfqkKVEAVMAELSLSHVADrLIGNYSLG----------GISTGERRRVSIAAQLLQD 210
Cdd:cd03245   92 G-TLRDNITLGAPLA-----------DDERILRAAELAGVTD-FVNKHPNGldlqigergrGLSGGQRQAVALARALLND 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767915020 211 P----MD--LTSVDTQSKEREIETSKRVqmiesaykksaICHKTL 249
Cdd:cd03245  159 PpillLDepTSAMDMNSEERLKERLRQL-----------LGDKTL 192
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
67-255 4.85e-07

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 50.00  E-value: 4.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAgtfLGEVYVNGR--ALRREQFQDCFSYVLQSDTLLSSlTV 144
Cdd:cd03247   16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ---QGEITLDGVpvSDLEKALSSLISVLNQRPYLFDT-TL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 145 RETLHytallaiRRgnpgsfqkkveavmaelslshvadrlignyslggISTGERRRVSIAAQLLQD-PMDLTSVDTQSKE 223
Cdd:cd03247   92 RNNLG-------RR----------------------------------FSGGERQRLALARILLQDaPIVLLDEPTVGLD 130
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767915020 224 REIETSKRVQMIESAYKKSA--ICHKtLKNIERM 255
Cdd:cd03247  131 PITERQLLSLIFEVLKDKTLiwITHH-LTGIEHM 163
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
67-228 4.99e-07

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 52.54  E-value: 4.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtFL---GEVYVNG---RALRREQFQDCFSYVLQSDTLLS 140
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-------FLpyqGSLKINGielRELDPESWRKHLSWVGQNPQLPH 436
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SlTVRETLhytaLLairrGNPGSFQKKVEAVMAELSLSHVADRL-------IGNYSlGGISTGERRRVSIAAQLLQDPMD 213
Cdd:PRK11174 437 G-TLRDNV----LL----GNPDASDEQLQQALENAWVSEFLPLLpqgldtpIGDQA-AGLSVGQAQRLALARALLQPCQL 506
                        170       180
                 ....*....|....*....|.
gi 767915020 214 L------TSVDTQSKEREIET 228
Cdd:PRK11174 507 LlldeptASLDAHSEQLVMQA 527
hmuV PRK13547
heme ABC transporter ATP-binding protein;
66-122 5.08e-07

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 51.37  E-value: 5.08e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL-----GRAGTFLGEVYVNGRALRR 122
Cdd:PRK13547  14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaPRGARVTGDVTLNGEPLAA 75
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
68-211 6.90e-07

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 51.57  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGRLgragtFLGEVYVN-----GRALrreqfqdcfSYVLQS 135
Cdd:PRK11000  18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLrmiagleDITSGDL-----FIGEKRMNdvppaERGV---------GMVFQS 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020 136 DTLLSSLTVRETLHYTALLAirRGNPGSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDP 211
Cdd:PRK11000  84 YALYPHLSVAENMSFGLKLA--GAKKEEINQRVNQVAEVLQLAHLLDR-----KPKALSGGQRQRVAIGRTLVAEP 152
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
66-150 7.46e-07

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 50.92  E-value: 7.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR---ALRREQFQDC---FSYVLQSDTLL 139
Cdd:PRK11831  20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH---GEILFDGEnipAMSRSRLYTVrkrMSMLFQSGALF 96
                         90
                 ....*....|.
gi 767915020 140 SSLTVRETLHY 150
Cdd:PRK11831  97 TDMNVFDNVAY 107
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
68-259 9.20e-07

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 52.22  E-value: 9.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020    68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAlrreQFQDCFSYVLQS---DTLLSSLTV 144
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE---GKIKHSGRI----SFSPQTSWIMPGtikDNIIFGLSY 513
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   145 REtLHYTALlairrgnpgsfqkkVEAVMAELSLSHVADRLIGNYSLGGI--STGERRRVSIAAQLLQDPmDLTSVDTQSK 222
Cdd:TIGR01271  514 DE-YRYTSV--------------IKACQLEEDIALFPEKDKTVLGEGGItlSGGQRARISLARAVYKDA-DLYLLDSPFT 577
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 767915020   223 EREIETSKrvQMIESAYKKSAICHKTLKNIERMKHLK 259
Cdd:TIGR01271  578 HLDVVTEK--EIFESCLCKLMSNKTRILVTSKLEHLK 612
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
69-211 1.12e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 50.62  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE-----QFQDCFSYVLQS-DTLLSSL 142
Cdd:PRK13636  22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSS---GRILFDGKPIDYSrkglmKLRESVGMVFQDpDNQLFSA 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 143 TVRETLHYTALlaiRRGNP-GSFQKKVEAVMAELSLSHVADRlignySLGGISTGERRRVSIAAQLLQDP 211
Cdd:PRK13636  99 SVYQDVSFGAV---NLKLPeDEVRKRVDNALKRTGIEHLKDK-----PTHCLSFGQKKRVAIAGVLVMEP 160
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
69-122 1.15e-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: 48.97  E-value: 1.15e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR 122
Cdd:cd03215   16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAS---GEITLDGKPVTR 66
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
73-214 1.53e-06

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 49.58  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  73 SLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGralrreqfQDC---------FSYVLQSDTLLSSLT 143
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPAS---GSLTLNG--------QDHtttppsrrpVSMLFQENNLFSHLT 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020 144 VRETLHytalLAIrrgNPG-----SFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLL-QDPMDL 214
Cdd:PRK10771  88 VAQNIG----LGL---NPGlklnaAQREKLHAIARQMGIEDLLARLPGQ-----LSGGQRQRVALARCLVrEQPILL 152
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
71-225 1.54e-06

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 50.26  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFS-------YVLQSDTLLSSLT 143
Cdd:PRK11144  16 TVNLTLPAQGITAIFGRSGAGKTSLINAISG-LTRPQK--GRIVLNGRVLFDAEKGICLPpekrrigYVFQDARLFPHYK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 144 VRETLHYtallAIRRGNPGSFQKKVEAvmaeLSLSHVADRLIGnySLGGistGERRRVSIAAQLLQDP----MD--LTSV 217
Cdd:PRK11144  93 VRGNLRY----GMAKSMVAQFDKIVAL----LGIEPLLDRYPG--SLSG---GEKQRVAIGRALLTAPelllMDepLASL 159

                 ....*...
gi 767915020 218 DTQSKeRE 225
Cdd:PRK11144 160 DLPRK-RE 166
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
67-211 1.65e-06

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 49.58  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLdamsgrlgRAGTFL-----GEVYVNGRALR-------------REQFQDC 128
Cdd:PRK10619  19 EVLKGVSLQANAGDVISIIGSSGSGKSTFL--------RCINFLekpseGSIVVNGQTINlvrdkdgqlkvadKNQLRLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 129 ---FSYVLQSDTLLSSLTVRETLHYTALLAIrrgnpgSFQKKVEAVMAELSLSHVA--DRLIGNYSLgGISTGERRRVSI 203
Cdd:PRK10619  91 rtrLTMVFQHFNLWSHMTVLENVMEAPIQVL------GLSKQEARERAVKYLAKVGidERAQGKYPV-HLSGGQQQRVSI 163

                 ....*...
gi 767915020 204 AAQLLQDP 211
Cdd:PRK10619 164 ARALAMEP 171
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
67-121 1.67e-06

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: 48.19  E-value: 1.67e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR 121
Cdd:cd03216   14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS---GEILVDGKEVS 65
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
66-211 1.74e-06

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 50.83  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLG-RAGTFlgevyVNGRALRreqfqdcFSYVLQS-DTLLSSLT 143
Cdd:COG0488  328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEpDSGTV-----KLGETVK-------IGYFDQHqEELDPDKT 395
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 144 VRETlhytallaIRRGNPGSFQKKVEAVMAELSLS-HVADRLIGnySLGGistGERRRVSIAAQLLQDP 211
Cdd:COG0488  396 VLDE--------LRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVG--VLSG---GEKARLALAKLLLSPP 451
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
69-220 1.86e-06

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 50.40  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgRAGTflGEVYVNGRALRREQFQDCF----SYVLQSDTLLSSLTV 144
Cdd:COG1129   20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVY-QPDS--GEILLDGEPVRFRSPRDAQaagiAIIHQELNLVPNLSV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 145 RETLhYTALLAIRRG--NPGSFQKKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDP----MD----- 213
Cdd:COG1129   97 AENI-FLGREPRRGGliDWRAMRRRARELLARLGLDIDPDTPVGDLSV-----AQQQLVEIARALSRDArvliLDeptas 170

                 ....*..
gi 767915020 214 LTSVDTQ 220
Cdd:COG1129  171 LTEREVE 177
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
67-210 1.86e-06

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 50.59  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSgrlgragtflGEVYVNGRALRR---EQFQDCFSYVLQSD 136
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLqlltrawDPQQ----------GEILLNGQPIADyseAALRQAISVVSQRV 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 137 TLLSSlTVRETLhytaLLAirrgNPGSFQKKVEAVMAELSLSHVADrliGNYSL------GG--ISTGERRRVSIAAQLL 208
Cdd:PRK11160 424 HLFSA-TLRDNL----LLA----APNASDEALIEVLQQVGLEKLLE---DDKGLnawlgeGGrqLSGGEQRRLGIARALL 491

                 ..
gi 767915020 209 QD 210
Cdd:PRK11160 492 HD 493
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
68-228 2.02e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 48.79  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQ--FQDCFSYVLQSDTLLSSLTVR 145
Cdd:PRK13540  16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK---GEILFERQSIKKDLctYQKQLCFVGHRSGINPYLTLR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 146 ETLHYTalLAIRRGNPGsfqkkVEAVMAELSLSHVADrlignYSLGGISTGERRRVSI--------AAQLLQDPmdLTSV 217
Cdd:PRK13540  93 ENCLYD--IHFSPGAVG-----ITELCRLFSLEHLID-----YPCGLLSSGQKRQVALlrlwmskaKLWLLDEP--LVAL 158
                        170
                 ....*....|.
gi 767915020 218 DtqskEREIET 228
Cdd:PRK13540 159 D----ELSLLT 165
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
40-211 2.30e-06

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 49.30  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  40 ILHASySVSHRVRPWWdiTSCRQQWtRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGR- 118
Cdd:PRK10419   3 LLNVS-GLSHHYAHGG--LSGKHQH-QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG-LESPSQ--GNVSWRGEp 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 119 --ALRREQ-----------FQDCFSYVLQSDTLLSSLtvRETL-HYTALLAIRRgnpgsfQKKVEAV--MAELSLSHvAD 182
Cdd:PRK10419  76 laKLNRAQrkafrrdiqmvFQDSISAVNPRKTVREII--REPLrHLLSLDKAER------LARASEMlrAVDLDDSV-LD 146
                        170       180
                 ....*....|....*....|....*....
gi 767915020 183 RLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:PRK10419 147 KRPPQ-----LSGGQLQRVCLARALAVEP 170
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
65-118 2.40e-06

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: 48.68  E-value: 2.40e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgraGTFLGEVYVNGR 118
Cdd:cd03220   34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIY---PPDSGTVTVRGR 84
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
65-118 2.52e-06

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 48.92  E-value: 2.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrlgrAGTFL---GEVYVNGR 118
Cdd:COG1134   38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLI------AGILEptsGRVEVNGR 88
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
69-210 3.12e-06

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 48.56  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESG-----QIMCILGSSGSGKTTLLDAMSGRL----GRAGTFLGEVyvngralrreqfqdcfSYVLQSDTLL 139
Cdd:cd03237   10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLkpdeGDIEIELDTV----------------SYKPQYIKAD 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915020 140 SSLTVRETLHytallAIRRGNPGSFQKKVEaVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQD 210
Cdd:cd03237   74 YEGTVRDLLS-----SITKDFYTHPYFKTE-IAKPLQIEQILDREVPE-----LSGGELQRVAIAACLSKD 133
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
65-204 3.26e-06

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 49.56  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtF----LGEVYVNGRALRR---EQFQdcFSYVLQSDT 137
Cdd:PRK09452  26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-------FetpdSGRIMLDGQDITHvpaENRH--VNTVFQSYA 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020 138 LLSSLTVRETLHYtALLAIRRGNPgSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIA 204
Cdd:PRK09452  97 LFPHMTVFENVAF-GLRMQKTPAA-EITPRVMEALRMVQLEEFAQRKPHQ-----LSGGQQQRVAIA 156
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
69-204 3.78e-06

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 49.68  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRAGtflGEVYVNG-----------RALRRE-Q--FQDCFsyvlq 134
Cdd:COG4172  302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALL-RLIPSE---GEIRFDGqdldglsrralRPLRRRmQvvFQDPF----- 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 135 sdtllSSL----TVRET------LHYTALLAIRRgnpgsfQKKVEAVMAELSLSH-VADRLIGNYSlGgistGERRRVSI 203
Cdd:COG4172  373 -----GSLsprmTVGQIiaeglrVHGPGLSAAER------RARVAEALEEVGLDPaARHRYPHEFS-G----GQRQRIAI 436

                 .
gi 767915020 204 A 204
Cdd:COG4172  437 A 437
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
64-210 4.52e-06

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: 48.10  E-value: 4.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  64 WTRQI--LKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrLGRAGTFLGEVYVNGRALRREQFQDCFS-------YVLQ 134
Cdd:cd03290   10 WGSGLatLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI---LGEMQTLEGKVHWSNKNESEPSFEATRSrnrysvaYAAQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 135 SDTLLSSlTVRETLHYtallairrGNPgsFQK-KVEAVMAELSLSHVADRL-------IGNYSLgGISTGERRRVSIAAQ 206
Cdd:cd03290   87 KPWLLNA-TVEENITF--------GSP--FNKqRYKAVTDACSLQPDIDLLpfgdqteIGERGI-NLSGGQRQRICVARA 154

                 ....
gi 767915020 207 LLQD 210
Cdd:cd03290  155 LYQN 158
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
65-211 4.85e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 48.45  E-value: 4.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE---QFQDCFSYVLQS-DTLLS 140
Cdd:PRK13632  21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS---GEIKIDGITISKEnlkEIRKKIGIIFQNpDNQFI 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915020 141 SLTVRETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:PRK13632  98 GATVEDDIAFG--LENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----LSGGQKQRVAIASVLALNP 161
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
69-270 5.57e-06

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: 49.05  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTFLGEVYVNGRALRREQFQDC----FSYVLQSDTLLSSLTV 144
Cdd:TIGR02633  17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGTWDGEIYWSGSPLKASNIRDTeragIVIIHQELTLVPELSV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  145 RET--LHYTALLAIRRGNPGSFQKKVEAVMAELSLSHVAD-RLIGNYSLggistGERRRVSIAAQLLQDPMDLTSVDTQS 221
Cdd:TIGR02633  96 AENifLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGG-----GQQQLVEIAKALNKQARLLILDEPSS 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020  222 KEREIETSKRVQMIESAYKKSAIC----HK---------TLKNIERMKHLKTLPMVPFKTKD 270
Cdd:TIGR02633 171 SLTEKETEILLDIIRDLKAHGVACvyisHKlnevkavcdTICVIRDGQHVATKDMSTMSEDD 232
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
69-211 9.12e-06

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 47.77  E-value: 9.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR--ALRREQFQDCFSYVL-QSDTLLSSLTVR 145
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTS---GEVRVLGYvpFKRRKEFARRIGVVFgQRSQLWWDLPAI 114
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020 146 ETLHYTAllAIRRGNPGSFQKKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDP 211
Cdd:COG4586  115 DSFRLLK--AIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSL-----GQRMRCELAAALLHRP 173
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
67-211 1.20e-05

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 46.80  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRlGRAGTflGEVYVNGRALRREQ----FQDCFSYVLQSDTLLSSL 142
Cdd:PRK11614  19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRATS--GRIVFDGKDITDWQtakiMREAVAIVPEGRRVFSRM 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 143 TVRETLHYTALLAIRRgnpgSFQKKVEAVMAelSLSHVADRLIgnYSLGGISTGERRRVSIAAQLLQDP 211
Cdd:PRK11614  96 TVEENLAMGGFFAERD----QFQERIKWVYE--LFPRLHERRI--QRAGTMSGGEQQMLAIGRALMSQP 156
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
65-103 1.41e-05

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 46.49  E-value: 1.41e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL 103
Cdd:COG2401   42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL 80
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
65-233 1.49e-05

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 47.65  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLL-------DAMSGRLGRAGTFLGEvyVNGRALRREqfqdcFSYVLQsDT 137
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLInllqrvfDPQSGRILIDGTDIRT--VTRASLRRN-----IAVVFQ-DA 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 138 LLSSLTVRETlhytallaIRRGNPGSFQKKV-EAVMAELSLSHVADRLIGNYSLGG-----ISTGERRRVSIAAQLLQDP 211
Cdd:PRK13657 419 GLFNRSIEDN--------IRVGRPDATDEEMrAAAERAQAHDFIERKPDGYDTVVGergrqLSGGERQRLAIARALLKDP 490
                        170       180
                 ....*....|....*....|..
gi 767915020 212 MDLTsVDTQSKEREIETSKRVQ 233
Cdd:PRK13657 491 PILI-LDEATSALDVETEAKVK 511
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
68-259 1.77e-05

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 46.77  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRAlrreQFQDCFSYVLQSdtllsslTVRET 147
Cdd:cd03291   52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSE---GKIKHSGRI----SFSSQFSWIMPG-------TIKEN 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 148 LHYTALLAIRRgnpgsFQKKVEAVMAELSLSHVADRLIGNYSLGGI--STGERRRVSIAAQLLQDPmDLTSVDTQSKERE 225
Cdd:cd03291  118 IIFGVSYDEYR-----YKSVVKACQLEEDITKFPEKDNTVLGEGGItlSGGQRARISLARAVYKDA-DLYLLDSPFGYLD 191
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767915020 226 IETSKrvQMIESAYKKSAICHKTLKNIERMKHLK 259
Cdd:cd03291  192 VFTEK--EIFESCVCKLMANKTRILVTSKMEHLK 223
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
67-211 1.85e-05

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 46.24  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAM-------SGRLGRAGTFLGEVYVNGRALRREQfqdcfSYVLQSDTLL 139
Cdd:PRK09493  15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKVNDPKVDERLIRQEA-----GMVFQQFYLF 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020 140 SSLTVRETLHYTAlLAIRRGNPGSFQKKVEAVMAELSLSHVAdrligNYSLGGISTGERRRVSIAAQLLQDP 211
Cdd:PRK09493  90 PHLTALENVMFGP-LRVRGASKEEAEKQARELLAKVGLAERA-----HHYPSELSGGQQQRVAIARALAVKP 155
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
68-204 1.91e-05

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 46.00  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDCFSYVLQSDTLLSSLTVRET 147
Cdd:PRK13543  26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAG-LLHVES--GQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLEN 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 148 LHYTALLAIRRGN--PGSfqkkveaVMAELSLSHVADRLIGNyslggISTGERRRVSIA 204
Cdd:PRK13543 103 LHFLCGLHGRRAKqmPGS-------ALAIVGLAGYEDTLVRQ-----LSAGQKKRLALA 149
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
76-260 2.00e-05

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 47.70  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020    76 VESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR--EQFQDCFSYVLQSDTLLSSLTVRETLHYTAL 153
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTS---GDATVAGKSILTniSDVHQNMGYCPQFDAIDDLLTGREHLYLYAR 2038
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   154 LairRGNPGsfqKKVEAV----MAELSLSHVADRLIGNYslggiSTGERRRVSIAAQLLQDP----MD--LTSVDTQSKE 223
Cdd:TIGR01257 2039 L---RGVPA---EEIEKVanwsIQSLGLSLYADRLAGTY-----SGGNKRKLSTAIALIGCPplvlLDepTTGMDPQARR 2107
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767915020   224 ----------RE----IETSKRVQMIESAYKKSAICHK-TLKNIERMKHLKT 260
Cdd:TIGR01257 2108 mlwntivsiiREgravVLTSHSMEECEALCTRLAIMVKgAFQCLGTIQHLKS 2159
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
66-223 2.05e-05

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: 45.92  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALrrEQFQDCF-----SYVLQSDTLLS 140
Cdd:cd03248   27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG---GQVLLDGKPI--SQYEHKYlhskvSLVGQEPVLFA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SlTVRETLHYtallairrgnpGSFQKKVEAVMAELSLSHvADRLIGNYSLG----------GISTGERRRVSIAAQLLQD 210
Cdd:cd03248  102 R-SLQDNIAY-----------GLQSCSFECVKEAAQKAH-AHSFISELASGydtevgekgsQLSGGQKQRVAIARALIRN 168
                        170
                 ....*....|....*....
gi 767915020 211 PMDL------TSVDTQSKE 223
Cdd:cd03248  169 PQVLildeatSALDAESEQ 187
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
71-211 2.16e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 47.43  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  71 DVSLYVESGQIMCILGSSGSGKTT-------LLDAMSGR---LGRagtflgEVYVNGRALRREqfqdcFSYVLQSDTLLS 140
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPASEGEawlFGQ------PVDAGDIATRRR-----VGYMSQAFSLYG 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SLTVRE--TLHytALLairrgnpgsFQ-------KKVEAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQLLQDP 211
Cdd:NF033858 353 ELTVRQnlELH--ARL---------FHlpaaeiaARVAEMLERFDLADVADALPDSLPL-----GIRQRLSLAVAVIHKP 416
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
66-102 2.63e-05

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: 45.21  E-value: 2.63e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGR 102
Cdd:cd03217   13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH 49
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
66-211 2.69e-05

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 45.90  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAM-------SGRLGragtfLGEVYVNG-RALRREQ-----FQDCFSYV 132
Cdd:PRK11264  16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIR-----VGDITIDTaRSLSQQKglirqLRQHVGFV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 133 LQSDTLLSSLTVRETLHYTALlaIRRGNP-GSFQKKVEAVMAELSLSHVAD----RLIGnyslggistGERRRVSIAAQL 207
Cdd:PRK11264  91 FQNFNLFPHRTVLENIIEGPV--IVKGEPkEEATARARELLAKVGLAGKETsyprRLSG---------GQQQRVAIARAL 159

                 ....
gi 767915020 208 LQDP 211
Cdd:PRK11264 160 AMRP 163
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
69-221 2.96e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 46.92  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGR-AGT--FLG-EVYVNGralRREQFQDCFSYVLQSDTLLSSLTV 144
Cdd:PRK10762  20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRdAGSilYLGkEVTFNG---PKSSQEAGIGIIHQELNLIPQLTI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 145 RETLhytaLLAIRRGNP-GSFQ-KKV----EAVMAELSLSHVADRLIGNYSLggistGERRRVSIAAQL--------LQD 210
Cdd:PRK10762  97 AENI----FLGREFVNRfGRIDwKKMyaeaDKLLARLNLRFSSDKLVGELSI-----GEQQMVEIAKVLsfeskviiMDE 167
                        170
                 ....*....|..
gi 767915020 211 PMD-LTSVDTQS 221
Cdd:PRK10762 168 PTDaLTDTETES 179
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
65-96 5.12e-05

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 45.03  E-value: 5.12e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLL 96
Cdd:COG1117   23 DKQALKDINLDIPENKVTALIGPSGCGKSTLL 54
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
66-211 5.91e-05

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 45.70  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtfLGEVYvNGRALRREQFQdcFSYVLQSDTLLSSLTVR 145
Cdd:TIGR03719  18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VDKDF-NGEARPQPGIK--VGYLPQEPQLDPTKTVR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  146 ETL--------------------------HYTALLAirrgNPGSFQKKVEAVMA---ELSLSHVADRL---IGNYSLGGI 193
Cdd:TIGR03719  87 ENVeegvaeikdaldrfneisakyaepdaDFDKLAA----EQAELQEIIDAADAwdlDSQLEIAMDALrcpPWDADVTKL 162
                         170
                  ....*....|....*...
gi 767915020  194 STGERRRVSIAAQLLQDP 211
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKP 180
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
67-244 6.21e-05

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 45.56  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG-------------------------RLGRAGT------------- 108
Cdd:TIGR03269  14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvalcekcgyveRPSKVGEpcpvcggtlepee 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  109 --FLGEVYVNGRALRRE---QFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIRRGnpgsfQKKVEAVMAELSLSHVADR 183
Cdd:TIGR03269  94 vdFWNLSDKLRRRIRKRiaiMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRA-----VDLIEMVQLSHRITHIARD 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020  184 LIGnyslggistGERRRVSIAAQLLQDPMDLTSvDTQSKEREIETSKRV-QMIESAYKKSAI 244
Cdd:TIGR03269 169 LSG---------GEKQRVVLARQLAKEPFLFLA-DEPTGTLDPQTAKLVhNALEEAVKASGI 220
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
71-211 7.88e-05

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 45.21  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  71 DVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlgragtF----LGEVYVNGRALRR-EQFQDCFSYVLQSDTLLSSLTVR 145
Cdd:PRK11607  37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAG-------FeqptAGQIMLDGVDLSHvPPYQRPINMMFQSYALFPHMTVE 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020 146 ETLHYTalLAIRRGNPGSFQKKVEAVMAELSLSHVADRliGNYSLGGistGERRRVSIAAQLLQDP 211
Cdd:PRK11607 110 QNIAFG--LKQDKLPKAEIASRVNEMLGLVHMQEFAKR--KPHQLSG---GQRQRVALARSLAKRP 168
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
78-235 1.08e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 43.46  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  78 SGQIMCILGSSGSGKTTLLDAMS----GRLGRAGTFLG--------------EVYVNGRALRREQFQDCFSYVLQSDT-- 137
Cdd:COG0419   22 DDGLNLIVGPNGAGKSTILEAIRyalyGKARSRSKLRSdlinvgseeasvelEFEHGGKRYRIERRQGEFAEFLEAKPse 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 138 ---LLSSLTvrETLHYTALLAIRRGNPGSFQKKVEAVMAELSL-SHVADRLIGNYSLGGISTGERRRVSIaAQLLQDPMD 213
Cdd:COG0419  102 rkeALKRLL--GLEIYEELKERLKELEEALESALEELAELQKLkQEILAQLSGLDPIETLSGGERLRLAL-ADLLSLILD 178
                        170       180
                 ....*....|....*....|..
gi 767915020 214 LTSVDTQSKEREIETSKRVQMI 235
Cdd:COG0419  179 FGSLDEERLERLLDALEELAII 200
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
68-185 1.11e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 45.04  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR---EQFQDCFSY-VLQSDTLLSSLT 143
Cdd:PRK15439  26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS---GTLEIGGNPCARltpAKAHQLGIYlVPQEPLLFPNLS 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767915020 144 VRETlhytalLAIRRGNPGSFQKKVEAVMAELSLS----------HVADRLI 185
Cdd:PRK15439 103 VKEN------ILFGLPKRQASMQKMKQLLAALGCQldldssagslEVADRQI 148
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
67-211 1.13e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 44.13  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG--RLGRAGTFLGEVYVNGRAL---------RREQFqdcfsyVLQS 135
Cdd:PRK14247  17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEARVSGEVYLDGQDIfkmdvielrRRVQM------VFQI 90
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020 136 DTLLSSLTVRETLHYTALLAIRRGNPGSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDP 211
Cdd:PRK14247  91 PNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLwDEVKDRL--DAPAGKLSGGQQQRLCIARALAFQP 165
GguA NF040905
sugar ABC transporter ATP-binding protein;
62-121 1.14e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 44.78  E-value: 1.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020  62 QQWTRQILKDVSLYVESGQIMCILGSSGSGKTTLldAMSgRLGRA-GTFL-GEVYVNGRALR 121
Cdd:NF040905 269 LHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTEL--AMS-VFGRSyGRNIsGTVFKDGKEVD 327
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
68-222 1.29e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 44.03  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG-RLGRAGT--FLGEVyVNGRALRREQFqdcFSYVLQSDTLLSSLTV 144
Cdd:PRK13537  22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPDAGSisLCGEP-VPSRARHARQR---VGVVPQFDNLDPDFTV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 145 RETL----HYTALLAirrgnpGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP----MD--L 214
Cdd:PRK13537  98 RENLlvfgRYFGLSA------AAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPdvlvLDepT 166

                 ....*...
gi 767915020 215 TSVDTQSK 222
Cdd:PRK13537 167 TGLDPQAR 174
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
66-211 1.33e-04

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 44.80  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflgevyvnGRALRREQFQDCF----SYvLQSDTLlss 141
Cdd:COG4178  376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYGS--------GRIARPAGARVLFlpqrPY-LPLGTL--- 442
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020 142 ltvRETLHYTALlairrgnPGSF-QKKVEAVMAELSLSHVADRLIGNYSLGGI-STGERRRVSIAAQLLQDP 211
Cdd:COG4178  443 ---REALLYPAT-------AEAFsDAELREALEAVGLGHLAERLDEEADWDQVlSLGEQQRLAFARLLLHKP 504
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
66-101 1.43e-04

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 43.90  E-value: 1.43e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG 101
Cdd:PRK11247  25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG 60
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
65-121 1.52e-04

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 44.62  E-value: 1.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALR 121
Cdd:COG1129  264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADS---GEIRLDGKPVR 317
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
69-191 1.76e-04

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 44.15  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTFLGEVYVNGRALR----REQFQDCFSYVLQSDTLLSSLTV 144
Cdd:PRK13549  21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGTYEGEIIFEGEELQasniRDTERAGIAIIHQELALVKELSV 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 145 RET------------LHYTALLAirrgnpgsfqkKVEAVMAELSLSHVADRLIGNYSLG 191
Cdd:PRK13549 100 LENiflgneitpggiMDYDAMYL-----------RAQKLLAQLKLDINPATPVGNLGLG 147
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
65-203 2.08e-04

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 42.78  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAgtfLGEVYVNGR---ALRREQFQDCFSYVLQSDTLLSS 141
Cdd:PRK10247  19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT---SGTLLFEGEdisTLKPEIYRQQVSYCAQTPTLFGD 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020 142 lTVRETLHYTALlaIRRGNPGsfQKKVEAVMAELSLshvaDRLIGNYSLGGISTGERRRVSI 203
Cdd:PRK10247  96 -TVYDNLIFPWQ--IRNQQPD--PAIFLDDLERFAL----PDTILTKNIAELSGGEKQRISL 148
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
65-211 2.18e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 43.25  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYV----LQSDTLLS 140
Cdd:PRK13652  16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTS---GSVLIRGEPITKENIREVRKFVglvfQNPDDQIF 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020 141 SLTVRETLhytALLAIRRG-NPGSFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:PRK13652  93 SPTVEQDI---AFGPINLGlDEETVAHRVSSALHMLGLEELRDRVPHH-----LSGGEKKRVAIAGVIAMEP 156
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
69-211 2.61e-04

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 43.48  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRLGRAGTflGEVYVNG-----------RALRREQfqdcFSYVLQSDT 137
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLN-RLIEPTR--GQVLIDGvdiakisdaelREVRRKK----IAMVFQSFA 116
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020 138 LLSSLTVRETLHYTALLAirrGNPGSFQKkveavmaELSLSHVADRLIGNYSLG---GISTGERRRVSIAAQLLQDP 211
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELA---GINAEERR-------EKALDALRQVGLENYAHSypdELSGGMRQRVGLARALAINP 183
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
69-210 2.75e-04

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 43.75  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALR----REQFQDCFSYVLQSDTLLSSLTV 144
Cdd:PRK11288  20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSG-NYQPDA--GSILIDGQEMRfastTAALAAGVAIIYQELHLVPEMTV 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020 145 RETLhYTALLAIRRgnpGSFQKKVEAVMAELSLSHVADRLIGNYSLGGISTGERRRVSIAAQLLQD 210
Cdd:PRK11288  97 AENL-YLGQLPHKG---GIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
69-117 2.76e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 43.15  E-value: 2.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG 117
Cdd:PRK13633  26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSE---GKVYVDG 71
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
69-122 3.33e-04

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 43.48  E-value: 3.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR 122
Cdd:COG3845  274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS---GSIRLDGEDITG 324
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
65-123 5.34e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 41.92  E-value: 5.34e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE 123
Cdd:PRK13635  19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA---GTITVGGMVLSEE 74
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
67-211 5.46e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 42.03  E-value: 5.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLdamsgrLGRAGTFL---GEVYVNGRALRREQ-----------FQDcfsyv 132
Cdd:PRK13647  19 KALKGLSLSIPEGSKTALLGPNGAGKSTLL------LHLNGIYLpqrGRVKVMGREVNAENekwvrskvglvFQD----- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 133 lqSDTLLSSLTVRETLhytALLAIRRG-NPGSFQKKVEAVMAELSLSHVADRliGNYSLggiSTGERRRVSIAAQLLQDP 211
Cdd:PRK13647  88 --PDDQVFSSTVWDDV---AFGPVNMGlDKDEVERRVEEALKAVRMWDFRDK--PPYHL---SYGQKKRVAIAGVLAMDP 157
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
34-211 6.42e-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: 6.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   34 EPHSLG--ILHASYSVShrvrpwWDITSCRqqwtRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlGRAGTFLG 111
Cdd:TIGR02633 249 EPHEIGdvILEARNLTC------WDVINPH----RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG--AYPGKFEG 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  112 EVYVNGRALRREQFQDCFSYVL-------QSDTLLSSLTVRETLHYTAL---LAIRRGNPGSFQKKVEAVMAELSLSHVA 181
Cdd:TIGR02633 317 NVFINGKPVDIRNPAQAIRAGIamvpedrKRHGIVPILGVGKNITLSVLksfCFKMRIDAAAELQIIGSAIQRLKVKTAS 396
                         170       180       190
                  ....*....|....*....|....*....|
gi 767915020  182 DRLignySLGGISTGERRRVSIAAQLLQDP 211
Cdd:TIGR02633 397 PFL----PIGRLSGGNQQKAVLAKMLLTNP 422
GguA NF040905
sugar ABC transporter ATP-binding protein;
69-121 7.36e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 42.08  E-value: 7.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGrAGTFLGEVYVNGRALR 121
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGSYEGEILFDGEVCR 68
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
68-247 7.82e-04

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 41.33  E-value: 7.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGR---ALRREQFQDCFSYVLQsDTLLSSLTV 144
Cdd:cd03244   19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSS---GSILIDGVdisKIGLHDLRSRISIIPQ-DPVLFSGTI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 145 RETL----HYTallairrgnpgsfQKKVEAVMAELSL-SHVADRLIGNYSL---GG--ISTGERRRVSIAAQLLQDP--- 211
Cdd:cd03244   95 RSNLdpfgEYS-------------DEELWQALERVGLkEFVESLPGGLDTVveeGGenLSVGQRQLLCLARALLRKSkil 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767915020 212 -MD--LTSVDtqskereIETSKRVQ-MIESAYKKS---AICHK 247
Cdd:cd03244  162 vLDeaTASVD-------PETDALIQkTIREAFKDCtvlTIAHR 197
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
68-211 8.12e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 41.74  E-value: 8.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  68 ILKDVSLYVESGQIMCILGSSGSGKTT----LLDAMSGRLGRAgTFLGE-VYVNGRALRREqfqdcFSYVLQSDTLLSSL 142
Cdd:PRK13536  56 VVNGLSFTVASGECFGLLGPNGAGKSTiarmILGMTSPDAGKI-TVLGVpVPARARLARAR-----IGVVPQFDNLDLEF 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020 143 TVRETL----HYTALLAirrgnpgsfqKKVEAVMAEL----SLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:PRK13536 130 TVRENLlvfgRYFGMST----------REIEAVIPSLlefaRLESKADARVSD-----LSGGMKRRLTLARALINDP 191
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
65-118 8.23e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 41.56  E-value: 8.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAmsgrLGRAGTFLGEVYVNGR 118
Cdd:PRK14258  19 TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC----LNRMNELESEVRVEGR 68
PLN03130 PLN03130
ABC transporter C family member; Provisional
55-204 9.01e-04

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 42.42  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   55 WDITScrqqwTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLgrAGTFLGEVYVNGRAlrreqfqdcfSYVLQ 134
Cdd:PLN03130  624 WDSKA-----ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL--PPRSDASVVIRGTV----------AYVPQ 686
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915020  135 SDTLLSSlTVRETLHYTALLairrgNPGSFQKKVEAVmaelSLSHVADRL-------IGNYSLGgISTGERRRVSIA 204
Cdd:PLN03130  687 VSWIFNA-TVRDNILFGSPF-----DPERYERAIDVT----ALQHDLDLLpggdlteIGERGVN-ISGGQKQRVSMA 752
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
78-127 9.18e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.05  E-value: 9.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767915020    78 SGQIMCILGSSGSGKTTLLDAMSGRLGRAGTflGEVYVNGRALRREQFQD 127
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGG--GVIYIDGEDILEEVLDQ 48
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
66-148 9.23e-04

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 42.20  E-value: 9.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020    66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAmsgrLGRAGTFLGEVYVNG---RALRREQFQDCFSYVLQSDTLLSSl 142
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSA----LLRLLSTEGEIQIDGvswNSVTLQTWRKAFGVIPQKVFIFSG- 1306

                   ....*.
gi 767915020   143 TVRETL 148
Cdd:TIGR01271 1307 TFRKNL 1312
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
80-210 1.05e-03

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: 42.31  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020    80 QIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR--EQFQDCFSYVLQSDTLLSSLTVRETLHYTALLAIR 157
Cdd:TIGR01257  957 QITAFLGHNGAGKTTTLSILTGLLPPTS---GTVLVGGKDIETnlDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGR 1033
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767915020   158 RGNPGsfQKKVEAVMAELSLSHVAdrligNYSLGGISTGERRRVSIAAQLLQD 210
Cdd:TIGR01257 1034 SWEEA--QLEMEAMLEDTGLHHKR-----NEEAQDLSGGMQRKLSVAIAFVGD 1079
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
17-257 1.07e-03

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 42.01  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  17 VNRGS------QSSLEGAPA----TAPEPHSLGILHAsysvshrvrpwwDITS-CRQQWTRQILKDVSLYVESGQIMCIL 85
Cdd:PRK10789 280 VERGSaaysriRAMLAEAPVvkdgSEPVPEGRGELDV------------NIRQfTYPQTDHPALENVNFTLKPGQMLGIC 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  86 GSSGSGKTTLLdAMSGRLGRAGTflGEVYVNGRALRREQFQDC---FSYVLQSDTLLSSlTVRETlhytallaIRRGNPG 162
Cdd:PRK10789 348 GPTGSGKSTLL-SLIQRHFDVSE--GDIRFHDIPLTKLQLDSWrsrLAVVSQTPFLFSD-TVANN--------IALGRPD 415
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 163 SFQKKVEAVMaelSLSHVAD---RLIGNY--SLGG----ISTGERRRVSIAAQLLQDP----MD--LTSVDTQSkEREI- 226
Cdd:PRK10789 416 ATQQEIEHVA---RLASVHDdilRLPQGYdtEVGErgvmLSGGQKQRISIARALLLNAeiliLDdaLSAVDGRT-EHQIl 491
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 767915020 227 ----ETSKRVQMIESAYKKSAICHKTlkNIERMKH 257
Cdd:PRK10789 492 hnlrQWGEGRTVIISAHRLSALTEAS--EILVMQH 524
ycf16 CHL00131
sulfate ABC transporter protein; Validated
65-101 1.10e-03

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 40.78  E-value: 1.10e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG 101
Cdd:CHL00131  19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
34-121 1.26e-03

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 41.45  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  34 EPHSLG--ILHA-SYSVSHRVRPwwditscrqqwTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrlGRAGTFL 110
Cdd:PRK13549 251 EPHTIGevILEVrNLTAWDPVNP-----------HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGRWE 317
                         90
                 ....*....|.
gi 767915020 111 GEVYVNGRALR 121
Cdd:PRK13549 318 GEIFIDGKPVK 328
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
66-241 1.30e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 40.80  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSgRL-----------GRAGTFLGEVY-VNGRALRREqfqdcFSYVL 133
Cdd:PRK14246  23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLN-RLieiydskikvdGKVLYFGKDIFqIDAIKLRKE-----VGMVF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 134 QSDTLLSSLTVRETLHYtALLAIRRGNPGSFQKKVEAVMAELSL-SHVADRLigNYSLGGISTGERRRVSIAAQLLQDPM 212
Cdd:PRK14246  97 QQPNPFPHLSIYDNIAY-PLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRL--NSPASQLSGGQQQRLTIARALALKPK 173
                        170       180
                 ....*....|....*....|....*....
gi 767915020 213 DLTsVDTQSKEREIETSKRVQMIESAYKK 241
Cdd:PRK14246 174 VLL-MDEPTSMIDIVNSQAIEKLITELKN 201
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
84-108 1.65e-03

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 40.65  E-value: 1.65e-03
                         10        20
                 ....*....|....*....|....*...
gi 767915020  84 ILGSSGSGKTTLLDAM---SGRLGRAGT 108
Cdd:cd04170    4 LVGHSGSGKTTLAEALlyaTGAIDRLGR 31
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
66-214 1.74e-03

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 41.25  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLdAMSGRLGRAGTflGEVYVNGRALrrEQFQDCFSY----VLQSDTLLSS 141
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVA-ALLQNLYQPTG--GQVLLDGVPL--VQYDHHYLHrqvaLVGQEPVLFS 568
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  142 LTVRETLHYtallairrgnpGSFQKKVEAVMAELSLSHvADRLIGNYSLGG----------ISTGERRRVSIAAQLLQDP 211
Cdd:TIGR00958 569 GSVRENIAY-----------GLTDTPDEEIMAAAKAAN-AHDFIMEFPNGYdtevgekgsqLSGGQKQRIAIARALVRKP 636

                  ...
gi 767915020  212 MDL 214
Cdd:TIGR00958 637 RVL 639
PTZ00243 PTZ00243
ABC transporter; Provisional
66-227 1.77e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 41.30  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLdamsgrlgraGTFLGEVYVN-GRALRREQfqdcFSYVLQSDTLLSSlTV 144
Cdd:PTZ00243  673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLL----------QSLLSQFEISeGRVWAERS----IAYVPQQAWIMNA-TV 737
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  145 RETlhytaLLAIRRGNPGSFQKKVEAVMAELSLSHVADRL---IGNYSLgGISTGERRRVSIA--------AQLLQDPmd 213
Cdd:PTZ00243  738 RGN-----ILFFDEEDAARLADAVRVSQLEADLAQLGGGLeteIGEKGV-NLSGGQKARVSLAravyanrdVYLLDDP-- 809
                         170
                  ....*....|....
gi 767915020  214 LTSVDTQSKEREIE 227
Cdd:PTZ00243  810 LSALDAHVGERVVE 823
PLN03232 PLN03232
ABC transporter C family member; Provisional
55-204 1.84e-03

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 41.50  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020   55 WDITScrqqwTRQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGTflGEVYVNGRAlrreqfqdcfSYVLQ 134
Cdd:PLN03232  624 WDSKT-----SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET--SSVVIRGSV----------AYVPQ 686
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020  135 SDTLLSSlTVRETLHYTAllairRGNPGSFQKKVEAVmaelSLSHVADRLIGN--YSLG----GISTGERRRVSIA 204
Cdd:PLN03232  687 VSWIFNA-TVRENILFGS-----DFESERYWRAIDVT----ALQHDLDLLPGRdlTEIGergvNISGGQKQRVSMA 752
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
67-221 2.12e-03

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 39.70  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTL-------LDAMSGRLGRAGTFLGEVYVngRALRREqfqdcFSYVLQSDTLL 139
Cdd:cd03369   22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLilalfrfLEAEEGKIEIDGIDISTIPL--EDLRSS-----LTIIPQDPTLF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 140 SSlTVRETL----HYTAllairrgnpgsfqkkvEAVMAELSLSHVADRLignyslggiSTGERRRVSIAAQLLQDP---- 211
Cdd:cd03369   95 SG-TIRSNLdpfdEYSD----------------EEIYGALRVSEGGLNL---------SQGQRQLLCLARALLKRPrvlv 148
                        170
                 ....*....|..
gi 767915020 212 MD--LTSVDTQS 221
Cdd:cd03369  149 LDeaTASIDYAT 160
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
67-210 2.87e-03

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 40.54  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRR----EQFQDCFSYVLQSDTLLSSL 142
Cdd:PRK09700  19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTK---GTITINNINYNKldhkLAAQLGIGIIYQELSVIDEL 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915020 143 TVRETLhYTALLAIRR--GNP----GSFQKKVEAVMAELSLSHVADRLIGNYSlggIStgERRRVSIAAQLLQD 210
Cdd:PRK09700  96 TVLENL-YIGRHLTKKvcGVNiidwREMRVRAAMMLLRVGLKVDLDEKVANLS---IS--HKQMLEIAKTLMLD 163
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
66-101 3.06e-03

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: 38.67  E-value: 3.06e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSG 101
Cdd:cd03223   14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG 49
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
69-211 3.87e-03

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 39.99  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRREQFQDCFSYVL-------QSDTLLSS 141
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTS---GYVTLDGHEVVTRSPQDGLANGIvyisedrKRDGLVLG 344
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915020 142 LTVRETLHYTALLAIRRGnPGSFQKKVE--AVMAELSLSHV----ADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:PRK10762 345 MSVKENMSLTALRYFSRA-GGSLKHADEqqAVSDFIRLFNIktpsMEQAIGL-----LSGGNQQKVAIARGLMTRP 414
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
65-120 4.50e-03

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 39.67  E-value: 4.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020  65 TRQILKDVSLYVESGQIMCILGSSGSGKT-TLLDAMsgRL--GRAGTFLGEVYVNGRAL 120
Cdd:COG4172   22 TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL--RLlpDPAAHPSGSILFDGQDL 78
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
66-211 4.53e-03

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 39.72  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrlgrAGT---FLGEVyvngralrreQFQDCFS--YVLQSDTLLS 140
Cdd:PRK11819  20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM------AGVdkeFEGEA----------RPAPGIKvgYLPQEPQLDP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020 141 SLTVRETL-----HYTALL------AIRRGNPGSFQKKVEAVMAEL--------------SLSHVADRL---IGNYSLGG 192
Cdd:PRK11819  84 EKTVRENVeegvaEVKAALdrfneiYAAYAEPDADFDALAAEQGELqeiidaadawdldsQLEIAMDALrcpPWDAKVTK 163
                        170
                 ....*....|....*....
gi 767915020 193 ISTGERRRVSIAAQLLQDP 211
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKP 182
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
66-103 5.68e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 39.49  E-value: 5.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL 103
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGEL 369
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
66-211 6.26e-03

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 38.56  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMsgrlgragtfLGEVYVNGRALRREQfQDCFSYVLQS---DTLLsSL 142
Cdd:PRK09544  17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV----------LGLVAPDEGVIKRNG-KLRIGYVPQKlylDTTL-PL 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915020 143 TVRETLhytallairRGNPGSFQKKVEAVMAELSLSHVADrlignYSLGGISTGERRRVSIAAQLLQDP 211
Cdd:PRK09544  85 TVNRFL---------RLRPGTKKEDILPALKRVQAGHLID-----APMQKLSGGETQRVLLARALLNRP 139
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
69-108 6.41e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 39.61  E-value: 6.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 767915020   69 LKDVSLYVESGQIMCILGSSGSGKTTLLD-----AMSGRLGRAGT 108
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypALANRLNGAKT 668
cbiO PRK13637
energy-coupling factor transporter ATPase;
69-117 7.34e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 38.49  E-value: 7.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 767915020  69 LKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNG 117
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTS---GKIIIDG 68
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
67-211 9.41e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 38.13  E-value: 9.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRLGRAGtflGEVYVNGRALRRE-----QFQDCFSYVLQ-SDTLLS 140
Cdd:PRK13639  16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS---GEVLIKGEPIKYDkksllEVRKTVGIVFQnPDDQLF 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915020 141 SLTVRETLHYTALlairrgNPG----SFQKKVEAVMAELSLSHVADRLIGNyslggISTGERRRVSIAAQLLQDP 211
Cdd:PRK13639  93 APTVEEDVAFGPL------NLGlskeEVEKRVKEALKAVGMEGFENKPPHH-----LSGGQKKRVAIAGILAMKP 156
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
66-211 9.70e-03

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 37.93  E-value: 9.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915020  66 RQILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGrLGRAGTflGEVYVNGRALRREQFQDC------FSYVLQSDTLL 139
Cdd:PRK10908  15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERPSA--GKIWFSGHDITRLKNREVpflrrqIGMIFQDHHLL 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915020 140 SSLTVRETLHYTALLAIRRGNpgSFQKKVEAVMAELSLSHVADrligNYSLgGISTGERRRVSIAAQLLQDP 211
Cdd:PRK10908  92 MDRTVYDNVAIPLIIAGASGD--DIRRRVSAALDKVGLLDKAK----NFPI-QLSGGEQQRVGIARAVVNKP 156
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
67-103 9.90e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 38.14  E-value: 9.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767915020  67 QILKDVSLYVESGQIMCILGSSGSGKTTLLDAMSGRL 103
Cdd:PRK13651  21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALL 57
 
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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