|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1-158 |
1.47e-103 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 308.90 E-value: 1.47e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGVQISPSsvRMLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATVRM 80
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGS--VLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRM 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 81 PRTMTQKQKIQRVDQVIQDLSLGKCQNTVIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 158
Cdd:TIGR00955 129 PRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1-158 |
2.07e-51 |
|
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: 163.60 E-value: 2.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGVQISpsSVRMLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATVRM 80
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLDAISGRVEGGGTTS--GQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRETLTYTAILRL 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 81 PRTMTQKQKIQRVDqviqDLSLGKCQNTVIGVPgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 158
Cdd:cd03234 111 PRKSSDAIRKKRVE----DVLLRDLALTRIGGN-LVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-158 |
2.13e-40 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 144.10 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGVqISpSSVRMLNGHPVDAKeMQARCAYVQQFDLFIGSLTAREHLIFQATVRM 80
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTGV-IT-GGDRLVNGRPLDSS-FQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQ 865
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 81 PRTMTQKQKIQRVDQVIQDLSLGKCQNTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLI-CDEPTSGLDSFMAASVV 158
Cdd:TIGR00956 866 PKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPG--EGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSIC 942
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-158 |
5.85e-40 |
|
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: 133.06 E-value: 5.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRsARGVQISpSSVRmLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQAtvrm 80
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGR-RTGLGVS-GEVL-INGRPLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAA---- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 81 prtmtqkqkiqrvdqviqdlslgkcqntvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 158
Cdd:cd03213 108 ----------------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1-158 |
7.02e-38 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 136.16 E-value: 7.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRsargVQISPSSVRMLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATVRM 80
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGR----IQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLRL 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 81 PRTMTQKQKIQRVDQVIQDLSLGKCQNTVIGvPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 158
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELGLTKCENTIIG-NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1-150 |
1.22e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 115.55 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRmLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIFQA 76
Cdd:COG1131 26 GEIFGLLGPNGAGKTTTIRMLL-----GL-LRPTSgeVR-VLGEDVarDPAEVRRRIGYVPQEPALYPDLTVRENLRFFA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065403 77 TVR-MPRtmtqKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG1131 99 RLYgLPR----KEARERIDELLELFGLTDAADR------KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-158 |
3.19e-30 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 114.94 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARG-----VQISpssvrmlnGHPvDAKEMQARCA-YVQQFDLFIGSLTAREHLIF 74
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiegdIRIS--------GFP-KKQETFARISgYCEQNDIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 QATVRMPRTMTQKQKIQRVDQVIQDLSLGKCQNTVIGVPGrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 154
Cdd:PLN03140 977 SAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPG-VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
....
gi 1151065403 155 ASVV 158
Cdd:PLN03140 1056 AIVM 1059
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1-147 |
1.21e-28 |
|
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: 102.73 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSSVRM-LNGHPVDAKEMQA---RCAYVQQFDLFIGSLTAREHLIFQA 76
Cdd:pfam00005 11 GEILALVGPNGAGKSTLLKLIA-----G-LLSPTEGTIlLDGQDLTDDERKSlrkEIGYVFQDPQLFPRLTVRENLRLGL 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065403 77 TVRMPRTMTQKQkiqRVDQVIQDLSLGKCQNTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTS 147
Cdd:pfam00005 85 LLKGLSKREKDA---RAEEALEKLGLGDLADRPVGERP--GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-158 |
1.25e-28 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 104.25 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGVqISPSSvrMLNGHPVDaKEMQARCAYVQQFDLFIGSLTAREHLIFQATVRm 80
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAGV-ITGEI--LINGRPLD-KNFQRSTGYVEQQDVHSPNLTVREALRFSALLR- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 81 prtmtqkqkiqrvdqviqdlslgkcqntvigvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 158
Cdd:cd03232 108 -------------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-153 |
5.99e-27 |
|
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: 100.66 E-value: 5.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSSVR-MLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIFQAT 77
Cdd:cd03263 28 GEIFGLLGHNGAGKTTTLKMLT-----G-ELRPTSGTaYINGYSIrtDRKAARQSLGYCPQFDALFDELTVREHLRFYAR 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 78 VRMPRtmtQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 153
Cdd:cd03263 102 LKGLP---KSEIKEEVELLLRVLGLTDKANK------RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS 168
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-150 |
7.03e-24 |
|
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: 93.00 E-value: 7.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARG-VQIspssvrmlNGHPVDAKEMQAR--CAYVQQFDLFIGSLTAREHLIFQ 75
Cdd:COG4555 27 GEITGLLGPNGAGKTTLLRMLAglLKPDSGsILI--------DGEDVRKEPREARrqIGVLPDERGLYDRLTVRENIRYF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065403 76 ATVRmprTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG4555 99 AELY---GLFDEELKKRIEELIELLGLEEFLDR------RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-150 |
1.25e-23 |
|
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: 91.39 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRmLNGHPVDAK--EMQARCAYVQQFDLFIGSLTAREHLIFQA 76
Cdd:COG4133 28 GEALALTGPNGSGKTTLLRILA-----G-LLPPSAgeVL-WNGEPIRDAreDYRRRLAYLGHADGLKPELTVRENLRFWA 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 77 TVRMPRtmtqkQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG4133 101 ALYGLR-----ADREAIDEALEAVGLAGLADL------PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-151 |
1.05e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.02 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVR-MLNGHPV---DAKEMQA-RCAYV----QQFDLfIGSLTAREH 71
Cdd:COG1136 34 GEFVAIVGPSGSGKSTLLNILG-----GLD-RPTSGEvLIDGQDIsslSERELARlRRRHIgfvfQFFNL-LPELTALEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 lifqatVRMP---RTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTS 147
Cdd:COG1136 107 ------VALPlllAGVSRKERRERARELLERVGLGDRLDH------RPSQLSGGQQQRVAIA-RALvNRPKLILADEPTG 173
|
....
gi 1151065403 148 GLDS 151
Cdd:COG1136 174 NLDS 177
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1-150 |
2.32e-21 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 85.60 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDA---KEMQARCAYV-QQFDLFIGSLTAREHLIFQa 76
Cdd:cd03225 27 GEFVLIVGPNGSGKSTLLRLLN-----GLLGPTSGEVLVDGKDLTKlslKELRRKVGLVfQNPDDQFFGPTVEEEVAFG- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 77 tvrmPRTMTQKQK--IQRVDQVIQDLSLGKCQNTVIgvpgrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03225 101 ----LENLGLPEEeiEERVEEALELVGLEGLRDRSP------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1-158 |
4.38e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 85.23 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRM-LNGHPVDAKEMQARCAYV--------QQFDLfIGSLTAREH 71
Cdd:cd03255 30 GEFVAIVGPSGSGKSTLLNILG-----GLD-RPTSGEVrVDGTDISKLSEKELAAFRrrhigfvfQSFNL-LPDLTALEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 lifqatVRMPRTMTQKQKIQRVDQVIQDLslgkcqnTVIGVPGR----VKGLSGGERKRLAFAsEAL-TDPPLLICDEPT 146
Cdd:cd03255 103 ------VELPLLLAGVPKKERRERAEELL-------ERVGLGDRlnhyPSELSGGQQQRVAIA-RALaNDPKIILADEPT 168
|
170
....*....|..
gi 1151065403 147 SGLDSFMAASVV 158
Cdd:cd03255 169 GNLDSETGKEVM 180
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-150 |
5.65e-21 |
|
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: 84.55 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 3 LLAVMGSSGAGKTTLLNALAfrsarGVQiSPSS--VRMlNGHPV--DAKEMQARCAYV-QQFDlFIGSLTAREHLIFQAT 77
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILA-----TLT-PPSSgtIRI-DGQDVlkQPQKLRRRIGYLpQEFG-VYPNFTVREFLDYIAW 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 78 VRmprTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03264 99 LK---GIPSKEVKARVDEVLELVNLGDRAKK------KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1-150 |
5.86e-21 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 83.60 E-value: 5.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRmLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIfqa 76
Cdd:cd03230 26 GEIYGLLGPNGAGKTTLIKIIL-----GL-LKPDSgeIK-VLGKDIkkEPEEVKRRIGYLPEEPSLYENLTVRENLK--- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 77 tvrmprtmtqkqkiqrvdqviqdlslgkcqntvigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03230 96 ------------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-150 |
1.11e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 87.12 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSSVR-MLNGHPV---DAKEMQARCAYV-QQFDLFIGSLtaREHLifq 75
Cdd:COG4988 363 GERVALVGPSGAGKSTLLNLLL-----G-FLPPYSGSiLINGVDLsdlDPASWRRQIAWVpQNPYLFAGTI--RENL--- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 atvRMPRTMTQKQKIQRV------DQVIQDLSLGkcQNTVIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:COG4988 432 ---RLGRPDASDEELEAAleaaglDEFVAALPDG--LDTPLGEGGR--GLSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
.
gi 1151065403 150 D 150
Cdd:COG4988 505 D 505
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-151 |
1.63e-19 |
|
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: 80.77 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrSARGVQISPSSVRMLNGHPvdAKEMQARC----AYVQQFDLFIGSLTAREHLIFQA 76
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNGIP--YKEFAEKYpgeiIYVSEEDVHFPTLTVRETLDFAL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 77 tvrmprtmtqkqkiqrvdqviqdlslgKCQNTVIgvpgrVKGLSGGERKRLAFAsEALTDPPLLIC-DEPTSGLDS 151
Cdd:cd03233 109 ---------------------------RCKGNEF-----VRGISGGERKRVSIA-EALVSRASVLCwDNSTRGLDS 151
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-157 |
2.12e-19 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 83.66 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPV---DAKEMQARCAYV-QQFDLFIGSLtaREHLIF- 74
Cdd:COG4987 361 GERVAIVGPSGSGKSTLLALLLrFLDPQSGSI------TLGGVDLrdlDEDDLRRRIAVVpQRPHLFDTTL--RENLRLa 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 --QATvrmPRTMtqKQKIQRV--DQVIQDLSLGkcQNTVIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG4987 433 rpDAT---DEEL--WAALERVglGDWLAALPDG--LDTWLGEGGR--RLSGGERRRLALARALLRDAPILLLDEPTEGLD 503
|
....*..
gi 1151065403 151 SFMAASV 157
Cdd:COG4987 504 AATEQAL 510
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-151 |
3.20e-19 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 83.23 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSaRGVQISPSSVRMLNGHPVD--AKEMQARCAYVQQFDLFIGSLTAREHLIFQATV 78
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNT-DGFHIGVEGVITYDGITPEeiKKHYRGDVVYNAETDVHFPHLTVGETLDFAARC 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 79 RMPRT----MTQKQKIQRV-DQVIQDLSLGKCQNTVIGvPGRVKGLSGGERKRLAFAsEALTDPPLLIC-DEPTSGLDS 151
Cdd:TIGR00956 166 KTPQNrpdgVSREEYAKHIaDVYMATYGLSHTRNTKVG-NDFVRGVSGGERKRVSIA-EASLGGAKIQCwDNATRGLDS 242
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1-150 |
3.43e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 79.86 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FrsargvqISPSSVRM-LNGHPVDAKEMQA---RCAYV-QQFDLFIGslTAREHLIF 74
Cdd:COG4619 26 GECVAITGPSGSGKSTLLRALAdL-------DPPTSGEIyLDGKPLSAMPPPEwrrQVAYVpQEPALWGG--TVRDNLPF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 QATVRmprtmTQKQKIQRVDQVIQDLSLGkcqntvigvPG----RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG4619 97 PFQLR-----ERKFDRERALELLERLGLP---------PDildkPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-158 |
3.47e-19 |
|
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: 80.79 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRmLNGHPVDA------KEMQARCAYVQQFD-LFiGSLTAREH 71
Cdd:COG1127 31 GEILAIIGGSGSGKSVLLKLII-----G-LLRPDSgeIL-VDGQDITGlsekelYELRRRIGMLFQGGaLF-DSLTVFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LIFQatVRMPRTMTQKQKIQRVDQVIQDLSLGKCQNTVigvPGRvkgLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLD 150
Cdd:COG1127 103 VAFP--LREHTDLSEAEIRELVLEKLELVGLPGAADKM---PSE---LSGGMRKRVALA-RALaLDPEILLYDEPTAGLD 173
|
....*...
gi 1151065403 151 SFMAASVV 158
Cdd:COG1127 174 PITSAVID 181
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1-150 |
2.79e-18 |
|
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: 78.31 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLnalafRSARGvQISPSSVRML-NGHPVDA---KEMQA---RCAYV-QQFDLFiGSLTAREHL 72
Cdd:cd03261 26 GEILAIIGPSGSGKSTLL-----RLIVG-LLRPDSGEVLiDGEDISGlseAELYRlrrRMGMLfQSGALF-DSLTVFENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 IFqaTVRMPRTMTqkqkiqrvDQVIQDLSLGKCQntVIGVPGRVK----GLSGGERKRLAFASEALTDPPLLICDEPTSG 148
Cdd:cd03261 99 AF--PLREHTRLS--------EEEIREIVLEKLE--AVGLRGAEDlypaELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
..
gi 1151065403 149 LD 150
Cdd:cd03261 167 LD 168
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-158 |
3.00e-18 |
|
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: 80.41 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPV---DAKEMQARCAYV-QQFDLFIGSLTArehlifq 75
Cdd:TIGR02857 348 GERVALVGPSGAGKSTLLNLLLgFVDPTEGSIA------VNGVPLadaDADSWRDQIAWVpQHPFLFAGTIAE------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 aTVRMPRTMTQKQKIQRV------DQVIQDLSLGkcQNTVIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:TIGR02857 415 -NIRLARPDASDAEIREAleraglDEFVAALPQG--LDTPIGEGGA--GLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
....*....
gi 1151065403 150 DSFMAASVV 158
Cdd:TIGR02857 490 DAETEAEVL 498
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1-150 |
3.25e-18 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 77.30 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGvQISpssvrmLNGHPVDAKEMQARCAYVQQfDLfigsltarEHLIFQATV 78
Cdd:cd03226 26 GEIIALTGKNGAGKTTLAKILAglIKESSG-SIL------LNGKPIKAKERRKSIGYVMQ-DV--------DYQLFTDSV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065403 79 RMPRTMTQKQ---KIQRVDQVIQDLSLG--KCQNTVIgvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03226 90 REELLLGLKEldaGNEQAETVLKDLDLYalKERHPLS--------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-157 |
3.81e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.14 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGVQISPSsvRMLNGHPVDAKEMQAR-CAYVQQFDLFIGSLTAREHLIFQatvr 79
Cdd:COG4136 27 GEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGE--VLLNGRRLTALPAEQRrIGILFQDDLLFPHLSVGENLAFA---- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 80 MPRTMTQKQKIQRVDQVIQDLSLGkcqntviGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 157
Cdd:COG4136 101 LPPTIGRAQRRARVEQALEEAGLA-------GFADRdPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQF 172
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-151 |
7.52e-18 |
|
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: 79.11 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGvQIspssvrMLNGHP---VDAKEMQARCAYVQQfdlfigsltarEHLIFQ 75
Cdd:COG2274 501 GERVAIVGRSGSGKSTLLKLLLglYEPTSG-RI------LIDGIDlrqIDPASLRRQIGVVLQ-----------DVFLFS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATVR----MPRTMTQKQKIQR------VDQVIQDLSLGKcqNTVIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEP 145
Cdd:COG2274 563 GTIRenitLGDPDATDEEIIEaarlagLHDFIEALPMGY--DTVVGEGGS--NLSGGQRQRLAIARALLRNPRILILDEA 638
|
....*.
gi 1151065403 146 TSGLDS 151
Cdd:COG2274 639 TSALDA 644
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-150 |
8.29e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 77.05 E-value: 8.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRmLNGHPVDAKemQARCAYVQQFDLFIGS--LTAREhlifqa 76
Cdd:COG1121 32 GEFVAIVGPNGAGKSTLLKAIL-----G-LLPPTSgtVR-LFGKPPRRA--RRRIGYVPQRAEVDWDfpITVRD------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 77 TVRMPRT--------MTQKQKiQRVDQVIQDLSLGKCQNTVIGvpgrvkGLSGGERKRLAFAsEAL-TDPPLLICDEPTS 147
Cdd:COG1121 97 VVLMGRYgrrglfrrPSRADR-EAVDEALERVGLEDLADRPIG------ELSGGQQQRVLLA-RALaQDPDLLLLDEPFA 168
|
...
gi 1151065403 148 GLD 150
Cdd:COG1121 169 GVD 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1-151 |
9.00e-18 |
|
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: 76.89 E-value: 9.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRMlNGHPV---DAKEMQARCAYVQQfDLFIGSLTAREHLIFQAT 77
Cdd:cd03251 28 GETVALVGPSGSGKSTLVNLIP----RFYDVDSGRILI-DGHDVrdyTLASLRRQIGLVSQ-DVFLFNDTVAENIAYGRP 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 78 VRMPRTMTQKQKIQRVDQVIQDLSLGkcQNTVIGVPGrVKgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:cd03251 102 GATREEVEEAARAANAHEFIMELPEG--YDTVIGERG-VK-LSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-150 |
1.58e-17 |
|
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: 75.87 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVR-MLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIFQAT 77
Cdd:cd03265 26 GEIFGLLGPNGAGKTTTIKMLT------TLLKPTSGRaTVAGHDVvrEPREVRRRIGIVFQDLSVDDELTGWENLYIHAR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 78 VR-MPRtmtqKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03265 100 LYgVPG----AERRERIDELLDFVGLLEAADR------LVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-150 |
1.94e-17 |
|
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: 75.65 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRMLnghPVDAKEMQARCAYVQQFDLFIGS--LTAREhlifqa 76
Cdd:cd03235 25 GEFLAIVGPNGAGKSTLLKAIL-----G-LLKPTSgsIRVF---GKPLEKERKRIGYVPQRRSIDRDfpISVRD------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 77 TVRMPRT--------MTQKQKiQRVDQVIQDLSLGKCQNTVIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSG 148
Cdd:cd03235 90 VVLMGLYghkglfrrLSKADK-AKVDEALERVGLSELADRQIG------ELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
..
gi 1151065403 149 LD 150
Cdd:cd03235 163 VD 164
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-150 |
2.05e-17 |
|
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: 75.41 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEM-------QARCAYV-QQFDLFiGSLTAREHL 72
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIA-----GLEKPDGGTIVLNGTVLFDSRKkinlppqQRKIGLVfQQYALF-PHLNVRENL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 73 IFQAtvrmpRTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03297 97 AFGL-----KRKRNREDRISVDELLDLLGLDHLLNR------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-157 |
2.44e-17 |
|
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: 74.34 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRmLNGHPV---DAKEMQARCAYVQQfdlfigsltarEHLIFQAT 77
Cdd:cd03228 28 GEKVAIVGPSGSGKSTLLKLLL----RLYDPTSGEIL-IDGVDLrdlDLESLRKNIAYVPQ-----------DPFLFSGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 78 VRmprtmtqkqkiqrvdqviqdlslgkcQNtvIgvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 157
Cdd:cd03228 92 IR--------------------------EN--I--------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1-150 |
5.23e-17 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 74.68 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRML-NGHPVDAKEMQA---RCAYVQQFDlfigsltarEHLIFQA 76
Cdd:COG1122 27 GEFVAIIGPNGSGKSTLLRLLN-----GL-LKPTSGEVLvDGKDITKKNLRElrrKVGLVFQNP---------DDQLFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 77 TVR-------MPRTMTQKQKIQRVDQVIQDLSLGKCQNTVIGVpgrvkgLSGGERKRLAFASeAL-TDPPLLICDEPTSG 148
Cdd:COG1122 92 TVEedvafgpENLGLPREEIRERVEEALELVGLEHLADRPPHE------LSGGQKQRVAIAG-VLaMEPEVLVLDEPTAG 164
|
..
gi 1151065403 149 LD 150
Cdd:COG1122 165 LD 166
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-150 |
5.29e-17 |
|
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: 75.08 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRmLNGHPV---DAKEMQARCAYVQQFDLFIGSLTAREhlifq 75
Cdd:COG1120 27 GEVTALLGPNGSGKSTLLRALA-----G-LLKPSSgeVL-LDGRDLaslSRRELARRIAYVPQEPPAPFGLTVRE----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 aTVRMPRT-------MTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASeALT-DPPLLICDEPTS 147
Cdd:COG1120 95 -LVALGRYphlglfgRPSAEDREAVEEALERTGLEHLADR------PVDELSGGERQRVLIAR-ALAqEPPLLLLDEPTS 166
|
...
gi 1151065403 148 GLD 150
Cdd:COG1120 167 HLD 169
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-150 |
1.43e-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: 75.32 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRmLNGHPVDA------KEMQARCAYVQQ--FDLFIGSLTARE 70
Cdd:COG1123 291 GETLGLVGESGSGKSTLARLLL-----GL-LRPTSgsIL-FDGKDLTKlsrrslRELRRRVQMVFQdpYSSLNPRMTVGD 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 71 HLIFQATVRmpRTMTQKQKIQRVDQVIQDLSLgkcqntvigvPGRVKG-----LSGGERKRLAFASeAL-TDPPLLICDE 144
Cdd:COG1123 364 IIAEPLRLH--GLLSRAERRERVAELLERVGL----------PPDLADrypheLSGGQRQRVAIAR-ALaLEPKLLILDE 430
|
....*.
gi 1151065403 145 PTSGLD 150
Cdd:COG1123 431 PTSALD 436
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-158 |
3.53e-16 |
|
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: 71.12 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFrsargvQISPSSVRM-LNGHPVDAKEMQARcayvqqfdlfigsltarehlifqatvr 79
Cdd:cd00267 25 GEIVALVGPNGSGKSTLLRAIAG------LLKPTSGEIlIDGKDIAKLPLEEL--------------------------- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 80 mprtmtqKQKIQRVDQviqdlslgkcqntvigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 158
Cdd:cd00267 72 -------RRRIGYVPQ-----------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-157 |
3.84e-16 |
|
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: 71.45 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQ-----ARCAYV-QQFDLFiGSLTAREHLIF 74
Cdd:cd03229 26 GEIVALLGPSGSGKSTLLRCIA-----GLEEPDSGSILIDGEDLTDLEDElpplrRRIGMVfQDFALF-PHLTVLENIAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 qatvrmprtmtqkqkiqrvdqviqdlslgkcqntvigvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 154
Cdd:cd03229 100 -------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
...
gi 1151065403 155 ASV 157
Cdd:cd03229 137 REV 139
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-150 |
5.16e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 72.14 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGvqispsSVRmLNGHPV---DAKEMQARCAYVQQfDLFiGSLTAREHLifQ 75
Cdd:COG1124 31 GESFGLVGESGSGKSTLLRALAglERPWSG------EVT-FDGRPVtrrRRKAFRRRVQMVFQ-DPY-ASLHPRHTV--D 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATVRMP-RTMTQKQKIQRVDQVIQDLslgkcqntviGVPGRVKG-----LSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:COG1124 100 RILAEPlRIHGLPDREERIAELLEQV----------GLPPSFLDryphqLSGGQRQRVAIARALILEPELLLLDEPTSAL 169
|
.
gi 1151065403 150 D 150
Cdd:COG1124 170 D 170
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-151 |
1.06e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.89 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPV---DAKEMQARCAYVQQfDLFIGSLTAREHLIF-- 74
Cdd:COG1132 366 GETVALVGPSGSGKSTLVNLLLrFYDPTSGRIL------IDGVDIrdlTLESLRRQIGVVPQ-DTFLFSGTIRENIRYgr 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 -QATvrmprtmtqKQKIQR------VDQVIQDLSLGkcQNTVIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTS 147
Cdd:COG1132 439 pDAT---------DEEVEEaakaaqAHEFIEALPDG--YDTVVGERGV--NLSGGQRQRIAIARALLKDPPILILDEATS 505
|
....
gi 1151065403 148 GLDS 151
Cdd:COG1132 506 ALDT 509
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1-150 |
2.21e-15 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 69.94 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRMLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATV 78
Cdd:cd03268 26 GEIYGFLGPNGAGKTTTMKIIL-----GL-IKPDSgeITFDGKSYQKNIEALRRIGALIEAPGFYPNLTARENLRLLARL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 79 RMPRTmtqkqkiQRVDQVIQDLSLGkcqntviGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03268 100 LGIRK-------KRIDEVLDVVGLK-------DSAKKkVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-151 |
3.02e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.52 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGvqispsSVRmLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATV 78
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAglLPPAAG------TIK-LDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 79 RmprtmtqKQKIQRVDQVIQDLSLGKcqntVIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:PRK13539 101 L-------GGEELDIAAALEAVGLAP----LAHLPFGY--LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-156 |
4.88e-15 |
|
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: 69.42 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSSVRML-NGHPVdaKEMQARCAYVQQFDLFIGSLTAREHLIFQATVR 79
Cdd:cd03293 30 GEFVALVGPSGCGKSTLLRIIA-----G-LERPTSGEVLvDGEPV--TGPGPDRGYVFQQDALLPWLTVLDNVALGLELQ 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 80 -MPRtmtqKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 156
Cdd:cd03293 102 gVPK----AEARERAEELLELVGLSGFENA------YPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQ 169
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-149 |
1.11e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 68.91 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRmLNGHPVDAKEMQARCAY-----VQQFDLFiGSLTAREHL- 72
Cdd:COG0411 30 GEIVGLIGPNGAGKTTLFNLIT-----GF-YRPTSgrIL-FDGRDITGLPPHRIARLgiartFQNPRLF-PELTVLENVl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 ----------IFQATVRMPRTMTQKQKI-QRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASeAL-TDPPLL 140
Cdd:COG0411 102 vaaharlgrgLLAALLRLPRARREEREArERAEELLERVGLADRADE------PAGNLSYGQQRRLEIAR-ALaTEPKLL 174
|
....*....
gi 1151065403 141 ICDEPTSGL 149
Cdd:COG0411 175 LLDEPAAGL 183
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-158 |
2.07e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 69.31 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQISPSSVRMlngHPVDAKEMQARCAYVQQfDLFIGSLTAREHLIFQATVR 79
Cdd:TIGR02868 361 GERVAILGPSGSGKSTLLATLAgLLDPLQGEVTLDGVPV---SSLDQDEVRRRVSVCAQ-DAHLFDTTVRENLRLARPDA 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 80 MPRTMTQKQKIQRVDQVIQDLSLGkcQNTVIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 158
Cdd:TIGR02868 437 TDEELWAALERVGLADWLRALPDG--LDTVLGEGGAR--LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELL 511
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-150 |
3.18e-14 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 66.77 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGvQISpssvrmLNGHPVDAKEMQAR-CAYV-QQFDLFiGSLTAREHLIFQA 76
Cdd:cd03259 26 GEFLALLGPSGCGKTTLLRLIAglERPDSG-EIL------IDGRDVTGVPPERRnIGMVfQDYALF-PHLTVAENIAFGL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065403 77 TVR-MPRTMTQKQKIQRVDQVIQDLSLGKcqntvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03259 98 KLRgVPKAEIRARVRELLELVGLEGLLNR----------YPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1-157 |
7.59e-14 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 67.03 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVR-MLNGHPV--DAKEMQARCAYV-QQFDLFIGsLTAREHLIFQA 76
Cdd:TIGR01188 19 GEVFGFLGPNGAGKTTTIRMLT------TLLRPTSGTaRVAGYDVvrEPRKVRRSIGIVpQYASVDED-LTGRENLEMMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 77 TVR-MPRtmtqKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 155
Cdd:TIGR01188 92 RLYgLPK----DEAEERAEELLELFELGEAADR------PVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
..
gi 1151065403 156 SV 157
Cdd:TIGR01188 162 AI 163
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1-150 |
7.60e-14 |
|
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: 65.41 E-value: 7.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVrMLNGHPVDAKEMQARCAyvqqfdlfIGSLTAREHLiFQATVRm 80
Cdd:cd03247 28 GEKIALLGRSGSGKSTLLQLLT----GDLKPQQGEI-TLDGVPVSDLEKALSSL--------ISVLNQRPYL-FDTTLR- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 81 prtmtqkqkiqrvdqviqdlslgkcQNtvIGVPgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03247 93 -------------------------NN--LGRR-----FSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1-149 |
9.70e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 65.92 E-value: 9.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVR-MLNGHPVDAKEMQARCAY-----VQQFDLFiGSLTAREHLIF 74
Cdd:cd03219 26 GEIHGLIGPNGAGKTTLFNLIS-----GF-LRPTSGSvLFDGEDITGLPPHEIARLgigrtFQIPRLF-PELTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 QATVRMPRTM-------TQKQKIQRVDQVIQDLSLGKCQNTVIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTS 147
Cdd:cd03219 99 AAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAG------ELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
..
gi 1151065403 148 GL 149
Cdd:cd03219 173 GL 174
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-151 |
1.06e-13 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 65.71 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGvQISPSSVrmlNGHPVDAKEMQARCAYVQQfDLFIGSLTAREHLifqatv 78
Cdd:cd03254 29 GETVAIVGPTGAGKTTLINLLMrfYDPQKG-QILIDGI---DIRDISRKSLRSMIGVVLQ-DTFLFSGTIMENI------ 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065403 79 RMPRTMTQKQKIQRVDQVIQ--DL--SLGKCQNTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:cd03254 98 RLGRPNATDEEVIEAAKEAGahDFimKLPNGYDTVLGENG--GNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1-151 |
1.10e-13 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 65.71 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNaLAFRSargvqISPSSVRML-NGHP---VDAKEMQARCAYVQQ----FDLFI------GSL 66
Cdd:cd03253 27 GKKVAIVGPSGSGKSTILR-LLFRF-----YDVSSGSILiDGQDireVTLDSLRRAIGVVPQdtvlFNDTIgyniryGRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 67 TAREHLIFQATvrmprtmtqkqKIQRVDQVIQDLSLGkcQNTVIGVPGrVKgLSGGERKRLAFASEALTDPPLLICDEPT 146
Cdd:cd03253 101 DATDEEVIEAA-----------KAAQIHDKIMRFPDG--YDTIVGERG-LK-LSGGEKQRVAIARAILKNPPILLLDEAT 165
|
....*
gi 1151065403 147 SGLDS 151
Cdd:cd03253 166 SALDT 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1-150 |
1.42e-13 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 65.30 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHP---VDAKEMQARCAYVQQ-FDLFIGSLtaREHLIFQ 75
Cdd:cd03245 30 GEKVAIIGRVGSGKSTLLKLLAgLYKPTSGSV------LLDGTDirqLDPADLRRNIGYVPQdVTLFYGTL--RDNITLG 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065403 76 ATVRMPRTMTQKQKIQRVDQVIQDLSLGkcQNTVIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03245 102 APLADDERILRAAELAGVTDFVNKHPNG--LDLQIGERGR--GLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1-150 |
1.51e-13 |
|
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: 65.26 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLlnalaFRSARGVqISPSSVRM-LNGHPVDAKEMQARC----AYV-QQFDLFIGsLTAREHLIf 74
Cdd:cd03218 26 GEIVGLLGPNGAGKTTT-----FYMIVGL-VKPDSGKIlLDGQDITKLPMHKRArlgiGYLpQEASIFRK-LTVEENIL- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 75 qATVRMpRTMTQKQKIQRVDQVIQDLSLGKCQNTVIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03218 98 -AVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKAS------SLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1-149 |
1.72e-13 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 65.15 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarG-VQISPSSVRmLNGHPVDAKEMQARC----AYVQQFDLFIGSLTAREHLIFQ 75
Cdd:cd03224 26 GEIVALLGRNGAGKTTLLKTIM-----GlLPPRSGSIR-FDGRDITGLPPHERAragiGYVPEGRRIFPELTVEENLLLG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 76 ATVRMPRtmTQKQKIQRVDQVIQDLSLGKCQntvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:cd03224 100 AYARRRA--KRKARLERVYELFPRLKERRKQ--------LAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-150 |
2.17e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 66.47 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGVQISpSSVRmLNGHPVDAKEMQARCAYV----QQFDLFIGSLTAREHLIFqa 76
Cdd:COG1123 32 GETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVL-LDGRDLLELSEALRGRRIgmvfQDPMTQLNPVTVGDQIAE-- 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 77 tVRMPRTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG1123 108 -ALENLGLSRAEARARVLELLEAVGLERRLDR------YPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-150 |
2.27e-13 |
|
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: 64.61 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAkEMQARCAYVQQFDLFIGSLTAREHLIFQATVRm 80
Cdd:cd03269 26 GEIFGLLGPNGAGKTTTIRMIL-----GIILPDSGEVLFDGKPLDI-AARNRIGYLPEERGLYPKMKVIDQLVYLAQLK- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 81 prTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03269 99 --GLKKEEARRRIDEWLERLELSEYANK------RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-155 |
2.40e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 65.11 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRmLNGHPVDAKemQARCAYV-QQFDLFigsLTAREHLIFQAT 77
Cdd:COG1116 37 GEFVALVGPSGCGKSTLLRLIA-----G-LEKPTSgeVL-VDGKPVTGP--GPDRGVVfQEPALLp-wLTVLDNVALGLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 78 VR-MPRtmtqKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDSFMAA 155
Cdd:COG1116 107 LRgVPK----AERRERARELLELVGLAGFEDA------YPHQLSGGMRQRVAIA-RALaNDPEVLLMDEPFGALDALTRE 175
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-150 |
2.81e-13 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 64.83 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRmLNGHPV---DAKEMQARCAYVQqfdlfigsltarehLIFQ-A 76
Cdd:cd03257 31 GETLGLVGESGSGKSTLARAIL----GLLKPTSGSII-FDGKDLlklSRRLRKIRRKEIQ--------------MVFQdP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 77 TVRMPRTMT-QKQ-----KIQRVDQVIQDLSLGKCQNTV-IGVPGRVKG-----LSGGERKRLAFASEALTDPPLLICDE 144
Cdd:cd03257 92 MSSLNPRMTiGEQiaeplRIHGKLSKKEARKEAVLLLLVgVGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLIADE 171
|
....*.
gi 1151065403 145 PTSGLD 150
Cdd:cd03257 172 PTSALD 177
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1-158 |
4.19e-13 |
|
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: 64.09 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLL---NALafrsargVQISPSSVRM----LNGHPVDAKEMQARCAYV-QQFDLFiGSLTAREHL 72
Cdd:cd03262 26 GEVVVIIGPSGSGKSTLLrciNLL-------EEPDSGTIIIdglkLTDDKKNINELRQKVGMVfQQFNLF-PHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 IF-QATVR-MPRTMTQKQKIQRVDQViqdlslgkcqntviGVPGRVKG----LSGGERKRLAFASEALTDPPLLICDEPT 146
Cdd:cd03262 98 TLaPIKVKgMSKAEAEERALELLEKV--------------GLADKADAypaqLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170
....*....|..
gi 1151065403 147 SGLDSFMAASVV 158
Cdd:cd03262 164 SALDPELVGEVL 175
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-150 |
5.37e-13 |
|
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: 64.34 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALafrSARGVQISPSSVRMLnGHP---VDAKEMQARCAYV--QQFDLFIGSLTAREHLI-- 73
Cdd:COG1119 29 GEHWAILGPNGAGKSTLLSLI---TGDLPPTYGNDVRLF-GERrggEDVWELRKRIGLVspALQLRFPRDETVLDVVLsg 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 74 FQATVRMPRTMTQKQkIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLD 150
Cdd:COG1119 105 FFDSIGLYREPTDEQ-RERARELLELLGLAHLADR------PFGTLSQGEQRRVLIA-RALvKDPELLILDEPTAGLD 174
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-157 |
8.45e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.68 E-value: 8.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQARCA-------YVQQFDLFIGSLTAREHli 73
Cdd:PRK11629 35 GEMMAIVGSSGSGKSTLLHLLG-----GLDTPTSGDVIFNGQPMSKLSSAAKAElrnqklgFIYQFHHLLPDFTALEN-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 74 fqatVRMPRTMTQKQKIQRVDQVIQDLslgkcqnTVIGVPGRVKG----LSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:PRK11629 108 ----VAMPLLIGKKKPAEINSRALEML-------AAVGLEHRANHrpseLSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
....*...
gi 1151065403 150 DSFMAASV 157
Cdd:PRK11629 177 DARNADSI 184
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-150 |
8.95e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.06 E-value: 8.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVD--AKEMQARCAYVQQFDLFIGSLTAREHL-IF--- 74
Cdd:PRK13537 33 GECFGLLGPNGAGKTTTLRMLL-----GLTHPDAGSISLCGEPVPsrARHARQRVGVVPQFDNLDPDFTVRENLlVFgry 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 ------QATVRMPRTMTQKQKIQRVDqviqdlslgkcqntvigvpGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSG 148
Cdd:PRK13537 108 fglsaaAARALVPPLLEFAKLENKAD-------------------AKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
..
gi 1151065403 149 LD 150
Cdd:PRK13537 169 LD 170
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1-150 |
1.16e-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: 62.38 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNG--HPVDAKEMQARCAYVQQFDLFIGSLTAREHL-----I 73
Cdd:TIGR01189 26 GEALQVTGPNGIGKTTLLRILA-----GLLRPDSGEVRWNGtpLAEQRDEPHENILYLGHLPGLKPELSALENLhfwaaI 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065403 74 FQATVRMPRTMTQKQKIQRVDQVIqdlslgkcqntvigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:TIGR01189 101 HGGAQRTIEDALAAVGLTGFEDLP------------------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-150 |
1.38e-12 |
|
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: 62.89 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLlnalafrsARGVQ--ISPSSVRML-NGHP---VDAKEMQARCAYVQQFD-LFIGSLtaREHLI 73
Cdd:cd03252 28 GEVVGIVGRSGSGKSTL--------TKLIQrfYVPENGRVLvDGHDlalADPAWLRRQVGVVLQENvLFNRSI--RDNIA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065403 74 FQATVRMPRTMTQKQKIQRVDQVIQDLSLGkcQNTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03252 98 LADPGMSMERVIEAAKLAGAHDFISELPEG--YDTIVGEQG--AGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-151 |
1.59e-12 |
|
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: 62.84 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQIsPSS--VRmLNGHPVDAKEMQARCA-------YVQQ-FDLfIGSLTARE 70
Cdd:COG4181 38 GESVAIVGASGSGKSTLLGLLA-----GLDR-PTSgtVR-LAGQDLFALDEDARARlrarhvgFVFQsFQL-LPTLTALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 71 HlifqatVRMP---RTMTQKQKIQR--VDQViqdlslgkcqntviGVPGRV----KGLSGGERKRLAFASEALTDPPLLI 141
Cdd:COG4181 110 N------VMLPlelAGRRDARARARalLERV--------------GLGHRLdhypAQLSGGEQQRVALARAFATEPAILF 169
|
170
....*....|
gi 1151065403 142 CDEPTSGLDS 151
Cdd:COG4181 170 ADEPTGNLDA 179
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-157 |
1.70e-12 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 62.37 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRML-NGHPVDAKEMQARCA-------YVQQFDLFIGSLTAREHl 72
Cdd:TIGR02211 31 GEIVAIVGSSGSGKSTLLHLLG-----GLD-NPTSGEVLfNGQSLSKLSSNERAKlrnkklgFIYQFHHLLPDFTALEN- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 ifqatVRMP---RTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:TIGR02211 104 -----VAMPlliGKKSVKEAKERAYEMLEKVGLEHRINH------RPSELSGGERQRVAIARALVNQPSLVLADEPTGNL 172
|
....*...
gi 1151065403 150 DSFMAASV 157
Cdd:TIGR02211 173 DNNNAKII 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1-150 |
1.74e-12 |
|
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: 62.70 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLL---NALafrsargvqISPSSVRML-NGHPV---DAKEMQARCAYV-QQFDLFiGSLTAREHL 72
Cdd:cd03295 27 GEFLVLIGPSGSGKTTTMkmiNRL---------IEPTSGEIFiDGEDIreqDPVELRRKIGYViQQIGLF-PHMTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 ifqATVRMPRTMTQKQKIQRVDQVIQDLSLGkcqntvigvPGRVKG-----LSGGERKRLAFASEALTDPPLLICDEPTS 147
Cdd:cd03295 97 ---ALVPKLLKWPKEKIRERADELLALVGLD---------PAEFADrypheLSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
...
gi 1151065403 148 GLD 150
Cdd:cd03295 165 ALD 167
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-150 |
1.88e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 62.87 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGvqispsSVRmLNGHPVD---AKEMQARCAyV--QQFDL-FigSLTAREhl 72
Cdd:PRK13548 28 GEVVAILGPNGAGKSTLLRALSgeLSPDSG------EVR-LNGRPLAdwsPAELARRRA-VlpQHSSLsF--PFTVEE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 ifqaTVRM---PRTMTQKQKIQRVDQVIQdlslgkcQNTVIGVPGR-VKGLSGGERKRLAFA------SEALTDPPLLIC 142
Cdd:PRK13548 96 ----VVAMgraPHGLSRAEDDALVAAALA-------QVDLAHLAGRdYPQLSGGEQQRVQLArvlaqlWEPDGPPRWLLL 164
|
....*...
gi 1151065403 143 DEPTSGLD 150
Cdd:PRK13548 165 DEPTSALD 172
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1-150 |
2.11e-12 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 62.59 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVRMLNGHPVdaKEMQARCAYV-QQFDLfIGSLTAREHLIFQA 76
Cdd:cd03256 27 GEFVALIGPSGAGKSTLLrclNGLVEPTSGSVLIDGTDINKLKGKAL--RQLRRQIGMIfQQFNL-IERLSVLENVLSGR 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 77 TVRMP--RTMTQ---KQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03256 104 LGRRStwRSLFGlfpKEEKQRALAALERVGLLDKAYQ------RADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-150 |
2.65e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.31 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRmLNGHPVDA-KEMQAR---CAYVQQFDLFIGSLtaREHLIFQA 76
Cdd:PRK11160 366 GEKVALLGRTGCGKSTLLQLLT----RAWDPQQGEIL-LNGQPIADySEAALRqaiSVVSQRVHLFSATL--RDNLLLAA 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 77 TvrmprTMTQKQKIQRVDQVIQD--LSLGKCQNTVIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK11160 439 P-----NASDEALIEVLQQVGLEklLEDDKGLNAWLGEGGR--QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1-151 |
2.76e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 63.23 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNAL--AFRSARGvqispsSVRmLNGHPVDAKEMQARCAYV----QQFDLFIGSltarehlIF 74
Cdd:COG4618 358 GEVLGVIGPSGSGKSTLARLLvgVWPPTAG------SVR-LDGADLSQWDREELGRHIgylpQDVELFDGT-------IA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 QATVRMPRTMTQK----QKIQRVDQVIQDLSLGkcQNTVIGVPGRvkGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGL 149
Cdd:COG4618 424 ENIARFGDADPEKvvaaAKLAGVHEMILRLPDG--YDTRIGEGGA--RLSGGQRQRIGLA-RALyGDPRLVVLDEPNSNL 498
|
..
gi 1151065403 150 DS 151
Cdd:COG4618 499 DD 500
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1-150 |
3.05e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 61.74 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQAR--CAYVQQFDLFigsltarEHLIFQATV 78
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA-----GFETPQSGRVLINGVDVTAAPPADRpvSMLFQENNLF-------AHLTVEQNV 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 79 ---RMPRTMTQKQKIQRVDQVIQDLSLGkcqntviGVPGRVKG-LSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03298 92 glgLSPGLKLTAEDRQAIEVALARVGLA-------GLEKRLPGeLSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-150 |
3.23e-12 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 62.82 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 2 ELLAVMGSSGAGKTTLLNALA-----------------FRSARGVQISPSsvrmlnghpvdakemQARCAYV-QQFDLFi 63
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAgltrpdegeivlngrtlFDSRKGIFLPPE---------------KRRIGYVfQEARLF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 64 GSLTAREHLIFQATVRMPrtmtqKQKIQRVDQVIQDLSLGkcqNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICD 143
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARP-----SERRISFERVIELLGIG---HLLGRLPGR---LSGGEKQRVAIGRALLSSPRLLLMD 156
|
....*..
gi 1151065403 144 EPTSGLD 150
Cdd:TIGR02142 157 EPLAALD 163
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1-150 |
3.65e-12 |
|
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: 60.91 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS-VRMLNGHPV---DAKEMQARCAYVQQFdlfigsltarehlifqa 76
Cdd:cd03214 25 GEIVGILGPNGAGKSTLLKTLA-----GL-LKPSSgEILLDGKDLaslSPKELARKIAYVPQA----------------- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065403 77 tvrmprtmtqkqkIQRVDqvIQDLSlGKCQNTvigvpgrvkgLSGGERKRLAFASeALT-DPPLLICDEPTSGLD 150
Cdd:cd03214 82 -------------LELLG--LAHLA-DRPFNE----------LSGGERQRVLLAR-ALAqEPPILLLDEPTSHLD 129
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-150 |
3.93e-12 |
|
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: 63.11 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTllnalAFRSARGVQISPSSVRMLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIFQATV 78
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTT-----TFKMLTGDTTVTSGDATVAGKSIltNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 79 R-MPrtmtqKQKIQRV-DQVIQDLSLGKCQNTVIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:TIGR01257 2040 RgVP-----AEEIEKVaNWSIQSLGLSLYADRLAGT------YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-150 |
3.95e-12 |
|
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: 61.61 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS-VRMLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIFQAT 77
Cdd:cd03266 31 GEVTGLLGPNGAGKTTTLRMLA-----GL-LEPDAgFATVDGFDVvkEPAEARRRLGFVSDSTGLYDRLTARENLEYFAG 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 78 VRmprTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03266 105 LY---GLKGDELTARLEELADRLGMEELLDR------RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-150 |
4.02e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.54 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNA-LAFRSARGVQISPSSVRMlnghPVDAKEMQARCAYVQQFDLFIGSLTAREHLI-FQATV 78
Cdd:PRK13536 67 GECFGLLGPNGAGKSTIARMiLGMTSPDAGKITVLGVPV----PARARLARARIGVVPQFDNLDLEFTVRENLLvFGRYF 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 79 RMprtmtqkqKIQRVDQVIQDL-SLGKCQNTVigvPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13536 143 GM--------STREIEAVIPSLlEFARLESKA---DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-152 |
5.05e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 61.80 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FrsargvqISPSSVR-MLNGHPVDAKEmqARCAYVQQFDLFIGSLTAREHLIFQATV 78
Cdd:COG4525 33 GEFVVALGASGCGKTTLLNLIAgF-------LAPSSGEiTLDGVPVTGPG--ADRGVVFQKDALLPWLNVLDNVAFGLRL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 79 R-MPRtmtqKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFAsEALT-DPPLLICDEPTSGLDSF 152
Cdd:COG4525 104 RgVPK----AERRARAEELLALVGLADFARR------RIWQLSGGMRQRVGIA-RALAaDPRFLLMDEPFGALDAL 168
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1-151 |
5.06e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 61.33 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQaRCAYVQQFDLFiGSLTAREHlIFQATVRM 80
Cdd:TIGR01184 11 GEFISLIGHSGCGKSTLLNLIS-----GLAQPTSGGVILEGKQITEPGPD-RMVVFQNYSLL-PWLTVREN-IALAVDRV 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065403 81 PRTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:TIGR01184 83 LPDLSKSERRAIVEEHIALVGLTEAADK------RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1-150 |
6.45e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTT-------LLNAlafrsargvqiSPSSVRMLnGHPVDAKEMQAR--CAYVQQ-FDLFiGSLTARE 70
Cdd:NF033858 292 GEIFGFLGSNGCGKSTtmkmltgLLPA-----------SEGEAWLF-GQPVDAGDIATRrrVGYMSQaFSLY-GELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 71 HLIFQATV-RMPRTMTQkqkiQRVDQVIQDLSLGKCQNTVigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:NF033858 359 NLELHARLfHLPAAEIA----ARVAEMLERFDLADVADAL---PDS---LPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
.
gi 1151065403 150 D 150
Cdd:NF033858 429 D 429
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-157 |
8.87e-12 |
|
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: 60.20 E-value: 8.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAK--EMQARCAYVQQFDLFIGSLTAREHLIFQATV 78
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILA-----GLSPPLAGRVLLNGGPLDFQrdSIARGLLYLGHAPGIKTTLSVLENLRFWHAD 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 79 RMPRTmtqkqkiqrVDQVIQDLSLGKCQNTVIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAASV 157
Cdd:cd03231 101 HSDEQ---------VEEALARVGLNGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLWILDEPTTALD---KAGV 161
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-150 |
9.38e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.62 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRMlnGHPVdakemqaRCAYV-QQFDLFIGSLTAREHLifqat 77
Cdd:COG0488 341 GDRIGLIGPNGAGKSTLLKLLA-----G-ELEPDSgtVKL--GETV-------KIGYFdQHQEELDPDKTVLDEL----- 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 78 vrmpRTMTQKQKIQRVDQVIQDLSL-GKCQNTVIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG0488 401 ----RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGV------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-150 |
1.07e-11 |
|
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: 60.29 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVRMLNGHPVdaKEMQARCAYV-QQFDLFiGSLTAREHlifqa 76
Cdd:cd03258 31 GEIFGIIGRSGAGKSTLIrciNGLERPTSGSVLVDGTDLTLLSGKEL--RKARRRIGMIfQHFNLL-SSRTVFEN----- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 77 tVRMPRTMTQKQKIQRVDQVIQDLSLgkcqntvIGVPGRVKG----LSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03258 103 -VALPLEIAGVPKAEIEERVLELLEL-------VGLEDKADAypaqLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-150 |
1.29e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.18 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQARCA-------YVQQFDLFIGSLTAREHli 73
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILA-----GLDDGSSGEVSLVGQPLHQMDEEARAKlrakhvgFVFQSFMLIPTLNALEN-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 74 fqatVRMP---RTMTQKQKIQRVDQVIQDLSLGKcqnTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK10584 109 ----VELPallRGESSRQSRNGAKALLEQLGLGK---RLDHLPAQ---LSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-150 |
1.68e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 60.04 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVR-MLNGhpVDAKEM---QARCAYV-QQFDLFiGSLTAREHLIFq 75
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIA-----GF-IKPDSGKiLLNG--KDITNLppeKRDISYVpQNYALF-PHMTVYKNIAY- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065403 76 aTVRMpRTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03299 95 -GLKK-RKVDKKEIERKVLEIAEMLGIDHLLNR------KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-151 |
1.91e-11 |
|
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: 59.66 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQAR-CAYV-QQFDLFiGSLTAREHLIFQATV 78
Cdd:cd03296 28 GELVALLGPSGSGKTTLLRLIA-----GLERPDSGTILFGGEDATDVPVQERnVGFVfQHYALF-RHMTVFDNVAFGLRV 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 79 RMPRTMTQKQKI-QRVDQVIQDLSLGKCQNTVigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:cd03296 102 KPRSERPPEAEIrAKVHELLKLVQLDWLADRY---PAQ---LSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-158 |
1.92e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 59.34 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRsargvqISPSS-VRMLNGHPVdAKEMQARCAYV--------QQFDLfIGSLTAREH 71
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLIYKE------ELPTSgTIRVNGQDV-SDLRGRAIPYLrrkigvvfQDFRL-LPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LIFQATV-RMPRTMTQKqkiqRVDQVIQDLSLGKCQNTVigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03292 99 VAFALEVtGVPPREIRK----RVPAALELVGLSHKHRAL------PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
....*...
gi 1151065403 151 SFMAASVV 158
Cdd:cd03292 169 PDTTWEIM 176
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-150 |
2.13e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.50 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FrsargvqISPSSVR-MLNGHPVDAKEMQAR-CAYV-QQFDLFiGSLTAREHLIFQA 76
Cdd:COG3842 31 GEFVALLGPSGCGKTTLLRMIAgF-------ETPDSGRiLLDGRDVTGLPPEKRnVGMVfQDYALF-PHLTVAENVAFGL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 77 TVR-MPRtmtqKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLD 150
Cdd:COG3842 103 RMRgVPK----AEIRARVAELLELVGLEGLADR------YPHQLSGGQQQRVALA-RALaPEPRVLLLDEPLSALD 167
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-150 |
2.18e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfRSARGVQISPSSVRMLnGHPV--------DAKEMQARCAYV-QQFDLfIGSLTAREH 71
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLS-GLITGDKSAGSHIELL-GRTVqregrlarDIRKSRANTGYIfQQFNL-VNRLSVLEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LIFQATVRMP------RTMTQKQKiQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEP 145
Cdd:PRK09984 107 VLIGALGSTPfwrtcfSWFTREQK-QRALQALTRVGMVHFAHQ------RVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
....*
gi 1151065403 146 TSGLD 150
Cdd:PRK09984 180 IASLD 184
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
5-150 |
2.26e-11 |
|
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: 60.50 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 5 AVMGSSGAGKTTLLNALA--FRSARGvQISpssvrmLNGHP-VDAKEMQA------RCAYV-QQFDLFigsltarEHLif 74
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAglERPDSG-RIR------LGGEVlQDSARGIFlpphrrRIGYVfQEARLF-------PHL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 qaTVR------MPRTMTQKQKIqRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSG 148
Cdd:COG4148 93 --SVRgnllygRKRAPRAERRI-SFDEVVELLGIGHLLDR------RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
..
gi 1151065403 149 LD 150
Cdd:COG4148 164 LD 165
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-158 |
2.69e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNAL-AFRSARGVQISPSSVRMLNGHPVDAKEMQARCAYV----QQFDLFiGSLTAREHLIfQ 75
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLnLLEMPRSGTLNIAGNHFDFSKTPSDKAIRELRRNVgmvfQQYNLW-PHLTVQQNLI-E 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATVRMpRTMTQKQKIQRVDQVIQDLSLGkcqNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 155
Cdd:PRK11124 106 APCRV-LGLSKDQALARAEKLLERLRLK---PYADRFPLH---LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
...
gi 1151065403 156 SVV 158
Cdd:PRK11124 179 QIV 181
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1-151 |
3.16e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.36 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNAL--AFrsargvqiSPSSVRMLnghpVDAkeMQARcayvqqfDLFIGSLtaREHL--IFQA 76
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLqrVF--------DPQSGRIL----IDG--TDIR-------TVTRASL--RRNIavVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 77 TVRMPRTMTQKQKIQRVDQVIQDLSLG--------------KCQNTVIGVPGRVkgLSGGERKRLAFASEALTDPPLLIC 142
Cdd:PRK13657 418 AGLFNRSIEDNIRVGRPDATDEEMRAAaeraqahdfierkpDGYDTVVGERGRQ--LSGGERQRLAIARALLKDPPILIL 495
|
....*....
gi 1151065403 143 DEPTSGLDS 151
Cdd:PRK13657 496 DEATSALDV 504
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-150 |
3.25e-11 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 59.12 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGVQISPSSVRMLNGHPV-----DAKEMQARCAYV-QQFDLFIGSLtarehlif 74
Cdd:cd03260 26 GEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIydldvDVLELRRRVGMVfQKPNPFPGSI-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 QATVRMPRTMTQKQKIQRVDQVIQDlSLGKcqntvIGVPGRVK------GLSGGERKRLAFASEALTDPPLLICDEPTSG 148
Cdd:cd03260 98 YDNVAYGLRLHGIKLKEELDERVEE-ALRK-----AALWDEVKdrlhalGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
..
gi 1151065403 149 LD 150
Cdd:cd03260 172 LD 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-150 |
6.60e-11 |
|
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: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLlnalaFRSARGVqISPSS--VRmLNGHPVDAKEMQArcayvqqfdlfIG----------SLTA 68
Cdd:COG4152 27 GEIFGLLGPNGAGKTTT-----IRIILGI-LAPDSgeVL-WDGEPLDPEDRRR-----------IGylpeerglypKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 69 REHLIFQATVR-MPRtmtqKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTS 147
Cdd:COG4152 89 GEQLVYLARLKgLSK----AEAKRRADEWLERLGLGDRANK------KVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
...
gi 1151065403 148 GLD 150
Cdd:COG4152 159 GLD 161
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-150 |
6.66e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 59.31 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRMLNGhpvdakemqARCAYVQQFDLFIGSLTAREHlIFQATV 78
Cdd:COG0488 24 GDRIGLVGRNGAGKSTLLKILA-----G-ELEPDSgeVSIPKG---------LRIGYLPQEPPLDDDLTVLDT-VLDGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 79 RMPRTMTQKQKI-QRVDQVIQDLS-LGKCQN---------------TVI---GVPG-----RVKGLSGGERKRLAFASEA 133
Cdd:COG0488 88 ELRALEAELEELeAKLAEPDEDLErLAELQEefealggweaearaeEILsglGFPEedldrPVSELSGGWRRRVALARAL 167
|
170
....*....|....*..
gi 1151065403 134 LTDPPLLICDEPTSGLD 150
Cdd:COG0488 168 LSEPDLLLLDEPTNHLD 184
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-150 |
1.14e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGvQISpssvrmLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATV 78
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAglLHVESG-QIQ------IDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGL 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 79 --RMPRTMTQKQKiqrvdqviqdlslgkcqnTVIGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13543 110 hgRRAKQMPGSAL------------------AIVGLAGYedtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-151 |
1.36e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.09 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargvqispSSVRMLNGHpvdaKEMQARCAYVQQFDlFIGSLTAREHLIFQATVRM 80
Cdd:cd03250 31 GELVAIVGPVGSGKSSLLSALL-----------GELEKLSGS----VSVPGSIAYVSQEP-WIQNGTIRENILFGKPFDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 81 prtmtqkqkiQRVDQVI------QDLS-LGKCQNTVIGvpgrVKG--LSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:cd03250 95 ----------ERYEKVIkacalePDLEiLPDGDLTEIG----EKGinLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-150 |
1.48e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 58.16 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRML-NGHPVDAKEMQAR-CAYV-QQFDLFiGSLTAREHLIFQAT 77
Cdd:COG3839 29 GEFLVLLGPSGCGKSTLLRMIA-----GL-EDPTSGEILiGGRDVTDLPPKDRnIAMVfQSYALY-PHMTVYENIAFPLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 78 VR-MPrtmtqKQKI-QRVDQV-----IQDLsLGKcqntvigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGL 149
Cdd:COG3839 102 LRkVP-----KAEIdRRVREAaellgLEDL-LDR----------KPKQLSGGQRQRVALG-RALvREPKVFLLDEPLSNL 164
|
.
gi 1151065403 150 D 150
Cdd:COG3839 165 D 165
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1-150 |
1.93e-10 |
|
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: 56.96 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRMLNGHPVDAKEmqarcAYVQQFDLFIGS-------LTAREH 71
Cdd:cd03267 47 GEIVGFIGPNGAGKTTTLKILS-----GL-LQPTSgeVRVAGLVPWKRRK-----KFLRRIGVVFGQktqlwwdLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LIFQATV-RMPRTMTQKqkiqRVDQVIQDLSLGKcqntVIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03267 116 FYLLAAIyDLPPARFKK----RLDELSELLDLEE----LLDTP--VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-150 |
2.29e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.69 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPVDAKEMQARCAYV--QQFDLFiGSLTAREHLIFQAT 77
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAgFLPPDSGRIL------WNGQDLTALPPAERPVSMlfQENNLF-PHLTVAQNIGLGLR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 78 VRMPRTMTQKqkiQRVDQVIQDLSLGKCQNTvigVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG3840 98 PGLKLTAEQR---AQVEQALERVGLAGLLDR---LPGQ---LSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-150 |
2.51e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPVDAkemqARCAYVQQFdLFIG-------SLTAREHL 72
Cdd:PRK13538 27 GELVQIEGPNGAGKTSLLRILAgLARPDAGEVL------WQGEPIRR----QRDEYHQDL-LYLGhqpgiktELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 IFQATVRMPrtmtqkqkiQRVDQVIQdlSLGKcqntvIGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDEPTSG 148
Cdd:PRK13538 96 RFYQRLHGP---------GDDEALWE--ALAQ-----VGLAGFedvpVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
..
gi 1151065403 149 LD 150
Cdd:PRK13538 160 ID 161
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-150 |
2.79e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 56.64 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVrmlNGHPVDAKEMQARCAYV-QQFDLFiGSLTAREHLIFQa 76
Cdd:PRK09493 27 GEVVVIIGPSGSGKSTLLrciNKLEEITSGDLIVDGLKV---NDPKVDERLIRQEAGMVfQQFYLF-PHLTALENVMFG- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 77 tvrmPRTmTQKQKIQRVDQVIQDLsLGKcqntvIGVPGRV----KGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK09493 102 ----PLR-VRGASKEEAEKQAREL-LAK-----VGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-151 |
2.89e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 57.34 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVrMLNGHPVDAKEMQA---RCAYV-QQFDLFIGSLT--------- 67
Cdd:PRK11176 369 GKTVALVGRSGSGKSTIANLLT----RFYDIDEGEI-LLDGHDLRDYTLASlrnQVALVsQNVHLFNDTIAnniayarte 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 68 --AREHLIFQAtvRMPRTMtqkQKIQRVDQVIqdlslgkcqNTVIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEP 145
Cdd:PRK11176 444 qySREQIEEAA--RMAYAM---DFINKMDNGL---------DTVIGENGVL--LSGGQRQRIAIARALLRDSPILILDEA 507
|
....*.
gi 1151065403 146 TSGLDS 151
Cdd:PRK11176 508 TSALDT 513
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-154 |
2.99e-10 |
|
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: 56.39 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRMlnghpvdakEMQARCAYVqqFDL---FIGSLTAREHLIFQAT 77
Cdd:cd03220 48 GERIGLIGRNGAGKSTLLRLLA-----GI-YPPDSGTV---------TVRGRVSSL--LGLgggFNPELTGRENIYLNGR 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 78 VrmpRTMTQKQKIQRVDQvIQDLS-LGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD-SFMA 154
Cdd:cd03220 111 L---LGLSRKEIDEKIDE-IIEFSeLGDFIDL------PVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaAFQE 179
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-150 |
3.40e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 56.33 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPV---DAKEMQARCAYV-QQFDLFIGSLtaREHLIF- 74
Cdd:cd03248 40 GEVTALVGPSGSGKSTVVALLEnFYQPQGGQV------LLDGKPIsqyEHKYLHSKVSLVgQEPVLFARSL--QDNIAYg 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 75 QATVRMPRTMTQKQKiQRVDQVIQDLSLGkcQNTVIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03248 112 LQSCSFECVKEAAQK-AHAHSFISELASG--YDTEVGEKGSQ--LSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-150 |
3.63e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.12 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGVQISPSSVRMLnghpvdakemqarcaYV-QQFDLFIGSLtaREHLIFQAT 77
Cdd:COG4178 389 GERLLITGPSGSGKSTLLRAIAglWPYGSGRIARPAGARVL---------------FLpQRPYLPLGTL--REALLYPAT 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 78 vrmPRTMTQkqkiQRVDQVIQDLSLGKcqntvigVPGRV-------KGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG4178 452 ---AEAFSD----AELREALEAVGLGH-------LAERLdeeadwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-150 |
3.88e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.19 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLlnalaFRSARGVqISPSSVR-MLNGHPVDAKEMQARC----AYVQQ----FdlfiGSLTAREH 71
Cdd:COG1137 29 GEIVGLLGPNGAGKTTT-----FYMIVGL-VKPDSGRiFLDGEDITHLPMHKRArlgiGYLPQeasiF----RKLTVEDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LifQATVRMpRTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgrvKG--LSGGERKRLAFAsEAL-TDPPLLICDEPTSG 148
Cdd:COG1137 99 I--LAVLEL-RKLSKKEREERLEELLEEFGITHLRKS--------KAysLSGGERRRVEIA-RALaTNPKFILLDEPFAG 166
|
..
gi 1151065403 149 LD 150
Cdd:COG1137 167 VD 168
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1-150 |
4.66e-10 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 55.51 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVD-----AKEMQARCAYVQQfdlfigsltAREHLIFQ 75
Cdd:TIGR01166 18 GEVLALLGANGAGKSTLLLHLN-----GLLRPQSGAVLIDGEPLDysrkgLLERRQRVGLVFQ---------DPDDQLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATVRM-----PRTM--TQKQKIQRVDQVIQDLSLGKCQNTVIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSG 148
Cdd:TIGR01166 84 ADVDQdvafgPLNLglSEAEVERRVREALTAVGASGLRERPTHC------LSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
..
gi 1151065403 149 LD 150
Cdd:TIGR01166 158 LD 159
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-158 |
6.53e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 55.79 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVRMLNghPVDAKEMQARCAYV----QQFDLFiGSLTAREHLI 73
Cdd:COG4161 28 GETLVLLGPSGAGKSSLLrvlNLLETPDSGQLNIAGHQFDFSQ--KPSEKAIRLLRQKVgmvfQQYNLW-PHLTVMENLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 74 fQATVRMPRtMTQKQKIQRVDQVIQDLSLgkcQNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 153
Cdd:COG4161 105 -EAPCKVLG-LSKEQAREKAMKLLARLRL---TDKADRFPLH---LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
....*
gi 1151065403 154 AASVV 158
Cdd:COG4161 177 TAQVV 181
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1-150 |
6.62e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 55.23 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSarGVQISPSSVRmLNGHPVDAKEMQARcayvqqfdlfigsltARE--HLIFQATV 78
Cdd:cd03217 26 GEVHALMGPNGSGKSTLAKTIMGHP--KYEVTEGEIL-FKGEDITDLPPEER---------------ARLgiFLAFQYPP 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065403 79 RMPRTmtqkqkiqRVDQVIQDLSlgkcqntvigvpgrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03217 88 EIPGV--------KNADFLRYVN---------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1-151 |
9.39e-10 |
|
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: 55.24 E-value: 9.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPV---DAKEMQARCAYVQQF-DLFIGSLtaREHLIFQ 75
Cdd:cd03249 29 GKTVALVGSSGCGKSTVVSLLErFYDPTSGEI------LLDGVDIrdlNLRWLRSQIGLVSQEpVLFDGTI--AENIRYG 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 76 ATvrmPRTMTQKQKIQRV---DQVIQDLSLGkcQNTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:cd03249 101 KP---DATDEEVEEAAKKaniHDFIMSLPDG--YDTLVGERG--SQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1-150 |
1.13e-09 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 54.97 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTllnalAFRSARGVqISPSSVRM-LNGHPVDAKEMQARC----AYVQQFDLFIGSLTAREHLIfq 75
Cdd:TIGR04406 27 GEIVGLLGPNGAGKTT-----SFYMIVGL-VRPDAGKIlIDGQDITHLPMHERArlgiGYLPQEASIFRKLTVEENIM-- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065403 76 ATVRMPRTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:TIGR04406 99 AVLEIRKDLDRAEREERLEALLEEFQISHLRDN------KAMSLSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-151 |
1.24e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 55.62 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNA-LAFRSARGvqispsSVRmLNGHP---VDAKEMQARCAYV-QQFDLFIGSLtaREHlifq 75
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNAlLGFLPYQG------SLK-INGIElreLDPESWRKHLSWVgQNPQLPHGTL--RDN---- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 atVRMPRTMTQKQKIQR------VDQVIQDLSLGkcQNTVIGvpGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:PRK11174 443 --VLLGNPDASDEQLQQalenawVSEFLPLLPQG--LDTPIG--DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
..
gi 1151065403 150 DS 151
Cdd:PRK11174 517 DA 518
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-149 |
1.28e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 54.60 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarG-VQISPSSVRmLNGHPVDAKEMQARC----AYVQQ----FdlfiGSLTAREH 71
Cdd:COG0410 29 GEIVALLGRNGAGKTTLLKAIS-----GlLPPRSGSIR-FDGEDITGLPPHRIArlgiGYVPEgrriF----PSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LIFQATVRMPRTmTQKQKIQRVDQVIQDL-----SLGkcqntvigvpGRvkgLSGGERKRLAFASeAL-TDPPLLICDEP 145
Cdd:COG0410 99 LLLGAYARRDRA-EVRADLERVYELFPRLkerrrQRA----------GT---LSGGEQQMLAIGR-ALmSRPKLLLLDEP 163
|
....
gi 1151065403 146 TSGL 149
Cdd:COG0410 164 SLGL 167
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-150 |
1.47e-09 |
|
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: 54.18 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRML-NGHPVDAKEMQAR-CAYV-QQFDLFiGSLTAREHLIFQAT 77
Cdd:cd03301 26 GEFVVLLGPSGCGKTTTLRMIA-----GL-EEPTSGRIYiGGRDVTDLPPKDRdIAMVfQNYALY-PHMTVYDNIAFGLK 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 78 VRMprtmTQKQKI-QRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03301 99 LRK----VPKDEIdERVREVAELLQIEHLLDR------KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-150 |
1.98e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.42 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 4 LAVMGSSGAGKTTLlnalaFRSARGVqISPSSVRML-NGHPVDAKEMQARCAYV----QQFDLFIGSLTAREHLIFQATV 78
Cdd:PRK13652 33 IAVIGPNGAGKSTL-----FRHFNGI-LKPTSGSVLiRGEPITKENIREVRKFVglvfQNPDDQIFSPTVEQDIAFGPIN 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065403 79 RMPRTMTQKQkiqRVDQVIQDLSLGKCQNTVigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13652 107 LGLDEETVAH---RVSSALHMLGLEELRDRV---PHH---LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-144 |
2.72e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.93 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRMlNGhpvdakemqaRCAYVqqFDL---FIGSLTAREHLIFQ 75
Cdd:COG1134 52 GESVGIIGRNGAGKSTLLKLIA-----GI-LEPTSgrVEV-NG----------RVSAL--LELgagFHPELTGRENIYLN 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATVrmpRTMTQKQKIQRVDQVIqDLS-LGKcqntVIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDE 144
Cdd:COG1134 113 GRL---LGLSRKEIDEKFDEIV-EFAeLGD----FIDQP--VKTYSSGMRARLAFAVATAVDPDILLVDE 172
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-150 |
3.39e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.76 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 5 AVMGSSGAGKTTLLNALAfrsaRGVQISPSS-VR---MLNGHPV---DAKEMQARCAYVQQFDLFIGSLTAREHLIFqaT 77
Cdd:PRK14247 33 ALMGPSGSGKSTLLRVFN----RLIELYPEArVSgevYLDGQDIfkmDVIELRRRVQMVFQIPNPIPNLSIFENVAL--G 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 78 VRMPRTMTQKQKIQ-RVDQVIQDLSLGKCQNTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK14247 107 LKLNRLVKSKKELQeRVRWALEKAQLWDEVKDRLDAPA--GKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-151 |
3.58e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.93 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHpvDAKEMQARCAYV----QQFDLFiGSLTAREHLIFQA 76
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIA-----GLEHQTSGHIRFHGT--DVSRLHARDRKVgfvfQHYALF-RHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 77 TV----RMPRTMTQKQKIQRVDQVIQdlsLGKCQNTVigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:PRK10851 100 TVlprrERPNAAAIKAKVTQLLEMVQ---LAHLADRY---PAQ---LSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1-151 |
3.63e-09 |
|
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: 52.60 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRmLNGHPV---DAKEMQARCAYVQQFD-LFIGSLTarehlif 74
Cdd:cd03246 28 GESLAIIGPSGSGKSTLARLIL-----GL-LRPTSgrVR-LDGADIsqwDPNELGDHVGYLPQDDeLFSGSIA------- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065403 75 qatvrmprtmtqkqkiqrvdqviqdlslgkcQNTvigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:cd03246 94 -------------------------------ENI----------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-158 |
3.96e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 53.13 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLN--ALAFRSARGvQIspssvrMLNGHPV---DAKEMQA---RCAYV-QQFDLfIGSLTAREH 71
Cdd:COG2884 28 GEFVFLTGPSGAGKSTLLKllYGEERPTSG-QV------LVNGQDLsrlKRREIPYlrrRIGVVfQDFRL-LPDRTVYEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LIF--QATvRMPRTMTQKqkiqRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:COG2884 100 VALplRVT-GKSRKEIRR----RVREVLDLVGLSDKAKA------LPHELSGGEQQRVAIARALVNRPELLLADEPTGNL 168
|
....*....
gi 1151065403 150 DSFMAASVV 158
Cdd:COG2884 169 DPETSWEIM 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-157 |
4.40e-09 |
|
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: 54.25 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 2 ELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAK--EMQARCAYVQQFDLFIGSLTAREHLIFQATVR 79
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILT-----GLLPPTSGTVLVGGKDIETNldAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 80 mprTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 157
Cdd:TIGR01257 1032 ---GRSWEEAQLEMEAMLEDTGLHHKRNE------EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-152 |
6.00e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.16 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKemQARCAYVQQFDLFIGSLTAREHLIFQATVR- 79
Cdd:PRK11248 27 GELLVVLGPSGCGKTTLLNLIA-----GFVPYQHGSITLDGKPVEGP--GAERGVVFQNEGLLPWRNVQDNVAFGLQLAg 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 80 MPRTmtqkQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 152
Cdd:PRK11248 100 VEKM----QRLEIAHQMLKKVGLEGAEKR------YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
6-151 |
6.01e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 6.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 6 VMGSSGAGKTTLLNALAFRSARGVQISPSSVrmLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATVR------ 79
Cdd:PLN03140 196 LLGPPSSGKTTLLLALAGKLDPSLKVSGEIT--YNGYRLNEFVPRKTSAYISQNDVHVGVMTVKETLDFSARCQgvgtry 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 80 ------------------------MPRTMTQKQKIQRV-DQVIQDLSLGKCQNTVIGvPGRVKGLSGGERKRLAfASEAL 134
Cdd:PLN03140 274 dllselarrekdagifpeaevdlfMKATAMEGVKSSLItDYTLKILGLDICKDTIVG-DEMIRGISGGQKKRVT-TGEMI 351
|
170
....*....|....*...
gi 1151065403 135 TDP-PLLICDEPTSGLDS 151
Cdd:PLN03140 352 VGPtKTLFMDEISTGLDS 369
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-150 |
6.05e-09 |
|
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: 53.53 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALafrsargVQISPSSVRM-LNGHPVDA---KEMQARCAYVQ---QfDLFiGSLTAR---- 69
Cdd:COG4172 312 GETLGLVGESGSGKSTLGLAL-------LRLIPSEGEIrFDGQDLDGlsrRALRPLRRRMQvvfQ-DPF-GSLSPRmtvg 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 70 ----EHLIFQAtvrmpRTMTQKQKIQRVDQVIQDlslgkcqntvIGVPGRVKG-----LSGGERKRLAFAsEAL-TDPPL 139
Cdd:COG4172 383 qiiaEGLRVHG-----PGLSAAERRARVAEALEE----------VGLDPAARHrypheFSGGQRQRIAIA-RALiLEPKL 446
|
170
....*....|.
gi 1151065403 140 LICDEPTSGLD 150
Cdd:COG4172 447 LVLDEPTSALD 457
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-150 |
6.63e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 53.13 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfRSARGVQISPSSVRmLNGHPV---DAKEMQA----RCAYVQQfDLFiGSL----TAR 69
Cdd:COG0444 31 GETLGLVGESGSGKSTLARAIL-GLLPPPGITSGEIL-FDGEDLlklSEKELRKirgrEIQMIFQ-DPM-TSLnpvmTVG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 70 EHLIfqATVRMPRTMTQKQKIQRVDQVIQDLSlgkcqntvIGVPGRVKG-----LSGGERKRLAFASeAL-TDPPLLICD 143
Cdd:COG0444 107 DQIA--EPLRIHGGLSKAEARERAIELLERVG--------LPDPERRLDrypheLSGGMRQRVMIAR-ALaLEPKLLIAD 175
|
....*..
gi 1151065403 144 EPTSGLD 150
Cdd:COG0444 176 EPTTALD 182
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-150 |
7.00e-09 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 53.03 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVrMLNGHPV---DAKEMQA----RCAYV-QQFDLFiGSLTAREHL 72
Cdd:cd03294 50 GEIFVIMGLSGSGKSTLLRCIN----RLIEPTSGKV-LIDGQDIaamSRKELRElrrkKISMVfQSFALL-PHRTVLENV 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 73 IFQATVR-MPRtmtqKQKIQRVDQVIQDLSLGKCQNTVIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03294 124 AFGLEVQgVPR----AEREERAAEALELVGLEGWEHKYPD------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1-152 |
7.07e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.94 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFrsargvQISPSSVRMlnghpvdakEMQARCAYVQQFDlFIGSLTAREHLIFQATVRM 80
Cdd:cd03291 63 GEMLAITGSTGSGKTSLLMLILG------ELEPSEGKI---------KHSGRISFSSQFS-WIMPGTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 81 PRTMTqkqkIQRVDQVIQDLS-LGKCQNTVIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 152
Cdd:cd03291 127 YRYKS----VVKACQLEEDITkFPEKDNTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-150 |
7.81e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.59 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTT---LLNALAFRSARGVQISPSSVRMLnghPVDAKEMQArCAYVQQFDLFIGSLTAREHLIfqAT 77
Cdd:PRK10895 29 GEIVGLLGPNGAGKTTtfyMVVGIVPRDAGNIIIDDEDISLL---PLHARARRG-IGYLPQEASIFRRLSVYDNLM--AV 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 78 VRMPRTMTQKQKIQRVDQVIQDLSLGKCQNTVigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK10895 103 LQIRDDLSAEQREDRANELMEEFHIEHLRDSM------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-158 |
8.07e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.66 E-value: 8.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAF---RSARGVQISPSSVRMlnghpVDAKEMQARCAYVQQFDLFIGSLTarehLIFQAt 77
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFlekPSEGSIVVNGQTINL-----VRDKDGQLKVADKNQLRLLRTRLT----MVFQH- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 78 VRMPRTMTQKQKIqrVDQVIQDLSLGKCQN--------TVIGVPGRVKG-----LSGGERKRLAFASEALTDPPLLICDE 144
Cdd:PRK10619 101 FNLWSHMTVLENV--MEAPIQVLGLSKQEAreravkylAKVGIDERAQGkypvhLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170
....*....|....
gi 1151065403 145 PTSGLDSFMAASVV 158
Cdd:PRK10619 179 PTSALDPELVGEVL 192
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-150 |
1.10e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.54 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALafrsaRGVqISPSSVRML-NGHPVDAKE---MQARCAYVQQFDlfigsltAREHLIFQA 76
Cdd:PRK13636 32 GEVTAILGGNGAGKSTLFQNL-----NGI-LKPSSGRILfDGKPIDYSRkglMKLRESVGMVFQ-------DPDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 77 TVR-------MPRTMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:PRK13636 99 SVYqdvsfgaVNLKLPEDEVRKRVDNALKRTGIEHLKDK------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
.
gi 1151065403 150 D 150
Cdd:PRK13636 173 D 173
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-150 |
1.11e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 52.28 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNG--HPVDAKEMQARCAYVQQFDLFiGSLTAREHLIFQATV 78
Cdd:PRK10771 25 GERVAILGPSGAGKSTLLNLIA-----GFLTPASGSLTLNGqdHTTTPPSRRPVSMLFQENNLF-SHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065403 79 RMPRTMTQKQKIQrvdQVIQDLSLGKCQNTvigVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK10771 99 GLKLNAAQREKLH---AIARQMGIEDLLAR---LPGQ---LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-150 |
1.26e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.06 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFR------SARGVQISPSSVRMLNGHPVDAKEMQARCAYV-QQFDLFiGSLTAREHLI 73
Cdd:PRK11264 29 GEVVAIIGPSGSGKTTLLRCINLLeqpeagTIRVGDITIDTARSLSQQKGLIRQLRQHVGFVfQNFNLF-PHRTVLENII 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 74 FQATV--RMPRtmtqKQKIQRVDQVIQDLSLGKCQNTVigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK11264 108 EGPVIvkGEPK----EEATARARELLAKVGLAGKETSY---PRR---LSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-150 |
1.40e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.40 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTL---LNALAFRSARGVQ-----------------------ISPSSVRMLNghpvDAKEMQARCA 54
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFiehLNALLLPDTGTIEwifkdeknkkktkekekvleklvIQKTRFKKIK----KIKEIRRRVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 55 YVQQFdlfigsltaREHLIFQATVRM-----PRTM--TQKQKIQRVDQVIQdlslgkcqntVIGVPGRVK-----GLSGG 122
Cdd:PRK13651 109 VVFQF---------AEYQLFEQTIEKdiifgPVSMgvSKEEAKKRAAKYIE----------LVGLDESYLqrspfELSGG 169
|
170 180
....*....|....*....|....*...
gi 1151065403 123 ERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-150 |
1.44e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 52.54 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLnalafRSARGVqISPS--SVRmLNGHPV---DAKEMQARCAYVQQFDLFIGSLTARehlifq 75
Cdd:PRK09536 29 GSLVGLVGPNGAGKTTLL-----RAINGT-LTPTagTVL-VAGDDVealSARAASRRVASVPQDTSLSFEFDVR------ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065403 76 ATVRMPRT--MTQKQKIQRVDQVIQDLSLGKCQNTVIgVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK09536 96 QVVEMGRTphRSRFDTWTETDRAAVERAMERTGVAQF-ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1-150 |
1.52e-08 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 51.85 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRMLnghpVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATVRM 80
Cdd:cd03300 26 GEFFTLLGPSGCGKTTLLRLIA-----GFE-TPTSGEIL----LDGKDITNLPPHKRPVNTVFQNYALFPHLTVFENIAF 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 81 PRTM--TQKQKI-QRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03300 96 GLRLkkLPKAEIkERVAEALDLVQLEGYANR------KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-150 |
2.14e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 51.62 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLL---NALAfrsargvqiSPSS--VRmLNGHPV---DAKEMQA---RCAYV-QQFDLFiGSLTA 68
Cdd:COG1135 31 GEIFGIIGYSGAGKSTLIrciNLLE---------RPTSgsVL-VDGVDLtalSERELRAarrKIGMIfQHFNLL-SSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 69 REHLIF---QAtvRMPRtmtqKQKIQRVDQVIqDLslgkcqntvIGVPGRVKG----LSGGERKRLAFAsEAL-TDPPLL 140
Cdd:COG1135 100 AENVALpleIA--GVPK----AEIRKRVAELL-EL---------VGLSDKADAypsqLSGGQKQRVGIA-RALaNNPKVL 162
|
170
....*....|
gi 1151065403 141 ICDEPTSGLD 150
Cdd:COG1135 163 LCDEATSALD 172
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-150 |
3.44e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.37 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHpvdakEMQARCAYVQQFDLFIGSLTAREHLIFQATVR 79
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAgFEQPTAGQI------MLDGV-----DLSHVPPYQRPINMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065403 80 MPRTMTQKQKIQRVDQVIQDLSLGKCQNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ---LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
5-150 |
3.59e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.03 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 5 AVMGSSGAGKTTLLNALAfrsarGVqISPSSVRM-LNGHP-VDAKEM------QARCAYVQQfdlfigsltarEHLIF-Q 75
Cdd:PRK11144 28 AIFGRSGAGKTSLINAIS-----GL-TRPQKGRIvLNGRVlFDAEKGiclppeKRRIGYVFQ-----------DARLFpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATVR------MPRTMTQKqkiqrVDQVIQDLSLGKCQNTVigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:PRK11144 91 YKVRgnlrygMAKSMVAQ-----FDKIVALLGIEPLLDRY---PGS---LSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
.
gi 1151065403 150 D 150
Cdd:PRK11144 160 D 160
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-150 |
3.78e-08 |
|
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: 50.12 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPVDAKEMQARcayvqqFDLFIGSLTA--REHLIFQat 77
Cdd:cd03215 26 GEIVGIAGLVGNGQTELAEALFgLRPPASGEIT------LDGKPVTRRSPRDA------IRAGIAYVPEdrKREGLVL-- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 78 vrmprtmtqkqkiqrvdqviqDLSLGkcQNTVIGVpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03215 92 ---------------------DLSVA--ENIALSS-----LLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-157 |
4.27e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.48 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargvqispSSVRMLNGHpvdaKEMQARCAYVQQfDLFIGSLTAREHLIFQATVRM 80
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALL-----------AEMDKVEGH----VHMKGSVAYVPQ-QAWIQNDSLRENILFGKALNE 727
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 81 PRTmtqkQKIQRVDQVIQDLS-LGKCQNTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 157
Cdd:TIGR00957 728 KYY----QQVLEACALLPDLEiLPSGDRTEIGEKG--VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-150 |
5.91e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 50.72 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPVDAKEMQARcaYV----QQFDLFiGSLTAREHLIFq 75
Cdd:PRK09452 40 GEFLTLLGPSGCGKTTVLRLIAgFETPDSGRI------MLDGQDITHVPAENR--HVntvfQSYALF-PHMTVFENVAF- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065403 76 aTVRMPRTmtQKQKIQRvdQVIQDLSLGKCQNTVigvPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK09452 110 -GLRMQKT--PAAEITP--RVMEALRMVQLEEFA---QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-150 |
1.02e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.54 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSArgvqisPS----SVRMLNGHPVDAKEM---------QARCAYVQQfdlfigslT 67
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLA------PDagevHYRMRDGQLRDLYALseaerrrllRTEWGFVHQ--------H 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 68 AREHLifqatvRM---------PRTMTQKqkiQRVDQVIQDLSLGKCQNTVIGvPGRVKGL----SGGERKRLAFASEAL 134
Cdd:PRK11701 98 PRDGL------RMqvsaggnigERLMAVG---ARHYGDIRATAGDWLERVEID-AARIDDLpttfSGGMQQRLQIARNLV 167
|
170
....*....|....*.
gi 1151065403 135 TDPPLLICDEPTSGLD 150
Cdd:PRK11701 168 THPRLVFMDEPTGGLD 183
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-157 |
1.03e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 49.70 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVR-MLNGHPVDAKEMQARCAYV----QqfDLFIG---SLTAREHL 72
Cdd:COG1101 32 GDFVTVIGSNGAGKSTLLNAIA-----GS-LPPDSGSiLIDGKDVTKLPEYKRAKYIgrvfQ--DPMMGtapSMTIEENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 IFQATVRMPRTMTQKQKIQRVDQVIQDLS-LGkcqntvIGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDEPTS 147
Cdd:COG1101 104 ALAYRRGKRRGLRRGLTKKRRELFRELLAtLG------LGLENRldtkVGLLSGGQRQALSLLMATLTKPKLLLLDEHTA 177
|
170
....*....|
gi 1151065403 148 GLDSFMAASV 157
Cdd:COG1101 178 ALDPKTAALV 187
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-150 |
1.07e-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: 50.29 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLnalafrsargvqispssvRMLNGH--PVDAK-EMQARCAYVQQFDlFIGSLTAREHLIFQAT 77
Cdd:TIGR01271 452 GQLLAVAGSTGSGKSSLL------------------MMIMGElePSEGKiKHSGRISFSPQTS-WIMPGTIKDNIIFGLS 512
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 78 VRMPRTMTqkqkIQRVDQVIQDLS-LGKCQNTVIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:TIGR01271 513 YDEYRYTS----VIKACQLEEDIAlFPEKDKTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-150 |
1.09e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargvqispssvrmlNGHPVDAKEMQ----ARCAYVQQfDlfigslTAREhliFQA 76
Cdd:PRK15064 345 GERLAIIGENGVGKTTLLRTLV-----------------GELEPDSGTVKwsenANIGYYAQ-D------HAYD---FEN 397
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 77 TVRMPRTMTQKQKIQRVDQVIQDLsLGKCQNTVIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK15064 398 DLTLFDWMSQWRQEGDDEQAVRGT-LGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
119-150 |
1.72e-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: 47.44 E-value: 1.72e-07
10 20 30
....*....|....*....|....*....|..
gi 1151065403 119 LSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-151 |
1.96e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.95 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRM-LNGHPVDAKEMQAR--CAYVQQFDLFigsltarEHLIFQAT 77
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVA-----GLE-KPTEGQIfIDGEDVTHRSIQQRdiCMVFQSYALF-------PHMSLGEN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065403 78 VRMPRTMTQKQKIQRVDQVIQDLSLGKcqntVIGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEALELVD----LAGFEDRyVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-157 |
2.05e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNA----LAFRSARGVQIspssvrmlnghpvdakemQARCAYVQQFDlFIGSLTAREHLIFQA 76
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAmlgeLPPRSDASVVI------------------RGTVAYVPQVS-WIFNATVRDNILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 77 TVRMPRTmtqkQKIQRVDQVIQDLSL--GKCQnTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 154
Cdd:PLN03130 704 PFDPERY----ERAIDVTALQHDLDLlpGGDL-TEIGERG--VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
...
gi 1151065403 155 ASV 157
Cdd:PLN03130 777 RQV 779
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-157 |
2.06e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 2 ELLAVMGSSGAGKTTLLNALAFRSARGVQISPSSVRMLNGHPV-----DAKEMQARCAYV-QQFDLFIGSltarehlIFQ 75
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIysprtDTVDLRKEIGMVfQQPNPFPMS-------IYE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATVRMPRTMTQKQKiQRVDQVIQDlSLgKCQNTVIGVPGRVK----GLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:PRK14239 105 NVVYGLRLKGIKDK-QVLDEAVEK-SL-KGASIWDEVKDRLHdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP 181
|
....*.
gi 1151065403 152 FMAASV 157
Cdd:PRK14239 182 ISAGKI 187
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-150 |
2.06e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.86 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTL---LNALAFRSARGVQISPssvRMLNGH--PVDAKEMQARCAYVQQFDlfigsltarEHLIFQ 75
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLlqhLNGLLQPTSGTVTIGE---RVITAGkkNKKLKPLRKKVGIVFQFP---------EHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATVR-------MPRTMTQKQKIQRVDQVIQdlslgkcqntVIGVPGRVKG-----LSGGERKRLAFASEALTDPPLLICD 143
Cdd:PRK13634 101 ETVEkdicfgpMNFGVSEEDAKQKAREMIE----------LVGLPEELLArspfeLSGGQMRRVAIAGVLAMEPEVLVLD 170
|
....*..
gi 1151065403 144 EPTSGLD 150
Cdd:PRK13634 171 EPTAGLD 177
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-150 |
2.38e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.54 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRMLNGHPVdaKEmqaRCAYVQQFDLFIGS-------LTAREH 71
Cdd:COG4586 48 GEIVGFIGPNGAGKSTTIKMLT-----GI-LVPTSgeVRVLGYVPF--KR---RKEFARRIGVVFGQrsqlwwdLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 L-IFQATVRMPRtmtqKQKIQRVDQVIQDLSLGKcqntVIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG4586 117 FrLLKAIYRIPD----AEYKKRLDELVELLDLGE----LLDTP--VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-151 |
2.63e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.95 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPV---DAKEMQARCAYVQQFD-LFIGSLtaREHLIFQ 75
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQnLYQPTGGQV------LLDGVPLvqyDHHYLHRQVALVGQEPvLFSGSV--RENIAYG 578
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 76 ATVRMPRTMTQKQKIQRVDQVIQDLSLGkcQNTVIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:TIGR00958 579 LTDTPDEEIMAAAKAANAHDFIMEFPNG--YDTEVGEKGSQ--LSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-150 |
4.78e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.09 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNAL--AFRSARGvqispsSVRmLNGHPVDAKE----MQARCAYV----QQFDLFIGsLTARE 70
Cdd:COG1129 278 GEILGIAGLVGAGRTELARALfgADPADSG------EIR-LDGKPVRIRSprdaIRAGIAYVpedrKGEGLVLD-LSIRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 71 HLIFQATVRMPRT--MTQKQKIQRVDQVIQDLSLgKCQNtvIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSG 148
Cdd:COG1129 350 NITLASLDRLSRGglLDRRRERALAEEYIKRLRI-KTPS--PEQP--VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
..
gi 1151065403 149 LD 150
Cdd:COG1129 425 ID 426
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
119-151 |
5.70e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 47.89 E-value: 5.70e-07
10 20 30
....*....|....*....|....*....|...
gi 1151065403 119 LSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1-150 |
6.07e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 47.37 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSarGVQISPSSVRmLNGHPVDAKEMQARcayvqqfdlfigsltARE--HLIFQATV 78
Cdd:COG0396 26 GEVHAIMGPNGSGKSTLAKVLMGHP--KYEVTSGSIL-LDGEDILELSPDER---------------ARAgiFLAFQYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 79 RMP--------RTMTQKQKIQRVDQViqdLSLGKCQNTVigvpGRVK------------GLSGGERKRLAFASEALTDPP 138
Cdd:COG0396 88 EIPgvsvsnflRTALNARRGEELSAR---EFLKLLKEKM----KELGldedfldryvneGFSGGEKKRNEILQMLLLEPK 160
|
170
....*....|..
gi 1151065403 139 LLICDEPTSGLD 150
Cdd:COG0396 161 LAILDETDSGLD 172
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-150 |
7.24e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 7.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGVQISPSSVR---MLNGHP---VDAKEMQARCAYVQQFDLFIGSLTAREHLIF 74
Cdd:PRK13547 27 GRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTgdvTLNGEPlaaIDAPRLARLRAVLPQAAQPAFAFSAREIVLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 QatvRMPRTMTQKQKIQRvDQVIQDLSLGKCQNTVIGvpGR-VKGLSGGERKRLAFA---------SEALTDPPLLICDE 144
Cdd:PRK13547 107 G---RYPHARRAGALTHR-DGEIAWQALALAGATALV--GRdVTTLSGGELARVQFArvlaqlwppHDAAQPPRYLLLDE 180
|
....*.
gi 1151065403 145 PTSGLD 150
Cdd:PRK13547 181 PTAALD 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-150 |
8.82e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNAL--AFRSARGvqispsSVRmLNGHPVDAKEMQ----ARCAYVQQfD-----LFIG----- 64
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLygALPRTSG------YVT-LDGHEVVTRSPQdglaNGIVYISE-DrkrdgLVLGmsvke 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 65 --SLTAREHLIfqatvRMPRTMTQKQKIQRVDQVIQDLSlgkcqntvIGVPGR---VKGLSGGERKRLAFASEALTDPPL 139
Cdd:PRK10762 350 nmSLTALRYFS-----RAGGSLKHADEQQAVSDFIRLFN--------IKTPSMeqaIGLLSGGNQQKVAIARGLMTRPKV 416
|
170
....*....|.
gi 1151065403 140 LICDEPTSGLD 150
Cdd:PRK10762 417 LILDEPTRGVD 427
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-150 |
9.79e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.91 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPVDAKEMQ--ARCAYVQQFD---LFiGSLTAREHL-- 72
Cdd:PRK11300 31 QEIVSLIGPNGAGKTTVFNCLTgFYKPTGGTI------LLRGQHIEGLPGHqiARMGVVRTFQhvrLF-REMTVIENLlv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 ---------IFQATVRMPR-TMTQKQKIQRVDQVIQDLSLGKCQNTVIGvpgrvkGLSGGERKRLAFASEALTDPPLLIC 142
Cdd:PRK11300 104 aqhqqlktgLFSGLLKTPAfRRAESEALDRAATWLERVGLLEHANRQAG------NLAYGQQRRLEIARCMVTQPEILML 177
|
....*...
gi 1151065403 143 DEPTSGLD 150
Cdd:PRK11300 178 DEPAAGLN 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-157 |
1.18e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.61 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLlnalaFRSARGVQISPSSVRMLNGHPV--DAK---EMQARCAYV-QQFDLFIGSLTAREHLIF 74
Cdd:PRK13639 28 GEMVALLGPNGAGKSTL-----FLHFNGILKPTSGEVLIKGEPIkyDKKsllEVRKTVGIVfQNPDDQLFAPTVEEDVAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 qATVRMPRTMTQKQKiqRVDQVIQDLSLGKCQNTVigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 154
Cdd:PRK13639 103 -GPLNLGLSKEEVEK--RVKEALKAVGMEGFENKP---PHH---LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
...
gi 1151065403 155 ASV 157
Cdd:PRK13639 174 SQI 176
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-150 |
1.21e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVRMLNGHPVDAkemqarcAYVQQFdlfigsltaREHLIFQATVrm 80
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLML------GQLQADSGRIHCGTKLEV-------AYFDQH---------RAELDPEKTV-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 81 prtmtqkqkiqrvdqvIQDLSLGKCQNTVIGV--------------PGR----VKGLSGGERKRLAFASEALTDPPLLIC 142
Cdd:PRK11147 401 ----------------MDNLAEGKQEVMVNGRprhvlgylqdflfhPKRamtpVKALSGGERNRLLLARLFLKPSNLLIL 464
|
....*...
gi 1151065403 143 DEPTSGLD 150
Cdd:PRK11147 465 DEPTNDLD 472
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-158 |
1.32e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 46.62 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRMLNGHPVDAKEMQARcayvqqfdlfigslTARE--HLIFQ--- 75
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAII----GLVKATDGEVAWLGKDLLGMKDDEWR--------------AVRSdiQMIFQdpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATV--RMP---------RTMTQKQKIQRVDQVIQD--LSLGKCQNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLIC 142
Cdd:PRK15079 109 ASLnpRMTigeiiaeplRTYHPKLSRQEVKDRVKAmmLKVGLLPNLINRYPHE---FSGGQCQRIGIARALILEPKLIIC 185
|
170
....*....|....*.
gi 1151065403 143 DEPTSGLDSFMAASVV 158
Cdd:PRK15079 186 DEPVSALDVSIQAQVV 201
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-150 |
1.39e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 46.16 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsaRgvQISPSSVR-MLNGHPV---DAKEMQARCAYVQQFDLFIGSLTAREhLIfqA 76
Cdd:PRK11231 28 GKITALIGPNGCGKSTLLKCFA----R--LLTPQSGTvFLGDKPIsmlSSRQLARRLALLPQHHLTPEGITVRE-LV--A 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 77 TVRMPRT-----MTQKQKiQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK11231 99 YGRSPWLslwgrLSAEDN-ARVNQAMEQTRINHLADR------RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-150 |
1.47e-06 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 46.27 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALaFRSARgvqisPSSVRML---NGHPVDAKEMQAR---------CAYVQQFdlfigsLTA 68
Cdd:COG4778 37 GECVALTGPSGAGKSTLLKCI-YGNYL-----PDSGSILvrhDGGWVDLAQASPReilalrrrtIGYVSQF------LRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 69 rehlifqatvrMPRTMTqkqkiqrVDQVIQDL-----SLGKCQNTV------IGVPGRVKGL-----SGGERKRLAFASE 132
Cdd:COG4778 105 -----------IPRVSA-------LDVVAEPLlergvDREEARARArellarLNLPERLWDLppatfSGGEQQRVNIARG 166
|
170
....*....|....*...
gi 1151065403 133 ALTDPPLLICDEPTSGLD 150
Cdd:COG4778 167 FIADPPLLLLDEPTASLD 184
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-157 |
1.74e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.99 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 3 LLAVMGSSGAGKTTLLNALAfrsaRGVQISPSS-----VRMLN----GHPVDAKEMQARCAYVQQFDLFIGSLTAREHLI 73
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFN----RLLELNEEArvegeVRLFGrniySPDVDPIEVRREVGMVFQYPNPFPHLTIYDNVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 74 FqaTVRMPRTMTQKQKI-QRVDQVIQDLSL-GKCQNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:PRK14267 108 I--GVKLNGLVKSKKELdERVEWALKKAALwDEVKDRLNDYPSN---LSGGQRQRLVIARALAMKPKILLMDEPTANIDP 182
|
....*.
gi 1151065403 152 FMAASV 157
Cdd:PRK14267 183 VGTAKI 188
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-150 |
1.91e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.19 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTL---LNALafrsargvqISPSSVR-MLNG-----HPVDAKEMQARCAYVQQFDlfigsltarEH 71
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLiqhLNGL---------LKPTSGKiIIDGvditdKKVKLSDIRKKVGLVFQYP---------EY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LIFQATVRM-----PRTM--TQKQKIQRVDQVIQdlslgkcqntVIGVPGRVKG------LSGGERKRLAFASEALTDPP 138
Cdd:PRK13637 95 QLFEETIEKdiafgPINLglSEEEIENRVKRAMN----------IVGLDYEDYKdkspfeLSGGQKRRVAIAGVVAMEPK 164
|
170
....*....|..
gi 1151065403 139 LLICDEPTSGLD 150
Cdd:PRK13637 165 ILILDEPTAGLD 176
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-149 |
1.96e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.03 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVD----AKEMQARCAYVQQFDLFIGSLTAREHLIFQA 76
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLC-----GDPRATSGRIVFDGKDITdwqtAKIMREAVAIVPEGRRVFSRMTVEENLAMGG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 77 TVrMPRTMTQkQKIQRVDQVIQDLSLGKCQntvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:PRK11614 106 FF-AERDQFQ-ERIKWVYELFPRLHERRIQ--------RAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
119-150 |
2.02e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 2.02e-06
10 20 30
....*....|....*....|....*....|..
gi 1151065403 119 LSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALD 188
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-150 |
2.40e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 45.48 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVRML-NGHPVDA---KEMQARCAYVQQFDLFIGSlTAREHLIFQA 76
Cdd:PRK10247 33 GEFKLITGPSGCGKSTLLKIVA------SLISPTSGTLLfEGEDISTlkpEIYRQQVSYCAQTPTLFGD-TVYDNLIFPW 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 77 TVRmprtmtqKQKIQRvDQVIQDLSLGKCQNTVIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK10247 106 QIR-------NQQPDP-AIFLDDLERFALPDTILTKN--IAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-150 |
2.48e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.55 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALafrsarGVQISPSSVR-MLNGHPV---DAKEMQARCAYV-QQFDLFIGsLTAREhliFQ 75
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKML------GRHQPPSEGEiLLDAQPLeswSSKAFARKVAYLpQQLPAAEG-MTVRE---LV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATVRMP------RTMTQKQkiQRVDQVIQDLSLGKCQNTVigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:PRK10575 107 AIGRYPwhgalgRFGAADR--EKVEEAISLVGLKPLAHRL------VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
.
gi 1151065403 150 D 150
Cdd:PRK10575 179 D 179
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1-150 |
2.63e-06 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 44.92 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRMlnghpvdAKEMQARCAYVQQfdlfIGSLTARehliFQATVRM 80
Cdd:NF040873 18 GSLTAVVGPNGSGKSTLLKVLA-----GV-LRPTSGTV-------RRAGGARVAYVPQ----RSEVPDS----LPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 81 PRTMTQKQK------IQRVDQVIQDLSLgkcqnTVIGVPG----RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:NF040873 77 LVAMGRWARrglwrrLTRDDRAAVDDAL-----ERVGLADlagrQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-151 |
2.76e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 60 DLFigSLTAREHLIFQATV----RMPRTMTQKQKIQR------VDQVIQdlSLGKCQNTVIGVPGrvKGLSGGERKRLAF 129
Cdd:PTZ00265 1296 NLF--SIVSQEPMLFNMSIyeniKFGKEDATREDVKRackfaaIDEFIE--SLPNKYDTNVGPYG--KSLSGGQKQRIAI 1369
|
90 100
....*....|....*....|..
gi 1151065403 130 ASEALTDPPLLICDEPTSGLDS 151
Cdd:PTZ00265 1370 ARALLREPKILLLDEATSSLDS 1391
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-151 |
2.91e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.87 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALafrsarGVQISPSS-VRMLNGHPVDAKEMQARCAYVQQFDLFIgslTAREHLIFQAT-- 77
Cdd:PRK10535 34 GEMVAIVGASGSGKSTLMNIL------GCLDKPTSgTYRVAGQDVATLDADALAQLRREHFGFI---FQRYHLLSHLTaa 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 78 --VRMPRT---MTQKQKIQRVDQVIQDLSLGKcqntviGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:PRK10535 105 qnVEVPAVyagLERKQRLLRAQELLQRLGLED------RVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-150 |
3.12e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.78 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRM-LNGHPV------DAKEmqARCAYVQQ-FDLFiGSLTAREHL 72
Cdd:COG1129 30 GEVHALLGENGAGKSTLMKILS-----GVY-QPDSGEIlLDGEPVrfrsprDAQA--AGIAIIHQeLNLV-PNLSVAENI 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 73 IFQATVRMPRTMTQKQKIQRVDQVIQDLSLGkcqntvIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG1129 101 FLGREPRRGGLIDWRAMRRRARELLARLGLD------IDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-150 |
3.83e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargvqispssvrmlnGHPvdakemqarcAY-VQQFDLF-----IGSLTA--REH- 71
Cdd:CHL00131 33 GEIHAIMGPNGSGKSTLSKVIA------------------GHP----------AYkILEGDILfkgesILDLEPeeRAHl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 ---LIFQATVRMP--------RT-MTQKQKIQRVDQV--IQDLSLGKCQNTVIGVPGRV------KGLSGGERKRLAFAS 131
Cdd:CHL00131 85 gifLAFQYPIEIPgvsnadflRLaYNSKRKFQGLPELdpLEFLEIINEKLKLVGMDPSFlsrnvnEGFSGGEKKRNEILQ 164
|
170
....*....|....*....
gi 1151065403 132 EALTDPPLLICDEPTSGLD 150
Cdd:CHL00131 165 MALLDSELAILDETDSGLD 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-150 |
4.66e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGK-TTLLNALAFRSARGvQIspssvrMLNGHPVDAKEMQARCAYVQQFDLFI----GSLTAR---EHL 72
Cdd:PRK15134 312 GETLGLVGESGSGKsTTGLALLRLINSQG-EI------WFDGQPLHNLNRRQLLPVRHRIQVVFqdpnSSLNPRlnvLQI 384
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 73 IFQATVRMPRTMTQKQKIQRVDQVIQDLSLGKcqNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK15134 385 IEEGLRVHQPTLSAAQREQQVIAVMEEVGLDP--ETRHRYPAE---FSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-149 |
4.66e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.04 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVD----AKEMQARCAYVQQFDLFIGSLTAREHLIFqa 76
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIA-----GIVPPDSGTLEIGGNPCArltpAKAHQLGIYLVPQEPLLFPNLSVKENILF-- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 77 tvRMPRTMTQKQKIQrvdQVIQDLSlgkCQntvIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:PRK15439 110 --GLPKRQASMQKMK---QLLAALG---CQ---LDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1-150 |
5.27e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 44.45 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVrMLNGHPVDAKEMQA---RCAYVQQFDLFIGSLTAREHLifqaT 77
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMA-----GLLPGQGEI-LLNGRPLSDWSAAElarHRAYLSQQQSPPFAMPVFQYL----A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 78 VRMPRTMTQKQKIQRVDQVIQDLSLGKcqntviGVPGRVKGLSGGE--RKRLAFA-----SEALTDPPLLICDEPTSGLD 150
Cdd:COG4138 92 LHQPAGASSEAVEQLLAQLAEALGLED------KLSRPLTQLSGGEwqRVRLAAVllqvwPTINPEGQLLLLDEPMNSLD 165
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-157 |
5.42e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFrsargvQISPSSVRMLnghpvdakEMQARCAYVQQFDlFIGSLTAREHLIFQATVRM 80
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLG------ELSHAETSSV--------VIRGSVAYVPQVS-WIFNATVRENILFGSDFES 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 81 PRTMtqkqKIQRVDQVIQDLSLGKCQN-TVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 157
Cdd:PLN03232 708 ERYW----RAIDVTALQHDLDLLPGRDlTEIGERG--VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-151 |
5.88e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.78 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRMlnghpvdakEMQARCAYVQQFDLFIGSLTAREHLIFQATVRM 80
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILA-----GV-LKPDEGEV---------DEDLKISYKPQYISPDYDGTVEEFLRSANTDDF 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065403 81 PRTMTQkqkiqrvDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:COG1245 431 GSSYYK-------TEIIKPLGLEKLLDK------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-150 |
6.55e-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: 43.57 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRM-LNGHPVDakemqarcayvqqfdlFIGSLTAREHlifqatvr 79
Cdd:cd03216 26 GEVHALLGENGAGKSTLMKILS-----GL-YKPDSGEIlVDGKEVS----------------FASPRDARRA-------- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065403 80 mprtmtqkqKIQRVDQviqdlslgkcqntvigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03216 76 ---------GIAMVYQ-----------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-147 |
6.90e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargvqispsSVRMLNGHPVDAKEMQARCAYVQQFDlfiGSLTAREHLIFQATVrM 80
Cdd:PRK13545 50 GEIVGIIGLNGSGKSTLSNLIA------------GVTMPNKGTVDIKGSAALIAISSGLN---GQLTGIENIELKGLM-M 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 81 PRTmtqKQKIQRV-DQVIQDLSLGKcqntVIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTS 147
Cdd:PRK13545 114 GLT---KEKIKEIiPEIIEFADIGK----FIYQP--VKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1-158 |
8.13e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVRMLNGHPVdakemqarcAYVQQfDLFIGSLTAREHLIFQATVRM 80
Cdd:PTZ00243 686 GKLTVVLGATGSGKSTLLQSLL------SQFEISEGRVWAERSI---------AYVPQ-QAWIMNATVRGNILFFDEEDA 749
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 81 PRTmtqkQKIQRVDQVIQDL-SLGKCQNTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 158
Cdd:PTZ00243 750 ARL----ADAVRVSQLEADLaQLGGGLETEIGEKG--VNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVV 822
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-149 |
8.38e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.25 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRML-NGHPV------DAkeMQARCAYVQQ-FDLFiGSLTAREHL 72
Cdd:COG3845 31 GEIHALLGENGAGKSTLMKILY-----GLY-QPDSGEILiDGKPVrirsprDA--IALGIGMVHQhFMLV-PNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 IFQATVRMPRTMTQKQKIQRVDQVIQDLSLgkcqntviGVP--GRVKGLSGGERKRLafasE---AL-TDPPLLICDEPT 146
Cdd:COG3845 102 VLGLEPTKGGRLDRKAARARIRELSERYGL--------DVDpdAKVEDLSVGEQQRV----EilkALyRGARILILDEPT 169
|
...
gi 1151065403 147 SGL 149
Cdd:COG3845 170 AVL 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1-150 |
8.56e-06 |
|
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: 43.30 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGVQISPSSVRMLnghpvdakemqarcaYVQQFDLF-IGSLtaREHLIFqat 77
Cdd:cd03223 27 GDRLLITGPSGTGKSSLFRALAglWPWGSGRIGMPEGEDLL---------------FLPQRPYLpLGTL--REQLIY--- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 78 vrmprtmtqkqkiqrvdqviqdlslgkcqntvigvP-GRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:cd03223 87 -----------------------------------PwDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-150 |
8.71e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 44.21 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLlnALAFRSARGVQISPSSVRMLN-GHPVDAKEMQARCAYVQQF--DLFIGSlTAREHLIF-QA 76
Cdd:PRK13644 28 GEYIGIIGKNGSGKSTL--ALHLNGLLRPQKGKVLVSGIDtGDFSKLQGIRKLVGIVFQNpeTQFVGR-TVEEDLAFgPE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 77 TVRMPRTMTQKqkiqRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13644 105 NLCLPPIEIRK----RVDRALAEIGLEKYRHR------SPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-150 |
8.98e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 43.88 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 3 LLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRmLNGH---------PVDAKEMQARCAYV-QQFDLFigsltarEHL 72
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLN----RLIEIYDSKIK-VDGKvlyfgkdifQIDAIKLRKEVGMVfQQPNPF-------PHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 IFQATVRMP---RTMTQKQKIQR-VDQVIQDLSLGKCQNTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSG 148
Cdd:PRK14246 106 SIYDNIAYPlksHGIKEKREIKKiVEECLRKVGLWKEVYDRLNSPA--SQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
..
gi 1151065403 149 LD 150
Cdd:PRK14246 184 ID 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-150 |
9.79e-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: 44.43 E-value: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNAL--AFRSARGVQIspssvrMLNGHPVD----AKEMQARCAYV---QQFDLFIGSLTAREH 71
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALfgAYPGKFEGNV------FINGKPVDirnpAQAIRAGIAMVpedRKRHGIVPILGVGKN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LIFQATVRMPRTMT--QKQKIQRVDQVIQDLSLGKCQNTVigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:TIGR02633 360 ITLSVLKSFCFKMRidAAAELQIIGSAIQRLKVKTASPFL-----PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
.
gi 1151065403 150 D 150
Cdd:TIGR02633 435 D 435
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-150 |
1.05e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.79 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLnalafrsargvqispssvRMLNGhpvdakemQARCAYVQ-QFDLFIGSLTAREHLIFQatvr 79
Cdd:COG2401 56 GEIVLIVGASGSGKSTLL------------------RLLAG--------ALKGTPVAgCVDVPDNQFGREASLIDA---- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065403 80 MPRTMTQKQKIQRvdqviqdlsLGKCQ-NTVIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG2401 106 IGRKGDFKDAVEL---------LNAVGlSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-158 |
1.10e-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: 44.02 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALafrsaRGV-QISPSSVRMLN-----------GHPVDAKEMQARCA---YVQQFDLFIGS 65
Cdd:TIGR03269 26 GEVLGILGRSGAGKSVLMHVL-----RGMdQYEPTSGRIIYhvalcekcgyvERPSKVGEPCPVCGgtlEPEEVDFWNLS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 66 LTAREHLIFQATVRMPRTMTQKQKIQRVDQVIQDLSlgkcqntVIGVPGR----------------------VKGLSGGE 123
Cdd:TIGR03269 101 DKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALE-------EIGYEGKeavgravdliemvqlshrithiARDLSGGE 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1151065403 124 RKRLAFASEALTDPPLLICDEPTSGLDSfMAASVV 158
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDP-QTAKLV 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-150 |
1.36e-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: 44.02 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS----VRmLNGHPVDAKEM----QARCA-YV----QQFDLFIGSlT 67
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIA-----GV-LEPTSgevnVR-VGDEWVDMTKPgpdgRGRAKrYIgilhQEYDLYPHR-T 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 68 AREHLIFQATVRMPRTMTQKQKIQRVDQViqDLSLGKCQNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTS 147
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVITLKMV--GFDEEKAEEILDKYPDE---LSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
...
gi 1151065403 148 GLD 150
Cdd:TIGR03269 457 TMD 459
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-150 |
1.67e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSArgVQISPSSVR-----MLNGHPVDAKEMQARCAYvqQFDLFIGSLTarEHLIFQ 75
Cdd:PRK09580 27 GEVHAIMGPNGSGKSTLSATLAGRED--YEVTGGTVEfkgkdLLELSPEDRAGEGIFMAF--QYPVEIPGVS--NQFFLQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ATVRMPRTMTQKQKIQRVDqvIQDLSLGKCQntVIGVPGRV------KGLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:PRK09580 101 TALNAVRSYRGQEPLDRFD--FQDLMEEKIA--LLKMPEDLltrsvnVGFSGGEKKRNDILQMAVLEPELCILDESDSGL 176
|
.
gi 1151065403 150 D 150
Cdd:PRK09580 177 D 177
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-150 |
1.92e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 43.18 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLlnalafrsARGVQ--ISPSSVRML-NGHPV---DAKEMQARCAYVQqfdlfigsltarehLIF 74
Cdd:COG4608 44 GETLGLVGESGCGKSTL--------GRLLLrlEEPTSGEILfDGQDItglSGRELRPLRRRMQ--------------MVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 Q-------------ATVRMP----RTMTQKQKIQRVDQVIQdlslgkcqntvigvpgRVkGL------------SGGERK 125
Cdd:COG4608 102 QdpyaslnprmtvgDIIAEPlrihGLASKAERRERVAELLE----------------LV-GLrpehadryphefSGGQRQ 164
|
170 180
....*....|....*....|....*.
gi 1151065403 126 RLAFAsEAL-TDPPLLICDEPTSGLD 150
Cdd:COG4608 165 RIGIA-RALaLNPKLIVCDEPVSALD 189
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-157 |
2.00e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.03 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLlnalafrsARGVQI--SPSSVR-MLNGHPV---DAKEMQARCAYVQQ-FDLFIGSLTAREHLi 73
Cdd:PRK11308 41 GKTLAVVGESGCGKSTL--------ARLLTMieTPTGGElYYQGQDLlkaDPEAQKLLRQKIQIvFQNPYGSLNPRKKV- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 74 fQATVRMPRTM-TQKQKIQRVDQVIQDLSlgkcqntvigvpgRVkGL------------SGGERKRLAFASEALTDPPLL 140
Cdd:PRK11308 112 -GQILEEPLLInTSLSAAERREKALAMMA-------------KV-GLrpehydryphmfSGGQRQRIAIARALMLDPDVV 176
|
170
....*....|....*..
gi 1151065403 141 ICDEPTSGLDSFMAASV 157
Cdd:PRK11308 177 VADEPVSALDVSVQAQV 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
116-157 |
2.06e-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: 43.39 E-value: 2.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1151065403 116 VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAASV 157
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESV 197
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-150 |
2.06e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.63 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARG-VQISPSSVRmlnghpvdakemQARCAYVQQFdLFIG-------SLTARE 70
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLLKLIAglLNPEKGeILFERQSIK------------KDLCTYQKQL-CFVGhrsginpYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 71 HLIFQatvrmprtMTQKQKIQRVDQVIQDLSLGKCQNTVIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13540 94 NCLYD--------IHFSPGAVGITELCRLFSLEHLIDYPCGL------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
118-150 |
2.91e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.53 E-value: 2.91e-05
10 20 30
....*....|....*....|....*....|...
gi 1151065403 118 GLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
116-157 |
3.70e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 3.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1151065403 116 VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAASV 157
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESV 199
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
83-150 |
4.25e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 4.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065403 83 TMTQKQKIQRVDQVIQDLSLGKCQNTVI---GVPGRVKGLSGGERK------RLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK01156 763 TSLTRKYLFEFNLDFDDIDVDQDFNITVsrgGMVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLD 839
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-150 |
4.46e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.12 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVRMLNGHPvDAKEMQARCAYVQQFDlfigsltarEHLIFQAT 77
Cdd:PRK13641 33 GSFVALVGHTGSGKSTLMqhfNALLKPSSGTITIAGYHITPETGNK-NLKKLRKKVSLVFQFP---------EAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 78 VRM-----PRTM---TQKQKIQRVDQVIQdlslgkcqntvIGVPGRVKG-----LSGGERKRLAFASEALTDPPLLICDE 144
Cdd:PRK13641 103 VLKdvefgPKNFgfsEDEAKEKALKWLKK-----------VGLSEDLISkspfeLSGGQMRRVAIAGVMAYEPEILCLDE 171
|
....*.
gi 1151065403 145 PTSGLD 150
Cdd:PRK13641 172 PAAGLD 177
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
91-153 |
5.16e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.94 E-value: 5.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065403 91 QRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 153
Cdd:PRK11000 112 QRVNQVAEVLQLAHLLDR------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-158 |
8.94e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.01 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDakemQARCAYVQQFDLFIGSLTAREHLIFQAT--- 77
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLIC-----GIERPSAGKIWFSGHDIT----RLKNREVPFLRRQIGMIFQDHHLLMDRTvyd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 78 -VRMPRTM---TQKQKIQRVDQVIQDLS-LGKCQNTVIgvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 152
Cdd:PRK10908 99 nVAIPLIIagaSGDDIRRRVSAALDKVGlLDKAKNFPI-------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
....*.
gi 1151065403 153 MAASVV 158
Cdd:PRK10908 172 LSEGIL 177
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-144 |
1.10e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 41.32 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALA--FRSARGvQISpssvrmLNGHPVDAKEMQarcAYVQQF-----D--LFigsltarEH 71
Cdd:COG4615 358 GELVFIVGGNGSGKSTLAKLLTglYRPESG-EIL------LDGQPVTADNRE---AYRQLFsavfsDfhLF-------DR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LIFQATVRMPrtmtqkqkiQRVDQVIQDLSLgkcQNTVigvpgRVKG-------LSGGERKRLAFASEALTDPPLLICDE 144
Cdd:COG4615 421 LLGLDGEADP---------ARARELLERLEL---DHKV-----SVEDgrfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
65-150 |
1.11e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 65 SLTAREHLIFqatVRMPRTMTQKQKIQRVDQVIQDLSLGKcqntvigVPGRVKG-LSGGERKRLAFASEALTDPPLLICD 143
Cdd:NF000106 100 SFSGRENLYM---IGR*LDLSRKDARARADELLERFSLTE-------AAGRAAAkYSGGMRRRLDLAASMIGRPAVLYLD 169
|
....*..
gi 1151065403 144 EPTSGLD 150
Cdd:NF000106 170 EPTTGLD 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
119-150 |
1.12e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 41.21 E-value: 1.12e-04
10 20 30
....*....|....*....|....*....|..
gi 1151065403 119 LSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-151 |
1.16e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 40.82 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRMLNGH-PVDAkemqarcayvqqfdlfigsltAREHLifqatvr 79
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLA-----GLE-TPSAGELLAGTaPLAE---------------------AREDT------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 80 mpRTMTQKQKIQRVDQVIQDLSLGKCQN---------TVIGVPGRVK----GLSGGERKRLAFASEALTDPPLLICDEPT 146
Cdd:PRK11247 84 --RLMFQDARLLPWKKVIDNVGLGLKGQwrdaalqalAAVGLADRANewpaALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
....*
gi 1151065403 147 SGLDS 151
Cdd:PRK11247 162 GALDA 166
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-150 |
1.17e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 41.07 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLlnalaFRSARGvQISPSSVRMLNGHPVDAkemqarcAYVQQFdlfigsltaREHLIFQATVRm 80
Cdd:TIGR03719 348 GGIVGVIGPNGAGKSTL-----FRMITG-QEQPDSGTIEIGETVKL-------AYVDQS---------RDALDPNKTVW- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 81 prtmtqkqkiqrvdQVIQD----LSLGKCQntvigVPGR----------------VKGLSGGERKRLAFASEALTDPPLL 140
Cdd:TIGR03719 405 --------------EEISGgldiIKLGKRE-----IPSRayvgrfnfkgsdqqkkVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|
gi 1151065403 141 ICDEPTSGLD 150
Cdd:TIGR03719 466 LLDEPTNDLD 475
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-150 |
1.38e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNAL-AFRSARGVQIspssvrMLNGHPVDAKEMQARCA----YV----QQFDLF--------I 63
Cdd:PRK15439 289 GEILGLAGVVGAGRTELAETLyGLRPARGGRI------MLNGKEINALSTAQRLArglvYLpedrQSSGLYldaplawnV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 64 GSLTAREHLIFQATVRMPRTMTQKQKiqrvdqviqdlSLG-KCQNtvigVPGRVKGLSGGERKRLAFASEALTDPPLLIC 142
Cdd:PRK15439 363 CALTHNRRGFWIKPARENAVLERYRR-----------ALNiKFNH----AEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
....*...
gi 1151065403 143 DEPTSGLD 150
Cdd:PRK15439 428 DEPTRGVD 435
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-150 |
1.41e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 40.48 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLnalafRSARGVqISPSSVRMLnghpvdaKEMQARCAYVQQfdlfigsltaREHLIFQATVRM 80
Cdd:PRK09544 30 GKILTLLGPNGAGKSTLV-----RVVLGL-VAPDEGVIK-------RNGKLRIGYVPQ----------KLYLDTTLPLTV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 81 PRTMTQKQKIQRVDqVIQDLSLGKCQNtVIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK09544 87 NRFLRLRPGTKKED-ILPALKRVQAGH-LIDAP--MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1-150 |
1.54e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.00 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGVQISPSSvrmlnghpvdakemqarcAYVQQFDLFIGSLtarehlifqatvrm 80
Cdd:cd03238 21 NVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLP------------------KFSRNKLIFIDQL-------------- 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065403 81 pRTMtqkqkiqrVDQVIQDLSLGKCQNTvigvpgrvkgLSGGERKRLAFASEALTDPP--LLICDEPTSGLD 150
Cdd:cd03238 69 -QFL--------IDVGLGYLTLGQKLST----------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-150 |
1.60e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 40.53 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTL---LNALAFRSARGVQISPSSVRmlngHPVDAKEMQ---ARCAYVQQFDlfigsltarEHLIF 74
Cdd:PRK13646 33 GKYYAIVGQTGSGKSTLiqnINALLKPTTGTVTVDDITIT----HKTKDKYIRpvrKRIGMVFQFP---------ESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 75 QATVRMPRTMTQKQKIQRVDQVIQD-----LSLGKCQNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 149
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYahrllMDLGFSRDVMSQSPFQ---MSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
.
gi 1151065403 150 D 150
Cdd:PRK13646 177 D 177
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1-158 |
2.03e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 40.08 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRsargvqISPSSVRM-LNGHPVDAKEMQARCAYVQQFDLFIGSLTAR--EHLIFQAT 77
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGV------LKPDEGDIeIELDTVSYKPQYIKADYEGTVRDLLSSITKDfyTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 78 VRMPRtmtqkQKIQRVDQviqdlslgkcqntvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS---FMA 154
Cdd:cd03237 99 IAKPL-----QIEQILDR-------------------EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMA 154
|
....
gi 1151065403 155 ASVV 158
Cdd:cd03237 155 SKVI 158
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
1-22 |
2.17e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.69 E-value: 2.17e-04
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-150 |
2.32e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.01 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGV-QISPSSVRmLNGHPV---DAKEM-QARCAYV----QQFDLfIGSLTAREH 71
Cdd:COG3845 284 GEILGIAGVAGNGQSELAEALA-----GLrPPASGSIR-LDGEDItglSPRERrRLGVAYIpedrLGRGL-VPDMSVAEN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 72 LIFQATVRMP---RTMTQKQKIQR-VDQVIQDLSLgKCQNtvIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTS 147
Cdd:COG3845 357 LILGRYRRPPfsrGGFLDRKAIRAfAEELIEEFDV-RTPG--PDTP--ARSLSGGNQQKVILARELSRDPKLLIAAQPTR 431
|
...
gi 1151065403 148 GLD 150
Cdd:COG3845 432 GLD 434
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
120-150 |
2.38e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.09 E-value: 2.38e-04
10 20 30
....*....|....*....|....*....|.
gi 1151065403 120 SGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-150 |
2.77e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 39.99 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 6 VMGSSGAGKTTLLnalafRSARGVQISPSSVRMLNGHPVDA--------KEMQARCAYVQQFDlfigsltarEHLIFQAT 77
Cdd:PRK13645 42 VIGTTGSGKSTMI-----QLTNGLIISETGQTIVGDYAIPAnlkkikevKRLRKEIGLVFQFP---------EYQLFQET 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 78 VRM-----PRTM-TQKQKI-QRVDQVIQDLSLGKcqNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13645 108 IEKdiafgPVNLgENKQEAyKKVPELLKLVQLPE--DYVKRSPFE---LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
119-150 |
3.49e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 39.59 E-value: 3.49e-04
10 20 30
....*....|....*....|....*....|..
gi 1151065403 119 LSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-158 |
4.09e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.39 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRML-NGHPVDAKEMQARCAYVQQ-FDLFIGSLTAREHL--IFQA 76
Cdd:PRK15112 39 GQTLAIIGENGSGKSTLAKMLA-----GM-IEPTSGELLiDDHPLHFGDYSYRSQRIRMiFQDPSTSLNPRQRIsqILDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 77 TVRMPRTMTQKQKIQRVDQVIQDLSLgkcqntvigVPGRVK----GLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 152
Cdd:PRK15112 113 PLRLNTDLEPEQREKQIIETLRQVGL---------LPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
....*.
gi 1151065403 153 MAASVV 158
Cdd:PRK15112 184 MRSQLI 189
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-150 |
5.22e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.01 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLL---NALAfrsargvqiSPSSVRML-NGHPV---DAKEM-QARcayvQQfdlfIGsltarehL 72
Cdd:PRK11153 31 GEIFGVIGASGAGKSTLIrciNLLE---------RPTSGRVLvDGQDLtalSEKELrKAR----RQ----IG-------M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 IFQ-----------ATVRMPRTM--TQKQKI-QRVDQVIQDLSLGKCQNTVigvPGRvkgLSGGERKRLAFAsEAL-TDP 137
Cdd:PRK11153 87 IFQhfnllssrtvfDNVALPLELagTPKAEIkARVTELLELVGLSDKADRY---PAQ---LSGGQKQRVAIA-RALaSNP 159
|
170
....*....|...
gi 1151065403 138 PLLICDEPTSGLD 150
Cdd:PRK11153 160 KVLLCDEATSALD 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
92-150 |
6.18e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.02 E-value: 6.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 92 RVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13409 192 KLDEVVERLGLENILDR------DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
115-158 |
6.42e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.02 E-value: 6.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1151065403 115 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS---FMAASVV 158
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKAI 496
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-157 |
6.56e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.53 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKT-TLLNALAFRSArGVQISPSSVRmLNGHPVDAKEMQAR-CAYVQQ--FDLFIGSLTAREHLIfqa 76
Cdd:PRK10418 29 GRVLALVGGSGSGKSlTCAAALGILPA-GVRQTAGRVL-LDGKPVAPCALRGRkIATIMQnpRSAFNPLHTMHTHAR--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 77 tvrmpRTMTQKQKIQRVDQVIQDLSLGKCQNtvigvPGRVKGL-----SGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:PRK10418 104 -----ETCLALGKPADDATLTAALEAVGLEN-----AARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
....*.
gi 1151065403 152 FMAASV 157
Cdd:PRK10418 174 VAQARI 179
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-150 |
7.13e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 38.93 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALafrsARGVQISPSSVRmLNGHPVDA---KEMQARCAYVQQFDlFIGSLTAREHLifqAT 77
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSLI----QRHFDVSEGDIR-FHDIPLTKlqlDSWRSRLAVVSQTP-FLFSDTVANNI---AL 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 78 VRMPRTMTQKQKIQRVDQVIQD-LSLGKCQNTVIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK10789 412 GRPDATQQEIEHVARLASVHDDiLRLPQGYDTEVGERGVM--LSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
92-150 |
7.59e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 38.61 E-value: 7.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065403 92 RVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:COG1245 192 KLDELAEKLGLENILDR------DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
119-150 |
7.84e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 38.57 E-value: 7.84e-04
10 20 30
....*....|....*....|....*....|..
gi 1151065403 119 LSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
119-150 |
8.36e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 38.56 E-value: 8.36e-04
10 20 30
....*....|....*....|....*....|..
gi 1151065403 119 LSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-150 |
8.78e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.37 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNAL--AFRSARGVQIspssvrMLNGHPVD----AKEMQARCAYVQQ--------FDLFIG-- 64
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLfgAYPGRWEGEI------FIDGKPVKirnpQQAIAQGIAMVPEdrkrdgivPVMGVGkn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 65 -SLTAREHLIFQATVRMPRtmtqkqKIQRVDQVIQDLSLgKCQNTVIgvpgRVKGLSGGERKRLAFASEALTDPPLLICD 143
Cdd:PRK13549 362 iTLAALDRFTGGSRIDDAA------ELKTILESIQRLKV-KTASPEL----AIARLSGGNQQKAVLAKCLLLNPKILILD 430
|
....*..
gi 1151065403 144 EPTSGLD 150
Cdd:PRK13549 431 EPTRGID 437
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-158 |
9.43e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 38.33 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNAL-AFrsargVQISPSSVRMLnGHPVDAKEMQARCAYVQQ-------FDLFIGSLTAREHL 72
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALmGF-----VRLASGKISIL-GQPTRQALQKNLVAYVPQseevdwsFPVLVEDVVMMGRY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 73 IFQATVRMPRTMTQkqkiQRVDQVIQDLSLGKCQNTVIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 152
Cdd:PRK15056 107 GHMGWLRRAKKRDR----QIVTAALARVDMVEFRHRQIG------ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
....*.
gi 1151065403 153 MAASVV 158
Cdd:PRK15056 177 TEARII 182
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-150 |
1.20e-03 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 38.04 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVRM-LNGHPVD---AKEMQARCAYVQQFDLFIGSLTAREhliFQA 76
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLS------RLMTPAHGHVwLDGEHIQhyaSKEVARRIGLLAQNATTPGDITVQE---LVA 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065403 77 TVRMPR----TMTQKQKIQRVDQVIQDLSLGKCQNTvigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK10253 104 RGRYPHqplfTRWRKEDEEAVTKAMQATGITHLADQ------SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
1-22 |
1.25e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.52 E-value: 1.25e-03
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
4-21 |
1.29e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 37.09 E-value: 1.29e-03
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
119-150 |
1.55e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 37.71 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|..
gi 1151065403 119 LSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-153 |
1.86e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 37.71 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTT---LLNALaFRSARGvQISPSSVRMLNGHPVDAKEMQARcayvqQFDLFIGSLTAREHLIFQAT 77
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTmvrLLNRL-IEPTRG-QVLIDGVDIAKISDAELREVRRK-----KIAMVFQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065403 78 VRMPRTMTQKQKIQRVDQVIQDLSLGKCQNTVIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 153
Cdd:PRK10070 127 TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE---LSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
89-149 |
2.08e-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: 37.69 E-value: 2.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065403 89 KIQRVDQVIQDLSLGKCQntvIGVPgrVKGLSGGERKRLAFASEAL---TDPPLLICDEPTSGL 149
Cdd:TIGR00630 805 SISRKLQTLCDVGLGYIR---LGQP--ATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGL 863
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
115-150 |
2.16e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.53 E-value: 2.16e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1151065403 115 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PLN03073 341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-88 |
2.18e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 37.64 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGVQISPSSVRMLNGHpvdakeMQARCAYVQ-QFDLFIGSLTAREHLIFQATVR 79
Cdd:TIGR00618 26 GPIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSL------YAAPSEAAFaELEFSLGTKIYRVHRTLRCTRS 99
|
....*....
gi 1151065403 80 MPRTMTQKQ 88
Cdd:TIGR00618 100 HRKTEQPEQ 108
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1-21 |
2.59e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 36.84 E-value: 2.59e-03
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-158 |
3.04e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 37.14 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKT-TLLNALAFRSARGVQISPSS--VRMLNGHPVDAKEM-QARCAYVQQFDLfigsltareHLIFQ- 75
Cdd:PRK10261 42 GETLAIVGESGSGKSvTALALMRLLEQAGGLVQCDKmlLRRRSRQVIELSEQsAAQMRHVRGADM---------AMIFQe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 76 ----------------ATVRMPRTMTQKQKIQRVDQVIQDLSLGKCQNTVIGVPGRvkgLSGGERKRLAFASEALTDPPL 139
Cdd:PRK10261 113 pmtslnpvftvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ---LSGGMRQRVMIAMALSCRPAV 189
|
170
....*....|....*....
gi 1151065403 140 LICDEPTSGLDSFMAASVV 158
Cdd:PRK10261 190 LIADEPTTALDVTIQAQIL 208
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
5-22 |
3.29e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 35.90 E-value: 3.29e-03
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
1-27 |
3.47e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 36.32 E-value: 3.47e-03
10 20
....*....|....*....|....*..
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSAR 27
Cdd:COG3709 5 GRLIYVVGPSGAGKDSLLAAARARLAA 31
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
4-25 |
3.83e-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: 36.42 E-value: 3.83e-03
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1-22 |
3.97e-03 |
|
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: 35.81 E-value: 3.97e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-149 |
4.34e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 36.73 E-value: 4.34e-03
10 20 30
....*....|....*....|....*....|....
gi 1151065403 119 LSGGERKRLAFASEALT---DPPLLICDEPTSGL 149
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGL 843
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
116-151 |
4.57e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 35.80 E-value: 4.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1151065403 116 VKGLSGGERKR----LAFASEALTDPPLLICDEPTSGLDS 151
Cdd:cd03227 75 RLQLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDP 114
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
1-95 |
4.63e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 36.42 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAFRSARGV-----QISPSSVRMLNGHpVDAKEMQARC-AYVQQFDLFIGSLTAREHLIf 74
Cdd:COG3598 13 GGVTLLAGPPGTGKSFLALQLAAAVAAGGpwlgrRVPPGKVLYLAAE-DDRGELRRRLkALGADLGLPFADLDGRLRLL- 90
|
90 100
....*....|....*....|.
gi 1151065403 75 QATVRMPRTMTQKQKIQRVDQ 95
Cdd:COG3598 91 SLAGDLDDTDDLEALERAIEE 111
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
119-150 |
5.13e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 36.38 E-value: 5.13e-03
10 20 30
....*....|....*....|....*....|..
gi 1151065403 119 LSGGERKRLAFASEALTDPPLLICDEPTSGLD 150
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-147 |
5.76e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 35.95 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALafrsarGVQISPSSVRMLNGHPVDAKEMQARCAyvqqfdlfiGSLTAREHLIFQAtvrM 80
Cdd:PRK13546 50 GDVIGLVGINGSGKSTLSNII------GGSLSPTVGKVDRNGEVSVIAISAGLS---------GQLTGIENIEFKM---L 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065403 81 PRTMTQKQKIQRVDQVIQDLSLGKcqntVIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTS 147
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGE----FIYQP--VKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
119-158 |
7.36e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 35.49 E-value: 7.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1151065403 119 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 158
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQII 193
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-151 |
8.32e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 35.85 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 5 AVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQA---RCAYVQQfDLFIGSLTarehliFQATVRMP 81
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLM-----GYYPLTEGEIRLDGRPLSSLSHSVlrqGVAMVQQ-DPVVLADT------FLANVTLG 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065403 82 RTMTQKQKIQRVDQV-----IQDLSLGkcQNTVIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 151
Cdd:PRK10790 439 RDISEEQVWQALETVqlaelARSLPDG--LYTPLGEQG--NNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-150 |
8.56e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 35.76 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 1 GELLAVMGSSGAGKTTLLNALAfrsargvqispssvrmlnghpvdakemqarcayvQQFDLFIGSLTARehliFQATVRM 80
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALA----------------------------------GELPLLSGERQSQ----FSHITRL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 81 prTMTQKQKI-----QR----------------VDQVIQDLS--LGKCQN--TVIGVPG----RVKGLSGGERKRLAFAS 131
Cdd:PRK10938 71 --SFEQLQKLvsdewQRnntdmlspgeddtgrtTAEIIQDEVkdPARCEQlaQQFGITAlldrRFKYLSTGETRKTLLCQ 148
|
170
....*....|....*....
gi 1151065403 132 EALTDPPLLICDEPTSGLD 150
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLD 167
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
89-149 |
8.73e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 35.77 E-value: 8.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065403 89 KIQRVDQVIQD-----LSLGKCQNTvigvpgrvkgLSGGERKRLAFASEaL----TDPPLLICDEPTSGL 149
Cdd:COG0178 802 KIARKLQTLQDvglgyIKLGQPATT----------LSGGEAQRVKLASE-LskrsTGKTLYILDEPTTGL 860
|
|
| |
