|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1-196 |
5.20e-134 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 388.64 E-value: 5.20e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARGVQISPSsvRMLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATVR 80
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGS--VLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPRTMTQKQKMQRVDQVIQDLSLGKCQNTIIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:TIGR00955 128 MPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ 207
|
170 180 190
....*....|....*....|....*....|....*.
gi 1151065379 161 VLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:TIGR00955 208 VLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEG 243
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-196 |
1.63e-73 |
|
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: 221.38 E-value: 1.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAFRSARGVQISpsSVRMLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATVRM 81
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLDAISGRVEGGGTTS--GQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRETLTYTAILRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 PRTMTQKQKMQRVDqviqDLSLGKCQNTIIGVPgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQV 161
Cdd:cd03234 111 PRKSSDAIRKKRVE----DVLLRDLALTRIGGN-LVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVST 185
|
170 180 190
....*....|....*....|....*....|....*
gi 1151065379 162 LKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:cd03234 186 LSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSG 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-196 |
2.45e-64 |
|
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: 196.62 E-value: 2.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRsARGVQISpSSVRmLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQAtvr 80
Cdd:cd03213 34 PGELTAIMGPSGAGKSTLLNALAGR-RTGLGVS-GEVL-INGRPLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAA--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 mprtmtqkqkmqrvdqviqdlslgkcqntiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:cd03213 108 -----------------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1151065379 161 VLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:cd03213 153 LLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQG 188
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-196 |
2.27e-58 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 197.25 E-value: 2.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARGVqISpSSVRMLNGHPVDAKeMQARCAYVQQFDLFIGSLTAREHLIFQATVR 80
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLAERVTTGV-IT-GGDRLVNGRPLDSS-FQRSIGYVQQQDLHLPTSTVRESLRFSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPRTMTQKQKMQRVDQVIQDLSLGKCQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLI-CDEPTSGLDSFMAASVV 159
Cdd:TIGR00956 865 QPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPG--EGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSIC 942
|
170 180 190
....*....|....*....|....*....|....*..
gi 1151065379 160 QVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:TIGR00956 943 KLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKG 979
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1-196 |
1.53e-54 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 183.54 E-value: 1.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRsargVQISPSSVRMLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATVR 80
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGR----IQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPRTMTQKQKMQRVDQVIQDLSLGKCQNTIIGvPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISELGLTKCENTIIG-NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190
....*....|....*....|....*....|....*.
gi 1151065379 161 VLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-196 |
7.40e-50 |
|
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: 159.72 E-value: 7.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARGVqISPSSvrMLNGHPVDaKEMQARCAYVQQFDLFIGSLTAREHLIFQATVR 80
Cdd:cd03232 32 PGTLTALMGESGAGKTTLLDVLAGRKTAGV-ITGEI--LINGRPLD-KNFQRSTGYVEQQDVHSPNLTVREALRFSALLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 mprtmtqkqkmqrvdqviqdlslgkcqntiigvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:cd03232 108 --------------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1151065379 161 VLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:cd03232 150 FLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-196 |
4.04e-46 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 162.32 E-value: 4.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARG-----VQISpssvrmlnGHPvDAKEMQARCA-YVQQFDLFIGSLTAREHLI 74
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAGRKTGGyiegdIRIS--------GFP-KKQETFARISgYCEQNDIHSPQVTVRESLI 975
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 FQATVRMPRTMTQKQKMQRVDQVIQDLSLGKCQNTIIGVPGrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 154
Cdd:PLN03140 976 YSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPG-VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 155 AASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PLN03140 1055 AAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRG 1096
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1-196 |
8.79e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.29 E-value: 8.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRmLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIFQ 76
Cdd:COG1131 25 PGEIFGLLGPNGAGKTTTIRMLL-----GL-LRPTSgeVR-VLGEDVarDPAEVRRRIGYVPQEPALYPDLTVRENLRFF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVR-MPRtmtqKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 155
Cdd:COG1131 98 ARLYgLPR----KEARERIDELLELFGLTDAADR------KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1151065379 156 ASVVQVLKKLSQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:COG1131 168 RELWELLRELAAEGKTVLLSTHYL-EEAERLCDRVAIIDKG 207
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-196 |
3.14e-34 |
|
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: 120.06 E-value: 3.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrSARGVQISPSSVRMLNGHPvdAKEMQARC----AYVQQFDLFIGSLTAREHLIFQ 76
Cdd:cd03233 32 PGEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNGIP--YKEFAEKYpgeiIYVSEEDVHFPTLTVRETLDFA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 AtvrmprtmtqkqkmqrvdqviqdlslgKCQNTIIgvpgrVKGLSGGERKRLAFAsEALTDPPLLIC-DEPTSGLDSFMA 155
Cdd:cd03233 108 L---------------------------RCKGNEF-----VRGISGGERKRVSIA-EALVSRASVLCwDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 156 ASVVQVLKKLSQR-GKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:cd03233 155 LEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-196 |
6.83e-34 |
|
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: 120.35 E-value: 6.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARG-VQIspssvrmlNGHPVDAKEMQAR--CAYVQQFDLFIGSLTAREHLIF 75
Cdd:COG4555 26 DGEITGLLGPNGAGKTTLLRMLAglLKPDSGsILI--------DGEDVRKEPREARrqIGVLPDERGLYDRLTVRENIRY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 QATVRmprTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 155
Cdd:COG4555 98 FAELY---GLFDEELKKRIEELIELLGLEEFLDR------RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMAR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1151065379 156 ASVVQVLKKLSQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:COG4555 169 RLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKG 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1-196 |
1.57e-32 |
|
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: 116.03 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDA---KEMQARCAYV-QQFDLFIGSLTAREHLIFQ 76
Cdd:cd03225 26 KGEFVLIVGPNGSGKSTLLRLLN-----GLLGPTSGEVLVDGKDLTKlslKELRRKVGLVfQNPDDQFFGPTVEEEVAFG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 atvrmPRTMTQKQKM--QRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 154
Cdd:cd03225 101 -----LENLGLPEEEieERVEEALELVGLEGLRDR------SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 155 AASVVQVLKKLSQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:cd03225 170 RRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDG 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1-196 |
2.40e-32 |
|
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: 114.42 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRmLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIfq 76
Cdd:cd03230 25 KGEIYGLLGPNGAGKTTLIKIIL-----GL-LKPDSgeIK-VLGKDIkkEPEEVKRRIGYLPEEPSLYENLTVRENLK-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 atvrmprtmtqkqkmqrvdqviqdlslgkcqntiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:cd03230 96 -------------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 157 SVVQVLKKLSQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:cd03230 133 EFWELLRELKKEGKTILLSSHIL-EEAERLCDRVAILNNG 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-196 |
4.38e-32 |
|
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: 115.29 E-value: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSSVR-MLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIFQA 77
Cdd:cd03263 27 KGEIFGLLGHNGAGKTTTLKMLT-----G-ELRPTSGTaYINGYSIrtDRKAARQSLGYCPQFDALFDELTVREHLRFYA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVRMPRtmtQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:cd03263 101 RLKGLP---KSEIKEEVELLLRVLGLTDKANK------RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRA 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 158 VVQVLKKLsQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:cd03263 172 IWDLILEV-RKGRSIILTTHSM-DEAEALCDRIAIMSDG 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1-196 |
2.36e-31 |
|
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: 113.35 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRM-LNGHPVDAKEMQARCAYV--------QQFDLfIGSLTARE 71
Cdd:cd03255 29 KGEFVAIVGPSGSGKSTLLNILG-----GLD-RPTSGEVrVDGTDISKLSEKELAAFRrrhigfvfQSFNL-LPDLTALE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HlifqatVRMPRTMTQKQKMQRVDQVIQDLslgkcqnTIIGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDEPT 147
Cdd:cd03255 102 N------VELPLLLAGVPKKERRERAEELL-------ERVGLGDRlnhyPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1151065379 148 SGLDSFMAASVVQVLKKLS-QRGKTVILTIHQPssELFELFDKILLMAEG 196
Cdd:cd03255 169 GNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDG 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-179 |
2.19e-30 |
|
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: 110.26 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRmLNGHPVDAK--EMQARCAYVQQFDLFIGSLTAREHLIFQ 76
Cdd:COG4133 27 AGEALALTGPNGSGKTTLLRILA-----G-LLPPSAgeVL-WNGEPIRDAreDYRRRLAYLGHADGLKPELTVRENLRFW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRMPRtmtqkQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:COG4133 100 AALYGLR-----ADREAIDEALEAVGLAGLADL------PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
170 180
....*....|....*....|...
gi 1151065379 157 SVVQVLKKLSQRGKTVILTIHQP 179
Cdd:COG4133 169 LLAELIAAHLARGGAVLLTTHQP 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1-196 |
8.32e-30 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 115.21 E-value: 8.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSaRGVQISPSSVRMLNGHPVD--AKEMQARCAYVQQFDLFIGSLTAREHLIFQAT 78
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIASNT-DGFHIGVEGVITYDGITPEeiKKHYRGDVVYNAETDVHFPHLTVGETLDFAAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRT----MTQKQKMQRV-DQVIQDLSLGKCQNTIIGvPGRVKGLSGGERKRLAFAsEALTDPPLLIC-DEPTSGLDS 152
Cdd:TIGR00956 165 CKTPQNrpdgVSREEYAKHIaDVYMATYGLSHTRNTKVG-NDFVRGVSGGERKRVSIA-EASLGGAKIQCwDNATRGLDS 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1151065379 153 FMAASVVQVLKKLSQRGK-TVILTIHQPSSELFELFDKILLMAEG 196
Cdd:TIGR00956 243 ATALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVLYEG 287
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-196 |
4.02e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 107.44 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVR-MLNGHPV---DAKEMQA-RCAYV----QQFDLfIGSLTARE 71
Cdd:COG1136 33 AGEFVAIVGPSGSGKSTLLNILG-----GLD-RPTSGEvLIDGQDIsslSERELARlRRRHIgfvfQFFNL-LPELTALE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HlifqatVRMP---RTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPT 147
Cdd:COG1136 106 N------VALPlllAGVSRKERRERARELLERVGLGDRLDH------RPSQLSGGQQQRVAIA-RALvNRPKLILADEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1151065379 148 SGLDSFMAASVVQVLKKLS-QRGKTVILTIHQPssELFELFDKILLMAEG 196
Cdd:COG1136 173 GNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDG 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1-196 |
1.46e-28 |
|
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: 106.26 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRML-NGHPVDAKEMQA---RCAYVQQFDlfigsltarEHLIFQ 76
Cdd:COG1122 26 KGEFVAIIGPNGSGKSTLLRLLN-----GL-LKPTSGEVLvDGKDITKKNLRElrrKVGLVFQNP---------DDQLFA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVR-------MPRTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASeAL-TDPPLLICDEPTS 148
Cdd:COG1122 91 PTVEedvafgpENLGLPREEIRERVEEALELVGLEHLADR------PPHELSGGQKQRVAIAG-VLaMEPEVLVLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1151065379 149 GLDSFMAASVVQVLKKLSQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:COG1122 164 GLDPRGRRELLELLKRLNKEGKTVIIVTHDL-DLVAELADRVIVLDDG 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-196 |
1.96e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 111.00 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSSVR-MLNGHPV---DAKEMQARCAYV-QQFDLFIGSLtaREHLif 75
Cdd:COG4988 362 PGERVALVGPSGAGKSTLLNLLL-----G-FLPPYSGSiLINGVDLsdlDPASWRRQIAWVpQNPYLFAGTI--RENL-- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 qatvRMPRTMTQKQKMQRV------DQVIQDLSLGkcQNTIIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSG 149
Cdd:COG4988 432 ----RLGRPDASDEELEAAleaaglDEFVAALPDG--LDTPLGEGGR--GLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1151065379 150 LDSFMAASVVQVLKKLSqRGKTVILTIHQPSseLFELFDKILLMAEG 196
Cdd:COG4988 504 LDAETEAEILQALRRLA-KGRTVILITHRLA--LLAQADRILVLDDG 547
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-196 |
3.14e-28 |
|
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: 103.48 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFrsargvQISPSSVRM-LNGHPV---DAKEMQARCAYVQQfdlfigsltarehlifq 76
Cdd:cd00267 24 AGEIVALVGPNGSGKSTLLRAIAG------LLKPTSGEIlIDGKDIaklPLEELRRRIGYVPQ----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 atvrmprtmtqkqkmqrvdqviqdlslgkcqntiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:cd00267 81 -------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 157 SVVQVLKKLSQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:cd00267 118 RLLELLRELAEEGRTVIIVTHDP-ELAELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1-148 |
3.18e-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: 103.11 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSSVRM-LNGHPVDAKEMQA---RCAYVQQFDLFIGSLTAREHLIFQ 76
Cdd:pfam00005 10 PGEILALVGPNGAGKSTLLKLIA-----G-LLSPTEGTIlLDGQDLTDDERKSlrkEIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065379 77 ATVRMPRTMTQKQkmqRVDQVIQDLSLGKCQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTS 148
Cdd:pfam00005 84 LLLKGLSKREKDA---RAEEALEKLGLGDLADRPVGERP--GTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-196 |
1.25e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.02 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRmLNGHPVDAKemQARCAYVQQFDLFIGS--LTAREhlifq 76
Cdd:COG1121 31 PGEFVAIVGPNGAGKSTLLKAIL-----G-LLPPTSgtVR-LFGKPPRRA--RRRIGYVPQRAEVDWDfpITVRD----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 aTVRMPRT--------MTQKQKmQRVDQVIQDLSLGKCQNTIIGvpgrvkGLSGGERKRLAFAsEAL-TDPPLLICDEPT 147
Cdd:COG1121 97 -VVLMGRYgrrglfrrPSRADR-EAVDEALERVGLEDLADRPIG------ELSGGQQQRVLLA-RALaQDPDLLLLDEPF 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1151065379 148 SGLDSFMAASVVQVLKKLSQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:COG1121 168 AGVDAATEEALYELLRELRREGKTILVVTHDL-GAVREYFDRVLLLNRG 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-194 |
1.50e-27 |
|
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: 103.38 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRMLnghPVDAKEMQARCAYVQQFDLFIGS--LTAREhlifq 76
Cdd:cd03235 24 PGEFLAIVGPNGAGKSTLLKAIL-----G-LLKPTSgsIRVF---GKPLEKERKRIGYVPQRRSIDRDfpISVRD----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 aTVRMPRT--------MTQKQKmQRVDQVIQDLSLGKCQNTIIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTS 148
Cdd:cd03235 90 -VVLMGLYghkglfrrLSKADK-AKVDEALERVGLSELADRQIG------ELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1151065379 149 GLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSeLFELFDKILLMA 194
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLN 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-196 |
2.25e-27 |
|
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: 107.93 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPV---DAKEMQARCAYV-QQFDLFIGSLtaREHLIF 75
Cdd:COG4987 360 PGERVAIVGPSGSGKSTLLALLLrFLDPQSGSI------TLGGVDLrdlDEDDLRRRIAVVpQRPHLFDTTL--RENLRL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 ---QATvrmPRTMtqKQKMQRV--DQVIQDLSLGkcQNTIIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:COG4987 432 arpDAT---DEEL--WAALERVglGDWLAALPDG--LDTWLGEGGR--RLSGGERRRLALARALLRDAPILLLDEPTEGL 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1151065379 151 DSFMAASVVQVLKKLSQrGKTVILTIHQPSseLFELFDKILLMAEG 196
Cdd:COG4987 503 DAATEQALLADLLEALA-GRTVLLITHRLA--GLERMDRILVLEDG 545
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-196 |
2.28e-27 |
|
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: 101.69 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRmLNGHPV---DAKEMQARCAYVQQfdlfigsltarEHLIFQA 77
Cdd:cd03228 27 PGEKVAIVGPSGSGKSTLLKLLL----RLYDPTSGEIL-IDGVDLrdlDLESLRKNIAYVPQ-----------DPFLFSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVRmprtmtqkqkmqrvdqviqdlslgkcqNTIigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:cd03228 91 TIR---------------------------ENI---------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 158 VVQVLKKLSQrGKTVILTIHQPSSelFELFDKILLMAEG 196
Cdd:cd03228 135 ILEALRALAK-GKTVIVIAHRLST--IRDADRIIVLDDG 170
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
1.80e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 97.58 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FrsargvqISPSSVRM-LNGHPVDAKEMQA---RCAYV-QQFDLFIGslTAREHLI 74
Cdd:COG4619 25 AGECVAITGPSGSGKSTLLRALAdL-------DPPTSGEIyLDGKPLSAMPPPEwrrQVAYVpQEPALWGG--TVRDNLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 FQATVRmprtmTQKQKMQRVDQVIQDLSLGKcqnTIIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 154
Cdd:COG4619 96 FPFQLR-----ERKFDRERALELLERLGLPP---DILDKP--VERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPEN 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1151065379 155 AASVVQVLKKLSQR-GKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:COG4619 166 TRRVEELLREYLAEeGRAVLWVSHDP-EQIERVADRVLTLEAG 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-196 |
3.24e-25 |
|
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: 96.10 E-value: 3.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQ-----ARCAYV-QQFDLFiGSLTAREHLIF 75
Cdd:cd03229 26 GEIVALLGPSGSGKSTLLRCIA-----GLEEPDSGSILIDGEDLTDLEDElpplrRRIGMVfQDFALF-PHLTVLENIAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 qatvrmprtmtqkqkmqrvdqviqdlslgkcqntiigvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 155
Cdd:cd03229 100 -------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 156 ASVVQVLKKLSQR-GKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:cd03229 137 REVRALLKSLQAQlGITVVLVTHDL-DEAARLADRVVVLRDG 177
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-193 |
8.54e-25 |
|
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: 100.44 E-value: 8.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPV---DAKEMQARCAYV-QQFDLFIGSLTArehlif 75
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLgFVDPTEGSIA------VNGVPLadaDADSWRDQIAWVpQHPFLFAGTIAE------ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 qaTVRMPRTMTQKQKMQRV------DQVIQDLSLGkcQNTIIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSG 149
Cdd:TIGR02857 415 --NIRLARPDASDAEIREAleraglDEFVAALPQG--LDTPIGEGGA--GLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1151065379 150 LDSFMAASVVQVLKKLSQrGKTVILTIHQPssELFELFDKILLM 193
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQ-GRTVLLVTHRL--ALAALADRIVVL 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-196 |
2.18e-24 |
|
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: 99.52 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGvQIspssvrMLNGHP---VDAKEMQARCAYV-QQFDLFIGSLtaREHLI 74
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLglYEPTSG-RI------LIDGIDlrqIDPASLRRQIGVVlQDVFLFSGTI--RENIT 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 FQATvrmprTMTQKQ-----KMQRVDQVIQDLSLGKcqNTIIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSG 149
Cdd:COG2274 571 LGDP-----DATDEEiieaaRLAGLHDFIEALPMGY--DTVVGEGGS--NLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1151065379 150 LDSFMAASVVQVLKKLSQrGKTVILTIHQPSseLFELFDKILLMAEG 196
Cdd:COG2274 642 LDAETEAIILENLRRLLK-GRTVIIIAHRLS--TIRLADRIIVLDKG 685
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-196 |
3.59e-24 |
|
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: 95.05 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRmLNGHPVDA------KEMQARCAYVQQFD-LFiGSLTARE 71
Cdd:COG1127 30 RGEILAIIGGSGSGKSVLLKLII-----G-LLRPDSgeIL-VDGQDITGlsekelYELRRRIGMLFQGGaLF-DSLTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HLIFQatVRMPRTMTQKQKMQRVDQVIQDLSLGKCQNTiigVPGRvkgLSGGERKRLAFAsEAL-TDPPLLICDEPTSGL 150
Cdd:COG1127 102 NVAFP--LREHTDLSEAEIRELVLEKLELVGLPGAADK---MPSE---LSGGMRKRVALA-RALaLDPEILLYDEPTAGL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1151065379 151 DSFMAASVVQVLKKLSQR-GKTVILTIHQPSSeLFELFDKILLMAEG 196
Cdd:COG1127 173 DPITSAVIDELIRELRDElGLTSVVVTHDLDS-AFAIADRVAVLADG 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-196 |
3.76e-24 |
|
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: 94.28 E-value: 3.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEM-------QARCAYV-QQFDLFiGSLTAREH 72
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIA-----GLEKPDGGTIVLNGTVLFDSRKkinlppqQRKIGLVfQQYALF-PHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQAtvrmpRTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:cd03297 96 LAFGL-----KRKRNREDRISVDELLDLLGLDHLLNR------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1151065379 153 FMAASVVQVLKKLSQR-GKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:cd03297 165 ALRLQLLPELKQIKKNlNIPVIFVTHDL-SEAEYLADRIVVMEDG 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1-196 |
6.17e-24 |
|
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: 94.49 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLnalafRSARGvQISPSSVRML-NGHPVDA---KEMQA---RCAYV-QQFDLFiGSLTA--- 69
Cdd:cd03261 25 RGEILAIIGPSGSGKSTLL-----RLIVG-LLRPDSGEVLiDGEDISGlseAELYRlrrRMGMLfQSGALF-DSLTVfen 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 70 -----REHLifqatvRMPRTMTQKQKMQRVDQViqdlslgkcqntiiGVPGRVK----GLSGGERKRLAFASEALTDPPL 140
Cdd:cd03261 98 vafplREHT------RLSEEEIREIVLEKLEAV--------------GLRGAEDlypaELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065379 141 LICDEPTSGLDSFMAASVVQVLKKLSQR-GKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHD-LDTAFAIADRIAVLYDG 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-196 |
6.49e-24 |
|
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: 93.80 E-value: 6.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 4 LLAVMGSSGAGKTTLLNALAfrsarGVQiSPSS--VRMlNGHPV--DAKEMQARCAYV-QQFDlFIGSLTAREHLIFQAT 78
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILA-----TLT-PPSSgtIRI-DGQDVlkQPQKLRRRIGYLpQEFG-VYPNFTVREFLDYIAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRmprTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:cd03264 99 LK---GIPSKEVKARVDEVLELVNLGDRAKK------KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRF 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1151065379 159 VQVLKKLSQrGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03264 170 RNLLSELGE-DRIVILSTHI-VEDVESLCNQVAVLNKG 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-196 |
1.33e-23 |
|
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: 93.20 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVR-MLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIFQA 77
Cdd:cd03265 25 RGEIFGLLGPNGAGKTTTIKMLT------TLLKPTSGRaTVAGHDVvrEPREVRRRIGIVFQDLSVDDELTGWENLYIHA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVR-MPRtmtqKQKMQRVDQVIQDLSLGKCQNTIigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:cd03265 99 RLYgVPG----AERRERIDELLDFVGLLEAADRL------VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1151065379 157 SVVQVLKKLSQR-GKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03265 169 HVWEYIEKLKEEfGMTILLTTHY-MEEAEQLCDRVAIIDHG 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-196 |
2.85e-23 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 92.80 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRmLNGHPV---DAKEMQARCAYVQQFDLFIGSLTAREhlif 75
Cdd:COG1120 26 PGEVTALLGPNGSGKSTLLRALA-----G-LLKPSSgeVL-LDGRDLaslSRRELARRIAYVPQEPPAPFGLTVRE---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 qaTVRMPRT-------MTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASeALT-DPPLLICDEPT 147
Cdd:COG1120 95 --LVALGRYphlglfgRPSAEDREAVEEALERTGLEHLADR------PVDELSGGERQRVLIAR-ALAqEPPLLLLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 148 SGLDSFMAASVVQVLKKLSQ-RGKTVILTIHQPssEL-FELFDKILLMAEG 196
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLAReRGRTVVMVLHDL--NLaARYADRLVLLKDG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1-196 |
4.78e-23 |
|
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: 91.16 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGvQISpssvrmLNGHPVDAKEMQARCAYVQQfDLfigsltarEHLIFQAT 78
Cdd:cd03226 25 AGEIIALTGKNGAGKTTLAKILAglIKESSG-SIL------LNGKPIKAKERRKSIGYVMQ-DV--------DYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTQKQ---KMQRVDQVIQDLSLG--KCQNTIIgvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 153
Cdd:cd03226 89 VREELLLGLKEldaGNEQAETVLKDLDLYalKERHPLS--------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1151065379 154 MAASVVQVLKKLSQRGKTVILTIHQPssE-LFELFDKILLMAEG 196
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDY--EfLAKVCDRVLLLANG 202
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1-196 |
1.53e-22 |
|
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: 94.04 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNAL--AFRSARGvqispsSVRmLNGHPVDAKEMQARCAYV----QQFDLFIGSltarehlI 74
Cdd:COG4618 357 PGEVLGVIGPSGSGKSTLARLLvgVWPPTAG------SVR-LDGADLSQWDREELGRHIgylpQDVELFDGT-------I 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 FQATVRMPRTMTQK----QKMQRVDQVIQDLSLGkcQNTIIGVPGRvkGLSGGERKRLAFAsEAL-TDPPLLICDEPTSG 149
Cdd:COG4618 423 AENIARFGDADPEKvvaaAKLAGVHEMILRLPDG--YDTRIGEGGA--RLSGGQRQRIGLA-RALyGDPRLVVLDEPNSN 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1151065379 150 LDSFMAASVVQVLKKLSQRGKTVILTIHQPSseLFELFDKILLMAEG 196
Cdd:COG4618 498 LDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDG 542
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-196 |
3.02e-22 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 89.50 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGvQISpssvrmLNGHPVDAKEMQAR-CAYV-QQFDLFiGSLTAREHLIFQ 76
Cdd:cd03259 25 PGEFLALLGPSGCGKTTLLRLIAglERPDSG-EIL------IDGRDVTGVPPERRnIGMVfQDYALF-PHLTVAENIAFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVR-MPRTMTQKQKMQRVDQVIQDLSLGKcqntiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 155
Cdd:cd03259 97 LKLRgVPKAEIRARVRELLELVGLEGLLNR----------YPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 156 ASVVQVLKKL-SQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:cd03259 167 EELREELKELqRELGITTIYVTHDQ-EEALALADRIAVMNEG 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1-196 |
1.45e-21 |
|
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: 87.66 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRMLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQAT 78
Cdd:cd03268 25 KGEIYGFLGPNGAGKTTTMKIIL-----GL-IKPDSgeITFDGKSYQKNIEALRRIGALIEAPGFYPNLTARENLRLLAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTmtqkqkmQRVDQVIQDLSLGkcqntiiGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:cd03268 99 LLGIRK-------KRIDEVLDVVGLK-------DSAKKkVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKE 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 158 VVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03268 165 LRELILSLRDQGITVLISSHL-LSEIQKVADRIGIINKG 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-196 |
2.04e-21 |
|
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: 87.94 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGvqispsSVRmLNGHPV---DAKEMQARCAYVQQfDLFiGSLTAREHLif 75
Cdd:COG1124 30 PGESFGLVGESGSGKSTLLRALAglERPWSG------EVT-FDGRPVtrrRRKAFRRRVQMVFQ-DPY-ASLHPRHTV-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 QATVRMP-RTMTQKQKMQRVDQVIQDLslgkcqntiiGVPGRVKG-----LSGGERKRLAFASEALTDPPLLICDEPTSG 149
Cdd:COG1124 99 DRILAEPlRIHGLPDREERIAELLEQV----------GLPPSFLDryphqLSGGQRQRVAIARALILEPELLLLDEPTSA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1151065379 150 LDSFMAASVVQVLKKL-SQRGKTVILTIHQPSSELFeLFDKILLMAEG 196
Cdd:COG1124 169 LDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAH-LCDRVAVMQNG 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1-196 |
2.30e-21 |
|
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: 86.34 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPV---DAKEMQARCAYVQQFdlfigsltarehlifq 76
Cdd:cd03214 24 AGEIVGILGPNGAGKSTLLKTLAgLLKPSSGEI------LLDGKDLaslSPKELARKIAYVPQA---------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 atvrmprtmtqkqkMQRVDqvIQDLSlGKCQNTiigvpgrvkgLSGGERKRLAFASeALT-DPPLLICDEPTSGLDSFMA 155
Cdd:cd03214 82 --------------LELLG--LAHLA-DRPFNE----------LSGGERQRVLLAR-ALAqEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 156 ASVVQVLKKLS-QRGKTVILTIHQPSSELfELFDKILLMAEG 196
Cdd:cd03214 134 IELLELLRRLArERGKTVVMVLHDLNLAA-RYADRVILLKDG 174
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1-196 |
6.02e-21 |
|
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: 86.52 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRMlNGHPV---DAKEMQARCAYVQQfDLFIGSLTAREHLIFQA 77
Cdd:cd03251 27 AGETVALVGPSGSGKSTLVNLIP----RFYDVDSGRILI-DGHDVrdyTLASLRRQIGLVSQ-DVFLFNDTVAENIAYGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVRMPRTMTQKQKMQRVDQVIQDLSLGkcQNTIIGVPGrVKgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:cd03251 101 PGATREEVEEAARAANAHEFIMELPEG--YDTVIGERG-VK-LSGGQRQRIAIARALLKDPPILILDEATSALDTESERL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 158 VVQVLKKLSQrGKTVILTIHQPSSelFELFDKILLMAEG 196
Cdd:cd03251 177 VQAALERLMK-NRTTFVIAHRLST--IENADRIVVLEDG 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1-196 |
6.95e-21 |
|
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: 85.66 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLL---NALafrsargVQISPSSVRM----LNGHPVDAKEMQARCAYV-QQFDLFiGSLTAREH 72
Cdd:cd03262 25 KGEVVVIIGPSGSGKSTLLrciNLL-------EEPDSGTIIIdglkLTDDKKNINELRQKVGMVfQQFNLF-PHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIF-QATVR-MPRTMTQKQKMQRVDQViqdlslgkcqntiiGVPGRVKG----LSGGERKRLAFASEALTDPPLLICDEP 146
Cdd:cd03262 97 ITLaPIKVKgMSKAEAEERALELLEKV--------------GLADKADAypaqLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1151065379 147 TSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSselF--ELFDKILLMAEG 196
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMG---FarEVADRVIFMDDG 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-196 |
7.29e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.45 E-value: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPV---DAKEMQARCAYVQQfdlfigsltarEHLIFQ 76
Cdd:COG1132 365 PGETVALVGPSGSGKSTLVNLLLrFYDPTSGRIL------IDGVDIrdlTLESLRRQIGVVPQ-----------DTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVR----MPR-TMTQKQ-----KMQRVDQVIQDLSLGkcQNTIIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEP 146
Cdd:COG1132 428 GTIRenirYGRpDATDEEveeaaKAAQAHEFIEALPDG--YDTVVGERGV--NLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1151065379 147 TSGLDSFMAASVVQVLKKLSqRGKTVILTIHQPSSelFELFDKILLMAEG 196
Cdd:COG1132 504 TSALDTETEALIQEALERLM-KGRTTIVIAHRLST--IRNADRILVLDDG 550
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1-196 |
1.35e-20 |
|
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: 85.33 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHP---VDAKEMQARCAYVQQ-FDLFIGSLtaREHLIF 75
Cdd:cd03245 29 AGEKVAIIGRVGSGKSTLLKLLAgLYKPTSGSV------LLDGTDirqLDPADLRRNIGYVPQdVTLFYGTL--RDNITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 QATVRMPRTMTQKQKMQRVDQVIQDLSLGkcQNTIIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 155
Cdd:cd03245 101 GAPLADDERILRAAELAGVTDFVNKHPNG--LDLQIGERGR--GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1151065379 156 ASVVQVLKKLSqRGKTVILTIHQPSseLFELFDKILLMAEG 196
Cdd:cd03245 177 ERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSG 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-196 |
1.45e-20 |
|
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: 85.52 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALafrSARGVQISPSSVRMLnGHP---VDAKEMQARCAYV--QQFDLFIGSLTAREHLI- 74
Cdd:COG1119 28 PGEHWAILGPNGAGKSTLLSLI---TGDLPPTYGNDVRLF-GERrggEDVWELRKRIGLVspALQLRFPRDETVLDVVLs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 -FQATVRMPRTMTQKQKmQRVDQVIQDLSLGKCQNTIIGvpgrvkGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDS 152
Cdd:COG1119 104 gFFDSIGLYREPTDEQR-ERARELLELLGLAHLADRPFG------TLSQGEQRRVLIA-RALvKDPELLILDEPTAGLDL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1151065379 153 FMAASVVQVLKKLSQRGKTVILTI-HQPsSELFELFDKILLMAEG 196
Cdd:COG1119 176 GARELLLALLDKLAAEGAPTLVLVtHHV-EEIPPGITHVLLLKDG 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-174 |
1.73e-20 |
|
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: 88.04 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRmLNGHPVDA------KEMQARCAYVQQ--FDLFIGSLTAR 70
Cdd:COG1123 290 RGETLGLVGESGSGKSTLARLLL-----GL-LRPTSgsIL-FDGKDLTKlsrrslRELRRRVQMVFQdpYSSLNPRMTVG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 71 EHLIFQATVRmpRTMTQKQKMQRVDQVIQDLSLgkcqntiigvPGRVKG-----LSGGERKRLAFASeAL-TDPPLLICD 144
Cdd:COG1123 363 DIIAEPLRLH--GLLSRAERRERVAELLERVGL----------PPDLADrypheLSGGQRQRVAIAR-ALaLEPKLLILD 429
|
170 180 190
....*....|....*....|....*....|.
gi 1151065379 145 EPTSGLDSFMAASVVQVLKKLSQR-GKTVIL 174
Cdd:COG1123 430 EPTSALDVSVQAQILNLLRDLQRElGLTYLF 460
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1-196 |
1.80e-20 |
|
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: 85.18 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVR-MLNGHPVDAKEMQARCAY-----VQQFDLFiGSLTAREHLI 74
Cdd:cd03219 25 PGEIHGLIGPNGAGKTTLFNLIS-----GF-LRPTSGSvLFDGEDITGLPPHEIARLgigrtFQIPRLF-PELTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 FQATVRMPRTM-------TQKQKMQRVDQVIQDLSLGKCQNTIIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPT 147
Cdd:cd03219 98 VAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAG------ELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1151065379 148 SGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSeLFELFDKILLMAEG 196
Cdd:cd03219 172 AGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQG 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-196 |
2.16e-20 |
|
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: 84.73 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS-VRMLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIFQA 77
Cdd:cd03266 30 PGEVTGLLGPNGAGKTTTLRMLA-----GL-LEPDAgFATVDGFDVvkEPAEARRRLGFVSDSTGLYDRLTARENLEYFA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVRmprTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:cd03266 104 GLY---GLKGDELTARLEELADRLGMEELLDR------RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRA 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 158 VVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03266 175 LREFIRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRG 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-179 |
4.17e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.69 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARGVQISPSsvRMLNGHPVDAKEMQAR-CAYVQQFDLFIGSLTAREHLIFQatv 79
Cdd:COG4136 26 PGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGE--VLLNGRRLTALPAEQRrIGILFQDDLLFPHLSVGENLAFA--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 80 rMPRTMTQKQKMQRVDQVIQDLSLGkcqntiiGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:COG4136 101 -LPPTIGRAQRRARVEQALEEAGLA-------GFADRdPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQF 172
|
170 180
....*....|....*....|..
gi 1151065379 159 VQ-VLKKLSQRGKTVILTIHQP 179
Cdd:COG4136 173 REfVFEQIRQRGIPALLVTHDE 194
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-196 |
7.54e-20 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 86.44 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARGVQISPSSVrmLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATVR 80
Cdd:PLN03140 190 PSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEIT--YNGYRLNEFVPRKTSAYISQNDVHVGVMTVKETLDFSARCQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPRT-------MTQKQK------------------MQRV------DQVIQDLSLGKCQNTIIGvPGRVKGLSGGERKRLA 129
Cdd:PLN03140 268 GVGTrydllseLARREKdagifpeaevdlfmkataMEGVksslitDYTLKILGLDICKDTIVG-DEMIRGISGGQKKRVT 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065379 130 fASEALTDP-PLLICDEPTSGLDSFMAASVVQVLKKLSQRGK-TVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PLN03140 347 -TGEMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILLSEG 414
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1-196 |
1.15e-19 |
|
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: 83.00 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVRMLNGHPVdaKEMQARCAYV-QQFDLfIGSLTAREHLIFQ 76
Cdd:cd03256 26 PGEFVALIGPSGAGKSTLLrclNGLVEPTSGSVLIDGTDINKLKGKAL--RQLRRQIGMIfQQFNL-IERLSVLENVLSG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRMP--RTMTQ---KQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:cd03256 103 RLGRRStwRSLFGlfpKEEKQRALAALERVGLLDKAYQ------RADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1151065379 152 SFMAASVVQVLKKL-SQRGKTVILTIHQPssELF-ELFDKILLMAEG 196
Cdd:cd03256 177 PASSRQVMDLLKRInREEGITVIVSLHQV--DLArEYADRIVGLKDG 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
2-196 |
1.28e-19 |
|
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: 83.98 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVR-MLNGHPV--DAKEMQARCAYV-QQFDLFIGsLTAREHLIFQA 77
Cdd:TIGR01188 19 GEVFGFLGPNGAGKTTTIRMLT------TLLRPTSGTaRVAGYDVvrEPRKVRRSIGIVpQYASVDED-LTGRENLEMMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVR-MPRtmtqKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:TIGR01188 92 RLYgLPK----DEAEERAEELLELFELGEAADR------PVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 157 SVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:TIGR01188 162 AIWDYIRALKEEGVTILLTTHY-MEEADKLCDRIAIIDHG 200
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-193 |
1.52e-19 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 82.52 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSSVRML-NGHPVdaKEMQARCAYVQQFDLFIGSLTAREHLIFQATV 79
Cdd:cd03293 29 EGEFVALVGPSGCGKSTLLRIIA-----G-LERPTSGEVLvDGEPV--TGPGPDRGYVFQQDALLPWLTVLDNVALGLEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 80 R-MPRtmtqKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:cd03293 101 QgVPK----AEARERAEELLELVGLSGFENA------YPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1151065379 159 VQVLKKL-SQRGKTVILTIHQpSSELFELFDKILLM 193
Cdd:cd03293 171 QEELLDIwRETGKTVLLVTHD-IDEAVFLADRVVVL 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-196 |
1.72e-19 |
|
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: 81.94 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAkEMQARCAYVQQFDLFIGSLTAREHLIFQATVR 80
Cdd:cd03269 25 KGEIFGLLGPNGAGKTTTIRMIL-----GIILPDSGEVLFDGKPLDI-AARNRIGYLPEERGLYPKMKVIDQLVYLAQLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 mprTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:cd03269 99 ---GLKKEEARRRIDEWLERLELSEYANK------RVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKD 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1151065379 161 VLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03269 170 VIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKG 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-196 |
3.53e-19 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 84.18 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARGVQISpSSVRmLNGHPVDAKEMQARCAYV----QQFDLFIGSLTAREHLIFq 76
Cdd:COG1123 31 PGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVL-LDGRDLLELSEALRGRRIgmvfQDPMTQLNPVTVGDQIAE- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 atVRMPRTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:COG1123 108 --ALENLGLSRAEARARVLELLEAVGLERRLDR------YPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1151065379 157 SVVQVLKKL-SQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:COG1123 180 EILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDG 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1-196 |
4.69e-19 |
|
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: 79.95 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRmLNGHPV---DAKEMQARCAYVQQFD-LFIGSLTarehli 74
Cdd:cd03246 27 PGESLAIIGPSGSGKSTLARLIL-----GL-LRPTSgrVR-LDGADIsqwDPNELGDHVGYLPQDDeLFSGSIA------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 fqatvrmprtmtqkqkmqrvdqviqdlslgkcQNTiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 154
Cdd:cd03246 94 --------------------------------ENI----------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 155 AASVVQVLKKLSQRGKTVILTIHQPssELFELFDKILLMAEG 196
Cdd:cd03246 132 ERALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDG 171
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-196 |
5.54e-19 |
|
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: 80.59 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsargvqispSSVRMLNGHpvdaKEMQARCAYVQQFDlFIGSLTAREHLIFQATVR 80
Cdd:cd03250 30 KGELVAIVGPVGSGKSSLLSALL-----------GELEKLSGS----VSVPGSIAYVSQEP-WIQNGTIRENILFGKPFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 mprtmtqkqkMQRVDQVI------QDLS-LGKCQNTIIGvpgrVKG--LSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:cd03250 94 ----------EERYEKVIkacalePDLEiLPDGDLTEIG----EKGinLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1151065379 152 SFMAASVVQ-VLKKLSQRGKTVILTIHQPssELFELFDKILLMAEG 196
Cdd:cd03250 160 AHVGRHIFEnCILGLLLNNKTRILVTHQL--QLLPHADQIVVLDNG 203
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-196 |
1.30e-18 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 79.96 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGvQISPSSVrmlNGHPVDAKEMQARCAYVQQfDLFIGSLTAREHLifqat 78
Cdd:cd03254 28 PGETVAIVGPTGAGKTTLINLLMrfYDPQKG-QILIDGI---DIRDISRKSLRSMIGVVLQ-DTFLFSGTIMENI----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 vRMPRTMTQKQKMQRVDQVIQ--DL--SLGKCQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 154
Cdd:cd03254 98 -RLGRPNATDEEVIEAAKEAGahDFimKLPNGYDTVLGENG--GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 155 AASVVQVLKKLSQrGKTVILTIHQPSSELFElfDKILLMAEG 196
Cdd:cd03254 175 EKLIQEALEKLMK-GRTSIIIAHRLSTIKNA--DKILVLDDG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-185 |
1.55e-18 |
|
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: 79.76 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAFRsargvqISPSS-VRMLNGHPVdAKEMQARCAYV--------QQFDLfIGSLTAREH 72
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLIYKE------ELPTSgTIRVNGQDV-SDLRGRAIPYLrrkigvvfQDFRL-LPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQATV-RMPRTMTQKqkmqRVDQVIQDLSLGKCQNTIigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:cd03292 99 VAFALEVtGVPPREIRK----RVPAALELVGLSHKHRAL------PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190
....*....|....*....|....*....|....
gi 1151065379 152 SFMAASVVQVLKKLSQRGKTVILTIHqpSSELFE 185
Cdd:cd03292 169 PDTTWEIMNLLKKINKAGTTVVVATH--AKELVD 200
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-196 |
1.61e-18 |
|
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: 80.22 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLlnalafrsARGVQ--ISPSSVRML-NGHP---VDAKEMQARCAYVQQFD-LFIGSLtaREHL 73
Cdd:cd03252 27 PGEVVGIVGRSGSGKSTL--------TKLIQrfYVPENGRVLvDGHDlalADPAWLRRQVGVVLQENvLFNRSI--RDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 IFQATVRMPRTMTQKQKMQRVDQVIQDLSLGkcQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 153
Cdd:cd03252 97 ALADPGMSMERVIEAAKLAGAHDFISELPEG--YDTIVGEQG--AGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1151065379 154 MAASVVQVLKKLSQrGKTVILTIHQPSSelFELFDKILLMAEG 196
Cdd:cd03252 173 SEHAIMRNMHDICA-GRTVIIIAHRLST--VKNADRIIVMEKG 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-179 |
1.78e-18 |
|
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: 82.41 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQISPSSVRMlngHPVDAKEMQARCAYV-QQFDLFigSLTAREHLIFQAT 78
Cdd:TIGR02868 360 PGERVAILGPSGSGKSTLLATLAgLLDPLQGEVTLDGVPV---SSLDQDEVRRRVSVCaQDAHLF--DTTVRENLRLARP 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTQKQKMQRVDQVIQDLSLGkcQNTIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:TIGR02868 435 DATDEELWAALERVGLADWLRALPDG--LDTVLGEGGAR--LSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
170 180
....*....|....*....|.
gi 1151065379 159 VQVLKKLSQrGKTVILTIHQP 179
Cdd:TIGR02868 511 LEDLLAALS-GRTVVLITHHL 530
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-196 |
2.07e-18 |
|
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: 80.04 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLL---NALafrsargvqISPSSVRML-NGHPV---DAKEMQARCAYV-QQFDLFiGSLTAREHL 73
Cdd:cd03295 27 GEFLVLIGPSGSGKTTTMkmiNRL---------IEPTSGEIFiDGEDIreqDPVELRRKIGYViQQIGLF-PHMTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 ifqATVRMPRTMTQKQKMQRVDQVIQDLSLGkcqntiigvPGRVKG-----LSGGERKRLAFASEALTDPPLLICDEPTS 148
Cdd:cd03295 97 ---ALVPKLLKWPKEKIRERADELLALVGLD---------PAEFADrypheLSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1151065379 149 GLDSFMAASVVQVLKKLSQR-GKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQElGKTIVFVTHD-IDEAFRLADRIAIMKNG 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-196 |
2.34e-18 |
|
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: 80.08 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRmLNGHPVDAKEMQARCAY-----VQQFDLFiGSLTAREHL 73
Cdd:COG0411 29 RGEIVGLIGPNGAGKTTLFNLIT-----GF-YRPTSgrIL-FDGRDITGLPPHRIARLgiartFQNPRLF-PELTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 -----------IFQATVRMPRTMTQKQKM-QRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASeAL-TDPPL 140
Cdd:COG0411 101 lvaaharlgrgLLAALLRLPRARREEREArERAEELLERVGLADRADE------PAGNLSYGQQRRLEIAR-ALaTEPKL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065379 141 LICDEPTSGLDSFMAASVVQVLKKLSQ-RGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDM-DLVMGLADRIVVLDFG 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-196 |
3.08e-18 |
|
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: 78.69 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQAR--CAYVQQFDLFigsltarEHLIFQATV 79
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA-----GFETPQSGRVLINGVDVTAAPPADRpvSMLFQENNLF-------AHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 80 ---RMPRTMTQKQKMQRVDQVIQDLSLGkcqntiiGVPGRVKG-LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 155
Cdd:cd03298 92 glgLSPGLKLTAEDRQAIEVALARVGLA-------GLEKRLPGeLSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 156 ASVVQVLKKL-SQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:cd03298 165 AEMLDLVLDLhAETKMTVLMVTHQP-EDAKRLAQRVVFLDNG 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-196 |
3.20e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.15 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLlnalaFRSARGVqISPSS--VRmLNGHPVDAKEMQArcayvqqfdlfIG----------SLT 68
Cdd:COG4152 26 KGEIFGLLGPNGAGKTTT-----IRIILGI-LAPDSgeVL-WDGEPLDPEDRRR-----------IGylpeerglypKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 69 AREHLIFQATVR-MPRtmtqKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPT 147
Cdd:COG4152 88 VGEQLVYLARLKgLSK----AEAKRRADEWLERLGLGDRANK------KVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1151065379 148 SGLDSFMAASVVQVLKKLSQRGKTVILTIHQ-PSSElfELFDKILLMAEG 196
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELVE--ELCDRIVIINKG 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1-196 |
3.90e-18 |
|
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: 77.74 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVrMLNGHPVDAKEMQARCAyvqqfdlfIGSLTAREHLiFQATVR 80
Cdd:cd03247 27 QGEKIALLGRSGSGKSTLLQLLT----GDLKPQQGEI-TLDGVPVSDLEKALSSL--------ISVLNQRPYL-FDTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 mprtmtqkqkmqrvdqviqdlslgkcQNtiIGVPgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:cd03247 93 --------------------------NN--LGRR-----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 1151065379 161 VLKKLSqRGKTVILTIHQPSSelFELFDKILLMAEG 196
Cdd:cd03247 140 LIFEVL-KDKTLIWITHHLTG--IEHMDKILFLENG 172
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-177 |
5.42e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.85 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVD--AKEMQARCAYVQQFDLFIGSLTAREHL-IF-- 75
Cdd:PRK13537 32 RGECFGLLGPNGAGKTTTLRMLL-----GLTHPDAGSISLCGEPVPsrARHARQRVGVVPQFDNLDPDFTVRENLlVFgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 -------QATVRMPRTMTQKQKMQRVDqviqdlslgkcqntiigvpGRVKGLSGGERKRLAFASEALTDPPLLICDEPTS 148
Cdd:PRK13537 107 yfglsaaAARALVPPLLEFAKLENKAD-------------------AKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180
....*....|....*....|....*....
gi 1151065379 149 GLDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1-196 |
9.05e-18 |
|
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: 78.04 E-value: 9.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNaLAFRSargvqISPSSVRML-NGHP---VDAKEMQARCAYVQQ----FDLFI------GS 66
Cdd:cd03253 26 AGKKVAIVGPSGSGKSTILR-LLFRF-----YDVSSGSILiDGQDireVTLDSLRRAIGVVPQdtvlFNDTIgyniryGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 67 LTAREHLIFQATvrmprtmtqkqKMQRVDQVIQDLSLGkcQNTIIGVPGrVKgLSGGERKRLAFASEALTDPPLLICDEP 146
Cdd:cd03253 100 PDATDEEVIEAA-----------KAAQIHDKIMRFPDG--YDTIVGERG-LK-LSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1151065379 147 TSGLDSFMAASVVQVLKKLSqRGKTVILTIHQPSSELFElfDKILLMAEG 196
Cdd:cd03253 165 TSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNA--DKIIVLKDG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-196 |
9.62e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.79 E-value: 9.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLN--ALAFRSARGvQIspssvrMLNGHPV---DAKEMQA---RCAYV-QQFDLfIGSLTARE 71
Cdd:COG2884 27 KGEFVFLTGPSGAGKSTLLKllYGEERPTSG-QV------LVNGQDLsrlKRREIPYlrrRIGVVfQDFRL-LPDRTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HLIF--QATvrmprTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSG 149
Cdd:COG2884 99 NVALplRVT-----GKSRKEIRRRVREVLDLVGLSDKAKA------LPHELSGGEQQRVAIARALVNRPELLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1151065379 150 LDSFMAASVVQVLKKLSQRGKTVILTIHQPssELFELFDK-ILLMAEG 196
Cdd:COG2884 168 LDPETSWEIMELLEEINRRGTTVLIATHDL--ELVDRMPKrVLELEDG 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-179 |
1.15e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGvqispsSVRmLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQAT 78
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAglLPPAAG------TIK-LDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLEFWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRmprtmtqKQKMQRVDQVIQDLSLGKcqntIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:PRK13539 100 FL-------GGEELDIAAALEAVGLAP----LAHLPFGY--LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|.
gi 1151065379 159 VQVLKKLSQRGKTVILTIHQP 179
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATHIP 187
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1-174 |
1.29e-17 |
|
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: 77.47 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarG-VQISPSSVRmLNGHPVDAKEMQARC----AYVQQFDLFIGSLTAREHLIF 75
Cdd:cd03224 25 EGEIVALLGRNGAGKTTLLKTIM-----GlLPPRSGSIR-FDGRDITGLPPHERAragiGYVPEGRRIFPELTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 QATVRMPRTmtQKQKMQRVDQVIQDLSLGKCQntiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 155
Cdd:cd03224 99 GAYARRRAK--RKARLERVYELFPRLKERRKQ--------LAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
|
170
....*....|....*....
gi 1151065379 156 ASVVQVLKKLSQRGKTVIL 174
Cdd:cd03224 169 EEIFEAIRELRDEGVTILL 187
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-196 |
2.08e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 76.81 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLlnalaFRSARGVqISPSSVRM-LNGHPVDAKEMQARC----AYV-QQFDLFIGsLTAREHLIf 75
Cdd:cd03218 26 GEIVGLLGPNGAGKTTT-----FYMIVGL-VKPDSGKIlLDGQDITKLPMHKRArlgiGYLpQEASIFRK-LTVEENIL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 qATVRMpRTMTQKQKMQRVDQVIQDLSLGKCQNTiigvPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 155
Cdd:cd03218 98 -AVLEI-RGLSKKEREEKLEELLEEFHITHLRKS----KAS--SLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1151065379 156 ASVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03218 170 QDIQKIIKILKDRGIGVLITDHN-VRETLSITDRAYIIYEG 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-177 |
2.94e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNA-LAFRSARGVQISPSSVRMlnghPVDAKEMQARCAYVQQFDLFIGSLTAREHLI-FQAT 78
Cdd:PRK13536 66 SGECFGLLGPNGAGKSTIARMiLGMTSPDAGKITVLGVPV----PARARLARARIGVVPQFDNLDLEFTVRENLLvFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMprtmtqkqKMQRVDQVIQDL-SLGKCQNTiigVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:PRK13536 142 FGM--------STREIEAVIPSLlEFARLESK---ADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180
....*....|....*....|
gi 1151065379 158 VVQVLKKLSQRGKTVILTIH 177
Cdd:PRK13536 211 IWERLRSLLARGKTILLTTH 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-196 |
3.64e-17 |
|
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: 76.47 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVRMLNGHPVdaKEMQARCAYV-QQFDLFiGSLTAREHlifq 76
Cdd:cd03258 30 KGEIFGIIGRSGAGKSTLIrciNGLERPTSGSVLVDGTDLTLLSGKEL--RKARRRIGMIfQHFNLL-SSRTVFEN---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 atVRMPRTMTQKQKMQRVDQVIQDLSLgkcqntiIGVPGRVKG----LSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:cd03258 103 --VALPLEIAGVPKAEIEERVLELLEL-------VGLEDKADAypaqLSGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1151065379 153 FMAASVVQVLKKLSQR-GKTVILTIHQPSSeLFELFDKILLMAEG 196
Cdd:cd03258 174 ETTQSILALLRDINRElGLTIVLITHEMEV-VKRICDRVAVMEKG 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1-179 |
6.79e-17 |
|
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: 75.09 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNG--HPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQAT 78
Cdd:TIGR01189 25 AGEALQVTGPNGIGKTTLLRILA-----GLLRPDSGEVRWNGtpLAEQRDEPHENILYLGHLPGLKPELSALENLHFWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTqkqkmqrVDQVIQDLSLGKCQNTIigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:TIGR01189 100 IHGGAQRT-------IEDALAAVGLTGFEDLP------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|.
gi 1151065379 159 VQVLKKLSQRGKTVILTIHQP 179
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-179 |
7.19e-17 |
|
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: 74.84 E-value: 7.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAK--EMQARCAYVQQFDLFIGSLTAREHLIFQATV 79
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILA-----GLSPPLAGRVLLNGGPLDFQrdSIARGLLYLGHAPGIKTTLSVLENLRFWHAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 80 RMPRTmtqkqkmqrVDQVIQDLSLGKCQNTIIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 159
Cdd:cd03231 101 HSDEQ---------VEEALARVGLNGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170 180
....*....|....*....|
gi 1151065379 160 QVLKKLSQRGKTVILTIHQP 179
Cdd:cd03231 166 EAMAGHCARGGMVVLTTHQD 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-196 |
1.04e-16 |
|
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: 74.01 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPVDAKEMQARcayvqqFDLFIGSLTA--REHLIFQa 77
Cdd:cd03215 25 AGEIVGIAGLVGNGQTELAEALFgLRPPASGEIT------LDGKPVTRRSPRDA------IRAGIAYVPEdrKREGLVL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 tvrmprtmtqkqkmqrvdqviqDLSLGkcQNTIIGVpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:cd03215 92 ----------------------DLSVA--ENIALSS-----LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 158 VVQVLKKLSQRGKTVILTihqpSSELFELF---DKILLMAEG 196
Cdd:cd03215 143 IYRLIRELADAGKAVLLI----SSELDELLglcDRILVMYEG 180
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-177 |
1.60e-16 |
|
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: 74.46 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRmLNGHPV---DAKEMQARCAYVQqfdlFI-----GSL----T 68
Cdd:cd03257 30 KGETLGLVGESGSGKSTLARAIL----GLLKPTSGSII-FDGKDLlklSRRLRKIRRKEIQ----MVfqdpmSSLnprmT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 69 AREHLIfqATVRMPRTMTQKQKMQRVdqVIQDLSLgkcqntiIGVPGRVKG-----LSGGERKRLAFASEALTDPPLLIC 143
Cdd:cd03257 101 IGEQIA--EPLRIHGKLSKKEARKEA--VLLLLVG-------VGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLIA 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1151065379 144 DEPTSGLDSFMAASVVQVLKKL-SQRGKTVILTIH 177
Cdd:cd03257 170 DEPTSALDVSVQAQILDLLKKLqEELGLTLLFITH 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-178 |
2.01e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.05 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfRSARGVQISPSSVRMLnGHPV--------DAKEMQARCAYV-QQFDLfIGSLTAREH 72
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLS-GLITGDKSAGSHIELL-GRTVqregrlarDIRKSRANTGYIfQQFNL-VNRLSVLEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQATVRMP------RTMTQKQKmQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEP 146
Cdd:PRK09984 107 VLIGALGSTPfwrtcfSWFTREQK-QRALQALTRVGMVHFAHQ------RVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190
....*....|....*....|....*....|...
gi 1151065379 147 TSGLDSFMAASVVQVLKKLSQR-GKTVILTIHQ 178
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNdGITVVVTLHQ 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-196 |
2.48e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.02 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRmLNGHPVDA-KEMQARCAyvqqfdlfIGSLTAREHlIFQATV 79
Cdd:PRK11160 365 AGEKVALLGRTGCGKSTLLQLLT----RAWDPQQGEIL-LNGQPIADySEAALRQA--------ISVVSQRVH-LFSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 80 RMPRTMTQKQKM-QRVDQVIQDLSLGKCQ------NTIIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:PRK11160 431 RDNLLLAAPNASdEALIEVLQQVGLEKLLeddkglNAWLGEGGR--QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1151065379 153 FMAASVVQVLKKLSQrGKTVILTIHQpsseLFEL--FDKILLMAEG 196
Cdd:PRK11160 509 ETERQILELLAEHAQ-NKTVLMITHR----LTGLeqFDRICVMDNG 549
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-196 |
2.48e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 74.36 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRmLNGHPVDAKemQARCAYV-QQFDLFigsLTAREHLIFQA 77
Cdd:COG1116 36 AGEFVALVGPSGCGKSTLLRLIA-----G-LEKPTSgeVL-VDGKPVTGP--GPDRGVVfQEPALLp-wLTVLDNVALGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVR-MPRtmtqKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDSFMA 155
Cdd:COG1116 106 ELRgVPK----AERRERARELLELVGLAGFEDA------YPHQLSGGMRQRVAIA-RALaNDPEVLLMDEPFGALDALTR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 156 ASVVQVLKKL-SQRGKTVILTIHQPSSELFeLFDKILLMAEG 196
Cdd:COG1116 175 ERLQDELLRLwQETGKTVLFVTHDVDEAVF-LADRVVVLSAR 215
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-196 |
3.11e-16 |
|
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: 73.54 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQARCA-------YVQQFDLFIGSLTAREHl 73
Cdd:TIGR02211 30 KGEIVAIVGSSGSGKSTLLHLLG-----GLDNPTSGEVLFNGQSLSKLSSNERAKlrnkklgFIYQFHHLLPDFTALEN- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 ifqatVRMP---RTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:TIGR02211 104 -----VAMPlliGKKSVKEAKERAYEMLEKVGLEHRINH------RPSELSGGERQRVAIARALVNQPSLVLADEPTGNL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1151065379 151 DSFMAASVVQVLKKLSQRGKT-VILTIHQPssELFELFDKILLMAEG 196
Cdd:TIGR02211 173 DNNNAKIIFDLMLELNRELNTsFLVVTHDL--ELAKKLDRVLEMKDG 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-176 |
4.24e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 73.70 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQARCA-------YVQQFDLFIGSLTAREHl 73
Cdd:PRK11629 34 EGEMMAIVGSSGSGKSTLLHLLG-----GLDTPTSGDVIFNGQPMSKLSSAAKAElrnqklgFIYQFHHLLPDFTALEN- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 ifqatVRMPRTMTQK---QKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:PRK11629 108 -----VAMPLLIGKKkpaEINSRALEMLAAVGLEHRANH------RPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180
....*....|....*....|....*.
gi 1151065379 151 DSFMAASVVQVLKKLSQRGKTVILTI 176
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTAFLVV 202
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-196 |
6.39e-16 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 72.85 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQIsPSS--VRmLNGHPVDAKEMQARCA-------YVQQ-FDLfIGSLTAR 70
Cdd:COG4181 37 AGESVAIVGASGSGKSTLLGLLA-----GLDR-PTSgtVR-LAGQDLFALDEDARARlrarhvgFVFQsFQL-LPTLTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 71 EHlifqatVRMPRTMT-QKQKMQRVDQVIQDLSLGKcqntiigvpgRV----KGLSGGERKRLAFASEALTDPPLLICDE 145
Cdd:COG4181 109 EN------VMLPLELAgRRDARARARALLERVGLGH----------RLdhypAQLSGGEQQRVALARAFATEPAILFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1151065379 146 PTSGLDSFMAASVVQVLKKL-SQRGKTVILTIHQPssELFELFDKILLMAEG 196
Cdd:COG4181 173 PTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDP--ALAARCDRVLRLRAG 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1-196 |
8.56e-16 |
|
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: 72.50 E-value: 8.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQaRCAYVQQFDLFiGSLTAREHlIFQATVR 80
Cdd:TIGR01184 10 QGEFISLIGHSGCGKSTLLNLIS-----GLAQPTSGGVILEGKQITEPGPD-RMVVFQNYSLL-PWLTVREN-IALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPRTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALVGLTEAADK------RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1151065379 161 VLKKLSQR-GKTVILTIHQPSSELFeLFDKILLMAEG 196
Cdd:TIGR01184 156 ELMQIWEEhRVTVLMVTHDVDEALL-LSDRVVMLTNG 191
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-179 |
9.24e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 9.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPVDAkemqARCAYVQQFdLFIG-------SLTAREH 72
Cdd:PRK13538 26 AGELVQIEGPNGAGKTSLLRILAgLARPDAGEVL------WQGEPIRR----QRDEYHQDL-LYLGhqpgiktELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQATVRMPrtmtqkqkmQRVDQVIQdlSLGKcqntiIGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDEPTS 148
Cdd:PRK13538 95 LRFYQRLHGP---------GDDEALWE--ALAQ-----VGLAGFedvpVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|....
gi 1151065379 149 GLDsfmAASVVQVLKKLSQ---RGKTVILTIHQP 179
Cdd:PRK13538 159 AID---KQGVARLEALLAQhaeQGGMVILTTHQD 189
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-196 |
1.55e-15 |
|
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: 71.79 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRMlnghpvdakEMQARCAYVqqFDL---FIGSLTAREHLIFQAT 78
Cdd:cd03220 48 GERIGLIGRNGAGKSTLLRLLA-----GI-YPPDSGTV---------TVRGRVSSL--LGLgggFNPELTGRENIYLNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VrmpRTMTQKQKMQRVDQvIQDLS-LGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:cd03220 111 L---LGLSRKEIDEKIDE-IIEFSeLGDFIDL------PVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 158 VVQVLKKLSQRGKTVILTIHQPSSeLFELFDKILLMAEG 196
Cdd:cd03220 181 CQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKG 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1-196 |
1.61e-15 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 73.22 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PG-ELLAVMGSSGAGKTTLLNALA-----------------FRSARGVQISPSsvrmlnghpvdakemQARCAYV-QQFD 61
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAgltrpdegeivlngrtlFDSRKGIFLPPE---------------KRRIGYVfQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 62 LFiGSLTAREHLIFQATVRMPrtmtqKQKMQRVDQVIQDLSLGkcqNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLL 141
Cdd:TIGR02142 86 LF-PHLSVRGNLRYGMKRARP-----SERRISFERVIELLGIG---HLLGRLPGR---LSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1151065379 142 ICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-175 |
2.50e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNAL-AFRSARGVQISPSSVRMLNGHPVDAKEMQARCAYV----QQFDLFiGSLTAREHLIfQ 76
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLnLLEMPRSGTLNIAGNHFDFSKTPSDKAIRELRRNVgmvfQQYNLW-PHLTVQQNLI-E 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRMpRTMTQKQKMQRVDQVIQDLSLGKCQNTIigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:PRK11124 106 APCRV-LGLSKDQALARAEKLLERLRLKPYADRF---PLH---LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
|
170 180
....*....|....*....|
gi 1151065379 157 SVVQVLKKLSQRGKT-VILT 175
Cdd:PRK11124 179 QIVSIIRELAETGITqVIVT 198
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-196 |
3.31e-15 |
|
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: 71.21 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVR-MLNGhpVDAKEM---QARCAYV-QQFDLFiGSLTAREHLIFq 76
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIA-----GF-IKPDSGKiLLNG--KDITNLppeKRDISYVpQNYALF-PHMTVYKNIAY- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 aTVRMpRTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:cd03299 95 -GLKK-RKVDKKEIERKVLEIAEMLGIDHLLNR------KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 157 SVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-196 |
4.05e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.57 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNA-LAFRSARGvqispsSVRmLNGHP---VDAKEMQARCAYV-QQFDLFIGSLtaREHLIF 75
Cdd:PRK11174 375 AGQRIALVGPSGAGKTSLLNAlLGFLPYQG------SLK-INGIElreLDPESWRKHLSWVgQNPQLPHGTL--RDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 QATvrmprTMTQKQKMQ-----RVDQVIQDLSLGkcQNTIIGvpGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:PRK11174 446 GNP-----DASDEQLQQalenaWVSEFLPLLPQG--LDTPIG--DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1151065379 151 DSFMAASVVQVLKKLSQrGKTVILTIHQpsseLFEL--FDKILLMAEG 196
Cdd:PRK11174 517 DAHSEQLVMQALNAASR-RQTTLMVTHQ----LEDLaqWDQIWVMQDG 559
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-196 |
4.85e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.96 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGvqispsSVRmLNGHPVD---AKEMQARCAyV--QQFDL-FigSLTAREh 72
Cdd:PRK13548 27 PGEVVAILGPNGAGKSTLLRALSgeLSPDSG------EVR-LNGRPLAdwsPAELARRRA-VlpQHSSLsF--PFTVEE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 lifqaTVRM---PRTMTQKQKMQRVDQVIQ--DLSlgkcqntiiGVPGR-VKGLSGGERKRLAFA------SEALTDPPL 140
Cdd:PRK13548 96 -----VVAMgraPHGLSRAEDDALVAAALAqvDLA---------HLAGRdYPQLSGGEQQRVQLArvlaqlWEPDGPPRW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065379 141 LICDEPTSGLDSFMAASVVQVLKKL-SQRGKTVILTIHQPSseLFELF-DKILLMAEG 196
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLN--LAARYaDRIVLLHQG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-196 |
6.17e-15 |
|
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: 72.35 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTllnalAFRSARGVQISPSSVRMLNGHPV--DAKEMQARCAYVQQFDLFIGSLTAREHLIFQAT 78
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTT-----TFKMLTGDTTVTSGDATVAGKSIltNISDVHQNMGYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VR-MPrtmtqKQKMQRV-DQVIQDLSLGKCQNTIIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:TIGR01257 2039 LRgVP-----AEEIEKVaNWSIQSLGLSLYADRLAGT------YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 157 SVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:TIGR01257 2108 MLWNTIVSIIREGRAVVLTSHS-MEECEALCTRLAIMVKG 2146
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-178 |
8.43e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.12 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVrmlNGHPVDAKEMQARCAYV-QQFDLFiGSLTAREHLIFQ 76
Cdd:PRK09493 26 QGEVVVIIGPSGSGKSTLLrciNKLEEITSGDLIVDGLKV---NDPKVDERLIRQEAGMVfQQFYLF-PHLTALENVMFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 AT-VR-MPRTMTQKQKMQRVDQViqdlslgkcqntiiGVPGRV----KGLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:PRK09493 102 PLrVRgASKEEAEKQARELLAKV--------------GLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180
....*....|....*....|....*...
gi 1151065379 151 DSFMAASVVQVLKKLSQRGKTVILTIHQ 178
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-177 |
9.61e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTL---LNALAFRSARGVQ-----------------------ISPSSVRMLNghpvDAKEMQARCA 55
Cdd:PRK13651 33 GEFIAIIGQTGSGKTTFiehLNALLLPDTGTIEwifkdeknkkktkekekvleklvIQKTRFKKIK----KIKEIRRRVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 56 YVQQFdlfigsltaREHLIFQATVRM-----PRTM--TQKQKMQRVDQVIQdlslgkcqntIIGVPGRVK-----GLSGG 123
Cdd:PRK13651 109 VVFQF---------AEYQLFEQTIEKdiifgPVSMgvSKEEAKKRAAKYIE----------LVGLDESYLqrspfELSGG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1151065379 124 ERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
1.19e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.89 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FrsargvqISPSSVR-MLNGHPVDAKEmqARCAYVQQFDLFIGSLTAREHLIFQAT 78
Cdd:COG4525 32 SGEFVVALGASGCGKTTLLNLIAgF-------LAPSSGEiTLDGVPVTGPG--ADRGVVFQKDALLPWLNVLDNVAFGLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VR-MPRtmtqKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFAsEALT-DPPLLICDEPTSGLDSFMAA 156
Cdd:COG4525 103 LRgVPK----AERRARAEELLALVGLADFARR------RIWQLSGGMRQRVGIA-RALAaDPRFLLMDEPFGALDALTRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1151065379 157 SVVQVLKKLSQR-GKTVILTIHQPSSELFeLFDKILLMAEG 196
Cdd:COG4525 172 QMQELLLDVWQRtGKGVFLITHSVEEALF-LATRLVVMSPG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-196 |
1.36e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 70.51 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FrsargvqISPSSVR-MLNGHPVDAKEMQAR-CAYV-QQFDLFiGSLTAREHLIFQ 76
Cdd:COG3842 30 PGEFVALLGPSGCGKTTLLRMIAgF-------ETPDSGRiLLDGRDVTGLPPEKRnVGMVfQDYALF-PHLTVAENVAFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVR-MPRtmtqKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDSFM 154
Cdd:COG3842 102 LRMRgVPK----AEIRARVAELLELVGLEGLADR------YPHQLSGGQQQRVALA-RALaPEPRVLLLDEPLSALDAKL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1151065379 155 AASVVQVLKKLSQR-GKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:COG3842 171 REEMREELRRLQRElGITFIYVTHDQ-EEALALADRIAVMNDG 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-179 |
1.74e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQARCA-------YVQQFDLFIGSLTAREHl 73
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILA-----GLDDGSSGEVSLVGQPLHQMDEEARAKlrakhvgFVFQSFMLIPTLNALEN- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 ifqatVRMP---RTMTQKQKMQRVDQVIQDLSLGKcqnTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:PRK10584 109 -----VELPallRGESSRQSRNGAKALLEQLGLGK---RLDHLPAQ---LSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180 190
....*....|....*....|....*....|
gi 1151065379 151 DSFMAASVVQVLKKLSQR-GKTVILTIHQP 179
Cdd:PRK10584 178 DRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2-196 |
1.91e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.64 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLnalafRSARGVqISPS--SVRmLNGHPV---DAKEMQARCAYVQQFDLFIGSLTARehlifq 76
Cdd:PRK09536 29 GSLVGLVGPNGAGKTTLL-----RAINGT-LTPTagTVL-VAGDDVealSARAASRRVASVPQDTSLSFEFDVR------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRMPRT--MTQKQKMQRVDQVIQDLSLGKCQNTIIgVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 154
Cdd:PRK09536 96 QVVEMGRTphRSRFDTWTETDRAAVERAMERTGVAQF-ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1151065379 155 AASVVQVLKKLSQRGKTVILTIHqpSSELFELF-DKILLMAEG 196
Cdd:PRK09536 175 QVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADG 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-196 |
2.18e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 68.63 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPVDAKEMQARCAYV--QQFDLFiGSLTAREHLIFQA 77
Cdd:COG3840 24 AGERVAILGPSGAGKSTLLNLIAgFLPPDSGRIL------WNGQDLTALPPAERPVSMlfQENNLF-PHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVRMPRTMTQKqkmQRVDQVIQDLSLGKCQNTIigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:COG3840 97 RPGLKLTAEQR---AQVEQALERVGLAGLLDRL---PGQ---LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 158 VVQVLKKL-SQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:COG3840 168 MLDLVDELcRERGLTVLMVTHDP-EDAARIADRVLLVADG 206
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
2-177 |
2.74e-14 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 67.83 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVD-----AKEMQARCAYVQQfdlfigsltAREHLIFQ 76
Cdd:TIGR01166 18 GEVLALLGANGAGKSTLLLHLN-----GLLRPQSGAVLIDGEPLDysrkgLLERRQRVGLVFQ---------DPDDQLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRM-----PRTM--TQKQKMQRVDQVIQDLSLGKCQNTIIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSG 149
Cdd:TIGR01166 84 ADVDQdvafgPLNLglSEAEVERRVREALTAVGASGLRERPTHC------LSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180
....*....|....*....|....*...
gi 1151065379 150 LDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1-196 |
4.07e-14 |
|
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: 67.55 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSarGVQISPSSVRmLNGHPVDAKEMQARcayvqqfdlfigsltARE--HLIFQAT 78
Cdd:cd03217 25 KGEVHALMGPNGSGKSTLAKTIMGHP--KYEVTEGEIL-FKGEDITDLPPEER---------------ARLgiFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPrtmtqkqkMQRVDQVIQDLSlgkcqntiigvpgrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:cd03217 87 PEIP--------GVKNADFLRYVN---------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 159 VQVLKKLSQRGKTVILTIHQPssELFELF--DKILLMAEG 196
Cdd:cd03217 144 AEVINKLREEGKSVLIITHYQ--RLLDYIkpDRVHVLYDG 181
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-177 |
4.19e-14 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 67.98 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARGVQISPSSVRMLNGHPV-----DAKEMQARCAYV-QQFDLFIGSLtarehli 74
Cdd:cd03260 25 KGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIydldvDVLELRRRVGMVfQKPNPFPGSI------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 fQATVRMPRTMTQKQKMQRVDQVIQDlSLGKcqntiIGVPGRVK------GLSGGERKRLAFASEALTDPPLLICDEPTS 148
Cdd:cd03260 98 -YDNVAYGLRLHGIKLKEELDERVEE-ALRK-----AALWDEVKdrlhalGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180
....*....|....*....|....*....
gi 1151065379 149 GLDSFMAASVVQVLKKLSQRgKTVILTIH 177
Cdd:cd03260 171 ALDPISTAKIEELIAELKKE-YTIVIVTH 198
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-178 |
4.30e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.46 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAF---RSARGVQISPSSVRMlnghpVDAKEMQARCAYVQQFDLFIGSLTarehLIFQAt 78
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFlekPSEGSIVVNGQTINL-----VRDKDGQLKVADKNQLRLLRTRLT----MVFQH- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTQKQKMqrVDQVIQDLSLGKCQN--------TIIGVPGRVKG-----LSGGERKRLAFASEALTDPPLLICDE 145
Cdd:PRK10619 101 FNLWSHMTVLENV--MEAPIQVLGLSKQEAreravkylAKVGIDERAQGkypvhLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190
....*....|....*....|....*....|...
gi 1151065379 146 PTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQ 178
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-177 |
4.68e-14 |
|
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: 68.13 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRMLNGHPVDAKEmqarcAYVQQFDLFIGS-------LTAREH 72
Cdd:cd03267 47 GEIVGFIGPNGAGKTTTLKILS-----GL-LQPTSgeVRVAGLVPWKRRK-----KFLRRIGVVFGQktqlwwdLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQATV-RMPRTMTQKqkmqRVDQVIQDLSLGKcqntIIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:cd03267 116 FYLLAAIyDLPPARFKK----RLDELSELLDLEE----LLDTP--VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180
....*....|....*....|....*..
gi 1151065379 152 SFMAASVVQVLKKLS-QRGKTVILTIH 177
Cdd:cd03267 186 VVAQENIRNFLKEYNrERGTTVLLTSH 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-179 |
7.46e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.98 E-value: 7.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALafrsarGVQISPSS-VRMLNGHPVDAKEMQARCAYVQQFDLFIgslTAREHLIFQAT- 78
Cdd:PRK10535 33 AGEMVAIVGASGSGKSTLMNIL------GCLDKPTSgTYRVAGQDVATLDADALAQLRREHFGFI---FQRYHLLSHLTa 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 ---VRMPRT---MTQKQKMQRVDQVIQDLSLGKcqntiiGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:PRK10535 104 aqnVEVPAVyagLERKQRLLRAQELLQRLGLED------RVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180
....*....|....*....|....*..
gi 1151065379 153 FMAASVVQVLKKLSQRGKTVILTIHQP 179
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-174 |
7.56e-14 |
|
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: 67.31 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarG-VQISPSSVRmLNGHPVDAKEMQARC----AYVQQ----FdlfiGSLTARE 71
Cdd:COG0410 28 EGEIVALLGRNGAGKTTLLKAIS-----GlLPPRSGSIR-FDGEDITGLPPHRIArlgiGYVPEgrriF----PSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HLIFQATVRMPRTmTQKQKMQRVDQVIQDLSlgkcqnTIIGVPGRVkgLSGGERKRLAFASeAL-TDPPLLICDEPTSGL 150
Cdd:COG0410 98 NLLLGAYARRDRA-EVRADLERVYELFPRLK------ERRRQRAGT--LSGGEQQMLAIGR-ALmSRPKLLLLDEPSLGL 167
|
170 180
....*....|....*....|....
gi 1151065379 151 DSFMAASVVQVLKKLSQRGKTVIL 174
Cdd:COG0410 168 APLIVEEIFEIIRRLNREGVTILL 191
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-196 |
8.54e-14 |
|
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: 67.36 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQAR-CAYV-QQFDLFiGSLTAREHLIFQAT 78
Cdd:cd03296 27 SGELVALLGPSGSGKTTLLRLIA-----GLERPDSGTILFGGEDATDVPVQERnVGFVfQHYALF-RHMTVFDNVAFGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTQKQKM-QRVDQVIQDLSLGKCQNTIigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:cd03296 101 VKPRSERPPEAEIrAKVHELLKLVQLDWLADRY---PAQ---LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 158 VVQVLKKLSQR-GKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03296 175 LRRWLRRLHDElHVTTVFVTHD-QEEALEVADRVVVMNKG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-178 |
9.85e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 9.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVRMLNghPVDAKEMQARCAYV----QQFDLFiGSLTAREHL 73
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLrvlNLLETPDSGQLNIAGHQFDFSQ--KPSEKAIRLLRQKVgmvfQQYNLW-PHLTVMENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 IfQATVRMPRtMTQKQKMQRVDQVIQDLSLgkcQNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 153
Cdd:COG4161 104 I-EAPCKVLG-LSKEQAREKAMKLLARLRL---TDKADRFPLH---LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180
....*....|....*....|....*
gi 1151065379 154 MAASVVQVLKKLSQRGKTVILTIHQ 178
Cdd:COG4161 176 ITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-196 |
1.36e-13 |
|
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: 66.51 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRML-NGHPVDAKEMQAR-CAYV-QQFDLFiGSLTAREHLIFQAT 78
Cdd:cd03301 26 GEFVVLLGPSGCGKTTTLRMIA-----GL-EEPTSGRIYiGGRDVTDLPPKDRdIAMVfQNYALY-PHMTVYDNIAFGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VR-MPRTMTQKqkmqRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:cd03301 99 LRkVPKDEIDE----RVREVAELLQIEHLLDR------KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 158 VVQVLKKLSQR-GKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03301 169 MRAELKRLQQRlGTTTIYVTHD-QVEAMTMADRIAVMNDG 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-196 |
2.14e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGVQISPSSVRMLnghpvdakemqarcaYV-QQFDLFIGSLtaREHLIFQA 77
Cdd:COG4178 388 PGERLLITGPSGSGKSTLLRAIAglWPYGSGRIARPAGARVL---------------FLpQRPYLPLGTL--REALLYPA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TvrmPRTMTQkqkmQRVDQVIQDLSLGKcqntiigVPGRV-------KGLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:COG4178 451 T---AEAFSD----AELREALEAVGLGH-------LAERLdeeadwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1151065379 151 DsfmAASVVQVLKKLSQR--GKTVILTIHQPSseLFELFDKILLMAEG 196
Cdd:COG4178 517 D---EENEAALYQLLREElpGTTVISVGHRST--LAAFHDRVLELTGD 559
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-196 |
2.44e-13 |
|
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: 67.73 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 3 ELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAK--EMQARCAYVQQFDLFIGSLTAREHLIFQATVR 80
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILT-----GLLPPTSGTVLVGGKDIETNldAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 mprTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:TIGR01257 1032 ---GRSWEEAQLEMEAMLEDTGLHHKRNE------EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190
....*....|....*....|....*....|....*.
gi 1151065379 161 VLKKLsQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:TIGR01257 1103 LLLKY-RSGRTIIMSTHH-MDEADLLGDRIAIISQG 1136
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-196 |
2.53e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 66.26 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRMlNGhpvdakemqaRCAYVqqFDL---FIGSLTAREHLIF 75
Cdd:COG1134 51 RGESVGIIGRNGAGKSTLLKLIA-----GI-LEPTSgrVEV-NG----------RVSAL--LELgagFHPELTGRENIYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 QATVrmpRTMTQKQKMQRVDQVIqDLS-LGKCqntiIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTS-GLDSF 153
Cdd:COG1134 112 NGRL---LGLSRKEIDEKFDEIV-EFAeLGDF----IDQP--VKTYSSGMRARLAFAVATAVDPDILLVDEVLAvGDAAF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1151065379 154 MAASvVQVLKKLSQRGKTVILTIHQPSSeLFELFDKILLMAEG 196
Cdd:COG1134 182 QKKC-LARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKG 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2-196 |
2.91e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLlnALAFRSARGVQISPSSVRMLN-GHPVDAKEMQARCAYVQQF--DLFIGSlTAREHLIF-QA 77
Cdd:PRK13644 28 GEYIGIIGKNGSGKSTL--ALHLNGLLRPQKGKVLVSGIDtGDFSKLQGIRKLVGIVFQNpeTQFVGR-TVEEDLAFgPE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVRMPRTMTQKqkmqRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:PRK13644 105 NLCLPPIEIRK----RVDRALAEIGLEKYRHR------SPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 158 VVQVLKKLSQRGKTVILTIHqpSSELFELFDKILLMAEG 196
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-193 |
3.15e-13 |
|
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: 64.37 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRM-LNGHPVDakemqarcayvqqfdlFIGSLTAREH---LIFQ 76
Cdd:cd03216 25 RGEVHALLGENGAGKSTLMKILS-----GL-YKPDSGEIlVDGKEVS----------------FASPRDARRAgiaMVYQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 atvrmprtmtqkqkmqrvdqviqdlslgkcqntiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 1151065379 157 SVVQVLKKLSQRGKTVILTIHQPsSELFELFDKILLM 193
Cdd:cd03216 120 RLFKVIRRLRAQGVAVIFISHRL-DEVFEIADRVTVL 155
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-177 |
3.26e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.65 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS--VRMLNGHPVdaKEmqaRCAYVQQFDLFIGS-------LTARE 71
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLT-----GI-LVPTSgeVRVLGYVPF--KR---RKEFARRIGVVFGQrsqlwwdLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HL-IFQATVRMPRtmtqKQKMQRVDQVIQDLSLGKcqntIIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:COG4586 116 SFrLLKAIYRIPD----AEYKKRLDELVELLDLGE----LLDTP--VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180
....*....|....*....|....*...
gi 1151065379 151 DSFMAASVVQVLKKLSQ-RGKTVILTIH 177
Cdd:COG4586 186 DVVSKEAIREFLKEYNReRGTTILLTSH 213
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-196 |
3.84e-13 |
|
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: 65.37 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTllnalAFRSARGVqISPSSVRM-LNGHPVDAKEMQARC----AYVQQFDLFIGSLTAREHLIfq 76
Cdd:TIGR04406 27 GEIVGLLGPNGAGKTT-----SFYMIVGL-VRPDAGKIlIDGQDITHLPMHERArlgiGYLPQEASIFRKLTVEENIM-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRMPRTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:TIGR04406 99 AVLEIRKDLDRAEREERLEALLEEFQISHLRDN------KAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 157 SVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:TIGR04406 173 DIKKIIKHLKERGIGVLITDHN-VRETLDICDRAYIISDG 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-196 |
5.10e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 66.25 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRML-NGHPVDAKEMQAR-CAYV-QQFDLFiGSLTAREHLIFQA 77
Cdd:COG3839 28 DGEFLVLLGPSGCGKSTLLRMIA-----GL-EDPTSGEILiGGRDVTDLPPKDRnIAMVfQSYALY-PHMTVYENIAFPL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVR-MPRtmtqKQKMQRVDQV-----IQDLsLGKcqntiigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGL 150
Cdd:COG3839 101 KLRkVPK----AEIDRRVREAaellgLEDL-LDR----------KPKQLSGGQRQRVALG-RALvREPKVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1151065379 151 DsfmAASVVQV---LKKLSQR-GKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:COG3839 165 D---AKLRVEMraeIKRLHRRlGTTTIYVTHDQ-VEAMTLADRIAVMNDG 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-196 |
5.17e-13 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 65.18 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPV---DAKEMQARCAYV-QQFDLFIGSLtaREHLIF 75
Cdd:cd03248 39 PGEVTALVGPSGSGKSTVVALLEnFYQPQGGQV------LLDGKPIsqyEHKYLHSKVSLVgQEPVLFARSL--QDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 -QATVRMPRTMTQKQKMQrVDQVIQDLSLGkcQNTIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 154
Cdd:cd03248 111 gLQSCSFECVKEAAQKAH-AHSFISELASG--YDTEVGEKGSQ--LSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 155 AASVVQVLKKLSQRgKTVILTIHQPSseLFELFDKILLMAEG 196
Cdd:cd03248 186 EQQVQQALYDWPER-RTVLVIAHRLS--TVERADQILVLDGG 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-196 |
5.75e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.59 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 5 LAVMGSSGAGKTTLlnalaFRSARGVqISPSSVRML-NGHPVDAKEMQARCAYV----QQFDLFIGSLTAREHLIFQATV 79
Cdd:PRK13652 33 IAVIGPNGAGKSTL-----FRHFNGI-LKPTSGSVLiRGEPITKENIREVRKFVglvfQNPDDQIFSPTVEQDIAFGPIN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 80 RMPRTMTQKQkmqRVDQVIQDLSLGKCQNTiigVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 159
Cdd:PRK13652 107 LGLDEETVAH---RVSSALHMLGLEELRDR---VPHH---LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1151065379 160 QVLKKLSQR-GKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK13652 178 DFLNDLPETyGMTVIFSTHQ-LDLVPEMADYIYVMDKG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2-196 |
7.23e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 65.10 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLlnalaFRSARGVQISPSSVRMLNGHPV--DAK---EMQARCAYV-QQFDLFIGSLTAREHLIF 75
Cdd:PRK13639 28 GEMVALLGPNGAGKSTL-----FLHFNGILKPTSGEVLIKGEPIkyDKKsllEVRKTVGIVfQNPDDQLFAPTVEEDVAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 qATVRMPRTMTQKQKmqRVDQVIQDLSLGKCQNTiigVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 155
Cdd:PRK13639 103 -GPLNLGLSKEEVEK--RVKEALKAVGMEGFENK---PPHH---LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 156 ASVVQVLKKLSQRGKTVILTIHQpsSELFELF-DKILLMAEG 196
Cdd:PRK13639 174 SQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDG 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-196 |
8.35e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNAL--AFRSARGvqispsSVRmLNGHPVDAKE----MQARCAYV----QQFDLFIGsLTAR 70
Cdd:COG1129 277 AGEILGIAGLVGAGRTELARALfgADPADSG------EIR-LDGKPVRIRSprdaIRAGIAYVpedrKGEGLVLD-LSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 71 EHLIFQATVRMPRT--MTQKQKMQRVDQVIQDLSLgKCQNtiIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTS 148
Cdd:COG1129 349 ENITLASLDRLSRGglLDRRRERALAEEYIKRLRI-KTPS--PEQP--VGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065379 149 GLDsfmaasvV-------QVLKKLSQRGKTVILTihqpSSELFELF---DKILLMAEG 196
Cdd:COG1129 424 GID-------VgakaeiyRLIRELAAEGKAVIVI----SSELPELLglsDRILVMREG 470
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-196 |
1.15e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.43 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVrMLNGHPVDAKEMQA---RCAYV-QQFDLFIGSLT-------- 68
Cdd:PRK11176 368 AGKTVALVGRSGSGKSTIANLLT----RFYDIDEGEI-LLDGHDLRDYTLASlrnQVALVsQNVHLFNDTIAnniayart 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 69 ---AREHLIFQAtvRMPRTMTQKQKMqrvDQVIqdlslgkcqNTIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDE 145
Cdd:PRK11176 443 eqySREQIEEAA--RMAYAMDFINKM---DNGL---------DTVIGENGVL--LSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 146 PTSGLDSFMAASVVQVLKKLsQRGKTVILTIHQPSSelFELFDKILLMAEG 196
Cdd:PRK11176 507 ATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEKADEILVVEDG 554
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-192 |
2.41e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.57 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKemQARCAYVQQFDlfiGSLTAREhliFQATVR 80
Cdd:PRK11248 26 SGELLVVLGPSGCGKTTLLNLIA-----GFVPYQHGSITLDGKPVEGP--GAERGVVFQNE---GLLPWRN---VQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPRTMTQKQKMQRVDQVIQDLSLgkcqntiIGVPG----RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:PRK11248 93 FGLQLAGVEKMQRLEIAHQMLKK-------VGLEGaekrYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1151065379 157 SVVQVLKKLSQR-GKTVILTIHQPSSELFELFDKILL 192
Cdd:PRK11248 166 QMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLL 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-196 |
2.42e-12 |
|
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: 64.35 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGvQISpssvrmLNGHP-VDAKEMQA------RCAYV-QQFDLFigsltar 70
Cdd:COG4148 24 GRGVTALFGPSGSGKTTLLRAIAglERPDSG-RIR------LGGEVlQDSARGIFlpphrrRIGYVfQEARLF------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 71 EHLifqaTVR------MPRTMTQKQKmQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICD 144
Cdd:COG4148 90 PHL----SVRgnllygRKRAPRAERR-ISFDEVVELLGIGHLLDR------RPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1151065379 145 EPTSGLDSFMAASVVQVLKKLSQRGKTVILTI-HQPsSELFELFDKILLMAEG 196
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDELDIPILYVsHSL-DEVARLADHVVLLEQG 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1-196 |
2.48e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.60 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNAL--AFRSARG-VQISPSSVRMLNghpvdAKEMQARCAYV-QQFDLFIGSLtaREHLifq 76
Cdd:PRK13657 360 PGQTVAIVGPTGAGKSTLINLLqrVFDPQSGrILIDGTDIRTVT-----RASLRRNIAVVfQDAGLFNRSI--EDNI--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 atvRMPRTMTQKQKMQRVDQVIQ--DLSLGK--CQNTIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:PRK13657 430 ---RVGRPDATDEEMRAAAERAQahDFIERKpdGYDTVVGERGRQ--LSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1151065379 153 FMAASVVQVLKKLSQrGKTVILTIHQPSSelFELFDKILLMAEG 196
Cdd:PRK13657 505 ETEAKVKAALDELMK-GRTTFIIAHRLST--VRNADRILVFDNG 545
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-178 |
3.35e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.94 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLL---NALAfrsargvqiSPSS--VRmLNGHPV---DAKEMQA---RCAYV-QQFDLFiGSLT 68
Cdd:COG1135 30 KGEIFGIIGYSGAGKSTLIrciNLLE---------RPTSgsVL-VDGVDLtalSERELRAarrKIGMIfQHFNLL-SSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 69 AREHLIF---QAtvRMPRtmtqKQKMQRVDQVIQdlslgkcqntIIGVPGRVKG----LSGGERKRLAFAsEAL-TDPPL 140
Cdd:COG1135 99 VAENVALpleIA--GVPK----AEIRKRVAELLE----------LVGLSDKADAypsqLSGGQKQRVGIA-RALaNNPKV 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 141 LICDEPTSGLDSFMAASVVQVLKKLSQR-GKTVILTIHQ 178
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHE 200
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-180 |
3.58e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.23 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFR------SARGVQISPSSVRMLNGHPVDAKEMQARCAYV-QQFDLFiGSLTAREHL 73
Cdd:PRK11264 28 PGEVVAIIGPSGSGKTTLLRCINLLeqpeagTIRVGDITIDTARSLSQQKGLIRQLRQHVGFVfQNFNLF-PHRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 IFQATV--RMPRtmtqKQKMQRVDQVIQDLSLGKCQNTiigVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:PRK11264 107 IEGPVIvkGEPK----EEATARARELLAKVGLAGKETS---YPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180
....*....|....*....|....*....
gi 1151065379 152 SFMAASVVQVLKKLSQRGKTVILTIHQPS 180
Cdd:PRK11264 177 PELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
119-196 |
5.34e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 5.34e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065379 119 GLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSELfELFDKILLMAEG 196
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKG 252
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-177 |
6.57e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.97 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLlnalaFRSARGVqISPSSVR-MLNGHPVDAKEMQARC----AYVQQ----FdlfiGSLTARE 71
Cdd:COG1137 28 QGEIVGLLGPNGAGKTTT-----FYMIVGL-VKPDSGRiFLDGEDITHLPMHKRArlgiGYLPQeasiF----RKLTVED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HLifQATVRMpRTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgrvKG--LSGGERKRLAFAsEAL-TDPPLLICDEPTS 148
Cdd:COG1137 98 NI--LAVLEL-RKLSKKEREERLEELLEEFGITHLRKS--------KAysLSGGERRRVEIA-RALaTNPKFILLDEPFA 165
|
170 180
....*....|....*....|....*....
gi 1151065379 149 GLDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:COG1137 166 GVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-174 |
7.04e-12 |
|
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: 62.76 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfRSARGVQISPSSVRmLNGHPV---DAKEMQA----RCAYVQQfDLFiGSL----TA 69
Cdd:COG0444 30 RGETLGLVGESGSGKSTLARAIL-GLLPPPGITSGEIL-FDGEDLlklSEKELRKirgrEIQMIFQ-DPM-TSLnpvmTV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 70 REHLIfqATVRMPRTMTQKQKMQRVDQVIQDLSlgkcqntiIGVPGRVKG-----LSGGERKRLAFASeAL-TDPPLLIC 143
Cdd:COG0444 106 GDQIA--EPLRIHGGLSKAEARERAIELLERVG--------LPDPERRLDrypheLSGGMRQRVMIAR-ALaLEPKLLIA 174
|
170 180 190
....*....|....*....|....*....|..
gi 1151065379 144 DEPTSGLDSFMAASVVQVLKKL-SQRGKTVIL 174
Cdd:COG0444 175 DEPTTALDVTIQAQILNLLKDLqRELGLAILF 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-196 |
9.22e-12 |
|
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: 61.89 E-value: 9.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVrMLNGHPV---DAKEMQA----RCAYV-QQFDLFiGSLTAREH 72
Cdd:cd03294 49 EGEIFVIMGLSGSGKSTLLRCIN----RLIEPTSGKV-LIDGQDIaamSRKELRElrrkKISMVfQSFALL-PHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQATVR-MPRtmtqKQKMQRVDQVIQDLSLGKCQNTIIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:cd03294 123 VAFGLEVQgVPR----AEREERAAEALELVGLEGWEHKYPD------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1151065379 152 SFMAASVVQVLKKL-SQRGKTVILTIHQPsSELFELFDKILLMAEG 196
Cdd:cd03294 193 PLIRREMQDELLRLqAELQKTIVFITHDL-DEALRLGDRIAIMKDG 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-177 |
1.17e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.45 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTT---LLNALAFRSARGVQISPSSVRMLnghPVDAKEMQArCAYVQQFDLFIGSLTAREHLIfqAT 78
Cdd:PRK10895 29 GEIVGLLGPNGAGKTTtfyMVVGIVPRDAGNIIIDDEDISLL---PLHARARRG-IGYLPQEASIFRRLSVYDNLM--AV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTQKQKMQRVDQVIQDLSLGKCQNTIigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:PRK10895 103 LQIRDDLSAEQREDRANELMEEFHIEHLRDSM------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
170
....*....|....*....
gi 1151065379 159 VQVLKKLSQRGKTVILTIH 177
Cdd:PRK10895 177 KRIIEHLRDSGLGVLITDH 195
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-177 |
1.26e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.57 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsaRgvQISPSSVR-MLNGHPV---DAKEMQARCAYVQQFDLFIGSLTAREhLIfq 76
Cdd:PRK11231 27 TGKITALIGPNGCGKSTLLKCFA----R--LLTPQSGTvFLGDKPIsmlSSRQLARRLALLPQHHLTPEGITVRE-LV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRMPRT-----MTQKQKmQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:PRK11231 98 AYGRSPWLslwgrLSAEDN-ARVNQAMEQTRINHLADR------RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180
....*....|....*....|....*.
gi 1151065379 152 SFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:PRK11231 171 INHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-196 |
1.28e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNAL--AFRSARGvqispsSVRmLNGHPVDAKEMQ----ARCAYVQQfD-----LFIG----- 65
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLygALPRTSG------YVT-LDGHEVVTRSPQdglaNGIVYISE-DrkrdgLVLGmsvke 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 66 --SLTAREHLIfqatvRMPRTMTQKQKMQRVDQVIQDLSlgkcqntiIGVPGR---VKGLSGGERKRLAFASEALTDPPL 140
Cdd:PRK10762 350 nmSLTALRYFS-----RAGGSLKHADEQQAVSDFIRLFN--------IKTPSMeqaIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065379 141 LICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTihqpSSELFELF---DKILLMAEG 196
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILV----SSEMPEVLgmsDRILVMHEG 471
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-151 |
1.47e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTT-------LLNAlafrsargvqiSPSSVRMLnGHPVDAKEMQAR--CAYVQQ-FDLFiGSLTARE 71
Cdd:NF033858 292 GEIFGFLGSNGCGKSTtmkmltgLLPA-----------SEGEAWLF-GQPVDAGDIATRrrVGYMSQaFSLY-GELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HLIFQATV-RMPRtmtqKQKMQRVDQVIQDLSLGKCQNTiigVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:NF033858 359 NLELHARLfHLPA----AEIAARVAEMLERFDLADVADA---LPDS---LPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
.
gi 1151065379 151 D 151
Cdd:NF033858 429 D 429
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-151 |
1.74e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.63 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGvQISpssvrmLNGHPVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQAT 78
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAglLHVESG-QIQ------IDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCG 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065379 79 V--RMPRTMTQKQKmqrvdqviqdlslgkcqnTIIGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:PRK13543 109 LhgRRAKQMPGSAL------------------AIVGLAGYedtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-196 |
2.14e-11 |
|
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: 61.76 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNAL--AFRSARGVQIspssvrMLNGHPVD----AKEMQARCAYV---QQFDLFIGSLTAREH 72
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALfgAYPGKFEGNV------FINGKPVDirnpAQAIRAGIAMVpedRKRHGIVPILGVGKN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQATVRMPRTMT--QKQKMQRVDQVIQDLSLGKCQNTIigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:TIGR02633 360 ITLSVLKSFCFKMRidAAAELQIIGSAIQRLKVKTASPFL-----PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1151065379 151 DSFMAASVVQVLKKLSQRGKTVILTihqpSSELFE---LFDKILLMAEG 196
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEGVAIIVV----SSELAEvlgLSDRVLVIGEG 479
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-168 |
2.17e-11 |
|
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: 61.62 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALafrsargVQISPSSVRM-LNGHPVDA---KEMQARCAYVQ---QfDLFiGSLTAR--- 70
Cdd:COG4172 311 RGETLGLVGESGSGKSTLGLAL-------LRLIPSEGEIrFDGQDLDGlsrRALRPLRRRMQvvfQ-DPF-GSLSPRmtv 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 71 -----EHLIFQAtvrmpRTMTQKQKMQRVDQVIQDlslgkcqntiIGVPGRVKG-----LSGGERKRLAFAsEAL-TDPP 139
Cdd:COG4172 382 gqiiaEGLRVHG-----PGLSAAERRARVAEALEE----------VGLDPAARHrypheFSGGQRQRIAIA-RALiLEPK 445
|
170 180
....*....|....*....|....*....
gi 1151065379 140 LLICDEPTSGLDSFMAASVVQVLKKLSQR 168
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLQRE 474
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-196 |
2.37e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAFrsargvQISPSSVRMLnghpvdakEMQARCAYVQQFDlFIGSLTAREHLIFQATVRM 81
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLG------ELSHAETSSV--------VIRGSVAYVPQVS-WIFNATVRENILFGSDFES 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 PRTMtqkqKMQRVDQVIQDLSLGKCQN-TIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:PLN03232 708 ERYW----RAIDVTALQHDLDLLPGRDlTEIGERG--VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
170 180 190
....*....|....*....|....*....|....*.
gi 1151065379 161 VLKKLSQRGKTVILTIHQpsSELFELFDKILLMAEG 196
Cdd:PLN03232 782 SCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEG 815
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-196 |
2.38e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 61.66 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPV---DAKEMQARCAYVQQFD-LFIGSLtaREHLIF 75
Cdd:TIGR00958 506 PGEVVALVGPSGSGKSTVAALLQnLYQPTGGQV------LLDGVPLvqyDHHYLHRQVALVGQEPvLFSGSV--RENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 QATVRMPRTMTQKQKMQRVDQVIQDLSLGkcQNTIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfma 155
Cdd:TIGR00958 578 GLTDTPDEEIMAAAKAANAHDFIMEFPNG--YDTEVGEKGSQ--LSGGQKQRIAIARALVRKPRVLILDEATSALD---- 649
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 156 ASVVQVLKKL-SQRGKTVILTIHQPSseLFELFDKILLMAEG 196
Cdd:TIGR00958 650 AECEQLLQESrSRASRTVLLIAHRLS--TVERADQILVLKKG 689
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-151 |
2.61e-11 |
|
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: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSSVRMLNGHPVdakemqaRCAYV-QQFDLFIGSLTAREHLifqatv 79
Cdd:COG0488 340 RGDRIGLIGPNGAGKSTLLKLLA-----G-ELEPDSGTVKLGETV-------KIGYFdQHQEELDPDKTVLDEL------ 400
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065379 80 rmpRTMTQKQKMQRVDQVIQDLSL-GKCQNTIIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:COG0488 401 ---RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGV------LSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-196 |
3.70e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.89 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRM-LNGHPVDAKEMQAR--CAYVQQFDLFigsltarEHLIFQAT 78
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVA-----GLE-KPTEGQIfIDGEDVTHRSIQQRdiCMVFQSYALF-------PHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTQKQKMQRVDQVIQDLSLGKcqntIIGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEALELVD----LAGFEDRyVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 158 VVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PRK11432 175 MREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-196 |
4.10e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAFRSAR--------GVQISPSSvrmlnghPVDA--KEMqarcAYV---QQFDLFIGSLT 68
Cdd:PRK09700 289 GEILGFAGLVGSGRTELMNCLFGVDKRaggeirlnGKDISPRS-------PLDAvkKGM----AYItesRRDNGFFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 69 AREHLIFQATVRMPR------TMTQKQKMQRVDQVIQDLSLgKCQNtiigVPGRVKGLSGGERKRLAFASEALTDPPLLI 142
Cdd:PRK09700 358 IAQNMAISRSLKDGGykgamgLFHEVDEQRTAENQRELLAL-KCHS----VNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065379 143 CDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTihqpSSELFELF---DKILLMAEG 196
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEG 485
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1-196 |
4.16e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 59.94 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRMLnghpVDAKEMQARCAYVQQFDLFIGSLTAREHLIFQATVR 80
Cdd:cd03300 25 EGEFFTLLGPSGCGKTTLLRLIA-----GFE-TPTSGEIL----LDGKDITNLPPHKRPVNTVFQNYALFPHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPRTMTQKQKM---QRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:cd03300 95 FGLRLKKLPKAeikERVAEALDLVQLEGYANR------KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 158 VVQVLKKLSQR-GKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:cd03300 169 MQLELKRLQKElGITFVFVTHD-QEEALTMSDRIAVMNKG 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1-179 |
4.73e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 59.17 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRMlnghpvdAKEMQARCAYVQQfdlfIGSLTARehliFQATVR 80
Cdd:NF040873 17 AGSLTAVVGPNGSGKSTLLKVLA-----GV-LRPTSGTV-------RRAGGARVAYVPQ----RSEVPDS----LPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPRTMTQKQK------MQRVDQVIQDLSLGKCQntIIGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 153
Cdd:NF040873 76 DLVAMGRWARrglwrrLTRDDRAAVDDALERVG--LADLAGRqLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180
....*....|....*....|....*.
gi 1151065379 154 MAASVVQVLKKLSQRGKTVILTIHQP 179
Cdd:NF040873 154 SRERIIALLAEEHARGATVVVVTHDL 179
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-196 |
5.97e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.86 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALafrsaRGVqISPSSVRML-NGHPVDAKE---MQARCAYVQQFDlfigsltAREHLIFQA 77
Cdd:PRK13636 32 GEVTAILGGNGAGKSTLFQNL-----NGI-LKPSSGRILfDGKPIDYSRkglMKLRESVGMVFQ-------DPDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVR-------MPRTMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:PRK13636 99 SVYqdvsfgaVNLKLPEDEVRKRVDNALKRTGIEHLKDK------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1151065379 151 DSFMAASVVQVLKKLSQR-GKTVILTIHqpSSELFELF-DKILLMAEG 196
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKElGLTIIIATH--DIDIVPLYcDNVFVMKEG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-151 |
6.08e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.46 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGvQISPSS--VRMLNGhpvdakemqARCAYVQQFDLFIGSLTAREHlIFQAT 78
Cdd:COG0488 23 PGDRIGLVGRNGAGKSTLLKILA-----G-ELEPDSgeVSIPKG---------LRIGYLPQEPPLDDDLTVLDT-VLDGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTQKQK-MQRVDQVIQDLS-LGKCQNTI------------------IGVPG-----RVKGLSGGERKRLAFASE 133
Cdd:COG0488 87 AELRALEAELEElEAKLAEPDEDLErLAELQEEFealggweaearaeeilsgLGFPEedldrPVSELSGGWRRRVALARA 166
|
170
....*....|....*...
gi 1151065379 134 ALTDPPLLICDEPTSGLD 151
Cdd:COG0488 167 LLSEPDLLLLDEPTNHLD 184
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-196 |
6.40e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.10 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHpvDAKEMQARCAYV----QQFDLFiGSLTAREHLIFQA 77
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIA-----GLEHQTSGHIRFHGT--DVSRLHARDRKVgfvfQHYALF-RHMTVFDNIAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TV----RMPRTMTQKQKMQRVDQVIQdlsLGKCQNTIigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 153
Cdd:PRK10851 100 TVlprrERPNAAAIKAKVTQLLEMVQ---LAHLADRY---PAQ---LSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1151065379 154 MAASVVQVLKKLSQRGK--TVILTIHQpsSELFELFDKILLMAEG 196
Cdd:PRK10851 171 VRKELRRWLRQLHEELKftSVFVTHDQ--EEAMEVADRVVVMSQG 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-177 |
1.07e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.03 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALafrsarGVQISPSSVR-MLNGHPV---DAKEMQARCAYVQQfdlfigSLTAREHLIFQ 76
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKML------GRHQPPSEGEiLLDAQPLeswSSKAFARKVAYLPQ------QLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRMPRTMTQ-------KQKMQRVDQVIQDLSLGKCQNTIigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSG 149
Cdd:PRK10575 104 ELVAIGRYPWHgalgrfgAADREKVEEAISLVGLKPLAHRL------VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180
....*....|....*....|....*....
gi 1151065379 150 LDSFMAASVVQVLKKLSQ-RGKTVILTIH 177
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQeRGLTVIAVLH 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-179 |
1.11e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.77 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSS-VR---MLNGHPV---DAKEMQARCAYVQQFDLFIGSLTAREHL 73
Cdd:PRK14247 28 DNTITALMGPSGSGKSTLLRVFN----RLIELYPEArVSgevYLDGQDIfkmDVIELRRRVQMVFQIPNPIPNLSIFENV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 IFqaTVRMPRTMTQKQKMQ-RVDQVIQDLSLGKCQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:PRK14247 104 AL--GLKLNRLVKSKKELQeRVRWALEKAQLWDEVKDRLDAPA--GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDP 179
|
170 180
....*....|....*....|....*..
gi 1151065379 153 FMAASVVQVLKKLsQRGKTVILTIHQP 179
Cdd:PRK14247 180 ENTAKIESLFLEL-KKDMTIVLVTHFP 205
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1-181 |
1.22e-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: 58.71 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPV---DAKEMQARCAYVQQF-DLFIGSLtaREHLIF 75
Cdd:cd03249 28 PGKTVALVGSSGCGKSTVVSLLErFYDPTSGEI------LLDGVDIrdlNLRWLRSQIGLVSQEpVLFDGTI--AENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 QATvrmPRTMTQKQKMQRV---DQVIQDLSLGkcQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDs 152
Cdd:cd03249 100 GKP---DATDEEVEEAAKKaniHDFIMSLPDG--YDTLVGERG--SQLSGGQKQRIAIARALLRNPKILLLDEATSALD- 171
|
170 180 190
....*....|....*....|....*....|.
gi 1151065379 153 fmAASVVQVLKKLSQ--RGKTVILTIHQPSS 181
Cdd:cd03249 172 --AESEKLVQEALDRamKGRTTIVIAHRLST 200
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-196 |
1.29e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNA----LAFRSARGVQIspssvrmlnghpvdakemQARCAYVQQFDlFIGSLTAREHLIFQ 76
Cdd:PLN03130 642 VGSLVAIVGSTGEGKTSLISAmlgeLPPRSDASVVI------------------RGTVAYVPQVS-WIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRMPRTmtqkQKMQRVDQVIQDLSL--GKCQnTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFM 154
Cdd:PLN03130 703 SPFDPERY----ERAIDVTALQHDLDLlpGGDL-TEIGERG--VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 155 AASVVQVLKKLSQRGKTVILTIHQpsSELFELFDKILLMAEG 196
Cdd:PLN03130 776 GRQVFDKCIKDELRGKTRVLVTNQ--LHFLSQVDRIILVHEG 815
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
6-196 |
1.50e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.12 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 6 AVMGSSGAGKTTLLNALAfrsarGVqISPSSVRM-LNGHP-VDAKEM------QARCAYVQQfdlfigsltarEHLIF-Q 76
Cdd:PRK11144 28 AIFGRSGAGKTSLINAIS-----GL-TRPQKGRIvLNGRVlFDAEKGiclppeKRRIGYVFQ-----------DARLFpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVR------MPRTMTQKqkmqrVDQVIQDLSLGKCQNTIigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:PRK11144 91 YKVRgnlrygMAKSMVAQ-----FDKIVALLGIEPLLDRY---PGS---LSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1151065379 151 DSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-174 |
1.54e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRML-NGHPV------DAkeMQARCAYVQQ-FDLFiGSLTAREH 72
Cdd:COG3845 30 PGEIHALLGENGAGKSTLMKILY-----GLY-QPDSGEILiDGKPVrirsprDA--IALGIGMVHQhFMLV-PNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIfqatVRMPRTMTQKQKMQRVDQVIQDLS--LGkcqntiIGVP--GRVKGLSGGERKRLafasE---AL-TDPPLLICD 144
Cdd:COG3845 101 IV----LGLEPTKGGRLDRKAARARIRELSerYG------LDVDpdAKVEDLSVGEQQRV----EilkALyRGARILILD 166
|
170 180 190
....*....|....*....|....*....|....*
gi 1151065379 145 EPTSGL-----DSFMAasvvqVLKKLSQRGKTVIL 174
Cdd:COG3845 167 EPTAVLtpqeaDELFE-----ILRRLAAEGKSIIF 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-196 |
3.17e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNAL-AFRSARGVQIspssvrMLNGHPVDAKEMQARCA----YV----QQFDLF-------- 63
Cdd:PRK15439 288 AGEILGLAGVVGAGRTELAETLyGLRPARGGRI------MLNGKEINALSTAQRLArglvYLpedrQSSGLYldaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 64 IGSLTAREHLIFQATVRMPRTMTQKQ-----KMQRVDQViqdlslgkcqntiigvpgrVKGLSGGERKRLAFASEALTDP 138
Cdd:PRK15439 362 VCALTHNRRGFWIKPARENAVLERYRralniKFNHAEQA-------------------ARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 139 PLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTihqpSSELFE---LFDKILLMAEG 196
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQG 479
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
117-191 |
3.49e-10 |
|
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: 56.21 E-value: 3.49e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065379 117 VKGLSGGERKR----LAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPssELFELFDKIL 191
Cdd:cd03227 75 RLQLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-179 |
4.10e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLnalafrsargvqispssvRMLNGhpvdakemQARCAYVQ-QFDLFIGSLTAREHLIFQatv 79
Cdd:COG2401 55 PGEIVLIVGASGSGKSTLL------------------RLLAG--------ALKGTPVAgCVDVPDNQFGREASLIDA--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 80 rMPRTMTQKQKMQRVDQV-IQDLSLGKcqntiigvpGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:COG2401 106 -IGRKGDFKDAVELLNAVgLSDAVLWL---------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|..
gi 1151065379 159 VQVLKKLSQR-GKTVILTIHQP 179
Cdd:COG2401 176 ARNLQKLARRaGITLVVATHHY 197
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-173 |
4.63e-10 |
|
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: 56.67 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALaFRSARgvqisPSSVRML---NGHPVDAKEMQAR---------CAYVQQFdlfigsLT 68
Cdd:COG4778 36 AGECVALTGPSGAGKSTLLKCI-YGNYL-----PDSGSILvrhDGGWVDLAQASPReilalrrrtIGYVSQF------LR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 69 ArehlifqatvrMPRTMTqkqkmqrVDQVIQDL-----SLGKCQN------TIIGVPGRVKGL-----SGGERKRLAFAS 132
Cdd:COG4778 104 V-----------IPRVSA-------LDVVAEPLlergvDREEARArarellARLNLPERLWDLppatfSGGEQQRVNIAR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1151065379 133 EALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVI 173
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1-191 |
5.28e-10 |
|
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: 55.62 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGVQISPSSVRMLnghpvdakemqarcaYVQQFDLF-IGSLtaREHLIFqa 77
Cdd:cd03223 26 PGDRLLITGPSGTGKSSLFRALAglWPWGSGRIGMPEGEDLL---------------FLPQRPYLpLGTL--REQLIY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 tvrmprtmtqkqkmqrvdqviqdlslgkcqntiigvP-GRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:cd03223 87 ------------------------------------PwDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190
....*....|....*....|....*....|....*
gi 1151065379 157 SVVQVLKklsQRGKTVILTIHQPSseLFELFDKIL 191
Cdd:cd03223 129 RLYQLLK---ELGITVISVGHRPS--LWKFHDRVL 158
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1-196 |
7.24e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.39 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVrMLNGHPVDAKEMQA---RCAYVQQFDLFIGSLTAREHLifqa 77
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMA-----GLLPGQGEI-LLNGRPLSDWSAAElarHRAYLSQQQSPPFAMPVFQYL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVRMPRTMTQKQKMQRVDQVIQDLSLGKcqntiiGVPGRVKGLSGGE--RKRLAFA-----SEALTDPPLLICDEPTSGL 150
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLAEALGLED------KLSRPLTQLSGGEwqRVRLAAVllqvwPTINPEGQLLLLDEPMNSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1151065379 151 DSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELfDKILLMAEG 196
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQG 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-196 |
9.25e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.26 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsargvqispSSVRMLNGHpvdaKEMQARCAYVQQfDLFIGSLTAREHLIFQATVRM 81
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALL-----------AEMDKVEGH----VHMKGSVAYVPQ-QAWIQNDSLRENILFGKALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 PRtmtQKQKMQRVdQVIQDLS-LGKCQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:TIGR00957 728 KY---YQQVLEAC-ALLPDLEiLPSGDRTEIGEKG--VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180 190
....*....|....*....|....*....|....*...
gi 1151065379 161 --VLKKLSQRGKTVILTIHQPSseLFELFDKILLMAEG 196
Cdd:TIGR00957 802 hvIGPEGVLKNKTRILVTHGIS--YLPQVDVIIVMSGG 837
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-168 |
1.04e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGK-TTLLNALAFRSARGvQIspssvrMLNGHPVDAKEMQARCAYVQQFDLFI----GSLTAR---EH 72
Cdd:PRK15134 311 PGETLGLVGESGSGKsTTGLALLRLINSQG-EI------WFDGQPLHNLNRRQLLPVRHRIQVVFqdpnSSLNPRlnvLQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQATVRMPRTMTQKQKMQRVDQVIQDLSLGKcqNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:PRK15134 384 IIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDP--ETRHRYPAE---FSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
|
170
....*....|....*.
gi 1151065379 153 FMAASVVQVLKKLSQR 168
Cdd:PRK15134 459 TVQAQILALLKSLQQK 474
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
2-196 |
1.12e-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: 56.40 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAFrsargvQISPSSVRMlnghpvdakEMQARCAYVQQFDlFIGSLTAREHLIFQATVRM 81
Cdd:cd03291 63 GEMLAITGSTGSGKTSLLMLILG------ELEPSEGKI---------KHSGRISFSSQFS-WIMPGTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 PRTMTqkqkMQRVDQVIQDLS-LGKCQNTIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:cd03291 127 YRYKS----VVKACQLEEDITkFPEKDNTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
170 180 190
....*....|....*....|....*....|....*...
gi 1151065379 161 --VLKKLSQrgKTVILTIHQpsSELFELFDKILLMAEG 196
Cdd:cd03291 201 scVCKLMAN--KTRILVTSK--MEHLKKADKILILHEG 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-193 |
1.19e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.64 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRMLNGHPVDAKEMQARcayvqqfdlfigslTARE--HLIFQ--- 76
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAII----GLVKATDGEVAWLGKDLLGMKDDEWR--------------AVRSdiQMIFQdpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATV--RMP---------RT----MTQKQKMQRVDQVIqdLSLGKCQNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLL 141
Cdd:PRK15079 109 ASLnpRMTigeiiaeplRTyhpkLSRQEVKDRVKAMM--LKVGLLPNLINRYPHE---FSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1151065379 142 ICDEPTSGLDSFMAASVVQVLKKLsQR--GKTVILTIHQPSSeLFELFDKILLM 193
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQL-QRemGLSLIFIAHDLAV-VKHISDRVLVM 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-196 |
1.29e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGV-QISPSSVRmLNGHPV---DAKEM-QARCAYV----QQFDLfIGSLTARE 71
Cdd:COG3845 283 AGEILGIAGVAGNGQSELAEALA-----GLrPPASGSIR-LDGEDItglSPRERrRLGVAYIpedrLGRGL-VPDMSVAE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HLIFQATVRMP---RTMTQKQKMQR-VDQVIQDLSLgKCQNtiIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPT 147
Cdd:COG3845 356 NLILGRYRRPPfsrGGFLDRKAIRAfAEELIEEFDV-RTPG--PDTP--ARSLSGGNQQKVILARELSRDPKLLIAAQPT 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1151065379 148 SGLDsFMAASVV-QVLKKLSQRGKTVILtIhqpSSELFELF---DKILLMAEG 196
Cdd:COG3845 431 RGLD-VGAIEFIhQRLLELRDAGAAVLL-I---SEDLDEILalsDRIAVMYEG 478
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-190 |
1.52e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRM-LNGHPV------DAKEmqARCAYVQQ-FDLFiGSLTAREH 72
Cdd:COG1129 29 PGEVHALLGENGAGKSTLMKILS-----GVY-QPDSGEIlLDGEPVrfrsprDAQA--AGIAIIHQeLNLV-PNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 lIFQAtvRMPRT--MTQKQKM-QRVDQVIQDLSLGkcqntiIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSG 149
Cdd:COG1129 100 -IFLG--REPRRggLIDWRAMrRRARELLARLGLD------IDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1151065379 150 LDSFMAASVVQVLKKLSQRGKTVILTIHQpSSELFELFDKI 190
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQGVAIIYISHR-LDEVFEIADRV 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-178 |
1.53e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 55.36 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNG--HPVDAKEMQARCAYVQQFDLFiGSLTAREHLIFQAT 78
Cdd:PRK10771 24 RGERVAILGPSGAGKSTLLNLIA-----GFLTPASGSLTLNGqdHTTTPPSRRPVSMLFQENNLF-SHLTVAQNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTQKQKMQrvdQVIQDLSLGKCQNTIigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:PRK10771 98 PGLKLNAAQREKLH---AIARQMGIEDLLARL---PGQ---LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180
....*....|....*....|.
gi 1151065379 159 VQVLKKL-SQRGKTVILTIHQ 178
Cdd:PRK10771 169 LTLVSQVcQERQLTLLMVSHS 189
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-177 |
1.55e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.90 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVrmlngHPVDAKEMQARCAYV-QQFDLFIGSLTAREHLIFQa 77
Cdd:PRK13647 31 GSKTALLGPNGAGKSTLLlhlNGIYLPQRGRVKVMGREV-----NAENEKWVRSKVGLVfQDPDDQVFSSTVWDDVAFG- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 tvrmPRTM--TQKQKMQRVDQVIQDLSLGKCqntiigvpgRVKG---LSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:PRK13647 105 ----PVNMglDKDEVERRVEEALKAVRMWDF---------RDKPpyhLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180
....*....|....*....|....*
gi 1151065379 153 FMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIVATH 196
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-196 |
2.00e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 55.72 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPVDAKEMQARcaYV----QQFDLFiGSLTAREHLIFq 76
Cdd:PRK09452 40 GEFLTLLGPSGCGKTTVLRLIAgFETPDSGRI------MLDGQDITHVPAENR--HVntvfQSYALF-PHMTVFENVAF- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 aTVRM---------PRTMtQKQKMQRVDQVIQDlslgkcqntiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPT 147
Cdd:PRK09452 110 -GLRMqktpaaeitPRVM-EALRMVQLEEFAQR---------------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 148 SGLDSFMAASVVQVLKKLsQR--GKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK09452 173 SALDYKLRKQMQNELKAL-QRklGITFVFVTHD-QEEALTMSDRIVVMRDG 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-196 |
2.34e-09 |
|
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: 55.96 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALafrsaRGV-QISPSSVRMLN-----------GHPVDAKEMQARCA---YVQQFDLFIGS 66
Cdd:TIGR03269 26 GEVLGILGRSGAGKSVLMHVL-----RGMdQYEPTSGRIIYhvalcekcgyvERPSKVGEPCPVCGgtlEPEEVDFWNLS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 67 LTAREHLIFQATVRMPRTMTQKQKMQRVDQVIQDL---------SLGKCQNTI--IGVPGRV----KGLSGGERKRLAFA 131
Cdd:TIGR03269 101 DKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALeeigyegkeAVGRAVDLIemVQLSHRIthiaRDLSGGEKQRVVLA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065379 132 SEALTDPPLLICDEPTSGLDSFMAASVVQVLKKL-SQRGKTVILTIHQPSSeLFELFDKILLMAEG 196
Cdd:TIGR03269 181 RQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEV-IEDLSDKAIWLENG 245
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1-196 |
2.44e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.07 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSarGVQISPSSVRmLNGHPVDAKEMQARcayvqqfdlfigsltARE--HLIFQAT 78
Cdd:COG0396 25 PGEVHAIMGPNGSGKSTLAKVLMGHP--KYEVTSGSIL-LDGEDILELSPDER---------------ARAgiFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMP--------RTMTQKQKMQRVDQViqdLSLGKCQNTIigvpGRVK------------GLSGGERKRLAFASEALTDP 138
Cdd:COG0396 87 VEIPgvsvsnflRTALNARRGEELSAR---EFLKLLKEKM----KELGldedfldryvneGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 139 PLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPssELFELF--DKILLMAEG 196
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDG 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-196 |
2.46e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.44 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTL---LNALafrsargvqISPSSVR-MLNG-----HPVDAKEMQARCAYVQQFDlfigsltarEH 72
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLiqhLNGL---------LKPTSGKiIIDGvditdKKVKLSDIRKKVGLVFQYP---------EY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQATVRM-----PRTM--TQKQKMQRVDQVIQdlslgkcqntIIGVPGRVKG------LSGGERKRLAFASEALTDPP 139
Cdd:PRK13637 95 QLFEETIEKdiafgPINLglSEEEIENRVKRAMN----------IVGLDYEDYKdkspfeLSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065379 140 LLICDEPTSGLDSFMAASVVQVLKKLSQRGK-TVILTIHqpSSE-LFELFDKILLMAEG 196
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSH--SMEdVAKLADRIIVMNKG 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-177 |
2.47e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSArgvqisPSS----VRMLNGHPVDAKEM-QAR--------CAYVQQfdlfigsl 67
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLA------PDAgevhYRMRDGQLRDLYALsEAErrrllrteWGFVHQ-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 68 TAREHLifqatvRM---------PRTMTQKQK------------MQRVDqviqdlslgkcqntiIGvPGRVKGL----SG 122
Cdd:PRK11701 97 HPRDGL------RMqvsaggnigERLMAVGARhygdiratagdwLERVE---------------ID-AARIDDLpttfSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065379 123 GERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKL-SQRGKTVILTIH 177
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTH 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
120-196 |
2.50e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 2.50e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-196 |
2.71e-09 |
|
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: 55.60 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNaLAFR----SARGVQI--------SPSSVRmlnghpvdakemqARCAYVQQfD--LF--- 63
Cdd:COG5265 383 AGKTVAIVGPSGAGKSTLAR-LLFRfydvTSGRILIdgqdirdvTQASLR-------------AAIGIVPQ-DtvLFndt 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 64 ----I--GSLTAREHLIFQATvrmprtmtqkqKMQRVDQVIQDLSLGKcqNTIIGVPGrVKgLSGGERKRLAFASEALTD 137
Cdd:COG5265 448 iaynIayGRPDASEEEVEAAA-----------RAAQIHDFIESLPDGY--DTRVGERG-LK-LSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065379 138 PPLLICDEPTSGLDSFMAASVVQVLKKLSqRGKTVILTIHQPS----SelfelfDKILLMAEG 196
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLStivdA------DEILVLEAG 568
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-196 |
3.09e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 55.23 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHpvdakEMQARCAYVQQFDLFIGSLTAREHLIFQATVR 80
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAgFEQPTAGQI------MLDGV-----DLSHVPPYQRPINMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPRTMTQKQKMQRVDQVIQDLSLGKCQNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS----FMAA 156
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQ---LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKklrdRMQL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 157 SVVQVLKKLsqrGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK11607 191 EVVDILERV---GVTCVMVTHD-QEEAMTMAGRIAIMNRG 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-196 |
3.29e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.03 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTL---LNALAFRSARGVQISPssvRMLNGH--PVDAKEMQARCAYVQQFDlfigsltarEHLIFQ 76
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLlqhLNGLLQPTSGTVTIGE---RVITAGkkNKKLKPLRKKVGIVFQFP---------EHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVR-------MPRTMTQKQKMQRVDQVIQdlslgkcqntIIGVPGRVKG-----LSGGERKRLAFASEALTDPPLLICD 144
Cdd:PRK13634 101 ETVEkdicfgpMNFGVSEEDAKQKAREMIE----------LVGLPEELLArspfeLSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1151065379 145 EPTSGLDSFMAASVVQVLKKLSQ-RGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHS-MEDAARYADQIVVMHKG 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-196 |
3.40e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVD----AKEMQARCAYVQQFDLFIGSLTAREHLIFq 76
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIA-----GIVPPDSGTLEIGGNPCArltpAKAHQLGIYLVPQEPLLFPNLSVKENILF- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 atvRMPRTMTQKQKMQrvdQVIQDLSlgkCQntiIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:PRK15439 110 ---GLPKRQASMQKMK---QLLAALG---CQ---LDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 157 SVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK15439 178 RLFSRIRELLAQGVGIVFISHK-LPEIRQLADRISVMRDG 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
2-178 |
3.49e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALA--FRSARG-VQISPSSVRmlnghpvdakemQARCAYVQQFdLFIG-------SLTARE 71
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLLKLIAglLNPEKGeILFERQSIK------------KDLCTYQKQL-CFVGhrsginpYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HLIFQatvrmprTMTQKQKMQrVDQVIQDLSLGKCQNTIIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:PRK13540 94 NCLYD-------IHFSPGAVG-ITELCRLFSLEHLIDYPCGL------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*..
gi 1151065379 152 SFMAASVVQVLKKLSQRGKTVILTIHQ 178
Cdd:PRK13540 160 ELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-175 |
3.61e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.78 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARGVQISPSSVRMLNGHPV-----DAKEMQARCAYV-QQFDLFIGSltarehlI 74
Cdd:PRK14239 30 PNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIysprtDTVDLRKEIGMVfQQPNPFPMS-------I 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 FQATVRMPRTMTQKQKmQRVDQVIQDlSLgKCQNTIIGVPGRVK----GLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:PRK14239 103 YENVVYGLRLKGIKDK-QVLDEAVEK-SL-KGASIWDEVKDRLHdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
|
170 180
....*....|....*....|....*
gi 1151065379 151 DSFMAASVVQVLKKLSQRGKTVILT 175
Cdd:PRK14239 180 DPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-196 |
4.54e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARGVQISPSSVR---MLNGHP---VDAKEMQARCAYVQQFDLFIGSLTAREHLI 74
Cdd:PRK13547 26 PGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTgdvTLNGEPlaaIDAPRLARLRAVLPQAAQPAFAFSAREIVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 FQatvRMPRTMTQKQKMQRvDQVIQDLSLGKCQNTIIGvpGR-VKGLSGGERKRLAFA---------SEALTDPPLLICD 144
Cdd:PRK13547 106 LG---RYPHARRAGALTHR-DGEIAWQALALAGATALV--GRdVTTLSGGELARVQFArvlaqlwppHDAAQPPRYLLLD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1151065379 145 EPTSGLDSFMAASVVQVLKKLSQRGKTVILTI-HQPSSELfELFDKILLMAEG 196
Cdd:PRK13547 180 EPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAA-RHADRIAMLADG 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-196 |
4.56e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.40 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTL---LNALAFRSARGVQISPSSVRmlngHPVDAKEMQ---ARCAYVQQFDlfigsltarEHLIF 75
Cdd:PRK13646 33 GKYYAIVGQTGSGKSTLiqnINALLKPTTGTVTVDDITIT----HKTKDKYIRpvrKRIGMVFQFP---------ESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 QATVRMPRTMTQKQKMQRVDQVIQD-----LSLGKCQNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYahrllMDLGFSRDVMSQSPFQ---MSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1151065379 151 DSFMAASVVQVLKKLS-QRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQtDENKTIILVSHD-MNEVARYADEVIVMKEG 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-177 |
4.96e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.11 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDakemQARCAYVQQFDLFIGSLTAREHLIFQAT-- 78
Cdd:PRK10908 27 PGEMAFLTGHSGAGKSTLLKLIC-----GIERPSAGKIWFSGHDIT----RLKNREVPFLRRQIGMIFQDHHLLMDRTvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 --VRMPRTM---TQKQKMQRVDQVIQDLS-LGKCQNTIIgvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:PRK10908 98 dnVAIPLIIagaSGDDIRRRVSAALDKVGlLDKAKNFPI-------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180
....*....|....*....|....*
gi 1151065379 153 FMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:PRK10908 171 ALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
120-177 |
6.15e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 52.45 E-value: 6.15e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQrgkTVILTIH 177
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG---TVILVSH 125
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-196 |
7.15e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.91 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVQiSPSSVRMLNGH-PVDAkemqarcayvqqfdlfigsltAREHLifqatvr 80
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLA-----GLE-TPSAGELLAGTaPLAE---------------------AREDT------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 mpRTMTQKQKMQRVDQVIQDLSLGKCQN---------TIIGVPGRVK----GLSGGERKRLAFASEALTDPPLLICDEPT 147
Cdd:PRK11247 84 --RLMFQDARLLPWKKVIDNVGLGLKGQwrdaalqalAAVGLADRANewpaALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1151065379 148 SGLDSFMAASVVQVLKKL-SQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK11247 162 GALDALTRIEMQDLIESLwQQHGFTVLLVTHD-VSEAVAMADRVLLIEEG 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
120-196 |
7.17e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.84 E-value: 7.17e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKL-SQRGKTVILTIHQPSSELfeLFDKILLMAEG 196
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrKTRKKTLISITHDMDEAI--LADKVIVFSEG 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-196 |
7.77e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVD----AKEMQARCAYVQQFDLFIGSLTAREHLIFQA 77
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLC-----GDPRATSGRIVFDGKDITdwqtAKIMREAVAIVPEGRRVFSRMTVEENLAMGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVrMPRTMTQkQKMQRVDQVIQDLSLGKCQntiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:PRK11614 106 FF-AERDQFQ-ERIKWVYELFPRLHERRIQ--------RAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 158 VVQVLKKLSQRGKTVILtIHQPSSELFELFDKILLMAEG 196
Cdd:PRK11614 176 IFDTIEQLREQGMTIFL-VEQNANQALKLADRGYVLENG 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-196 |
8.66e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.68 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLL---NALAFRSARGVQISPSSVRMLNGHPvDAKEMQARCAYVQQFDlfigsltarEHLIFQAT 78
Cdd:PRK13641 33 GSFVALVGHTGSGKSTLMqhfNALLKPSSGTITIAGYHITPETGNK-NLKKLRKKVSLVFQFP---------EAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRM-----PRTM---TQKQKMQRVDQVIQdlsLGKCQNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 150
Cdd:PRK13641 103 VLKdvefgPKNFgfsEDEAKEKALKWLKK---VGLSEDLISKSPFE---LSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1151065379 151 DSFMAASVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHG 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-196 |
9.54e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALafrsargvqispssvrmLNGHPVDAKEMQAR--CAYVQQfDLFIGSLTAREHLIFQATV 79
Cdd:PTZ00243 686 GKLTVVLGATGSGKSTLLQSL-----------------LSQFEISEGRVWAErsIAYVPQ-QAWIMNATVRGNILFFDEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 80 RMPRTmtqkQKMQRVDQVIQDL-SLGKCQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:PTZ00243 748 DAARL----ADAVRVSQLEADLaQLGGGLETEIGEKG--VNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
170 180 190
....*....|....*....|....*....|....*...
gi 1151065379 159 VQVLKKLSQRGKTVILTIHQpsSELFELFDKILLMAEG 196
Cdd:PTZ00243 822 VEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDG 857
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-180 |
1.04e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.31 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 4 LLAVMGSSGAGKTTLLNALafrsARGVQISPSS-----VRMLN----GHPVDAKEMQARCAYVQQFDLFIGSLTAREHLI 74
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTF----NRLLELNEEArvegeVRLFGrniySPDVDPIEVRREVGMVFQYPNPFPHLTIYDNVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 FqaTVRMPRTMTQKQKM-QRVDQVIQDLSL-GKCQNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:PRK14267 108 I--GVKLNGLVKSKKELdERVEWALKKAALwDEVKDRLNDYPSN---LSGGQRQRLVIARALAMKPKILLMDEPTANIDP 182
|
170 180
....*....|....*....|....*...
gi 1151065379 153 FMAASVVQVLKKLsQRGKTVILTIHQPS 180
Cdd:PRK14267 183 VGTAKIEELLFEL-KKEYTIVLVTHSPA 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-196 |
1.09e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.95 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALafrsARGVQISPSSVRmLNGHPVDA---KEMQARCAYVQQFDlFIGSLTAREHLifqA 77
Cdd:PRK10789 340 PGQMLGICGPTGSGKSTLLSLI----QRHFDVSEGDIR-FHDIPLTKlqlDSWRSRLAVVSQTP-FLFSDTVANNI---A 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVRMPRTMTQKQKMQRVDQVIQD-LSLGKCQNTIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAA 156
Cdd:PRK10789 411 LGRPDATQQEIEHVARLASVHDDiLRLPQGYDTEVGERGVM--LSGGQKQRISIARALLLNAEILILDDALSAVD---GR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 157 SVVQVLKKLSQ--RGKTVILTIHQPSSeLFELfDKILLMAEG 196
Cdd:PRK10789 486 TEHQILHNLRQwgEGRTVIISAHRLSA-LTEA-SEILVMQHG 525
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1-196 |
1.58e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 52.50 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALaFRSargVQISPSSVRmlnghpVDAKEMQArcayvqqfdlfIGSLTAREHL------- 73
Cdd:cd03244 29 PGEKVGIVGRTGSGKSSLLLAL-FRL---VELSSGSIL------IDGVDISK-----------IGLHDLRSRIsiipqdp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 -IFQATVRM---PRTMTQKQKMQrvdQVIQDLSLGK-CQNTIIGVPGRV----KGLSGGERKRLAFASEALTDPPLLICD 144
Cdd:cd03244 88 vLFSGTIRSnldPFGEYSDEELW---QALERVGLKEfVESLPGGLDTVVeeggENLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065379 145 EPTSGLDSFMAASVVQVLK-KLSQRgkTVIL------TIHQpsselfelFDKILLMAEG 196
Cdd:cd03244 165 EATASVDPETDALIQKTIReAFKDC--TVLTiahrldTIID--------SDRILVLDKG 213
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-177 |
2.17e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsargvqispssvrmlnGHPvdakemqarcAY-VQQFDLF-----IGSLTA--REH 72
Cdd:CHL00131 32 KGEIHAIMGPNGSGKSTLSKVIA------------------GHP----------AYkILEGDILfkgesILDLEPeeRAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 ----LIFQATVRMP--------RT-MTQKQKMQRVDQV--IQDLSLGKCQNTIIGVPGRV------KGLSGGERKRLAFA 131
Cdd:CHL00131 84 lgifLAFQYPIEIPgvsnadflRLaYNSKRKFQGLPELdpLEFLEIINEKLKLVGMDPSFlsrnvnEGFSGGEKKRNEIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1151065379 132 SEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-181 |
3.00e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.19 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNAL-AFrsargVQISPSSVRMLnGHPVDAKEMQARCAYVQQFDLFIGSLTarehLIFQATVR 80
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALmGF-----VRLASGKISIL-GQPTRQALQKNLVAYVPQSEEVDWSFP----VLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPR-------TMTQKQKMQRVDQVIQDLSLGKCQNTIIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 153
Cdd:PRK15056 103 MGRyghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIG------ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180
....*....|....*....|....*...
gi 1151065379 154 MAASVVQVLKKLSQRGKTVILTIHQPSS 181
Cdd:PRK15056 177 TEARIISLLRELRDEGKTMLVSTHNLGS 204
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
116-196 |
3.08e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 116 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTihqpSSELFE---LFDKILL 192
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI----SSELPEvlgLSDRVLV 477
|
....
gi 1151065379 193 MAEG 196
Cdd:PRK13549 478 MHEG 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-196 |
3.21e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.61 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLnalafrsargvqispssvRMLNGH--PVDAK-EMQARCAYVQQFDlFIGSLTAREHLIFQAT 78
Cdd:TIGR01271 452 GQLLAVAGSTGSGKSSLL------------------MMIMGElePSEGKiKHSGRISFSPQTS-WIMPGTIKDNIIFGLS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTqkqkMQRVDQVIQDLS-LGKCQNTIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:TIGR01271 513 YDEYRYTS----VIKACQLEEDIAlFPEKDKTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1151065379 158 VVQ--VLKKLSQrgKTVILTihqpSSELFEL--FDKILLMAEG 196
Cdd:TIGR01271 587 IFEscLCKLMSN--KTRILV----TSKLEHLkkADKILLLHEG 623
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-196 |
3.46e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.91 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQIspssvrMLNGHPVDAKEMQ--ARCAYVQQFD---LFiGSLTAREHL- 73
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTgFYKPTGGTI------LLRGQHIEGLPGHqiARMGVVRTFQhvrLF-REMTVIENLl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 ----------IFQATVRMPR-TMTQKQKMQRVDQVIQDLSLGKCQNtiigvpgRVKG-LSGGERKRLAFASEALTDPPLL 141
Cdd:PRK11300 103 vaqhqqlktgLFSGLLKTPAfRRAESEALDRAATWLERVGLLEHAN-------RQAGnLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1151065379 142 ICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1-196 |
4.19e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.47 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRmLNGHPV---DAKEMQARCAYV--QQFDLFIGSltarehlIF 75
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMA-----GLLPGSGSIQ-FAGQPLeawSAAELARHRAYLsqQQTPPFAMP-------VF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 Q-ATVRMPRTMTQKQKMQRVDQVIQDLSLGKCQNTIIGvpgrvkGLSGGE--RKRLAFA-----SEALTDPPLLICDEPT 147
Cdd:PRK03695 88 QyLTLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVN------QLSGGEwqRVRLAAVvlqvwPDINPAGQLLLLDEPM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1151065379 148 SGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELfDKILLMAEG 196
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQG 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-177 |
6.10e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 51.24 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVR-MLNGHPVDAKEMQARCAYV----QqfDLFIG---SLTAREH 72
Cdd:COG1101 31 EGDFVTVIGSNGAGKSTLLNAIA-----GS-LPPDSGSiLIDGKDVTKLPEYKRAKYIgrvfQ--DPMMGtapSMTIEEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQATVRMPRTMTQKQKMQRVDQVIQDLS-LGkcqntiIGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDEPT 147
Cdd:COG1101 103 LALAYRRGKRRGLRRGLTKKRRELFRELLAtLG------LGLENRldtkVGLLSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
170 180 190
....*....|....*....|....*....|.
gi 1151065379 148 SGLDSFMAASVVQVLKKLSQRGK-TVILTIH 177
Cdd:COG1101 177 AALDPKTAALVLELTEKIVEENNlTTLMVTH 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-196 |
8.41e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKT-TLLNALAFRSARGVQISPSS--VRMLNGHPVDAKEM-QARCAYVQQFDLfigsltareHLIFQA 77
Cdd:PRK10261 42 GETLAIVGESGSGKSvTALALMRLLEQAGGLVQCDKmlLRRRSRQVIELSEQsAAQMRHVRGADM---------AMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 -----------------TVRMPRTMTQKQKMQRVDQVIQDLSLGKCQNTIIGVPGRvkgLSGGERKRLAFASEALTDPPL 140
Cdd:PRK10261 113 pmtslnpvftvgeqiaeSIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ---LSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065379 141 LICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-196 |
9.77e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 7 VMGSSGAGKTTLLnalafRSARGVQISPSSVRMLNGHPVDA--------KEMQARCAYVQQFDlfigsltarEHLIFQAT 78
Cdd:PRK13645 42 VIGTTGSGKSTMI-----QLTNGLIISETGQTIVGDYAIPAnlkkikevKRLRKEIGLVFQFP---------EYQLFQET 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRM-----PRTM--TQKQKMQRVDQVIQDLSLGKcqNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:PRK13645 108 IEKdiafgPVNLgeNKQEAYKKVPELLKLVQLPE--DYVKRSPFE---LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1151065379 152 SFMAASVVQVLKKLSQ-RGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK13645 183 PKGEEDFINLFERLNKeYKKRIIMVTHN-MDQVLRIADEVIVMHEG 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
120-196 |
1.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 1.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKG 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-196 |
1.50e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.07 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-FRSARGVQISpssvrmLNGHPVDAKEMQARCAY---VQQ-FDLFIGSLTAREHL-- 73
Cdd:PRK10419 37 SGETVALLGRSGCGKSTLARLLVgLESPSQGNVS------WRGEPLAKLNRAQRKAFrrdIQMvFQDSISAVNPRKTVre 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 IFQATVRMPRTMTQKQKMQRVDQVIQ--DLSLGKCQNtiigVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:PRK10419 111 IIREPLRHLLSLDKAERLARASEMLRavDLDDSVLDK----RPPQ---LSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1151065379 152 SFMAASVVQVLKKLSQRGKTVILTI-HQPSseLFELF-DKILLMAEG 196
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTACLFItHDLR--LVERFcQRVMVMDNG 228
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2-196 |
1.56e-07 |
|
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: 49.24 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAFRSARGVQISPSSvrmlnghpvdakemqarcAYVQQFDLFIGSLtarehlifqatvrm 81
Cdd:cd03238 21 NVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLP------------------KFSRNKLIFIDQL-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 pRTMtqkqkmqrVDQVIQDLSLGKCQNTiigvpgrvkgLSGGERKRLAFASEALTDPP--LLICDEPTSGLDSFMAASVV 159
Cdd:cd03238 69 -QFL--------IDVGLGYLTLGQKLST----------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLL 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 1151065379 160 QVLKKLSQRGKTVILTIHQPssELFELFDKILLMAEG 196
Cdd:cd03238 130 EVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFGPG 164
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-180 |
1.61e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.66 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsargvqispsSVRMLNGHPVDAKEMQARCAYVQQFDlfiGSLTAREHLIFQAtvrM 81
Cdd:PRK13545 50 GEIVGIIGLNGSGKSTLSNLIA------------GVTMPNKGTVDIKGSAALIAISSGLN---GQLTGIENIELKG---L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 PRTMTQKQKMQRVDQVIQDLSLGKcqntIIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQV 161
Cdd:PRK13545 112 MMGLTKEKIKEIIPEIIEFADIGK----FIYQP--VKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170
....*....|....*....
gi 1151065379 162 LKKLSQRGKTVILTIHQPS 180
Cdd:PRK13545 186 MNEFKEQGKTIFFISHSLS 204
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
120-196 |
1.76e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTihqpSSELFELF---DKILLMAEG 196
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII----SSEMPELLgitDRILVMSNG 467
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-168 |
1.93e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 50.12 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLlnalafrsARGVQ--ISPSSVRML-NGHPV---DAKEMQARCAYVQqfdlfigsltarehLI 74
Cdd:COG4608 43 RGETLGLVGESGCGKSTL--------GRLLLrlEEPTSGEILfDGQDItglSGRELRPLRRRMQ--------------MV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 FQ-------------ATVRMP----RTMTQKQKMQRVDQVIQdlslgkcqntiigvpgRVkGL------------SGGER 125
Cdd:COG4608 101 FQdpyaslnprmtvgDIIAEPlrihGLASKAERRERVAELLE----------------LV-GLrpehadryphefSGGQR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1151065379 126 KRLAFAsEAL-TDPPLLICDEPTSGLDSFMAASVVQVLKKLSQR 168
Cdd:COG4608 164 QRIGIA-RALaLNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDE 206
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
117-196 |
2.33e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.62 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 117 VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK13638 134 IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD-IDLIYEISDAVYVLRQG 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
120-177 |
2.83e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.36 E-value: 2.83e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
121-196 |
2.91e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.34 E-value: 2.91e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065379 121 SGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
92-196 |
3.42e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 49.26 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 92 QRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAASVVQV---LKKLSQR 168
Cdd:PRK11000 112 QRVNQVAEVLQLAHLLDR------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD---AALRVQMrieISRLHKR 182
|
90 100
....*....|....*....|....*....
gi 1151065379 169 -GKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK11000 183 lGRTMIYVTHD-QVEAMTLADKIVVLDAG 210
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-177 |
3.87e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 3.87e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 120 LSGGERKRLAFASEALT---DPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-196 |
4.17e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.56 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVRML-NGHPVDA---KEMQARCAYVQQFDLFIGSlTAREHLIFQ 76
Cdd:PRK10247 32 AGEFKLITGPSGCGKSTLLKIVA------SLISPTSGTLLfEGEDISTlkpEIYRQQVSYCAQTPTLFGD-TVYDNLIFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRmprtmtqKQKMQRvDQVIQDLSLGKCQNTIIgvPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAA 156
Cdd:PRK10247 105 WQIR-------NQQPDP-AIFLDDLERFALPDTIL--TKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 157 SVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
120-178 |
4.54e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.03 E-value: 4.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 120 LSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDSFMAASVVQVLKKLSQR-GKTVILTIHQ 178
Cdd:PRK11153 141 LSGGQKQRVAIA-RALaSNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHE 200
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-151 |
5.57e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsargvqispssvrmlNGHPVDAKEMQ----ARCAYVQQfDlfigslTAREhliFQ 76
Cdd:PRK15064 344 AGERLAIIGENGVGKTTLLRTLV-----------------GELEPDSGTVKwsenANIGYYAQ-D------HAYD---FE 396
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1151065379 77 ATVRMPRTMTQKQKMQRVDQVIQDLsLGKCQNTIIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:PRK15064 397 NDLTLFDWMSQWRQEGDDEQAVRGT-LGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
66-175 |
5.86e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 66 SLTAREHLIFqatVRMPRTMTQKQKMQRVDQVIQDLSLGKcqntiigVPGRVKG-LSGGERKRLAFASEALTDPPLLICD 144
Cdd:NF000106 100 SFSGRENLYM---IGR*LDLSRKDARARADELLERFSLTE-------AAGRAAAkYSGGMRRRLDLAASMIGRPAVLYLD 169
|
90 100 110
....*....|....*....|....*....|.
gi 1151065379 145 EPTSGLDSFMAASVVQVLKKLSQRGKTVILT 175
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-177 |
6.47e-07 |
|
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: 48.63 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRMlnghpvdakEMQARCAYVQQFDLFIGSLTAREHLIFQATVRM 81
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILA-----GV-LKPDEGEV---------DEDLKISYKPQYISPDYDGTVEEFLRSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 PRTMTQkqkmqrvDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQV 161
Cdd:COG1245 431 GSSYYK-------TEIIKPLGLEKLLDK------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
|
170
....*....|....*..
gi 1151065379 162 LKKLS-QRGKTVILTIH 177
Cdd:COG1245 498 IRRFAeNRGKTAMVVDH 514
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
93-177 |
7.10e-07 |
|
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: 48.63 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 93 RVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTV 172
Cdd:COG1245 192 KLDELAEKLGLENILDR------DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYV 265
|
....*
gi 1151065379 173 ILTIH 177
Cdd:COG1245 266 LVVEH 270
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
120-180 |
7.96e-07 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 48.15 E-value: 7.96e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065379 120 LSGGERKRLAFAS---EALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPS 180
Cdd:pfam13304 237 LSDGTKRLLALLAallSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
90-192 |
9.01e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 90 KMQRVDQVIQdlSLGKCQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS----FMAASVVQVLKKL 165
Cdd:PTZ00265 1333 KFAAIDEFIE--SLPNKYDTNVGPYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnsekLIEKTIVDIKDKA 1408
|
90 100
....*....|....*....|....*..
gi 1151065379 166 SqrgKTVILTIHQPSSelFELFDKILL 192
Cdd:PTZ00265 1409 D---KTIITIAHRIAS--IKRSDKIVV 1430
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
120-196 |
1.02e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTihqpSSELFELF---DKILLMAEG 196
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI----SSELPELLgmcDRIYVMNEG 480
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-196 |
1.36e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 47.72 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTT---LLNALaFRSARGvQISPSSVRMLNGHPVDAKEMQARcayvqQFDLFIGSLTAREHLIFQAT 78
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTmvrLLNRL-IEPTRG-QVLIDGVDIAKISDAELREVRRK-----KIAMVFQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 79 VRMPRTMTQKQKMQRVDQVIQDLSLGKCQNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASV 158
Cdd:PRK10070 127 TAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE---LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190
....*....|....*....|....*....|....*...
gi 1151065379 159 VQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-179 |
1.42e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.35 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 4 LLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRmLNGH---------PVDAKEMQARCAYV-QQFDLFigsltarEHL 73
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLN----RLIEIYDSKIK-VDGKvlyfgkdifQIDAIKLRKEVGMVfQQPNPF-------PHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 IFQATVRMP---RTMTQKQKMQR-VDQVIQDLSLGKCQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSG 149
Cdd:PRK14246 106 SIYDNIAYPlksHGIKEKREIKKiVEECLRKVGLWKEVYDRLNSPA--SQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190
....*....|....*....|....*....|
gi 1151065379 150 LDSFMAASVVQVLKKLSQRgKTVILTIHQP 179
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNP 212
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-174 |
1.98e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsargvqispssvrmlnghpvdakemqarcayvQQFDLFIGSLTARehliFQATVRM 81
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALA----------------------------------GELPLLSGERQSQ----FSHITRL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 prTMTQKQKM-----QR----------------VDQVIQDLS--LGKCQN--TIIGVPG----RVKGLSGGERKRLAFAS 132
Cdd:PRK10938 71 --SFEQLQKLvsdewQRnntdmlspgeddtgrtTAEIIQDEVkdPARCEQlaQQFGITAlldrRFKYLSTGETRKTLLCQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1151065379 133 EALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVIL 174
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-196 |
2.18e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.71 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVqISPSSVRML-NGHPVDAKEMQARCAYVQQ-FDLFIGSLTAREHL--IFQ 76
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLA-----GM-IEPTSGELLiDDHPLHFGDYSYRSQRIRMiFQDPSTSLNPRQRIsqILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRMPRTMTQKQKMQRVDQVIQDLSLgkcqntiigVPGRVK----GLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:PRK15112 112 FPLRLNTDLEPEQREKQIIETLRQVGL---------LPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1151065379 153 FMAASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-196 |
2.55e-06 |
|
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: 47.10 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsarGVqISPSS----VRmLNGHPVDAKEM----QARCA-YV----QQFDLFIGSlT 68
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIA-----GV-LEPTSgevnVR-VGDEWVDMTKPgpdgRGRAKrYIgilhQEYDLYPHR-T 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 69 AREHLIFQATVRMPrtmtqkQKMQRVDQVIQDLSLG----KCQNTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICD 144
Cdd:TIGR03269 382 VLDNLTEAIGLELP------DELARMKAVITLKMVGfdeeKAEEILDKYPDE---LSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1151065379 145 EPTSGLDSFMAASVVQ-VLKKLSQRGKTVILTIHQPSSELfELFDKILLMAEG 196
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVL-DVCDRAALMRDG 504
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-177 |
3.07e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.23 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKT-TLLNALAFRSArGVQISPSSVRmLNGHPVDAKEMQAR-CAYVQQ--FDLFIGSLTAREHLIfqa 77
Cdd:PRK10418 29 GRVLALVGGSGSGKSlTCAAALGILPA-GVRQTAGRVL-LDGKPVAPCALRGRkIATIMQnpRSAFNPLHTMHTHAR--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 tvrmpRTMTQKQKMQRVDQVIQDLSLGKCQNtiigvPGRVKGL-----SGGERKRLAFASEALTDPPLLICDEPTSGLDS 152
Cdd:PRK10418 104 -----ETCLALGKPADDATLTAALEAVGLEN-----AARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180
....*....|....*....|....*.
gi 1151065379 153 FMAASVVQVLKKLSQ-RGKTVILTIH 177
Cdd:PRK10418 174 VAQARILDLLESIVQkRALGMLLVTH 199
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-167 |
3.87e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.11 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLlnalafrsARGVQI--SPSSVR-MLNGHPV---DAKEMQARCAYVQQ-FDLFIGSLTAREHL 73
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTL--------ARLLTMieTPTGGElYYQGQDLlkaDPEAQKLLRQKIQIvFQNPYGSLNPRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 74 --IFQATVRMPRTMTQKQKMQRVDQVIQdlslgkcqntiigvpgRVkGL------------SGGERKRLAFASEALTDPP 139
Cdd:PRK11308 112 gqILEEPLLINTSLSAAERREKALAMMA----------------KV-GLrpehydryphmfSGGQRQRIAIARALMLDPD 174
|
170 180
....*....|....*....|....*...
gi 1151065379 140 LLICDEPTSGLDSFMAASVVQVLKKLSQ 167
Cdd:PRK11308 175 VVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-177 |
3.88e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSArgVQISPSSVR-----MLNGHPVDAKEMQARCAYvqQFDLFIGSLTarEHLIF 75
Cdd:PRK09580 26 PGEVHAIMGPNGSGKSTLSATLAGRED--YEVTGGTVEfkgkdLLELSPEDRAGEGIFMAF--QYPVEIPGVS--NQFFL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 76 QATVRMPRTMTQKQKMQRVDqvIQDLSLGKCQntIIGVPGRV------KGLSGGERKRLAFASEALTDPPLLICDEPTSG 149
Cdd:PRK09580 100 QTALNAVRSYRGQEPLDRFD--FQDLMEEKIA--LLKMPEDLltrsvnVGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180
....*....|....*....|....*...
gi 1151065379 150 LDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:PRK09580 176 LDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
117-177 |
4.16e-06 |
|
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: 46.47 E-value: 4.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 117 VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAASVVQVLKKLSQRGKTVILTIH 177
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTH 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-196 |
4.84e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGH------PVDAKEMQARCAYvQQFDLfIGSLTAREHLI 74
Cdd:PRK09700 30 PGEIHALLGENGAGKSTLMKVLS-----GIHEPTKGTITINNInynkldHKLAAQLGIGIIY-QELSV-IDELTVLENLY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 75 fqatvrMPRTMTQK---------QKMQRVDQVIQD-LSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICD 144
Cdd:PRK09700 103 ------IGRHLTKKvcgvniidwREMRVRAAMMLLrVGLKVDLDE------KVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1151065379 145 EPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDG 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-175 |
6.24e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.47 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 6 AVMGSSGAGKTTLLNALAFRSARGVQISPSSVRMLNGHPV----DAKEMQARCAYV-QQFDLFIGSLTAREHLIFQATVR 80
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIfnyrDVLEFRRRVGMLfQRPNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 MPRTMTQKQKMQRVDQV-IQDLSLGKCQNTiigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVV 159
Cdd:PRK14271 131 VPRKEFRGVAQARLTEVgLWDAVKDRLSDS----PFR---LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170
....*....|....*.
gi 1151065379 160 QVLKKLSQRGKTVILT 175
Cdd:PRK14271 204 EFIRSLADRLTVIIVT 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-151 |
6.97e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVRMLNGHPVDAkemqarcAYVQQFdlfigsltaREHLIFQATVrm 81
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLML------GQLQADSGRIHCGTKLEV-------AYFDQH---------RAELDPEKTV-- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 prtmtqkqkmqrvdqvIQDLSLGKCQNTIIGV--------------PGR----VKGLSGGERKRLAFASEALTDPPLLIC 143
Cdd:PRK11147 401 ----------------MDNLAEGKQEVMVNGRprhvlgylqdflfhPKRamtpVKALSGGERNRLLLARLFLKPSNLLIL 464
|
....*...
gi 1151065379 144 DEPTSGLD 151
Cdd:PRK11147 465 DEPTNDLD 472
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1-177 |
7.73e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.05 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA-------------------FRSARGVQISPSSVRMLNGHPVDAKEMQarcaYV---- 57
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAgklkpnlgkfddppdwdeiLDEFRGSELQNYFTKLLEGDVKVIVKPQ----YVdlip 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 58 QQFDLFIGSLtarehlifqatvrmprtMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTD 137
Cdd:cd03236 101 KAVKGKVGEL-----------------LKKKDERGKLDELVDQLELRHVLDR------NIDQLSGGELQRVAIAAALARD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1151065379 138 PPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-178 |
7.99e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 44.63 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNAL--AFRSARGVQISPSSVRMLNGHPVDAKEMQARCAYVQQFDLFIGSlTAREHLIFQATV 79
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAIlgEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-TVEENITFGSPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 80 rmprtmtQKQKMQRVDQV------IQDLSLGkcQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 153
Cdd:cd03290 106 -------NKQRYKAVTDAcslqpdIDLLPFG--DQTEIGERG--INLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180
....*....|....*....|....*..
gi 1151065379 154 MAASVVQ--VLKKLSQRGKTVILTIHQ 178
Cdd:cd03290 175 LSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
93-177 |
9.20e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 93 RVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQrGKTV 172
Cdd:PRK13409 192 KLDEVVERLGLENILDR------DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE-GKYV 264
|
....*
gi 1151065379 173 ILTIH 177
Cdd:PRK13409 265 LVVEH 269
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
120-196 |
1.05e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.69 E-value: 1.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQR-GKTVILTIHQpSSELFELfDKILLMAEG 196
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHY-MEEAVEA-DRIIVMDSG 220
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
120-196 |
2.44e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.96 E-value: 2.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLMAEG 196
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
120-176 |
2.55e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 43.90 E-value: 2.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTI 176
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLI 213
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-177 |
2.59e-05 |
|
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: 44.23 E-value: 2.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 120 LSGGERKRLAFASEAL---TDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-173 |
2.63e-05 |
|
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: 44.02 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALA--FRSARGvQISpssvrmLNGHPVDAKEMQarcAYVQQF-----D--LFigsltarE 71
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTglYRPESG-EIL------LDGQPVTADNRE---AYRQLFsavfsDfhLF-------D 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 72 HLIFQATVRMPrtmtqkqkmQRVDQVIQDLSL-GKCqntiigvpgRVKG-------LSGGERKRLAFASEALTDPPLLIC 143
Cdd:COG4615 420 RLLGLDGEADP---------ARARELLERLELdHKV---------SVEDgrfsttdLSQGQRKRLALLVALLEDRPILVF 481
|
170 180 190
....*....|....*....|....*....|....*.
gi 1151065379 144 DE------PTsgldsFMAASVVQVLKKLSQRGKTVI 173
Cdd:COG4615 482 DEwaadqdPE-----FRRVFYTELLPELKARGKTVI 512
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-151 |
3.51e-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: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLlnalaFRSARGvQISPSSVRMLNGHPVDAkemqarcAYVQQFdlfigsltaREHLIFQATVR 80
Cdd:TIGR03719 347 PGGIVGVIGPNGAGKSTL-----FRMITG-QEQPDSGTIEIGETVKL-------AYVDQS---------RDALDPNKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 mprtmtqkqkmqrvdQVIQD----LSLGKCQntiigVPGR----------------VKGLSGGERKRLAFASEALTDPPL 140
Cdd:TIGR03719 405 ---------------EEISGgldiIKLGKRE-----IPSRayvgrfnfkgsdqqkkVGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|.
gi 1151065379 141 LICDEPTSGLD 151
Cdd:TIGR03719 465 LLLDEPTNDLD 475
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-196 |
4.49e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVD---AKE-MQARCAYVQQfdlfigsltaREHLIFQ 76
Cdd:PRK10982 23 PHSIHALMGENGAGKSTLLKCLF-----GIYQKDSGSILFQGKEIDfksSKEaLENGISMVHQ----------ELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATV-------RMPRT--MTQKQKMQRVDQVIQDlSLGkcqntiIGVPGRVKG--LSGGERKRLAFASEALTDPPLLICDE 145
Cdd:PRK10982 88 RSVmdnmwlgRYPTKgmFVDQDKMYRDTKAIFD-ELD------IDIDPRAKVatLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 146 PTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHK-MEEIFQLCDEITILRDG 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
120-177 |
6.40e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 42.33 E-value: 6.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGK-TVILTIH 177
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSH 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-196 |
7.19e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNAL--AFRSARGvQIspssvrMLNGHPVDAKEMQ-------ARCAYVQQFDLFIGSLTAREH 72
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLygATRRTAG-QV------YLDGKPIDIRSPRdairagiMLCPEDRKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LIFQA---TVRMPRTMTQKQKMQRVDQVIQDLSlgkcqntiIGVPGR---VKGLSGGERKRLAFASEALTDPPLLICDEP 146
Cdd:PRK11288 352 INISArrhHLRAGCLINNRWEAENADRFIRSLN--------IKTPSReqlIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1151065379 147 TSGLDSFMAASVVQVLKKLSQRGKTVILTihqpSSELFE---LFDKILLMAEG 196
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQGVAVLFV----SSDLPEvlgVADRIVVMREG 472
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-177 |
7.29e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 42.28 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAfrsargVQISPSSVRM-LNGHPVD---AKEMQARCAYVQQFDLFIGSLTAREhliFQA 77
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLS------RLMTPAHGHVwLDGEHIQhyaSKEVARRIGLLAQNATTPGDITVQE---LVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 78 TVRMPR----TMTQKQKMQRVDQVIQDLSLGKCQNTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 153
Cdd:PRK10253 104 RGRYPHqplfTRWRKEDEEAVTKAMQATGITHLADQ------SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180
....*....|....*....|....*
gi 1151065379 154 MAASVVQVLKKLS-QRGKTVILTIH 177
Cdd:PRK10253 178 HQIDLLELLSELNrEKGYTLAAVLH 202
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
109-176 |
7.44e-05 |
|
ATP-binding cassette domain 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 more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.40 E-value: 7.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1151065379 109 TIIGVPGRVKgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTI 176
Cdd:cd03222 62 TPVYKPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVV 128
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
117-158 |
7.54e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 7.54e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1151065379 117 VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAASV 158
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESV 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-151 |
8.35e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 42.02 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLnalafRSARGVqISPSSVRMLnghpvdaKEMQARCAYVQQfdlfigsltaREHLIFQATVR 80
Cdd:PRK09544 29 PGKILTLLGPNGAGKSTLV-----RVVLGL-VAPDEGVIK-------RNGKLRIGYVPQ----------KLYLDTTLPLT 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 81 MPRTMTQKQKMQRVDqVIQDLSLGKCQNtIIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 151
Cdd:PRK09544 86 VNRFLRLRPGTKKED-ILPALKRVQAGH-LIDAP--MQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1-193 |
1.02e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAfrsaRGVQISPSSVRMLNGHPVDAKEMQarcayvqqfdlfigsltarehlifqatvr 80
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA----RELGPPGGGVIYIDGEDILEEVLD----------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 81 mprtmtqkqkmqrvdqviqdlslgkcQNTIIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQ 160
Cdd:smart00382 48 --------------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1151065379 161 ------VLKKLSQRGKTVILTIHQP----SSELFELFDKILLM 193
Cdd:smart00382 102 leelrlLLLLKSEKNLTVILTTNDEkdlgPALLRRRFDRRIVL 144
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-196 |
1.04e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.12 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSARGvqiSPSSVRMLNGHPVDAKEM----QARCAYVQQFDLFIGSLTAREHLIFQ 76
Cdd:TIGR02633 26 PGECVGLCGENGAGKSTLMKILSGVYPHG---TWDGEIYWSGSPLKASNIrdteRAGIVIIHQELTLVPELSVAENIFLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 77 ATVRMPRTMTQKQKM-QRVDQVIQDLSLgkcqnTIIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMA 155
Cdd:TIGR02633 103 NEITLPGGRMAYNAMyLRAKNLLRELQL-----DADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKET 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1151065379 156 ASVVQVLKKLSQRGKTVILTIHQpSSELFELFDKILLMAEG 196
Cdd:TIGR02633 178 EILLDIIRDLKAHGVACVYISHK-LNEVKAVCDTICVIRDG 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
120-193 |
1.76e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 1.76e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLM 193
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-196 |
1.96e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 41.24 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 6 AVMGSSGAGKTTLLNALAfrsarGVQISPSSVRMLNGHPVDAKEMQA---RCAYVQQfDLFIGSLTarehliFQATVRMP 82
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLM-----GYYPLTEGEIRLDGRPLSSLSHSVlrqGVAMVQQ-DPVVLADT------FLANVTLG 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 83 RTMTQKQKMQRVDQV-----IQDLSLGkcQNTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAAS 157
Cdd:PRK10790 439 RDISEEQVWQALETVqlaelARSLPDG--LYTPLGEQG--NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
|
170 180 190
....*....|....*....|....*....|....*....
gi 1151065379 158 VVQVLKKLsqRGKTVILTIHQPSSELFELfDKILLMAEG 196
Cdd:PRK10790 515 IQQALAAV--REHTTLVVIAHRLSTIVEA-DTILVLHRG 550
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-177 |
2.03e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALafrsarGVQISPSSVRMLNGHPVDAKEMQARCAyvqqfdlfiGSLTAREHLIFQAtvrM 81
Cdd:PRK13546 50 GDVIGLVGINGSGKSTLSNII------GGSLSPTVGKVDRNGEVSVIAISAGLS---------GQLTGIENIEFKM---L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 PRTMTQKQKMQRVDQVIQDLSLGKcqntIIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQV 161
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGE----FIYQP--VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDK 185
|
170
....*....|....*.
gi 1151065379 162 LKKLSQRGKTVILTIH 177
Cdd:PRK13546 186 IYEFKEQNKTIFFVSH 201
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
84-151 |
2.07e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 2.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1151065379 84 TMTQKQKMQRVDQVIQDLSLGKCQNTII---GVPGRVKGLSGGERK------RLAFASEALTDPPLLICDEPTSGLD 151
Cdd:PRK01156 763 TSLTRKYLFEFNLDFDDIDVDQDFNITVsrgGMVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLD 839
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
120-175 |
2.11e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.92 E-value: 2.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILT 175
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT 207
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-196 |
2.13e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.11 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALA--FRSARGvQIspssvrMLNGHPVDAKEMQarcAYVQQFD-------LFigsltarEH 72
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTglYQPQSG-EI------LLDGKPVTAEQPE---DYRKLFSavftdfhLF-------DQ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 73 LI----FQATVRMPRTMTQKQKMQrvDQViqDLSLGKCQNTiigvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTS 148
Cdd:PRK10522 412 LLgpegKPANPALVEKWLERLKMA--HKL--ELEDGRISNL---------KLSKGQKKRLALLLALAEERDILLLDEWAA 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1151065379 149 GLD-SFMAASVVQVLKKLSQRGKTVILTIHQPSseLFELFDKILLMAEG 196
Cdd:PRK10522 479 DQDpHFRREFYQVLLPLLQEMGKTIFAISHDDH--YFIHADRLLEMRNG 525
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-191 |
2.21e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 2.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1151065379 120 LSGGERKRLAFASE--ALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQpsSELFELFDKIL 191
Cdd:PRK00635 477 LSGGEQERTALAKHlgAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--EQMISLADRII 548
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
2-160 |
3.35e-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: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 2 GELLAVMGSSGAGKTTLLNALAFRsargvqISPSSVrmlnghpvdakemqarcayvqqfdlfigsltarEHLIFQATVRM 81
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGV------LKPDEG---------------------------------DIEIELDTVSY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 82 -PRTMTQKQKMqRVDQVIQDLSLGKCQ----NTIIGVP--------GRVKGLSGGERKRLAFASEALTDPPLLICDEPTS 148
Cdd:cd03237 66 kPQYIKADYEG-TVRDLLSSITKDFYThpyfKTEIAKPlqieqildREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170
....*....|....*
gi 1151065379 149 GLDS---FMAASVVQ 160
Cdd:cd03237 145 YLDVeqrLMASKVIR 159
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
2-23 |
3.66e-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: 3.66e-04
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
9-191 |
4.80e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.51 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 9 GSSGAGKTTLLNALAFrsargvQISPSSVRMLNGHPVDAKemqarcayvqqfDLFIGSLTAREHLIFqaTVRMPRTMTQK 88
Cdd:cd03240 29 GQNGAGKTTIIEALKY------ALTGELPPNSKGGAHDPK------------LIREGEVRAQVKLAF--ENANGKKYTIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 89 QKMQRVDQVI---QDLSlgkcqNTIIgvPGRVKGLSGGERK------RLAFAsEALTDP-PLLICDEPTSGLDSF-MAAS 157
Cdd:cd03240 89 RSLAILENVIfchQGES-----NWPL--LDMRGRCSGGEKVlasliiRLALA-ETFGSNcGILALDEPTTNLDEEnIEES 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1151065379 158 VVQVLKK-LSQRGKTVILTIHQPssELFELFDKIL 191
Cdd:cd03240 161 LAEIIEErKSQKNFQLIVITHDE--ELVDAADHIY 193
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
116-177 |
4.93e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.18 E-value: 4.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065379 116 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLS-QRGKTVILTIH 177
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDH 512
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
89-175 |
9.06e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 89 QKMQRVDQV-IQDLSLGKCQNTiigvpgrvkgLSGGERKRLAFA---SEALTDPPLLIcDEPTSGLDSFMAASVVQVLKK 164
Cdd:PRK00635 1366 NRLTFIDKVgLSYITLGQEQDT----------LSDGEHYRLHLAkkiSSNLTDIIYLL-EDPLSGLHPQDAPTLLQLIKE 1434
|
90
....*....|.
gi 1151065379 165 LSQRGKTVILT 175
Cdd:PRK00635 1435 LVTNNNTVIAT 1445
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1-22 |
9.13e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.15 E-value: 9.13e-04
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
1-28 |
9.91e-04 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 38.25 E-value: 9.91e-04
10 20
....*....|....*....|....*...
gi 1151065379 1 PGELLAVMGSSGAGKTTLLNALAFRSAR 28
Cdd:COG3709 4 PGRLIYVVGPSGAGKDSLLAAARARLAA 31
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
120-173 |
1.47e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 120 LSGGERKRLAFASEaL----TDPPLLICDEPTSGL---DsfmAASVVQVLKKLSQRGKTVI 173
Cdd:COG0178 827 LSGGEAQRVKLASE-LskrsTGKTLYILDEPTTGLhfhD---IRKLLEVLHRLVDKGNTVV 883
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
117-191 |
1.52e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1151065379 117 VKGLSGGERK------RLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQpssELFELFDKI 190
Cdd:COG4717 556 VEELSRGTREqlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHE---ELVELFQEE 632
|
.
gi 1151065379 191 L 191
Cdd:COG4717 633 G 633
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
138-193 |
1.56e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 38.35 E-value: 1.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065379 138 PPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQPSSELFELFDKILLM 193
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
2-23 |
2.21e-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: 37.14 E-value: 2.21e-03
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
5-22 |
2.34e-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: 36.70 E-value: 2.34e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
116-177 |
3.17e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.92 E-value: 3.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1151065379 116 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsfmAASVVQVLKKLSQRGKTVILTIH 177
Cdd:PLN03073 341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
120-179 |
3.77e-03 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 36.85 E-value: 3.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1151065379 120 LSGGERKRLAFASE---ALTDPpLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIHQP 179
Cdd:cd03270 138 LSGGEAQRIRLATQigsGLTGV-LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
6-23 |
5.17e-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: 5.17e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-177 |
5.46e-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: 36.91 E-value: 5.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1151065379 120 LSGGERKRLAFASE---ALTDpPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:TIGR00630 489 LSGGEAQRIRLATQigsGLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEH 548
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
5-26 |
6.01e-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: 6.01e-03
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
120-177 |
7.69e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 36.64 E-value: 7.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1151065379 120 LSGGERKRLAFA--------SEALTDPPLLICDEPTSGLDSFMAASVVQVLKKLSQRGKTVILTIH 177
Cdd:COG4694 492 LSEGEKTAIALAyflaelegDENDLKKKIVVIDDPVSSLDSNHRFAVASLLKELSKKAKQVIVLTH 557
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
120-162 |
9.52e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 36.38 E-value: 9.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1151065379 120 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFMAASVVQVL 162
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL 670
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
6-38 |
9.94e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 35.01 E-value: 9.94e-03
10 20 30
....*....|....*....|....*....|...
gi 1151065379 6 AVMGSSGAGKTTLLNALAfrsarGVQISPSSVR 38
Cdd:cd11383 1 GLMGKTGAGKSSLCNALF-----GTEVAAVGDR 28
|
|
| |
