|
Name |
Accession |
Description |
Interval |
E-value |
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-300 |
2.10e-170 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 473.83 E-value: 2.10e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHLMGYLPEER 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 GLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGL 162
Cdd:COG4152 81 GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 163 DPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKGYPREEVVLRTAGEVNGLTEIA 242
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAGWLRALP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 243 GVTGVQRQERGYVLSINDLGAAQRILQLAVAQGEVEHFEIKEPTLNQIFIRAVGESNE 300
Cdd:COG4152 241 GVTVVEEDGDGAELKLEDGADAQELLRALLARGPVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-213 |
3.09e-107 |
|
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: 310.37 E-value: 3.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHLMGYLPEERG 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 LYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1133779397 164 PVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-234 |
2.25e-87 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 260.77 E-value: 2.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY---SKELQHLMGYLPE 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVardPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 161 GLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKGYPrEEVVLRTAGE 234
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL-EDVFLELTGE 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-227 |
6.94e-78 |
|
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: 237.06 E-value: 6.94e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKP---YSKELQHLMGYLPE 80
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDvrkEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 161 GLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKGYPREEV 227
Cdd:COG4555 162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENL 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-206 |
3.51e-66 |
|
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: 204.55 E-value: 3.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK---ELQHLMGYLPE 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKepeEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIiylaqlrgmsaseadkslkywlerfdvpeyynkkieELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1133779397 161 GLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDR 206
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-213 |
1.82e-57 |
|
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: 184.11 E-value: 1.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 18 AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK---ELQHLMGYLPEERGLYPKVKVSDQI 94
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepaEARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 95 IYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTV 174
Cdd:cd03266 100 EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1133779397 175 REMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:cd03266 180 RQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-213 |
1.20e-51 |
|
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: 168.91 E-value: 1.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGeIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK---ELQHLMGYLPE 80
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqpqKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 161 GLDPVNvellKDTVREM-RDLGTS--ILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:cd03264 160 GLDPEE----RIRFRNLlSELGEDriVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-213 |
2.74e-50 |
|
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: 165.08 E-value: 2.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHL--MGYLPEE 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALrrIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERfdvpEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSG 161
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLK----DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 162 LDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-219 |
4.57e-50 |
|
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: 164.99 E-value: 4.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYG--EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHL---MGYL 78
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAArqsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEA 158
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 159 FSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIK 219
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-295 |
1.64e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 166.80 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 12 QYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK-PYSKELQHL------MG-------Y 77
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvPFKRRKEFArrigvvFGqrsqlwwD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPeerglypkvkVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDE 157
Cdd:COG4586 111 LP----------AIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 158 AFSGLDPVNVELLKDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKGY-PREEVVLRTAGEV 235
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFgPYKTIVLELAEPV 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 236 NGLTEIAGVTGVQRQERGYVLSINDLGAAQRILQLAVAQGEVEHFEIKEPTLNQIfIRAV 295
Cdd:COG4586 261 PPLELPRGGEVIEREGNRVRLEVDPRESLAEVLARLLARYPVRDLTIEEPPIEEV-IRRI 319
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-218 |
7.99e-47 |
|
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: 157.11 E-value: 7.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQY-GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLMGYL 78
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKknlrELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 ---PEerglypkvkvsDQIIY----------LAQLrGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAA 145
Cdd:COG1122 81 fqnPD-----------DQLFAptveedvafgPENL-GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133779397 146 VVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
9.77e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.17 E-value: 9.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKElQHLMGYLPE 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-RRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ER----------------GLYPKVKVsdqiiylaqLRGMSASEADKSLKyWLERFDVPEYYNKKIEELSKGNQQKMgFVA 144
Cdd:COG1121 83 RAevdwdfpitvrdvvlmGRYGRRGL---------FRRPSRADREAVDE-ALERVGLEDLADRPIGELSGGQQQRV-LLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 145 -AVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSnTVVQGDIREI 218
Cdd:COG1121 152 rALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEV 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-225 |
2.43e-44 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 153.04 E-value: 2.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHL---MGYLP 79
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHArqrVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAF 159
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 160 SGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSntvvqgdiREIKKGYPRE 225
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG--------RKIAEGAPHA 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-206 |
1.36e-43 |
|
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: 148.07 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 5 QLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKElQHLMGYLPEER-- 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-RKRIGYVPQRRsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 --------------GLYPKVKVsdqiiylaqLRGMSASEADKsLKYWLERFDVPEYYNKKIEELSKGNQQKMgFVA-AVV 147
Cdd:cd03235 80 drdfpisvrdvvlmGLYGHKGL---------FRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRV-LLArALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 148 HKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDR 206
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-189 |
4.28e-43 |
|
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: 146.47 E-value: 4.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK---ELQHLMGYLPE 80
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDareDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIIYLAQLRGMSASEADksLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180
....*....|....*....|....*....
gi 1133779397 161 GLDPVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-218 |
1.30e-42 |
|
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: 153.14 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQY-----GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS-------KEL 71
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrrslREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 72 QHLMGYLPE--ERGLYPKVKVSDQIIY-LAQLRGMSASEADKSLKYWLERFD-VPEYYNKKIEELSKGNQQKMGFVAAVV 147
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGlPPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 148 HKPKILILDEAFSGLDPVN----VELLKDTVREmrdLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVqaqiLNLLRDLQRE---LGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-219 |
5.87e-42 |
|
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: 144.05 E-value: 5.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE---LQHLMGYLPE 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREpreVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 161 GLDPVNVELLKDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIK 219
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-215 |
1.31e-41 |
|
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: 143.45 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG-----KPYSKELQHLMGYL 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditkLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEA 158
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 159 FSGLDPVNVELLKDTVREMRDLGTSILFSTHrmeHVEELcrnITILDRSNTVVQGDI 215
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDH---NVRET---LSITDRAYIIYEGKV 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-189 |
5.21e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 145.24 E-value: 5.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSkelqHLmgyLPE 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GL---PPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERG---------LYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKmgfVA---AVVH 148
Cdd:COG3842 76 KRNvgmvfqdyaLFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQR---VAlarALAP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1133779397 149 KPKILILDEAFSGLDPVNVELLKDTVREM-RDLGTSILFSTH 189
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTH 194
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-228 |
9.50e-41 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 141.71 E-value: 9.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGkpysKELQHL------ 74
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG----EDITHLpmhkra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 ---MGYLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPK 151
Cdd:COG1137 77 rlgIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 152 ILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHrmeHVEELcrnITILDRSNTVVQGDIreIKKGYPrEEVV 228
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH---NVRET---LGICDRAYIISEGKV--LAEGTP-EEIL 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-206 |
1.29e-40 |
|
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: 138.53 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 5 QLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKelqhlmgylpeergl 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 YPKVKVSDQIIYLAQlrgmsaseadkslkywlerfdvpeyynkkieeLSKGNQQKMGFVAAVVHKPKILILDEAFSGLDP 164
Cdd:cd00267 66 LPLEELRRRIGYVPQ--------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1133779397 165 VNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDR 206
Cdd:cd00267 114 ASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-206 |
1.55e-40 |
|
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: 140.29 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 5 QLKQVVKQY--GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGYL 78
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTklslKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 ---PEERGLYPKVKvsDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:cd03225 81 fqnPDDQFFGPTVE--EEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 156 DEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDR 206
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-218 |
1.77e-40 |
|
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: 140.90 E-value: 1.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGE-KTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLMGYL 78
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdpvELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVP--EYYNKKIEELSKGNQQKMGFVAAVVHKPKILILD 156
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133779397 157 EAFSGLDPVNVELLKDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-206 |
1.90e-40 |
|
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: 139.96 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHL--MGYLPEE 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSG 161
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1133779397 162 LDPVNVELLKDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDR 206
Cdd:cd03259 161 LDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-215 |
6.57e-39 |
|
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: 136.64 E-value: 6.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHL-----MGYL 78
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHErarlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYPKVKVSDQIIYLAQLRG-MSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDE 157
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 158 AFSGLDPVNVELLKDTVREMRDLGTSILFSTHrmeHVEELcrnITILDRSNTVVQGDI 215
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDH---NVRET---LDICDRAYIISDGKV 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-300 |
7.89e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 139.58 E-value: 7.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY---SKELQHLMGYLP 79
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVparARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAF 159
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 160 SGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG------------DIREIKKGYPRE-- 225
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGrphalidehigcQVIEIYGGDPHEls 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 226 EVVLRTAGEVngltEIAGVT---------GVQRQERGYvlsindlgAAQRILQlavaqgevehfeiKEPTLNQIFIRAVG 296
Cdd:PRK13536 281 SLVKPYARRI----EVSGETlfcyapdpeQVRVQLRGR--------AGLRLLQ-------------RPPNLEDVFLRLTG 335
|
....
gi 1133779397 297 ESNE 300
Cdd:PRK13536 336 REME 339
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-220 |
1.09e-38 |
|
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: 136.26 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHL---M 75
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYELrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 76 GYLPEERGLYPKVKVSDQIIY-LAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSkGNQQKMgfVA---AVVHKPK 151
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFpLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELS-GGMRKR--VAlarALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 152 ILILDEAFSGLDPVNVELLKDTVREMRD-LGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKK 220
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDeLGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-219 |
1.99e-38 |
|
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: 134.87 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHL-----MGYL 78
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYPKVKVSDQIIYLAQLRGMSASEADksLKYWLERFDV-PEYYNKKIEELSkGNQQKMgfVA---AVVHKPKILI 154
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKAR--LERVYELFPRlKERRKQLAGTLS-GGEQQM--LAiarALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 155 LDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIK 219
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-220 |
3.18e-38 |
|
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: 134.94 E-value: 3.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHL---MG 76
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLrrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YLPEERGLYPKVKVSDQIIY-LAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFpLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 156 DEAFSGLDPVNVELLKDTVREMRD-LGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKK 220
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-213 |
1.33e-37 |
|
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: 133.23 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 6 LKQVVK-QYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK-PYSKELQHL--MGYLPEE 81
Cdd:cd03267 23 LKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKKFLrrIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RG-LYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:cd03267 103 KTqLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 161 GLDPVNVELLKDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:cd03267 183 GLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-205 |
5.30e-37 |
|
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: 130.00 E-value: 5.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKP------YSKELQHLMGY 77
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPEERGLYPKVKVSDQIIYLaqlrgmsaseadkslkywlerfdvpeyynkkieeLSKGNQQKMGFVAAVVHKPKILILDE 157
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1133779397 158 AFSGLDPVNVELLKDTVREMRD-LGTSILFSTHRMEHVEELCRNITILD 205
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-189 |
6.09e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 134.43 E-value: 6.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGkpysKELQHLMgylPE 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTDLP---PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERG---------LYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKmgfVA---AVVH 148
Cdd:COG3839 74 DRNiamvfqsyaLYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR---VAlgrALVR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1133779397 149 KPKILILDEAFSGLDPvnveLLKDTVRE-----MRDLGTSILFSTH 189
Cdd:COG3839 151 EPKVFLLDEPLSNLDA----KLRVEMRAeikrlHRRLGTTTIYVTH 192
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-220 |
6.16e-37 |
|
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: 131.41 E-value: 6.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPyskelqhLMGYLPEER- 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED-------ITGLPPHEIa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 -----------GLYPKVKVSDQIIYLAQLRGMSASEADKSLKY----------WLERFDVPEYYNKKIEELSKGNQQKMG 141
Cdd:cd03219 74 rlgigrtfqipRLFPELTVLENVMVAAQARTGSGLLLARARREereareraeeLLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 142 FVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKK 220
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-189 |
1.14e-36 |
|
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: 130.28 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYG----EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPySKELQHLMGYLP 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-VTGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAF 159
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190
....*....|....*....|....*....|.
gi 1133779397 160 SGLDPVNVELLKDTVREM-RDLGTSILFSTH 189
Cdd:cd03293 160 SALDALTREQLQEELLDIwRETGKTVLLVTH 190
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-225 |
1.15e-36 |
|
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: 130.82 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPyskelqhLMGYLPEERG 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD-------ITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 ---------LYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:cd03300 74 vntvfqnyaLFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 155 LDEAFSGLDpvnVELLKDTVREM----RDLGTSILFSTHRMEhvEELcrniTILDRSNTVVQGDIREIkkGYPRE 225
Cdd:cd03300 154 LDEPLGALD---LKLRKDMQLELkrlqKELGITFVFVTHDQE--EAL----TMSDRIAVMNKGKIQQI--GTPEE 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-218 |
1.51e-36 |
|
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: 130.39 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 6 LKQVVKQYGEK----TAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHL--- 74
Cdd:cd03258 4 LKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKArrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 MGYLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 155 LDEAFSGLDPVN----VELLKDTVREmrdLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:cd03258 164 CDEATSALDPETtqsiLALLRDINRE---LGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-246 |
8.87e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.99 E-value: 8.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY-------SKEL---- 71
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsprdAQAAgiai 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 72 --QHL-------------MGYLPEERGLYPKVKVSDQiiylaqlrgmsASEAdkslkywLERFDVPEYYNKKIEELSKGN 136
Cdd:COG1129 84 ihQELnlvpnlsvaenifLGREPRRGGLIDWRAMRRR-----------AREL-------LARLGLDIDPDTPVGDLSVAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 137 QQkmgFVA---AVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:COG1129 146 QQ---LVEiarALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 214 DI--------------REIKKGYPRE-----EVVLrtagEVNGLT---------------EIAGVTG 246
Cdd:COG1129 223 PVaeltedelvrlmvgRELEDLFPKRaaapgEVVL----EVEGLSvggvvrdvsfsvragEILGIAG 285
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-213 |
9.03e-36 |
|
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: 128.39 E-value: 9.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEK----TAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS-------KELQ 72
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrrlrKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 73 HLMGYLPEE--RGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVP---EYYNKKIEELSKGNQQKMGFVAAVV 147
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 148 HKPKILILDEAFSGLDPVNVELLKDTVREMRD-LGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-204 |
1.17e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 134.00 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS-------KEL---- 71
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdaIALgigm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 72 --QHLM-------------GYLPEERGLYPKVKVSDQIIYLAQlrgmsaseadkslKYwleRFDVPEyyNKKIEELSKGN 136
Cdd:COG3845 85 vhQHFMlvpnltvaenivlGLEPTKGGRLDRKAARARIRELSE-------------RY---GLDVDP--DAKVEDLSVGE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 137 QQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITIL 204
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVL 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-204 |
1.83e-35 |
|
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: 125.23 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSkelqhlmGYLPEErg 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-------FASPRD-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 lypkvkvsdqiiylAQLRGMSAseadkslkywlerfdvpeyynkkIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:cd03216 72 --------------ARRAGIAM-----------------------VYQLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1133779397 164 PVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITIL 204
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-205 |
5.00e-35 |
|
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: 126.07 E-value: 5.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYG----EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHL- 74
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 ---MGYLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPK 151
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 152 ILILDEAFSGLDPVN----VELLKDTVREMrdlGTSILFSTHRMEHVEELCRNITILD 205
Cdd:cd03255 161 IILADEPTGNLDSETgkevMELLRELNKEA---GTTIVVVTHDPELAEYADRIIELRD 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-218 |
1.03e-34 |
|
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: 126.31 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGYL 78
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAslsrRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYPKVKVSDQIIY--LAQLRGMSA-SEADKSLKYW-LERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgrYPHLGLFGRpSAEDREAVEEaLERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 155 LDEAFSGLDPVN-VELLkDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:COG1120 161 LDEPTSHLDLAHqLEVL-ELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-213 |
1.44e-34 |
|
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: 123.70 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 5 QLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKelqhlmgylpeergl 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 YPKVKVSDQIIYLAQLrgmsaseadkslkywLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDP 164
Cdd:cd03214 66 LSPKELARKIAYVPQA---------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 165 VN-VELLkDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:cd03214 131 AHqIELL-ELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-160 |
1.93e-34 |
|
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: 122.37 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 19 VNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKP-YSKELQHL---MGYLPEERGLYPKVKVSDQI 94
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDlTDDERKSLrkeIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 95 IYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIE----ELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-218 |
3.45e-34 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 124.62 E-value: 3.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK-----PYSKELQHLM 75
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 76 GYLPEERGLYPKVKVSDQIIYLAQLR-GMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 155 LDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-218 |
3.87e-34 |
|
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: 124.32 E-value: 3.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGkpysKELQHL------ 74
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDITGLpphria 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 ---MGYLPEERGLYPKVKVSDQIIyLAQLRGMSASEADKSLKYWLERFdvP---EYYNKKIEELSkGNQQKMgfVA---A 145
Cdd:COG0410 77 rlgIGYVPEGRRIFPSLTVEENLL-LGAYARRDRAEVRADLERVYELF--PrlkERRRQRAGTLS-GGEQQM--LAigrA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133779397 146 VVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-218 |
4.34e-34 |
|
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: 123.52 E-value: 4.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKpyskelqhLMGYL-PEER 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--------DVTDLpPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 G---------LYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKIL 153
Cdd:cd03301 73 DiamvfqnyaLYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 154 ILDEAFSGLDP-VNVELLKDTVREMRDLGTSILFSTHrmEHVEELcrniTILDRSNTVVQGDIREI 218
Cdd:cd03301 153 LMDEPLSNLDAkLRVQMRAELKRLQQRLGTTTIYVTH--DQVEAM----TMADRIAVMNDGQIQQI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-277 |
6.18e-34 |
|
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: 129.25 E-value: 6.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 ME-ALQLKQVVKQY--GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPD---EGSILYNGKPYSKELQHL 74
Cdd:COG1123 1 MTpLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 ----MGYLPEE--RGLYPkVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVH 148
Cdd:COG1123 81 rgrrIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 149 KPKILILDEAFSGLDPVNVELLKDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKGYPREEV 227
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 228 VLRtagevngLTEIAGVTGVQRQERGYVLSINDL--------GAAQRILQ---LAVAQGEV 277
Cdd:COG1123 240 VPR-------LGAARGRAAPAAAAAEPLLEVRNLskrypvrgKGGVRAVDdvsLTLRRGET 293
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-220 |
3.99e-33 |
|
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: 122.07 E-value: 3.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSkelqhlmGYLPE 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-------GLPPH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ER------------GLYPKVKVSDQIIyLAQLRGMSASEADKSLKYW----------------LERFDVPEYYNKKIEEL 132
Cdd:COG0411 75 RIarlgiartfqnpRLFPELTVLENVL-VAAHARLGRGLLAALLRLPrarreereareraeelLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 133 SKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRD-LGTSILFSTHRMEHVEELCRNITILDRSNTVV 211
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
|
....*....
gi 1133779397 212 QGDIREIKK 220
Cdd:COG0411 234 EGTPAEVRA 242
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-218 |
4.03e-33 |
|
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: 122.12 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEG---SILynGKPYSK----ELQH 73
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGedvwELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 74 LMGYL-PE-ERGLYPKVKVSDQII--YLAQL-RGMSASEADKSL-KYWLERFDVPEYYNKKIEELSKGnQQKMGFVA-AV 146
Cdd:COG1119 79 RIGLVsPAlQLRFPRDETVLDVVLsgFFDSIgLYREPTDEQRERaRELLELLGLAHLADRPFGTLSQG-EQRRVLIArAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 147 VHKPKILILDEAFSGLDPVNVELLKDTVREMRDLG-TSILFSTHrmeHVEELCRNIT---ILDRSNTVVQGDIREI 218
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTH---HVEEIPPGIThvlLLKDGRVVAAGPKEEV 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-191 |
1.73e-30 |
|
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: 114.16 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHL------MGY 77
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelrqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPEERGLYPKVKVSDQIIY-LAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILD 156
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1133779397 157 EAFSGLDPvnvELLKDTVREMRDL---GTSILFSTHRM 191
Cdd:cd03262 161 EPTSALDP---ELVGEVLDVMKDLaeeGMTMVVVTHEM 195
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-189 |
5.22e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 112.84 E-value: 5.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQY-GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHL---M 75
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 76 GYLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKmgfVA---AVVHKPKI 152
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQR---VAiarALVNRPEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1133779397 153 LILDEAFSGLDPVN----VELLKdtvrEMRDLGTSILFSTH 189
Cdd:COG2884 159 LLADEPTGNLDPETsweiMELLE----EINRRGTTVLIATH 195
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-218 |
1.42e-29 |
|
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: 113.12 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 7 KQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHL----MGYL 78
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsrKELRELrrkkISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEA 158
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 159 FSGLDPvnveLLKdtvREMRD--------LGTSILFSTHRMEHVEELCRNITILdRSNTVVQ-GDIREI 218
Cdd:cd03294 188 FSALDP----LIR---REMQDellrlqaeLQKTIVFITHDLDEALRLGDRIAIM-KDGRLVQvGTPEEI 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-218 |
8.06e-29 |
|
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: 110.35 E-value: 8.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGE-KTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE-------LQHLM 75
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkalrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 76 GYLPEERGLYPKVKVSDQII-----YLAQLRGMSA--SEADKSL-KYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVV 147
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLsgrlgRRSTWRSLFGlfPKEEKQRaLAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 148 HKPKILILDEAFSGLDPVNVELLKDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-189 |
8.16e-29 |
|
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: 109.05 E-value: 8.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKP--YSK----ELQHLMGYL---PEERGL 84
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPldYSRkgllERRQRVGLVfqdPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 YPKVkvsDQIIYLAQLR-GMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:TIGR01166 83 AADV---DQDVAFGPLNlGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*.
gi 1133779397 164 PVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-213 |
9.06e-29 |
|
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: 109.93 E-value: 9.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 10 VKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK-ELQhlMGYLPEERGLypkv 88
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLlGLG--GGFNPELTGR---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 89 kvsDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVE 168
Cdd:cd03220 103 ---ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1133779397 169 LLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-205 |
1.46e-28 |
|
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: 107.47 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYG--EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLMGY 77
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDldleSLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPeerglypkvkvsdQIIYLaqlrgMSASeadkslkywlerfdvpeyynkkIEE--LSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:cd03228 81 VP-------------QDPFL-----FSGT----------------------IREniLSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1133779397 156 DEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHVeELCRNITILD 205
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTI-RDADRIIVLD 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-222 |
1.69e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.40 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 11 KQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK-ELQhlMGYLPEERGLypkvk 89
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALlELG--AGFHPELTGR----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 90 vsDQIIYLAQLRGMSASEADkslkywlERFD-------VPEYYNKKIEELSKGNQQKMGF-VAAVVhKPKILILDEAFSG 161
Cdd:COG1134 107 --ENIYLNGRLLGLSRKEID-------EKFDeivefaeLGDFIDQPVKTYSSGMRARLAFaVATAV-DPDILLVDEVLAV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 162 LDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKGY 222
Cdd:COG1134 177 GDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-300 |
2.43e-28 |
|
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: 115.11 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKT--AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY---SKELQHLMGYL 78
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEA 158
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 159 FSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKK----GY--------PREE 226
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSkfgdGYivtmkiksPKDD 2177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 227 vVLRTAGEVNGLTEIAGVTGVQRQERGYVLSIN-DLGAAQRILQLAVAQGE---VEHFEIKEPTLNQIFIRAVGESNE 300
Cdd:TIGR01257 2178 -LLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQvSSSSLARIFQLLISHKDsllIEEYSVTQTTLDQVFVNFAKQQTE 2254
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-191 |
7.26e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 113.30 E-value: 7.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 11 KQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY-SKELQHLM--GYLPEERGLYPK 87
Cdd:NF033858 274 MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDIATRRrvGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 88 VKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNV 167
Cdd:NF033858 354 LTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
170 180
....*....|....*....|....*...
gi 1133779397 168 ----ELLKDTVRemRDlGTSILFSTHRM 191
Cdd:NF033858 434 dmfwRLLIELSR--ED-GVTIFISTHFM 458
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-213 |
3.29e-27 |
|
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: 111.64 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 6 LKQVVKQYGeKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKEL---QHLMGYLPEER 82
Cdd:TIGR01257 934 LVKIFEPSG-RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLdavRQSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 GLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGL 162
Cdd:TIGR01257 1013 ILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 163 DPVNVELLKDTVREMRDlGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-228 |
5.02e-27 |
|
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: 105.50 E-value: 5.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 21 GISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK---PYSKElQHLMGYLPEERGLYPKVKVSDQIIYL 97
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPE-KRDISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 98 AQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREM 177
Cdd:cd03299 96 LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 178 RD-LGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKgYPREEVV 228
Cdd:cd03299 176 RKeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK-KPKNEFV 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-218 |
6.56e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.47 E-value: 6.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQY----GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KEL---- 71
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalseRELraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 72 -------QH------------------LMGYLPEERglypKVKVSDqiiyLAQLRGMSaseaDKSLKYwlerfdvPeyyn 126
Cdd:COG1135 82 rkigmifQHfnllssrtvaenvalpleIAGVPKAEI----RKRVAE----LLELVGLS----DKADAY-------P---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 127 kkiEELSKGNQQKMGfVA-AVVHKPKILILDEAFSGLDPVN----VELLKDtVRemRDLGTSILFSTHRMEHVEELCRNI 201
Cdd:COG1135 139 ---SQLSGGQKQRVG-IArALANNPKVLLCDEATSALDPETtrsiLDLLKD-IN--RELGLTIVLITHEMDVVRRICDRV 211
|
250
....*....|....*..
gi 1133779397 202 TILDRSNTVVQGDIREI 218
Cdd:COG1135 212 AVLENGRIVEQGPVLDV 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-218 |
9.37e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.09 E-value: 9.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKT-AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKP--YSK----ELQHLMG 76
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidYSRkglmKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 --YLPEERGLYpKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:PRK13636 86 mvFQDPDNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 155 LDEAFSGLDPVNV-ELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK13636 165 LDEPTAGLDPMGVsEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-225 |
1.33e-26 |
|
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: 109.54 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYG--EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLMG 76
Cdd:COG2274 473 DIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQidpaSLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YLPEERGLYP----------KVKVSD-QIIYLAQLRGmsASEADKSLkywlerfdvPEYYNKKIEE----LSKGNQQKMG 141
Cdd:COG2274 553 VVLQDVFLFSgtirenitlgDPDATDeEIIEAARLAG--LHDFIEAL---------PMGYDTVVGEggsnLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 142 FVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHVeELCRNITILDRSNTVVQGDIREI--K 219
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELlaR 699
|
....*.
gi 1133779397 220 KGYPRE 225
Cdd:COG2274 700 KGLYAE 705
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-206 |
1.56e-26 |
|
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: 103.64 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKT-AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK-------ELQHLM 75
Cdd:cd03292 1 IEFINVTKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraipYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 76 GYLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 156 DEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDR 206
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-211 |
6.15e-26 |
|
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: 101.95 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 9 VVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS-KELQHLMGYLPEE--RGLY 85
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKaKERRKSIGYVMQDvdYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 86 pKVKVSDQIIYLAQLRGMSASEADKSLKywleRFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPV 165
Cdd:cd03226 86 -TDSVREELLLGLKELDAGNEQAETVLK----DLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1133779397 166 NVELLKDTVREMRDLGTSILFSTHRMEHVEELCrNITILDRSNTVV 211
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITHDYEFLAKVC-DRVLLLANGAIV 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-236 |
1.83e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 104.26 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGkpyskelQHLMGYLPEER- 82
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG-------QDITHVPAENRh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 --------GLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:PRK09452 88 vntvfqsyALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 155 LDEAFSGLDpvnVELLKDTVREM----RDLGTSILFSTHRMEhvEELcrniTILDRSNTVVQGDIREIkkGYPRE--E-- 226
Cdd:PRK09452 168 LDESLSALD---YKLRKQMQNELkalqRKLGITFVFVTHDQE--EAL----TMSDRIVVMRDGRIEQD--GTPREiyEep 236
|
250
....*....|...
gi 1133779397 227 ---VVLRTAGEVN 236
Cdd:PRK09452 237 knlFVARFIGEIN 249
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-218 |
2.72e-25 |
|
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: 100.72 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIY-----PDEGSILYNGKPYSK------ELQ 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldvdvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 73 HLMGYLPEERGLYPKvKVSDQIIYLAQLRGMSASEADKSLKYW-LERFDVPEYYNKKIE--ELSKGNQQKMGFVAAVVHK 149
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVEEaLRKAALWDEVKDRLHalGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 150 PKILILDEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-225 |
3.01e-25 |
|
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: 100.88 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE--LQHLMGYLPE 80
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVpvQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIIYLAQLR----GMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILD 156
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 157 EAFSGLDPVNVELLKDTVREMRD-LGTSILFSTHRMEHVEELCRNITILDrsntvvQGDIREIkkGYPRE 225
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDeLHVTTVFVTHDQEEALEVADRVVVMN------KGRIEQV--GTPDE 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-228 |
4.07e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.75 E-value: 4.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK---ELQHLMG-YL- 78
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpAKAHQLGiYLv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYPKVKVSDQIIYlaqlrGMSASEADKS-LKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDE 157
Cdd:PRK15439 92 PQEPLLFPNLSVKENILF-----GLPKRQASMQkMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 158 AFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREikkgYPREEVV 228
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD----LSTDDII 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-230 |
1.25e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.09 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRmVLGLIYPD---EGSILYNGKPysKELQHLMGylPE 80
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEIIFEGEE--LQASNIRD--TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLypkvkvsdQIIY--LAQLRGMSASE----------------------ADKslkyWLERFDVPEYYNKKIEELSKGN 136
Cdd:PRK13549 81 RAGI--------AIIHqeLALVKELSVLEniflgneitpggimdydamylrAQK----LLAQLKLDINPATPVGNLGLGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 137 QQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITIL--------DRSN 208
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIrdgrhigtRPAA 228
|
250 260 270
....*....|....*....|....*....|...
gi 1133779397 209 TVVQGDI------REIKKGYPRE-----EVVLR 230
Cdd:PRK13549 229 GMTEDDIitmmvgRELTALYPREphtigEVILE 261
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-218 |
1.27e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.42 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 5 QLKQVVKQY----GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY----SKEL----- 71
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 72 ------QHLmgYLPEERglypkvKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAA 145
Cdd:PRK11153 83 qigmifQHF--NLLSSR------TVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 146 VVHKPKILILDEAFSGLDPVN----VELLKDTVREmrdLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATtrsiLELLKDINRE---LGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-189 |
4.03e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.18 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE--LQHLMGYLPEE 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRsiQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSG 161
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180
....*....|....*....|....*....
gi 1133779397 162 LDPVNVELLKDTVREMRD-LGTSILFSTH 189
Cdd:PRK11432 167 LDANLRRSMREKIRELQQqFNITSLYVTH 195
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-213 |
1.92e-23 |
|
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: 94.93 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLI--YPDEGSILYNGKP-YSKELQHLMGYLPEERGLYPKVKV 90
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPlDKRSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 91 SDQIIYLAQLRGMSASEadkslkywlerfdvpeyynKKieELSKGNQqkmgfvaaVVHKPKILILDEAFSGLDPVNVELL 170
Cdd:cd03213 100 RETLMFAAKLRGLSGGE-------------------RK--RVSIALE--------LVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1133779397 171 KDTVREMRDLGTSILFSTHRM-EHVEELCRNITILDRSNTVVQG 213
Cdd:cd03213 151 MSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-246 |
3.46e-23 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 97.50 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAG--KTTTMRMVLGliyPDEGSILYNGKPY---SKELQHLMG- 76
Cdd:NF000106 13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWcanRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILD 156
Cdd:NF000106 90 HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 157 EAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKGYPREEVVLRT--AGE 234
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPahAAE 249
|
250 260
....*....|....*....|.
gi 1133779397 235 VN---------GLTEIAGVTG 246
Cdd:NF000106 250 LDrmvgaiaqaGLDGIAGATA 270
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-204 |
1.32e-22 |
|
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: 93.13 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 29 GEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY---SKEL-----QHLMGYLPEERGLYPKVKVSDQIIYlaQL 100
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsRKKInlppqQRKIGLVFQQYALFPHLNVRENLAF--GL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 101 RGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD-PVNVELLKDTVREMRD 179
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDrALRLQLLPELKQIKKN 180
|
170 180
....*....|....*....|....*
gi 1133779397 180 LGTSILFSTHRMEHVEELCRNITIL 204
Cdd:cd03297 181 LNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-189 |
1.63e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGYLP 79
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkpEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EERGLYPKVkVSDQIIYLAQLRGMSASEadKSLKYWLERFDVPEY-YNKKIEELSKGNQQKMGFVAAVVHKPKILILDEA 158
Cdd:PRK10247 88 QTPTLFGDT-VYDNLIFPWQIRNQQPDP--AIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|..
gi 1133779397 159 FSGLDPVNVELLKDTV-REMRDLGTSILFSTH 189
Cdd:PRK10247 165 TSALDESNKHNVNEIIhRYVREQNIAVLWVTH 196
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-196 |
1.94e-22 |
|
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: 97.14 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQY-GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGY 77
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdldpASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPEERGLYP----------KVKVSD-QIIYLAQLRGMSAseadkslkyWLERFdvPEYYNKKIEE----LSKGNQQKMGF 142
Cdd:COG4988 416 VPQNPYLFAgtirenlrlgRPDASDeELEAALEAAGLDE---------FVAAL--PDGLDTPLGEggrgLSGGQAQRLAL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 143 VAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHVEE 196
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ 537
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
2.11e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.99 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKT-AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKP--YSK----ELQHLMG 76
Cdd:PRK13639 2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikYDKksllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YL---PEERGLYPKVKvsDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKIL 153
Cdd:PRK13639 82 IVfqnPDDQLFAPTVE--EDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 154 ILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILdrsntvVQGDIreIKKGYPRE 225
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVM------SDGKI--IKEGTPKE 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-280 |
5.91e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.62 E-value: 5.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKeLQHLMGYlpeERG 83
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK-LDHKLAA---QLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 ---LYPKVKVSDQI-----IYLAQLRG--------MSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVV 147
Cdd:PRK09700 82 igiIYQELSVIDELtvlenLYIGRHLTkkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 148 HKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDI------------ 215
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVsdvsnddivrlm 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 216 --REIKKGYP-REEVVLRTAGEVnglteIAGVTGVQRQERGYVLSINdlgaaqrilqLAVAQGEVEHF 280
Cdd:PRK09700 242 vgRELQNRFNaMKENVSNLAHET-----VFEVRNVTSRDRKKVRDIS----------FSVCRGEILGF 294
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-197 |
7.35e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 95.05 E-value: 7.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQY-GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY----SKELQHLMGY 77
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadadADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPEERGLYPKvKVSDQIIyLAQlRGMSASEADKSL-KYWLERF--DVPEYYNKKIEE----LSKGNQQKMGFVAAVVHKP 150
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIR-LAR-PDASDAEIREALeRAGLDEFvaALPQGLDTPIGEggagLSGGQAQRLALARAFLRDA 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1133779397 151 KILILDEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHVEEL 197
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALA 523
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-219 |
9.72e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.59 E-value: 9.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPyskeLQHLMGYLPEERG 83
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQH----IEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 L---YPKVKVSDQIIYL-----AQ--------LRGM--------SASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQK 139
Cdd:PRK11300 82 VvrtFQHVRLFREMTVIenllvAQhqqlktglFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 140 MGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRD-LGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
.
gi 1133779397 219 K 219
Cdd:PRK11300 242 R 242
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-198 |
1.73e-21 |
|
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: 89.03 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 16 KTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY-----SKELQHLMGYLPEER---GLYPK 87
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrrspRDAIRAGIAYVPEDRkreGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 88 VKVSDQIIyLAQLrgmsaseadkslkywlerfdvpeyynkkieeLSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNV 167
Cdd:cd03215 93 LSVAENIA-LSSL-------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190
....*....|....*....|....*....|.
gi 1133779397 168 ELLKDTVREMRDLGTSILFSTHRMEHVEELC 198
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSELDELLGLC 171
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-218 |
2.12e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK------PYSKELQHLMgy 77
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvpPYQRPINMMF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 lpEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDE 157
Cdd:PRK11607 98 --QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 158 AFSGLDpvnvELLKDTVR-EMRDL----GTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK11607 176 PMGALD----KKLRDRMQlEVVDIlervGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-186 |
2.31e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.32 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK-----PYSKELQHLM 75
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 76 GYLPEERGLYPKVKVSDQIiylaqlrGMSASEADKslKYWLERFD-----VPEYYNKKIEE---LSKGNQQKMGFVAAVV 147
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENL-------AMGGFFAER--DQFQERIKwvyelFPRLHERRIQRagtMSGGEQQMLAIGRALM 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1133779397 148 HKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILF 186
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFL 192
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-240 |
3.01e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.84 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 12 QYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKP--YSKE----LQHLMGYL---PEER 82
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKRgllaLRQQVATVfqdPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 GLYPKVKvSDQIIYLAQLrGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGL 162
Cdd:PRK13638 90 IFYTDID-SDIAFSLRNL-GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 163 DPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIkkgYPREEVVlrtagEVNGLTE 240
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV---FACTEAM-----EQAGLTQ 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
3.15e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY----SKELQHLMG 76
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YLPEERGLYPKVKVsDQIIYLAQL----RGMSASEADK-SLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPK 151
Cdd:PRK09536 81 SVPQDTSLSFEFDV-RQVVEMGRTphrsRFDTWTETDRaAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 152 ILILDEAFSGLDpVN--VELLkDTVREMRDLGTSILFSTHRMEHVEELCRNITILdrsntvVQGDIREIkkGYPRE 225
Cdd:PRK09536 160 VLLLDEPTASLD-INhqVRTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLL------ADGRVRAA--GPPAD 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-198 |
3.69e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 90.71 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 17 TAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKEL-QHLMGYLP--EERGLYPKVKVSDQ 93
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqKNLVAYVPqsEEVDWSFPVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 94 II-----YLAQLRgMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVE 168
Cdd:PRK15056 101 VMmgrygHMGWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190
....*....|....*....|....*....|
gi 1133779397 169 LLKDTVREMRDLGTSILFSTHRMEHVEELC 198
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-266 |
4.05e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.14 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEA-LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRmVLGLIYP-DEGSILYNGKPYS----KELQHL 74
Cdd:PRK10762 1 MQAlLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMK-VLTGIYTrDAGSILYLGKEVTfngpKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 -MGYLPEERGLYPKVKVSDQiIYLA----------QLRGMSAsEADKSLKywleRFDVPEYYNKKIEELSKGNQQKMGFV 143
Cdd:PRK10762 80 gIGIIHQELNLIPQLTIAEN-IFLGrefvnrfgriDWKKMYA-EADKLLA----RLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 144 AAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKG-- 221
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDsl 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 222 ------------YPREEVVL-RTAGEVNGLTEiAGVTGVQRQ-ERGYVLSINDLGAAQR 266
Cdd:PRK10762 234 iemmvgrkledqYPRLDKAPgEVRLKVDNLSG-PGVNDVSFTlRKGEILGVSGLMGAGR 291
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-214 |
4.07e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 89.77 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG------KPYSKELQHLMGY 77
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPEERGLYPKVKVSDQIIY-LAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILD 156
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 157 EAFSGLDPvnvELLKDTVREMRDL---GTSILFSTHRMEHVEELCRNITILDRSNTVVQGD 214
Cdd:PRK09493 162 EPTSALDP---ELRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-192 |
4.27e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.14 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHlMGYLPEER 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE-RGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 GLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGL 162
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190
....*....|....*....|....*....|.
gi 1133779397 163 DPVNVELLKD-TVREMRDLGTSILFSTHRME 192
Cdd:PRK11248 160 DAFTREQMQTlLLKLWQETGKQVLLITHDIE 190
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-204 |
4.97e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.43 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAvnGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKelqhlmgYLPEERG 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-------LPPAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 ---------LYPKVKVSdQIIYLAqLR-GMSASEADKS-LKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKI 152
Cdd:COG3840 73 vsmlfqennLFPHLTVA-QNIGLG-LRpGLKLTAEQRAqVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 153 LILDEAFSGLDPVnvelLKdtvREMRDLgtsilfsthrmehVEELC--RNITIL 204
Cdd:COG3840 151 LLLDEPFSALDPA----LR---QEMLDL-------------VDELCreRGLTVL 184
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-224 |
5.14e-21 |
|
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: 92.91 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQY--GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMG 76
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdldeDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YLPEErglypkvkvsdqiIYL--AQLRG------MSASEAD-------KSLKYWLERFdvPEYYNKKIEE----LSKGNQ 137
Cdd:COG4987 413 VVPQR-------------PHLfdTTLREnlrlarPDATDEElwaalerVGLGDWLAAL--PDGLDTWLGEggrrLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 138 QKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHVEELCRnITILDRSNTVVQGDIRE 217
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERMDR-ILVLEDGRIVEQGTHEE 555
|
....*..
gi 1133779397 218 IKKGYPR 224
Cdd:COG4987 556 LLAQNGR 562
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-189 |
6.80e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.39 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY-SKELQHLMGYLPEERGLYPKVKVSD 92
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIdDPDVAEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 93 QIIYLAQLRGMSASEADKSlkywLERFDVPEYYNKKIEELSKGNQQKMGFvaA---VVHKPkILILDEAFSGLDPVNVEL 169
Cdd:PRK13539 93 NLEFWAAFLGGEELDIAAA----LEAVGLAPLAHLPFGYLSAGQKRRVAL--ArllVSNRP-IWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|
gi 1133779397 170 LKDTVREMRDLGTSILFSTH 189
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATH 185
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-205 |
9.54e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.36 E-value: 9.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQY---------GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK-- 69
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 70 ---------ELQhlMGYLPEERGLYPKVKVSDqIIY--LAQLRGMSASEADKSLKYWLERFDV-PEYYNKKIEELSKGNQ 137
Cdd:PRK10419 81 raqrkafrrDIQ--MVFQDSISAVNPRKTVRE-IIRepLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 138 QKMGFVAAVVHKPKILILDEAFSGLDPV----NVELLKDTVREmrdLGTSILFSTHRMEHVEELCRNITILD 205
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVlqagVIRLLKKLQQQ---FGTACLFITHDLRLVERFCQRVMVMD 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-230 |
1.01e-20 |
|
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: 91.81 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGlIYPD---EGSILYNGKPYskELQHL------ 74
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPL--KASNIrdtera 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 -MGYLPEERGLYPKVKVSDQI-----IYLAQLRgMSASEADKSLKYWLERFDVPEYYN-KKIEELSKGNQQKMGFVAAVV 147
Cdd:TIGR02633 79 gIVIIHQELTLVPELSVAENIflgneITLPGGR-MAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 148 HKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDI------------ 215
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMstmseddiitmm 237
|
250 260
....*....|....*....|..
gi 1133779397 216 --REIKKGYPRE-----EVVLR 230
Cdd:TIGR02633 238 vgREITSLYPHEpheigDVILE 259
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-213 |
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: 87.65 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQY--GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLMG 76
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldpaDLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YLPEERGL-YPKVK---------VSDQIIylaqLRGMSASEADKSLKywlerfDVPEYYNKKIEE----LSKGNQQKMGF 142
Cdd:cd03245 82 YVPQDVTLfYGTLRdnitlgaplADDERI----LRAAELAGVTDFVN------KHPNGLDLQIGErgrgLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 143 VAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEhVEELCRNITILDRSNTVVQG 213
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-192 |
1.39e-20 |
|
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: 86.50 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYG--EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKelqhlmgYLPEE 81
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ-------WDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RGlypkvkvsDQIIYLAQlrgmsaseadkslkywlerfDVpEYYNKKIEE--LSKGNQQKMGFVAAVVHKPKILILDEAF 159
Cdd:cd03246 74 LG--------DHVGYLPQ--------------------DD-ELFSGSIAEniLSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190
....*....|....*....|....*....|...
gi 1133779397 160 SGLDPVNVELLKDTVREMRDLGTSILFSTHRME 192
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPE 157
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-204 |
2.07e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.74 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 18 AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----------------KELQhlmgylpee 81
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfasttaalaagvaiiyQELH--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 rgLYPKVKVSDQiIYLAQLRGMSASEADKSLKYW----LERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDE 157
Cdd:PRK11288 90 --LVPEMTVAEN-LYLGQLPHKGGIVNRRLLNYEareqLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1133779397 158 AFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITIL 204
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVF 213
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-213 |
2.72e-20 |
|
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: 86.78 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 23 SLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG----------KPYSKELQhlmgylpeERGLYPKVKVsD 92
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaappadRPVSMLFQ--------ENNLFAHLTV-E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 93 QIIYLAQLRGMSASEAD-KSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLK 171
Cdd:cd03298 89 QNVGLGLSPGLKLTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1133779397 172 DTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:cd03298 169 DLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-190 |
3.04e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 90.61 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGYLPEERGL----- 84
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdltlESLRRQIGVVPQDTFLfsgti 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 -----YPKVKVSDQIIYLAqLRgmsASEADKslkyWLERFdvPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:COG1132 431 renirYGRPDATDEEVEEA-AK---AAQAHE----FIEAL--PDGYDTVVGErgvnLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190
....*....|....*....|....*....|....*
gi 1133779397 156 DEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHR 190
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMK-GRTTIVIAHR 534
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-218 |
8.16e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 8.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 2 EALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHL--- 74
Cdd:PRK10070 27 QGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVrrk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 -MGYLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKIL 153
Cdd:PRK10070 107 kIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 154 ILDEAFSGLDP-VNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK10070 187 LMDEAFSALDPlIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-218 |
8.31e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.61 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGYLP 79
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlssRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EERgLYPK-VKVSDQIIYlaqlrGMSA--------SEADKSLKYW-LERFDVPEYYNKKIEELSKGNQQKMgFVAAVV-H 148
Cdd:PRK11231 83 QHH-LTPEgITVRELVAY-----GRSPwlslwgrlSAEDNARVNQaMEQTRINHLADRRLTDLSGGQRQRA-FLAMVLaQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 149 KPKILILDEAFSGLDpVN--VELLKdTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK11231 156 DTPVVLLDEPTTYLD-INhqVELMR-LMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-164 |
9.35e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.36 E-value: 9.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 2 EALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGY 77
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPE--------------ERGLYPkvkvsdqiiylaqlRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGF- 142
Cdd:PRK13548 81 LPQhsslsfpftveevvAMGRAP--------------HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLa 146
|
170 180
....*....|....*....|....*..
gi 1133779397 143 -----VAAVVHKPKILILDEAFSGLDP 164
Cdd:PRK13548 147 rvlaqLWEPDGPPRWLLLDEPTSALDL 173
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-220 |
9.98e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.03 E-value: 9.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG-KPYSKELQhlMGYLPEERGL---YPKVKV 90
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvDITDKKVK--LSDIRKKVGLvfqYPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 91 SDQIIY--LA---QLRGMSASEADKSLKYWLE--RFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:PRK13637 97 FEETIEkdIAfgpINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 164 PVNVELLKDTVREMRD-LGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKK 220
Cdd:PRK13637 177 PKGRDEILNKIKELHKeYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-225 |
1.07e-19 |
|
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: 85.74 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 5 QLKQVVKQYGEKT-AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGYLP 79
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRdisrKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EERGLYPKvKVSDQIIYLAQLRGM-SASEADKSLKYWLERFDVPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILI 154
Cdd:cd03254 84 QDTFLFSG-TIMENIRLGRPNATDeEVIEAAKEAGAHDFIMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 155 LDEAFSGLDPVNVELLKDTVREMRDLGTSILFStHRMEhveelcrniTILDRSNTVVQGDIREIKKGYPRE 225
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLS---------TIKNADKILVLDDGKIIEEGTHDE 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-243 |
1.98e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.06 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQhlMGYL 78
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSrlhaRDRK--VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYPKVKVSDQIIY----LAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 155 LDEAFSGLDpvnVELLKDTVREMRDLG-----TSIlFSTHRMEHVEElcrnitILDRSNTVVQGDIREIkkGYPRE---- 225
Cdd:PRK10851 160 LDEPFGALD---AQVRKELRRWLRQLHeelkfTSV-FVTHDQEEAME------VADRVVVMSQGNIEQA--GTPDQvwre 227
|
250 260
....*....|....*....|..
gi 1133779397 226 ---EVVLRTAGEVNGLT-EIAG 243
Cdd:PRK10851 228 patRFVLEFMGEVNRLQgTIRG 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-198 |
3.76e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 10 VKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS-----KELQHLMGYLPEER-- 82
Cdd:COG1129 259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprDAIRAGIAYVPEDRkg 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 -GLYPKVKVSDQIIyLAQLRGMS-------ASEADKSLKYwLERFDV----PEyynKKIEELSKGNQQKmgfvaaVV--- 147
Cdd:COG1129 339 eGLVLDLSIRENIT-LASLDRLSrgglldrRRERALAEEY-IKRLRIktpsPE---QPVGNLSGGNQQK------VVlak 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 148 ---HKPKILILDEAFSGLDpVN--VELLKdTVREMRDLGTSILFSTHRMEHVEELC 198
Cdd:COG1129 408 wlaTDPKVLILDEPTRGID-VGakAEIYR-LIRELAAEGKAVIVISSELPELLGLS 461
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-218 |
4.91e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.42 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSI------LYNGKPYSKE---- 70
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 71 --LQHLMGYLPEERGLYPKVKVSDQIIY-LAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVV 147
Cdd:PRK11264 81 rqLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 148 HKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| DUF4162 |
pfam13732 |
Domain of unknown function (DUF4162); This domain is found at the C-terminus of bacterial ABC ... |
213-295 |
5.73e-19 |
|
Domain of unknown function (DUF4162); This domain is found at the C-terminus of bacterial ABC transporter proteins. The function is not known.
Pssm-ID: 463971 [Multi-domain] Cd Length: 82 Bit Score: 79.56 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 213 GDIREIKKGYPREEVVLRTAGEVNgLTEIAGVTGVQRQERGYVLSINDLGAAQRILQLAVAQGEVEHFEIKEPTLNQIFI 292
Cdd:pfam13732 1 GTLEEIKRSYGRNRIEVETADAEE-LLELPGVEEVEEEGGGLELKLEDEEAANELLAALLSGGEIRSFEEEEPSLNDIFI 79
|
...
gi 1133779397 293 RAV 295
Cdd:pfam13732 80 EKV 82
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-189 |
6.09e-19 |
|
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: 82.79 E-value: 6.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK---ELQHLMGYLPE 80
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqrdEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIIYLAQLRGmsasEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 1133779397 161 GLDPVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-200 |
6.79e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.01 E-value: 6.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 6 LKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILyngkpysKELQHLMGYLPEERGLY 85
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNGKLRIGYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 86 PKVKVSdqIIYLAQLR-GMSASEADKSLKywleRFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDp 164
Cdd:PRK09544 80 TTLPLT--VNRFLRLRpGTKKEDILPALK----RVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1133779397 165 VNVEL-LKDTVREMR-DLGTSILFSTHRMEHV-----EELCRN 200
Cdd:PRK09544 153 VNGQVaLYDLIDQLRrELDCAVLMVSHDLHLVmaktdEVLCLN 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-218 |
8.19e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 84.30 E-value: 8.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQY--GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE----LQHLMGY 77
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwdVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 L---PEERglYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:PRK13635 86 VfqnPDNQ--FVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 155 LDEAFSGLDPVNVELLKDTVREMRD-LGTSILFSTHRMEHVEELCRnITILDRSNTVVQGDIREI 218
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQADR-VIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-194 |
8.87e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.01 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE----LQHLMG 76
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnvwdIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YL---PEERglYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKIL 153
Cdd:PRK13650 85 MVfqnPDNQ--FVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1133779397 154 ILDEAFSGLDPVNVELLKDTVREMRD-LGTSILFSTHRMEHV 194
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDdYQMTVISITHDLDEV 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-231 |
1.10e-18 |
|
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: 86.01 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 2 EALQLKQVVKQY-----GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILY-------------- 62
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 63 ----NGKPYskelqhlMGYLPEERGLYPKVKVSDQI---IYLA---QLRGMSASEADKSLKYWLERfdVPEYYNKKIEEL 132
Cdd:TIGR03269 358 dgrgRAKRY-------IGILHQEYDLYPHRTVLDNLteaIGLElpdELARMKAVITLKMVGFDEEK--AEEILDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 133 SKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMR-DLGTSILFSTHRMEHVEELCrnitilDRSNTVV 211
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAReEMEQTFIIVSHDMDFVLDVC------DRAALMR 502
|
250 260
....*....|....*....|
gi 1133779397 212 QGDIreIKKGYPREEVVLRT 231
Cdd:TIGR03269 503 DGKI--VKIGDPEEIVEELT 520
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-204 |
1.45e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.55 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 6 LKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY----SKE-LQHLMGYLPE 80
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEaLENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIiYLAQ--LRGMSASEAD--KSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILD 156
Cdd:PRK10982 81 ELNLVLQRSVMDNM-WLGRypTKGMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1133779397 157 EAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITIL 204
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-218 |
2.40e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.36 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 11 KQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSI----LYNGKPYS----------------KE 70
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNnhelitnpyskkiknfKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 71 LQHLMGYL---PEERgLYpKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPE-YYNKKIEELSKGNQQKMGFVAAV 146
Cdd:PRK13631 114 LRRRVSMVfqfPEYQ-LF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 147 VHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
3.06e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.54 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQY-GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLM 75
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenirEVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 76 GYL---PEERGLYPKVkvsDQIIYLAQLR-GMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPK 151
Cdd:PRK13652 81 GLVfqnPDDQIFSPTV---EQDIAFGPINlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 152 ILILDEAFSGLDPVNVellKDTVREMRDL----GTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIkkgYPREEV 227
Cdd:PRK13652 158 VLVLDEPTAGLDPQGV---KELIDFLNDLpetyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDL 231
|
....
gi 1133779397 228 VLRT 231
Cdd:PRK13652 232 LARV 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-218 |
4.81e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.85 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPD---EGSILYNGKPY----SKELQHL------MGYLPE 80
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpEKELNKLraeqisMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIIYLAQL-RGMSASEA-DKSLKYwLERFDVPEyYNKKI----EELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:PRK09473 107 MTSLNPYMRVGEQLMEVLMLhKGMSKAEAfEESVRM-LDAVKMPE-ARKRMkmypHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 155 LDEAFSGLDpVNVE-----LLKDTVREmrdLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK09473 185 ADEPTTALD-VTVQaqimtLLNELKRE---FNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-189 |
5.93e-18 |
|
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: 80.23 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPyskelqhlmgyLPEERG 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-----------LDFQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 LYPKvkvsdQIIYLAQLRGMSAS-EADKSLKYW------------LERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKP 150
Cdd:cd03231 70 SIAR-----GLLYLGHAPGIKTTlSVLENLRFWhadhsdeqveeaLARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1133779397 151 KILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-213 |
6.02e-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: 79.66 E-value: 6.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGE--KTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKP---YSKELQHLMGYL 78
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvsdLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGLYpkvkvsdqiiylaqlrgmsaseaDKSLkywlerfdvpeyYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEA 158
Cdd:cd03247 81 NQRPYLF-----------------------DTTL------------RNNLGRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 159 FSGLDPVN-VELLKDTVREMRDlgTSILFSTHR---MEHVEELCrnitILDRSNTVVQG 213
Cdd:cd03247 126 TVGLDPITeRQLLSLIFEVLKD--KTLIWITHHltgIEHMDKIL----FLENGKIIMQG 178
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-225 |
7.17e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.17 E-value: 7.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS--------------K 69
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 70 ELQHLMGYLP---EERGLYPKVKVSDQIIYL-AQLRGMSASEADKSLKYWLERFDVPEYYNKKIE-ELSKGNQQKMGFVA 144
Cdd:PRK10619 86 QLRLLRTRLTmvfQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPvHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 145 AVVHKPKILILDEAFSGLDPvnvELLKDTVREMRDL---GTSILFSTHRMEHVEELCRNITILDrsntvvQGDIREikKG 221
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDP---ELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLH------QGKIEE--EG 234
|
....
gi 1133779397 222 YPRE 225
Cdd:PRK10619 235 APEQ 238
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-193 |
8.59e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 8.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYG-----EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQH----- 73
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYkraky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 74 --------LMGYLP----EE-----------RGLYPKVKVSDQIIYLAQLrgmsaseadKSLKYWLE-RFDVpeyynkKI 129
Cdd:COG1101 82 igrvfqdpMMGTAPsmtiEEnlalayrrgkrRGLRRGLTKKRRELFRELL---------ATLGLGLEnRLDT------KV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 130 EELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDP---VNV-ELLKDTVREMRdLGTsiLFSTHRMEH 193
Cdd:COG1101 147 GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPktaALVlELTEKIVEENN-LTT--LMVTHNMEQ 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-218 |
8.64e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 8.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKT-----AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYN--------------- 63
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 64 -------GKPYS------KELQHLMGYLPE--ERGLYpKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKK 128
Cdd:PRK13651 83 vleklviQKTRFkkikkiKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 129 IE-ELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRS 207
Cdd:PRK13651 162 SPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
250
....*....|.
gi 1133779397 208 NTVVQGDIREI 218
Cdd:PRK13651 242 KIIKDGDTYDI 252
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-217 |
3.26e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.43 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMV--LGLIYPD---EGSILYNGKP-YSK-----ELQ 72
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNiYSPrtdtvDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 73 HLMGYLPEERGLYPkVKVSDQIIYLAQLRGMSASE-----ADKSLK---YWLErfdVPEYYNKKIEELSKGNQQKMGFVA 144
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQvldeaVEKSLKgasIWDE---VKDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133779397 145 AVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTsILFSTHRMEHVEElcrnitILDRSNTVVQGDIRE 217
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASR------ISDRTGFFLDGDLIE 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-157 |
4.10e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 4.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 6 LKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILyngkpYSKELQhlMGYLPEERGLY 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-----IPKGLR--IGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 86 PKVKVSDQII--------YLAQLRGMSASEADKSLKY-----WLERFDV--------------------PEYYNKKIEEL 132
Cdd:COG0488 74 DDLTVLDTVLdgdaelraLEAELEELEAKLAEPDEDLerlaeLQEEFEAlggweaearaeeilsglgfpEEDLDRPVSEL 153
|
170 180
....*....|....*....|....*
gi 1133779397 133 SKGNQQKMGFVAAVVHKPKILILDE 157
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDE 178
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-213 |
4.78e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.90 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPD---EGSILYNGKPYSKE---------L 71
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQREgrlardirkS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 72 QHLMGYLPEERGLYPKVKVSDQIIYLAQ---------LRGMSASEADKSLKYwLERFDVPEYYNKKIEELSKGNQQKMGF 142
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQRALQA-LTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 143 VAAVVHKPKILILDEAFSGLDPVNVELLKDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-189 |
4.86e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.57 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGL-IY-PDEGSILYNGkpyskelQHLMGYLPEER---GLY--- 85
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpKYeVTSGSILLDG-------EDILELSPDERaraGIFlaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 86 ------PKVKVSD--QIIYLAQLRG-MSASEADKSLKYWLERFDVPE-----YYNkkiEELSKGNQQKMGFVAAVVHKPK 151
Cdd:COG0396 84 qypveiPGVSVSNflRTALNARRGEeLSAREFLKLLKEKMKELGLDEdfldrYVN---EGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1133779397 152 ILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-191 |
5.64e-17 |
|
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: 80.95 E-value: 5.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKP---YSKE-LQHLMGYLPEERGLYP--- 86
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADlsqWDREeLGRHIGYLPQDVELFDgti 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 87 --------KVKvSDQIIYLAQLRGMSAseadkslkyWLERFdvPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILI 154
Cdd:COG4618 423 aeniarfgDAD-PEKVVAAAKLAGVHE---------MILRL--PDGYDTRIGEggarLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190
....*....|....*....|....*....|....*..
gi 1133779397 155 LDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRM 191
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP 527
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-218 |
8.55e-17 |
|
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: 80.11 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 11 KQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIyPDEGSILYNGKPYS----KELQHLmgylpeeR---- 82
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDglsrRALRPL-------Rrrmq 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 --------GLYPKVKVSdQII---YLAQLRGMSASEADKSLKYWLErfDV---PEYYNKKIEELSKGNQQKMGFVAAVVH 148
Cdd:COG4172 366 vvfqdpfgSLSPRMTVG-QIIaegLRVHGPGLSAAERRARVAEALE--EVgldPAARHRYPHEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 149 KPKILILDEAFSGLDpVNV-----ELLKDTVREmrdLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:COG4172 443 EPKLLVLDEPTSALD-VSVqaqilDLLRDLQRE---HGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-218 |
1.04e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.11 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYG--EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE-LQHLMGYL- 78
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 -----PEERglYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKIL 153
Cdd:PRK13632 87 iifqnPDNQ--FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 154 ILDEAFSGLDPVNVELLKDTVREMRDLGTSILFS-THRMEHVeELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-206 |
1.08e-16 |
|
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: 75.18 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILyngkpyskelqhlmgylpeerg 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 LYPKVKVSdqiiYLAQlrgmsaseadkslkywlerfdvpeyynkkieeLSKGNQQKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:cd03221 59 WGSTVKIG----YFEQ--------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1133779397 164 PVNVELLKDTVREMRdlGTsILFSTHRMEHVEELCRNITILDR 206
Cdd:cd03221 103 LESIEALEEALKEYP--GT-VILVSHDRYFLDQVATKIIELED 142
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-214 |
1.76e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRmVLGLI-YPDEG--SILYN-----GKPYSKELQHL 74
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLeMPRSGtlNIAGNhfdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 ---MGYLPEERGLYPKVKVSDQIIYL-AQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKP 150
Cdd:PRK11124 81 rrnVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 151 KILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGD 214
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-213 |
1.85e-16 |
|
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: 76.54 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 8 QVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDE---GSILYNGKPYSKEL-QHLMGYLPEERG 83
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQfQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 LYPKVKVSDQIIYLAQLRG---MSASEADKSLKYWLERfDVPEYY--NKKIEELSKGNQQKMGFVAAVVHKPKILILDEA 158
Cdd:cd03234 92 LLPGLTVRETLTYTAILRLprkSSDAIRKKRVEDVLLR-DLALTRigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 159 FSGLDPVN----VELLKDTVREMRdlgtSILFSTH--RMEhVEELCRNITILDRSNTVVQG 213
Cdd:cd03234 171 TSGLDSFTalnlVSTLSQLARRNR----IVILTIHqpRSD-LFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-189 |
2.43e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.82 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 18 AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKpyskelqHLMGYLPEER--------------- 82
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGK-------DLLGMKDDEWravrsdiqmifqdpl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 -GLYPKVKVSDQI-----IYLAQlrgMSASEADKSLKYWLERFDV-PEYYNKKIEELSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:PRK15079 109 aSLNPRMTIGEIIaeplrTYHPK---LSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1133779397 156 DEAFSGLDpVN-----VELLKDTVREMrdlGTSILFSTH 189
Cdd:PRK15079 186 DEPVSALD-VSiqaqvVNLLQQLQREM---GLSLIFIAH 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-186 |
3.71e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 2 EALQLKQV-VKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHL-M 75
Cdd:COG3845 256 VVLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITglspRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 76 GYLPEER---GLYPKVKVSDQIIyLAQLRG--------MSASEADKSLKYWLERFDV----PEYynkKIEELSKGNQQKm 140
Cdd:COG3845 336 AYIPEDRlgrGLVPDMSVAENLI-LGRYRRppfsrggfLDRKAIRAFAEELIEEFDVrtpgPDT---PARSLSGGNQQK- 410
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1133779397 141 gFVAA--VVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILF 186
Cdd:COG3845 411 -VILAreLSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL 457
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-218 |
4.93e-16 |
|
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: 75.60 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY----SKELQHLMGYLPEE-----RGLY 85
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaladPAWLRRQVGVVLQEnvlfnRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 86 PKVKVSD------QIIYLAQLRGMSAseadkslkYWLErfdVPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:cd03252 94 DNIALADpgmsmeRVIEAAKLAGAHD--------FISE---LPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 156 DEAFSGLDpvnVELLKDTVREMRDL--GTSILFSTHRMEHVEELCRnITILDRSNTVVQGDIREI 218
Cdd:cd03252 163 DEATSALD---YESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADR-IIVMEKGRIVEQGSHDEL 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-242 |
7.20e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 7.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKElQHL--------MGYLPEERGLYP 86
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE-ENLwdirnkagMVFQNPDNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 87 KVkVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVN 166
Cdd:PRK13633 101 TI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 167 VELLKDTVREM-RDLGTSILFSTHRMEHVEELCRnITILDRSNTVVQGDIREIkkgYPREEVVLRTAGEVNGLTEIA 242
Cdd:PRK13633 180 RREVVNTIKELnKKYGITIILITHYMEEAVEADR-IIVMDSGKVVMEGTPKEI---FKEVEMMKKIGLDVPQVTELA 252
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-190 |
7.27e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 77.39 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG---KPYSKE-LQHLMGYLPEERGLYP-KV 88
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlKQWDREtFGKHIGYLPQDVELFPgTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 89 KV----------SDQIIYLAQLRGmsASEADKSLkywlerfdvPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILI 154
Cdd:TIGR01842 409 AEniarfgenadPEKIIEAAKLAG--VHELILRL---------PDGYDTVIGPggatLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190
....*....|....*....|....*....|....*.
gi 1133779397 155 LDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHR 190
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKARGITVVVITHR 513
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-213 |
7.28e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.78 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 11 KQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPD---EGSILYNGKPYSKELQHLM-GYLPEERGLYP 86
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIsAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 87 KVKVSDQIIYLAQLR---GMSASEADKSLKYWLERFDVPEYYNKKI------EELSKGNQQKMGFVAAVVHKPKILILDE 157
Cdd:TIGR00955 113 TLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 158 AFSGLDPVNVELLKDTVREMRDLGTSILFSTHR-MEHVEELCRNITILDRSNTVVQG 213
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLG 249
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-222 |
1.18e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 75.24 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 18 AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKpyskelqhlMGYLPEERGLYPKVKVSDQIIYL 97
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE---------VSVIAISAGLSGQLTGIENIEFK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 98 AQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREM 177
Cdd:PRK13546 110 MLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEF 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1133779397 178 RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKGY 222
Cdd:PRK13546 190 KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-190 |
1.32e-15 |
|
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: 73.72 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGL-IY-PDEGSILYNGkpysKELQHLmgyLPEER---GLY--- 85
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpKYeVTEGEILFKG----EDITDL---PPEERarlGIFlaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 86 ------PKVKVSDQIIYLAQlrGMSASEadkslkywlerfdvpeyyNKKIEELSkgnqqkmgfvaAVVHKPKILILDEAF 159
Cdd:cd03217 84 qyppeiPGVKNADFLRYVNE--GFSGGE------------------KKRNEILQ-----------LLLLEPDLAILDEPD 132
|
170 180 190
....*....|....*....|....*....|.
gi 1133779397 160 SGLDPVNVELLKDTVREMRDLGTSILFSTHR 190
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKSVLIITHY 163
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-214 |
1.61e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.02 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKT-AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG---KPYSK--ELQHLMGY 77
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKlqGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 L---PEERglYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:PRK13644 82 VfqnPETQ--FVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 155 LDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRnITILDRSNTVVQGD 214
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADR-IIVMDRGKIVLEGE 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-190 |
1.72e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.45 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 13 YGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKEL---QHLMGYLPEERGLYPKVK 89
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLctyQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 90 VSDQIIYlaqlrGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVEL 169
Cdd:PRK13540 91 LRENCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|.
gi 1133779397 170 LKDTVREMRDLGTSILFSTHR 190
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-194 |
1.85e-15 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 73.68 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQY--GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLMGY 77
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiglhDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPEE----RG-----LYPKVKVSDQIIYLAqLRGMSASEADKSLKYWLerfdvpeyyNKKIEE----LSKGNQQKMGFVA 144
Cdd:cd03244 83 IPQDpvlfSGtirsnLDPFGEYSDEELWQA-LERVGLKEFVESLPGGL---------DTVVEEggenLSVGQRQLLCLAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1133779397 145 AVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHV 194
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRLDTI 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-189 |
2.08e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.65 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKT-AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSkELQhlmgylP 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-ELE------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EERG---------LYPKVKVSDQIIYLAQLRGMSASE-------ADKSLKywLErfdvpEYYNKKIEELSKGNQQK--MG 141
Cdd:PRK11650 74 ADRDiamvfqnyaLYPHMSVRENMAYGLKIRGMPKAEieervaeAARILE--LE-----PLLDRKPRELSGGQRQRvaMG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 142 fvAAVVHKPKILILDEAFSGLDP-----VNVELlkdtvREM-RDLGTSILFSTH 189
Cdd:PRK11650 147 --RAIVREPAVFLFDEPLSNLDAklrvqMRLEI-----QRLhRRLKTTSLYVTH 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-218 |
2.39e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.05 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK-----------PYSKELQHLmgYLPEERG 83
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgklqALRRDIQFI--FQDPYAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 LYPKVKVSDQIIYLAQLRGMSASEADKSLKYW-LERFDV-PEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSG 161
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWlLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 162 LD-PVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK10261 494 LDvSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-216 |
2.98e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.37 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQY-GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE-------LQHLM 75
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 76 GYLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 156 DEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEElcRNITILDRSNTVVQGDIR 216
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISR--RSYRMLTLSDGHLHGGVG 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-233 |
3.56e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.07 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGS---ILYNGKPYSKELqhlMGYLPEERGL------- 84
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKT---VWDIREKVGIvfqnpdn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 -YPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:PRK13640 96 qFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 164 PVNVELLKDTVRE-MRDLGTSILFSTHRMEHVeELCRNITILDRSNTVVQGDIREIkkgYPREEvVLRTAG 233
Cdd:PRK13640 176 PAGKEQILKLIRKlKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI---FSKVE-MLKEIG 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-236 |
4.52e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS--------KELQHLMGYL---PEERg 83
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnknlKKLRKKVSLVfqfPEAQ- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 LYPKVKVSDqIIYLAQLRGMSASEADKSLKYWLERFDVPE-YYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGL 162
Cdd:PRK13641 98 LFENTVLKD-VEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 163 DPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI-------KKGYPREEVVLRTAGEV 235
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIfsdkewlKKHYLDEPATSRFASKL 256
|
.
gi 1133779397 236 N 236
Cdd:PRK13641 257 E 257
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-189 |
6.57e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK---ELQHLMGYLPE 80
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRqrdEYHQDLLYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSDQIIYLAQLRGMSASEAdksLKYWLERF------DVPeyynkkIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:PRK13538 82 QPGIKTELTALENLRFYQRLHGPGDDEA---LWEALAQVglagfeDVP------VRQLSAGQQRRVALARLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1133779397 155 LDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-157 |
7.37e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILyngkpYSKELQhlMGYLPEER- 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-----LGETVK--IGYFDQHQe 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 GLYPKVKVSDQIiylaqlRGMSASEADKSLKYWLERF-----DVpeyyNKKIEELSKGNQQKMGFVAAVVHKPKILILDE 157
Cdd:COG0488 389 ELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFlfsgdDA----FKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-217 |
8.65e-15 |
|
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: 72.26 E-value: 8.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKT--AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG---KPYS-KELQHLMGY 77
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPEERGLYPKVkVSDQIIYLAqlRGMSASEADKSLKY-----WLERFdvPEYYNKKIEE----LSKGNQQKMGFVAAVVH 148
Cdd:cd03251 81 VSQDVFLFNDT-VAENIAYGR--PGATREEVEEAARAanaheFIMEL--PEGYDTVIGErgvkLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 149 KPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFStHRMEHVEELCRnITILDRSNTVVQGDIRE 217
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIA-HRLSTIENADR-IVVLEDGKIVERGTHEE 222
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-222 |
1.35e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.77 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 18 AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGkpySKELqhlmgyLPEERGLYPKVKVSDQIIYL 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---SAAL------IAISSGLNGQLTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 98 AQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREM 177
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1133779397 178 RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKGY 222
Cdd:PRK13545 190 KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHY 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-225 |
1.64e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 6 LKQVVkqyGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIyPDEGSILYNGKPYSKELQHLMgyLPEER--- 82
Cdd:PRK15134 292 LKRTV---DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQL--LPVRHriq 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 --------GLYPKVKVSdQIIylAQ-LR----GMSASEADKSLKYWLERFDV-PEYYNKKIEELSKGNQQKMGFVAAVVH 148
Cdd:PRK15134 366 vvfqdpnsSLNPRLNVL-QII--EEgLRvhqpTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 149 KPKILILDEAFSGLD-PVN---VELLKdTVREMRDLgtSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI----KK 220
Cdd:PRK15134 443 KPSLIILDEPTSSLDkTVQaqiLALLK-SLQQKHQL--AYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVfaapQQ 519
|
....*
gi 1133779397 221 GYPRE 225
Cdd:PRK15134 520 EYTRQ 524
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-208 |
2.11e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 70.52 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 18 AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLMGYLPEERGLYpkvkvsdq 93
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTipleDLRSSLTIIPQDPTLF-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 94 iiylaqlrgmsaseaDKSLKYWLERFDvpEYYNKKI----------EELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:cd03369 95 ---------------SGTIRSNLDPFD--EYSDEEIygalrvseggLNLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1133779397 164 PVNVELLKDTVREMRDlGTSILFSTHRMEHVEElCRNITILDRSN 208
Cdd:cd03369 158 YATDALIQKTIREEFT-NSTILTIAHRLRTIID-YDKILVMDAGE 200
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-216 |
2.22e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.69 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKT-AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKElqhlmgylpEE 81
Cdd:PRK13647 4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAE---------NE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RGLYPKV--------------KVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVV 147
Cdd:PRK13647 75 KWVRSKVglvfqdpddqvfssTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 148 HKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIR 216
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-218 |
2.53e-14 |
|
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: 72.79 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIyPD-----EGSILYNGkpysKELQHlmgyLPEE-----RG 83
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDpaahpSGSILFDG----QDLLG----LSERelrriRG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 -------------LYPKVKVSDQIIYLAQL-RGMSASEADKSLKYWLERFDVPEyYNKKIE----ELSKGNQQKMGFVAA 145
Cdd:COG4172 92 nriamifqepmtsLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPD-PERRLDayphQLSGGQRQRVMIAMA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 146 VVHKPKILILDEAFSGLDpVNV-----ELLKDTVREMrdlGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:COG4172 171 LANEPDLLIADEPTTALD-VTVqaqilDLLKDLQREL---GMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-213 |
2.59e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.69 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 18 AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG------------KPYSKELQHLMGYlPEERgLY 85
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeiKPVRKKVGVVFQF-PESQ-LF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 86 PKVKVSDqIIYLAQLRGMSASEADKSLKYWLERFDVP-EYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDP 164
Cdd:PRK13643 99 EETVLKD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1133779397 165 -VNVELLKdTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQG 213
Cdd:PRK13643 178 kARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-189 |
2.89e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS--KELQHLMgyLPEE 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAeaREDTRLM--FQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RgLYPKVKVSDQIIYlaqlrGMSASEADKSLKYwLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSG 161
Cdd:PRK11247 91 R-LLPWKKVIDNVGL-----GLKGQWRDAALQA-LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1133779397 162 LDPVnvellkdTVREMRDL--------GTSILFSTH 189
Cdd:PRK11247 164 LDAL-------TRIEMQDLieslwqqhGFTVLLVTH 192
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-192 |
3.39e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 71.28 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVN---GISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE----LQHLMG 76
Cdd:PRK13642 5 LEVENLVFKYEKESDVNqlnGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnvwnLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YL---PEERglYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKIL 153
Cdd:PRK13642 85 MVfqnPDNQ--FVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1133779397 154 ILDEAFSGLDPVNVELLKDTVREMRD-LGTSILFSTHRME 192
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEkYQLTVLSITHDLD 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-191 |
3.50e-14 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 70.34 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLMGYLPEERGL------ 84
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtldSLRRAIGVVPQDTVLfndtig 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 ----YPKVKVSDQIIYLAQLRGMSASEadkslkywLERFdvPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILD 156
Cdd:cd03253 93 ynirYGRPDATDEEVIEAAKAAQIHDK--------IMRF--PDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1133779397 157 EAFSGLDPVNVELLKDTVREMRDLGTSIlFSTHRM 191
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKGRTTI-VIAHRL 196
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-190 |
3.75e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.60 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 11 KQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPD--EGSILYNGKPYSKELQHLMGYLPEERGLYPKV 88
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 89 KVSDQIIYLAQLR-GMSASEADKSL-------KYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:PLN03211 156 TVRETLVFCSLLRlPKSLTKQEKILvaesvisELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190
....*....|....*....|....*....|
gi 1133779397 161 GLDPVNVELLKDTVREMRDLGTSILFSTHR 190
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-190 |
3.92e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.53 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 2 EALQLKQV-VKQYGEKTAVNGISLKVEQGEiyGLL--GANGAGKTTTMRMVLGL--------IYPDEGSILYngkpyske 70
Cdd:COG4178 361 GALALEDLtLRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLF-------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 71 L-QHLmgYLPEerG------LYPKV--KVSDQII--YLAQLRgmsaseadksLKYWLERFDVPEYYNKkieELSKGNQQK 139
Cdd:COG4178 431 LpQRP--YLPL--GtlrealLYPATaeAFSDAELreALEAVG----------LGHLAERLDEEADWDQ---VLSLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 140 MGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREmRDLGTSILFSTHR 190
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHR 543
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-190 |
4.24e-14 |
|
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: 68.72 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 22 ISLKVEQGEIYGLLGANGAGKTTTMRMVLGLiYPdegsiLYNGKPYSKELQHLMgYLPEeRGLYPKVKVSDQIIYLaqlr 101
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGL-WP-----WGSGRIGMPEGEDLL-FLPQ-RPYLPLGTLREQLIYP---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 102 gmsaseadkslkyWLErfdvpeyynkkieELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPvNVEllkDTVREM-RDL 180
Cdd:cd03223 88 -------------WDD-------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE-ESE---DRLYQLlKEL 137
|
170
....*....|
gi 1133779397 181 GTSILFSTHR 190
Cdd:cd03223 138 GITVISVGHR 147
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-190 |
6.45e-14 |
|
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: 69.88 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 20 NGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGYLPEERGLYPkVKVSDQII 95
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRdlnlRWLRSQIGLVSQEPVLFD-GTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 96 YlaQLRGMSASEADK-SLKYWLERF--DVPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVE 168
Cdd:cd03249 99 Y--GKPDATDEEVEEaAKKANIHDFimSLPDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEK 176
|
170 180
....*....|....*....|..
gi 1133779397 169 LLKDTVREMRdLGTSILFSTHR 190
Cdd:cd03249 177 LVQEALDRAM-KGRTTIVIAHR 197
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-221 |
1.18e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.29 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 21 GISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHLM----GYLPEERGLYPKvKVSDQIIY 96
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLhrqvALVGQEPVLFSG-SVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 97 laqlrGMSASEADKSLKYWLERF------DVPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILDEAFSGLDpVN 166
Cdd:TIGR00958 578 -----GLTDTPDEEIMAAAKAANahdfimEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD-AE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 167 VELLKDTVREMRDLgtSILFSTHRMEHVEElCRNITILDRSNTVVQGDIREIKKG 221
Cdd:TIGR00958 652 CEQLLQESRSRASR--TVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-205 |
1.21e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.44 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKpyskelqhLMGYL-P 79
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--------RMNDVpP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EERG---------LYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKP 150
Cdd:PRK11000 73 AERGvgmvfqsyaLYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 151 KILILDEAFSGLDP-VNVELLKDTVREMRDLGTSILFSTHrmEHVE--ELCRNITILD 205
Cdd:PRK11000 153 SVFLLDEPLSNLDAaLRVQMRIEISRLHKRLGRTMIYVTH--DQVEamTLADKIVVLD 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-277 |
1.35e-13 |
|
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: 70.60 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGL--IYPDEGSILYN----------------GK 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 66 PYSK-----ELQHLMGYLPEER-----------------GLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPE 123
Cdd:TIGR03269 81 PCPVcggtlEPEEVDFWNLSDKlrrrirkriaimlqrtfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 124 YYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVRE-MRDLGTSILFSTHRMEHVEELCRNIT 202
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 203 ILDRSNTVVQGDIREIKKGYPREEVVLRTAGEVNGLTEIAGVTGVQRQ----ERGYVLSINDlgaaqriLQLAVAQGEV 277
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRyisvDRGVVKAVDN-------VSLEVKEGEI 312
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-205 |
1.90e-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: 68.27 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 21 GISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGYLPEERGLYPKvKVSDQIIY 96
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyehKYLHSKVSLVGQEPVLFAR-SLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 97 -LAQLRGMSASEAdkSLKYWLERF--DVPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVEL 169
Cdd:cd03248 111 gLQSCSFECVKEA--AQKAHAHSFisELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 1133779397 170 LKDTVREMRDlGTSILFSTHRMEHVEElCRNITILD 205
Cdd:cd03248 189 VQQALYDWPE-RRTVLVIAHRLSTVER-ADQILVLD 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-215 |
2.03e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.04 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 5 QLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGlIYPDEGS---ILYNGKPYSKEL-----QHLmG 76
Cdd:PRK10938 262 VLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSndlTLFGRRRGSGETiwdikKHI-G 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YLPEERGLYPKVKVS----------DQI-IYLAqlrgmsASEADKSL-KYWLERFDVPEYY-NKKIEELSKGnQQKMGFV 143
Cdd:PRK10938 340 YVSSSLHLDYRVSTSvrnvilsgffDSIgIYQA------VSDRQQKLaQQWLDILGIDKRTaDAPFHSLSWG-QQRLALI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 144 A-AVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLG-TSILFSTHrmeHVEELCRNITilDRSNTVVQGDI 215
Cdd:PRK10938 413 VrALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGeTQLLFVSH---HAEDAPACIT--HRLEFVPDGDI 481
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-218 |
2.91e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLI------YPDEGSILYNGKPYSK----ELQHLMGYLPEERGL 84
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQidaiKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 YPKVKVSDQIIYLAQLRGMS--------ASEADKSLKYWLERFDvpeYYNKKIEELSKGNQQKMGFVAAVVHKPKILILD 156
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKekreikkiVEECLRKVGLWKEVYD---RLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 157 EAFSGLDPVNVELLKDTVREMRDLGTSILFStHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-215 |
3.57e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.68 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 23 SLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE--LQHLMGYLPEERGLYPKVKVSdQIIYLAQL 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppSRRPVSMLFQENNLFSHLTVA-QNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 101 RGMSASEADK-SLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPV----NVELLKDTVR 175
Cdd:PRK10771 98 PGLKLNAAQReKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAlrqeMLTLVSQVCQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1133779397 176 EmRDLgtSILFSTHrmeHVEELCRnitILDRSNTVVQGDI 215
Cdd:PRK10771 178 E-RQL--TLLMVSH---SLEDAAR---IAPRSLVVADGRI 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-163 |
3.62e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 19 VNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGlIYPD--EGSILYNGKPYS-----KELQHLMGYLPEER---GLYPKV 88
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGrwEGEIFIDGKPVKirnpqQAIAQGIAMVPEDRkrdGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 89 KVSDQIIY--LAQLRGMSASEADKSLKYWLE---RFDV----PEYynkKIEELSKGNQQKMGFVAAVVHKPKILILDEAF 159
Cdd:PRK13549 357 GVGKNITLaaLDRFTGGSRIDDAAELKTILEsiqRLKVktasPEL---AIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
....
gi 1133779397 160 SGLD 163
Cdd:PRK13549 434 RGID 437
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
8-189 |
4.57e-13 |
|
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: 66.50 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 8 QVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTM-----RMVLGLIypdEGSILYNGKPYSKELQHLMGYLPEER 82
Cdd:cd03232 12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLdvlagRKTAGVI---TGEILINGRPLDKNFQRSTGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 GLYPKVKVSDQIIYLAQLRGMSASEadkslkywlerfdvpeyynKKIeeLSKGNQqkmgfvaaVVHKPKILILDEAFSGL 162
Cdd:cd03232 89 VHSPNLTVREALRFSALLRGLSVEQ-------------------RKR--LTIGVE--------LAAKPSILFLDEPTSGL 139
|
170 180
....*....|....*....|....*..
gi 1133779397 163 DPVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:cd03232 140 DSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-197 |
5.07e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIY--PDEGSILYNGKPYSKELQHLmgylpeeRGLYPKVKVSD 92
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREASLI-------DAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 93 QIIYLAQLrGMSaseaDKSLkyWLERFDvpeyynkkieELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKD 172
Cdd:COG2401 115 AVELLNAV-GLS----DAVL--WLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|....*.
gi 1133779397 173 TVREM-RDLGTSILFSTHRMEHVEEL 197
Cdd:COG2401 178 NLQKLaRRAGITLVVATHHYDVIDDL 203
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-218 |
6.80e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.46 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG------------KPYSKELQhLMGYLPEER 82
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknkdiKQIRKKVG-LVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 gLYPKVKVSDqIIYLAQLRGMSASEADKSLKYWLERFDVPE-YYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSG 161
Cdd:PRK13649 98 -LFEETVLKD-VAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 162 LDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-190 |
8.81e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 68.16 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLMGYLPEERGLYP--- 86
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSldqdEVRRRVSVCAQDAHLFDttv 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 87 -------KVKVSDQIIYLAqLRGMsaseadkSLKYWLERfdVPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:TIGR02868 426 renlrlaRPDATDEELWAA-LERV-------GLADWLRA--LPDGLDTVLGEggarLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 1133779397 156 DEAFSGLDP-VNVELLKDTVREMRdlGTSILFSTHR 190
Cdd:TIGR02868 496 DEPTEHLDAeTADELLEDLLAALS--GRTVVLITHH 529
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-189 |
1.56e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.69 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKT-AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHlmgylpEER 82
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE------DYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 GLYPKVkVSDqiIYL-AQLRGMSASEADKSL-KYWLERFDVpeyyNKKIEE---------LSKGNQQKMGFVAAVVHKPK 151
Cdd:PRK10522 397 KLFSAV-FTD--FHLfDQLLGPEGKPANPALvEKWLERLKM----AHKLELedgrisnlkLSKGQKKRLALLLALAEERD 469
|
170 180 190
....*....|....*....|....*....|....*....
gi 1133779397 152 ILILDEAFSGLDPV-NVELLKDTVREMRDLGTSILFSTH 189
Cdd:PRK10522 470 ILLLDEWAADQDPHfRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-214 |
2.56e-12 |
|
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: 67.24 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 22 ISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIyPDEGSILYNGKPY-SKELQH---LMGYLPEE---------RGLYPKV 88
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWnSVTLQTwrkAFGVIPQKvfifsgtfrKNLDPYE 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 89 KVSDQIIYLAqlrgmsASEAdkSLKYWLERFdvPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILDEAFSGLDP 164
Cdd:TIGR01271 1317 QWSDEEIWKV------AEEV--GLKSVIEQF--PDKLDFVLVDggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1133779397 165 VNVELLKDTVREMRDLGTSILfSTHRMEHVEElCRNITILDrSNTVVQGD 214
Cdd:TIGR01271 1387 VTLQIIRKTLKQSFSNCTVIL-SEHRVEALLE-CQQFLVIE-GSSVKQYD 1433
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-205 |
2.57e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.22 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGE---KTAV-NGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK-------ELQ 72
Cdd:PRK11629 6 LQCDNLCKRYQEgsvQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 73 -HLMGYLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPK 151
Cdd:PRK11629 86 nQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 152 ILILDEAFSGLDPVNVELLKDTVREM-RDLGTSILFSTHRMEHVEELCRNITILD 205
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-230 |
3.79e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.93 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLI--YPD---EGSILYNGKPYSK----EL 71
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelYPEarvSGEVYLDGQDIFKmdviEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 72 QHLMGYLPEERGLYPKVKVSDQIIYLAQLRGM--SASEADKSLKYWLERF----DVPEYYNKKIEELSKGNQQKMGFVAA 145
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAqlwdEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 146 VVHKPKILILDEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKGyPRE 225
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN-PRH 238
|
....*
gi 1133779397 226 EVVLR 230
Cdd:PRK14247 239 ELTEK 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-212 |
5.00e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 11 KQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGL------IYPdEGSILYNGKPY----SKELQHLMG---- 76
Cdd:PRK15134 17 QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvVYP-SGDIRFHGESLlhasEQTLRGVRGnkia 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 --YLPEERGLYPKVKVSDQIIYLAQL-RGMSASEADKSLKYWLERFDV---PEYYNKKIEELSKGNQQKMGFVAAVVHKP 150
Cdd:PRK15134 96 miFQEPMVSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 151 KILILDEAFSGLDpVNVE-----LLKDTVREmrdLGTSILFSTHRMEHVEELCRNITILDRSNTVVQ 212
Cdd:PRK15134 176 ELLIADEPTTALD-VSVQaqilqLLRELQQE---LNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-197 |
5.03e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRmVLGLIYPDEGSILYNGKP-------YSKE----- 70
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRVeffnqniYERRvnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 71 LQHLMGYLPEERGLYPkVKVSDQIIYLAQLRGMS--------ASEADKSLKYWLErfdVPEYYNKKIEELSKGNQQKMGF 142
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRpkleiddiVESALKDADLWDE---IKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 143 VAAVVHKPKILILDEAFSGLDPV---NVELLKDTVREMRDLgtSILFSTHRMEHVEEL 197
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIasmKVESLIQSLRLRSEL--TMVIVSHNLHQVSRL 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
4-251 |
5.96e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVvkqyGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIyPDEGSILYNGKPYSK----ELQHLMGYLP 79
Cdd:PRK03695 1 MQLNDV----AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EERGLYPKVKVSDqiiYLAQLRGMSASEAD--KSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAV--VHkPKI--- 152
Cdd:PRK03695 76 QQQTPPFAMPVFQ---YLTLHQPDKTRTEAvaSALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVW-PDInpa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 153 ---LILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGdireikkgyPREEVVl 229
Cdd:PRK03695 152 gqlLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG---------RRDEVL- 221
|
250 260
....*....|....*....|..
gi 1133779397 230 rtagEVNGLTEIAGVTgVQRQE 251
Cdd:PRK03695 222 ----TPENLAQVFGVN-FRRLD 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-163 |
6.13e-12 |
|
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: 65.62 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 19 VNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGlIYPD--EGSILYNGKPYS-----KELQHLMGYLPEER---GLYPKV 88
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKPVDirnpaQAIRAGIAMVPEDRkrhGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 89 KVSdQIIYLAQLRGMS------ASEADKSLKYWLERFDVPEYY-NKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSG 161
Cdd:TIGR02633 355 GVG-KNITLSVLKSFCfkmridAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
..
gi 1133779397 162 LD 163
Cdd:TIGR02633 434 VD 435
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-65 |
7.08e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 63.98 E-value: 7.08e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK 65
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT 72
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-189 |
7.75e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 26 VEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK-ELQHLMGYLPEERGLYPKVKVSDQIIYLAQLRGMS 104
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 105 ASEADKSLkywLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSI 184
Cdd:PRK13543 114 AKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAA 190
|
....*
gi 1133779397 185 LFSTH 189
Cdd:PRK13543 191 LVTTH 195
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-204 |
1.07e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRmVLGLIYPD---EGSILYNGKPysKELQHLMGylPE 80
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMK-VLSGVYPHgsyEGEILFDGEV--CRFKDIRD--SE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYpkvkvsdqIIY--LAQLRGMSASE--------ADKSLKYW----------LERFDVPEYYNKKIEELSKGNQQKM 140
Cdd:NF040905 77 ALGIV--------IIHqeLALIPYLSIAEniflgnerAKRGVIDWnetnrrarelLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 141 GFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLG-TSILFStHRMEHVEELCRNITIL 204
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIIIS-HKLNEIRRVADSITVL 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-218 |
1.37e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.87 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 6 LKQVVKQYGEKT-----AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHL--MGYL 78
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkeVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 79 PEERGL---YPKVK-----VSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIE-ELSKGNQQKMGFVAAVVHK 149
Cdd:PRK13645 89 RKEIGLvfqFPEYQlfqetIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 150 PKILILDEAFSGLDPVNVE-LLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEdFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-214 |
1.61e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.46 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQY--GEKTAVNGISLKVEQGEIYGLLGANGAGKTTtmrmVLGLIY----PDEGSILYNGKP---YSKE-LQ 72
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLTrawdPQQGEILLNGQPiadYSEAaLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 73 HLMGYLPE----------ERGLYPKVKVSDQ--IIYLAQLrGMSA-SEADKSLKYWL---ERfdvpeyynkkieELSKGN 136
Cdd:PRK11160 414 QAISVVSQrvhlfsatlrDNLLLAAPNASDEalIEVLQQV-GLEKlLEDDKGLNAWLgegGR------------QLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 137 QQKMGFVAAVVHKPKILILDEAFSGLDpvnvellKDTVREMRDL------GTSILFSTHR---MEHVEELCrnitILDRS 207
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLD-------AETERQILELlaehaqNKTVLMITHRltgLEQFDRIC----VMDNG 549
|
....*..
gi 1133779397 208 NTVVQGD 214
Cdd:PRK11160 550 QIIEQGT 556
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-189 |
1.64e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.23 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTA--VNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGY 77
Cdd:PRK13648 8 IVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddnfEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 L---PEERGLYPKVKVSdqIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILI 154
Cdd:PRK13648 88 VfqnPDNQFVGSIVKYD--VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1133779397 155 LDEAFSGLDPVNVELLKDTVREMR-DLGTSILFSTH 189
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKsEHNITIISITH 201
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-218 |
2.32e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG-----KPYSKELQHL-----MGYLPEERGL 84
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithKTKDKYIRPVrkrigMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 YPKvKVSDQIIYLAQLRGMSASEA-DKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:PRK13646 99 FED-TVEREIIFGPKNFKMNLDEVkNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 164 PVNVELLKDTVREMR-DLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-189 |
3.39e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 20 NGISLKVEQGEIYGLLGANGAGKTTTM-----RMVLGLIypDEGSILYNGKPYSKELQHLMGYLPEERGLYPKVKVSDQI 94
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVI--TGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 95 IYLAQLR---GMSASEADKSLKYWLERFDVPEYYNKKI----EELSKGNQQKMGFVAAVVHKPKILI-LDEAFSGLDPVN 166
Cdd:TIGR00956 858 RFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
170 180
....*....|....*....|...
gi 1133779397 167 VELLKDTVREMRDLGTSILFSTH 189
Cdd:TIGR00956 938 AWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-218 |
4.36e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.26 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 19 VNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK------PYSKeLQHLMGYLPEER---GLYPKVK 89
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprsPLDA-VKKGMAYITESRrdnGFFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 90 VSDQIIYLAQLR------GMSASEADKSLKYWLERFDVPEY----YNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAF 159
Cdd:PRK09700 358 IAQNMAISRSLKdggykgAMGLFHEVDEQRTAENQRELLALkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 160 SGLD-PVNVELLKdTVREMRDLGTSILFSThrmehvEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK09700 438 RGIDvGAKAEIYK-VMRQLADDGKVILMVS------SELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-163 |
4.77e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.11 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 18 AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKP-----YSKELQHL-MGYLPEERGLYPKVKVS 91
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdYSYRSQRIrMIFQDPSTSLNPRQRIS 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 92 dQIIYLAqLR---GMSASEADKSLKYWLERFDV-PEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:PRK15112 108 -QILDFP-LRlntDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-157 |
5.36e-11 |
|
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: 62.89 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 2 EALQLKQVVKQYGEKT-----AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELqhlmg 76
Cdd:COG4615 326 QTLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN----- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 yLPEERGLYPKVkVSDQiiYL-AQLRGMSASEADKSLKYWLERF---DVPEYYNKKIE--ELSKGnQQK-MGFVAAVV-H 148
Cdd:COG4615 401 -REAYRQLFSAV-FSDF--HLfDRLLGLDGEADPARARELLERLeldHKVSVEDGRFSttDLSQG-QRKrLALLVALLeD 475
|
....*....
gi 1133779397 149 KPkILILDE 157
Cdd:COG4615 476 RP-ILVFDE 483
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-208 |
7.34e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 61.41 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPdEGSILYNGKPYSK----ELQHLMGYLPEE-------- 81
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSvplqKWRKAFGVIPQKvfifsgtf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 -RGLYPKVKVSDQIIYLAqlrgmsASEAdkSLKYWLERFdvPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILD 156
Cdd:cd03289 94 rKNLDPYGKWSDEEIWKV------AEEV--GLKSVIEQF--PGQLDFVLVDggcvLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 157 EAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHVEElCRNITILDRSN 208
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAMLE-CQRFLVIEENK 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-192 |
7.94e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 13 YGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMV--LGLIYPD---EGSILYNGKP-YSK-----ELQHLMGYLPEE 81
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNlYAPdvdpvEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RGLYPKvKVSDQIIYLAQLRGMSASE---ADKSLK---YWLErfdVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARINGYKGDMdelVERSLRqaaLWDE---VKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1133779397 156 DEAFSGLDPVNVELLKDTVREMRDLGTsILFSTHRME 192
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYT-IIIVTHNMQ 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-221 |
8.29e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.34 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 16 KTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY----SKELQHLMGYLPEErglypkvkvs 91
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFARKVAYLPQQ---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 92 dqiiyLAQLRGMSASEADKSLKY-W---LERFDVPE---------------YYNKKIEELSKGNQQKMGFVAAVVHKPKI 152
Cdd:PRK10575 94 -----LPAAEGMTVRELVAIGRYpWhgaLGRFGAADrekveeaislvglkpLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 153 LILDEAFSGLDPVN-VELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKKG 221
Cdd:PRK10575 169 LLLDEPTSALDIAHqVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRG 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-189 |
9.56e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.01 E-value: 9.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 13 YGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDE-----------GSILYNGKPYSKELQHLMGYLPEE 81
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegevrlfGRNIYSPDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RGLYPKVKVSDQIIYLAQLRGM--SASEADKSLKYWLERF----DVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190
....*....|....*....|....*....|....
gi 1133779397 156 DEAFSGLDPVNVELLKDTVREMRDLGTsILFSTH 189
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEYT-IVLVTH 206
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-163 |
1.05e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 19 VNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE-----LQHLMGYLPEER---GLYPKVKV 90
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdgLANGIVYISEDRkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 91 SDQiIYLAQLRGMsaSEADKSLKYWLERFDVPEY---YNKK-------IEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:PRK10762 348 KEN-MSLTALRYF--SRAGGSLKHADEQQAVSDFirlFNIKtpsmeqaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
...
gi 1133779397 161 GLD 163
Cdd:PRK10762 425 GVD 427
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-163 |
1.69e-10 |
|
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: 61.34 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 9 VVKQYGektavnGISLKVEQGEIY-----GLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKpyskelqhlMGYLPEerg 83
Cdd:COG1245 347 LTKSYG------GFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK---------ISYKPQ--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 lYPKVKVSDQIIYLaqLRGMSASEADKSlkYW----LERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAF 159
Cdd:COG1245 409 -YISPDYDGTVEEF--LRSANTDDFGSS--YYkteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
....
gi 1133779397 160 SGLD 163
Cdd:COG1245 484 AHLD 487
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-189 |
1.83e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.79 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQyGEK--TAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK--------- 69
Cdd:PRK10584 7 VEVHHLKKSVGQ-GEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 70 ELQHLmGYLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHK 149
Cdd:PRK10584 86 RAKHV-GFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1133779397 150 PKILILDEAFSGLDPVNVELLKDTVREM-RDLGTSILFSTH 189
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTH 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-163 |
2.29e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 10 VKQYGektavnGISLKVEQGEIY-----GLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKpyskelqhlMGYLPEERGL 84
Cdd:PRK13409 347 TKKLG------DFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK---------ISYKPQYIKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 YPKVKVSDqiiYLAQLRGMSASEadkslkYW----LERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:PRK13409 412 DYDGTVED---LLRSITDDLGSS------YYkseiIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
...
gi 1133779397 161 GLD 163
Cdd:PRK13409 483 HLD 485
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-220 |
2.46e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK-------ELQHLMGYLPEERGLYP 86
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsrlyTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 87 KVKVSDQIIY-LAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPV 165
Cdd:PRK11831 98 DMNVFDNVAYpLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 166 NVELLKDTVREMRD-LGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREIKK 220
Cdd:PRK11831 178 TMGVLVKLISELNSaLGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-194 |
2.57e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQV--VKQ---YGEKT--AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGkpyskelQH 73
Cdd:PRK11308 6 LQAIDLKKHypVKRglfKPERLvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG-------QD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 74 LMGYLPEER----------------GLYPKVKVSDQIIY-LAQLRGMSASE-ADKSLKYwLERFDV-PEYYNKKIEELSK 134
Cdd:PRK11308 79 LLKADPEAQkllrqkiqivfqnpygSLNPRKKVGQILEEpLLINTSLSAAErREKALAM-MAKVGLrPEHYDRYPHMFSG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 135 GNQQKMGFVAAVVHKPKILILDEAFSGLDpVNVE-----LLKDTVREMrdlGTSILFSTHRM---EHV 194
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALD-VSVQaqvlnLMMDLQQEL---GLSYVFISHDLsvvEHI 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-218 |
2.68e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 19 VNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPD----EGSILYNGKPYSKE----------LQ---------HLM 75
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCalrgrkiatiMQnprsafnplHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 76 GYLPEERGLYPKVKVSDQIIyLAQLRGMSASEADKSLKywLERFdvpeyynkkieELSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:PRK10418 99 HTHARETCLALGKPADDATL-TAALEAVGLENAARVLK--LYPF-----------EMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 156 DEAFSGLDPVN----VELLKDTVREmRDLGtsILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK10418 165 DEPTTDLDVVAqariLDLLESIVQK-RALG--MLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-197 |
4.17e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEG--------SILYNGKPYSKELQHL 74
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGtvkwsenaNIGYYAQDHAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 MGyLPEERGLYPKVKVSDQIIylaqlRGM------SASEADKSLKYwlerfdvpeyynkkieeLSKGNQQKMGFVAAVVH 148
Cdd:PRK15064 399 LT-LFDWMSQWRQEGDDEQAV-----RGTlgrllfSQDDIKKSVKV-----------------LSGGEKGRMLFGKLMMQ 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1133779397 149 KPKILILDEAFSGLDPVNVELLkDTVREMRDlGTSIlFSTHRMEHVEEL 197
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESL-NMALEKYE-GTLI-FVSHDREFVSSL 501
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-189 |
4.90e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 57.96 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 36 GANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHLMGYLPEERGLYPKVKVSDQIIYLAQLRGmSASEADKSLKYw 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYN-SAETLYAAIHY- 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 116 lerFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:PRK13541 111 ---FKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-60 |
5.78e-10 |
|
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: 59.95 E-value: 5.78e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSI 60
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-189 |
7.38e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGliYPD----EGSILYNGKpyskelqHLMGYLP 79
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGE-------SILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EER---GLY---------PKVKVSD--QIIYLAQLRGMSASEAD--KSLKYWLERFDV----PEYYNKKIEE-LSKGNQQ 138
Cdd:CHL00131 79 EERahlGIFlafqypieiPGVSNADflRLAYNSKRKFQGLPELDplEFLEIINEKLKLvgmdPSFLSRNVNEgFSGGEKK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1133779397 139 KMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-192 |
7.62e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.75 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTtmrmVLGLI----YPDEGSILYNGKPYSK-----ELQH 73
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIagarKIQQGRVEVLGGDMADarhrrAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 74 LMGYLPEERG--LYPKVKVSDQIIYLAQLRGMSASEADKslkywlerfdvpeyynkKIEEL-----------------SK 134
Cdd:NF033858 77 RIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRR-----------------RIDELlratglapfadrpagklSG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 135 GNQQKMGFVAAVVHKPKILILDEAFSGLDPvnveL-------LKDTVREMRDlGTSILFSTHRME 192
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPTTGVDP----LsrrqfweLIDRIRAERP-GMSVLVATAYME 199
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-190 |
8.57e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 59.38 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 19 VNGISLKVEQGEIYGLLGANGAGKTTTMRmVLGLIYPdegsiLYNGKPYSKELQHLMgYLPEeRGLYPKVKVSDQIIYL- 97
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWP-----VYGGRLTKPAKGKLF-YVPQ-RPYMTLGTLRDQIIYPd 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 98 ----AQLRGMSASEADK-----SLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGldpVNVE 168
Cdd:TIGR00954 540 ssedMKRRGLSDKDLEQildnvQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA---VSVD 616
|
170 180
....*....|....*....|..
gi 1133779397 169 LLKDTVREMRDLGTSILFSTHR 190
Cdd:TIGR00954 617 VEGYMYRLCREFGITLFSVSHR 638
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-221 |
8.92e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 22 ISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKE-----LQHLMGYLPEER---GLYPKVKVSDQ 93
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALstaqrLARGLVYLPEDRqssGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 94 IIYLAQLRgmsaseadksLKYWL----ERFDVPEYY----------NKKIEELSKGNQQKMGFVAAVVHKPKILILDEAF 159
Cdd:PRK15439 362 VCALTHNR----------RGFWIkparENAVLERYRralnikfnhaEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 160 SGLDpvnVELLKDTVREMRDL---GTSILFSTHRMEHVEELCrnitilDRSNTVVQGDIREIKKG 221
Cdd:PRK15439 432 RGVD---VSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQMA------DRVLVMHQGEISGALTG 487
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-189 |
9.99e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.01 E-value: 9.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS---------KELQHL 74
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyalseAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 M----GYL---PEErGLYPKV----KVSDQIIYL-----AQLRGMSASeadkslkyWLERFDVPEyynKKIEEL----SK 134
Cdd:PRK11701 87 LrtewGFVhqhPRD-GLRMQVsaggNIGERLMAVgarhyGDIRATAGD--------WLERVEIDA---ARIDDLpttfSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 135 GNQQKMGFVAAVVHKPKILILDEAFSGLDpVNVE--LLkDTVREM-RDLGTSILFSTH 189
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQarLL-DLLRGLvRELGLAVVIVTH 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-218 |
1.01e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.20 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 14 GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS----KELQHLMGYLPEERGLYPKvK 89
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvtrASLRRNIAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 90 VSDQI------IYLAQLRGmsASEADKSLKYWLERfdvPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILDEAF 159
Cdd:PRK13657 425 IEDNIrvgrpdATDEEMRA--AAERAQAHDFIERK---PDGYDTVVGErgrqLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 160 SGLDPVNVELLKDTVRE-MRDLGTSILfsTHRMEHVEELCRnITILDRSNTVVQGDIREI 218
Cdd:PRK13657 500 SALDVETEAKVKAALDElMKGRTTFII--AHRLSTVRNADR-ILVFDNGRVVESGSFDEL 556
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-218 |
1.63e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.96 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 31 IYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKELQHL--------MGYLPEERGLYPKVKVSDQIIYlaqlrG 102
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppekrrIGYVFQDARLFPHYKVRGNLRY-----G 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 103 MSASEADK--------SLKYWLERFDVpeyynkkieELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD-PVNVELLKDT 173
Cdd:PRK11144 101 MAKSMVAQfdkivallGIEPLLDRYPG---------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPYL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1133779397 174 VREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK11144 172 ERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-244 |
2.10e-09 |
|
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: 58.42 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 22 ISLKVEQGEIYGLLGANGAGKTTtmrMVLGLIYPDE---GSILYNGKPYSK----ELQHLMGYLPEERGLY--------- 85
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSS---LTLGLFRINEsaeGEIIIDGLNIAKiglhDLRFKITIIPQDPVLFsgslrmnld 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 86 PKVKVSDQIIY----LAQLRGMSASEADKSlkywleRFDVPEyynkKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSG 161
Cdd:TIGR00957 1382 PFSQYSDEEVWwaleLAHLKTFVSALPDKL------DHECAE----GGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 162 LDPVNVELLKDTVREMRDLGTsILFSTHRMEhveelcrniTILDRSNTVV--QGDIREIkkGYPREevVLRTAGEVNGLT 239
Cdd:TIGR00957 1452 VDLETDNLIQSTIRTQFEDCT-VLTIAHRLN---------TIMDYTRVIVldKGEVAEF--GAPSN--LLQQRGIFYSMA 1517
|
....*
gi 1133779397 240 EIAGV 244
Cdd:TIGR00957 1518 KDAGL 1522
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-218 |
2.19e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.34 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSI------LYNGKPySKELQHL---MGYL---PEER 82
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervITAGKK-NKKLKPLrkkVGIVfqfPEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 gLYPKVkVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPE-YYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSG 161
Cdd:PRK13634 98 -LFEET-VEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 162 LDPVNVELLKDTVREM-RDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-163 |
5.24e-09 |
|
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: 56.72 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 7 KQVVKQYGEktavNGISL----KVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSilYNGKPySKE--LQHLMG---- 76
Cdd:COG1245 77 EDPVHRYGE----NGFRLyglpVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGD--YDEEP-SWDevLKRFRGtelq 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 -YLpeeRGLYPK-VKVS--DQIIYLA--QLRGmSASE----AD--KSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVA 144
Cdd:COG1245 150 dYF---KKLANGeIKVAhkPQYVDLIpkVFKG-TVREllekVDerGKLDELAEKLGLENILDRDISELSGGELQRVAIAA 225
|
170
....*....|....*....
gi 1133779397 145 AVVHKPKILILDEAFSGLD 163
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLD 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-218 |
5.77e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.76 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPY----SKELQHLMGYLP 79
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyaSKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 80 EE--------------RGLYPKVKVsdqiiyLAQLRgmsaSEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAA 145
Cdd:PRK10253 88 QNattpgditvqelvaRGRYPHQPL------FTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 146 VVHKPKILILDEAFSGLDPVN----VELLKDTVRE--------MRDLGTSILFSTHrmehveelcrnITILDRSNTVVQG 213
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHqidlLELLSELNREkgytlaavLHDLNQACRYASH-----------LIALREGKIVAQG 226
|
....*
gi 1133779397 214 DIREI 218
Cdd:PRK10253 227 APKEI 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-60 |
7.32e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 7.32e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 7 KQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSI 60
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-163 |
9.79e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 2 EALQlKQVVKQYGEktavNGISL----KVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSilYNGKP--------YS- 68
Cdd:PRK13409 73 EELE-EEPVHRYGV----NGFKLyglpIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPswdevlkrFRg 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 69 KELQhlmGYLpeeRGLYP-KVKVSDQIIYLAQLRG----------MSASEADKsLKYWLERFDVPEYYNKKIEELSKGNQ 137
Cdd:PRK13409 146 TELQ---NYF---KKLYNgEIKVVHKPQYVDLIPKvfkgkvrellKKVDERGK-LDEVVERLGLENILDRDISELSGGEL 218
|
170 180
....*....|....*....|....*.
gi 1133779397 138 QKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:PRK13409 219 QRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-190 |
1.25e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.01 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 29 GEIYGLLGANGAGKTTTM-----RMVLGLIypdEGSILYNGKPYSKE-LQHLMGYLPEERGLYPKVKVSDQIIYLAQLRG 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMdvlagRKTGGYI---EGDIRISGFPKKQEtFARISGYCEQNDIHSPQVTVRESLIYSAFLRL 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 103 MSASEADKSLKYWLERFDVPEYYNKK--------IEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTV 174
Cdd:PLN03140 983 PKEVSKEEKMMFVDEVMELVELDNLKdaivglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
170
....*....|....*.
gi 1133779397 175 REMRDLGTSILFSTHR 190
Cdd:PLN03140 1063 RNTVDTGRTVVCTIHQ 1078
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-223 |
4.01e-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: 54.53 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 22 ISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKpyskelqhlMGYLPEERGLYPKVkVSDQIIY---LA 98
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR---------ISFSPQTSWIMPGT-IKDNIIFglsYD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 99 QLRGMSASEADKsLKYWLERFdvPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVN-VELLKDT 173
Cdd:TIGR01271 515 EYRYTSVIKACQ-LEEDIALF--PEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEIFESC 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1133779397 174 VREMRDLGTSILFsTHRMEHVEElCRNITILDRSNTVVQGDIREIKKGYP 223
Cdd:TIGR01271 592 LCKLMSNKTRILV-TSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKRP 639
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-163 |
4.64e-08 |
|
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: 52.80 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 20 NGISLKVEQG-----EIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSkelqhlmgYLPEErgLYPKVKVSDQI 94
Cdd:cd03237 11 GEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------YKPQY--IKADYEGTVRD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 95 IYLAQLRGMSA-----SEADKSLKywLERFdvpeyYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLD 163
Cdd:cd03237 81 LLSSITKDFYThpyfkTEIAKPLQ--IEQI-----LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
15-189 |
1.21e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGL--IYPDEGSILYNGKpyskelqHLMGYLPEERG--------L 84
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGK-------DLLELSPEDRAgegifmafQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 YPK--VKVSDQIIYLAQLRGMSASEADKSlkywLERFDVPEYYNKKIEEL---------------SKGNQQKMGFVAAVV 147
Cdd:PRK09580 86 YPVeiPGVSNQFFLQTALNAVRSYRGQEP----LDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1133779397 148 HKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-163 |
1.54e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSI-LYNGKPYSKELQHLMGYL-PEE 81
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLrADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RGLYPKVKVSDQiiylaqlrgmsasEADKSLKYWLERFDvpeYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILDE 157
Cdd:PRK10636 393 SPLQHLARLAPQ-------------ELEQKLRDYLGGFG---FQGDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDE 456
|
....*.
gi 1133779397 158 AFSGLD 163
Cdd:PRK10636 457 PTNHLD 462
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-206 |
1.72e-07 |
|
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: 50.55 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 20 NGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKpyskelqhlMGYLPeerglypkvkvsdQIIYLaq 99
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---------IAYVS-------------QEPWI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 100 lrgMSASEADKSLkyWLERFDvPEYYNKKIE--------------------E----LSKGNQQKMGFVAAVVHKPKILIL 155
Cdd:cd03250 78 ---QNGTIRENIL--FGKPFD-EERYEKVIKacalepdleilpdgdlteigEkginLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1133779397 156 DEAFSGLDP-VNVELLKDTVR-EMRDLGTSILfSTHRMEHVEElCRNITILDR 206
Cdd:cd03250 152 DDPLSAVDAhVGRHIFENCILgLLLNNKTRIL-VTHQLQLLPH-ADQIVVLDN 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-197 |
2.73e-07 |
|
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: 49.29 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 28 QGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYngkpyskelqhlmgylpeerglypkvkVSDQIIYLAQLRGMSase 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------IDGEDILEEVLDQLL--- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 108 adkslkywlerfdvPEYYNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVR------EMRDLG 181
Cdd:smart00382 51 --------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllLKSEKN 116
|
170
....*....|....*.
gi 1133779397 182 TSILFSTHRMEHVEEL 197
Cdd:smart00382 117 LTVILTTNDEKDLGPA 132
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-218 |
6.72e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.62 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 18 AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSI--------------LYNGKPYSKELQHLMG------Y 77
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvIELSEQSAAQMRHVRGadmamiF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 78 LPEERGLYPKVKVSDQI---IYLAQlrGMSASEADKSLKYWLERFDVPE---YYNKKIEELSKGNQQKMGFVAAVVHKPK 151
Cdd:PRK10261 111 QEPMTSLNPVFTVGEQIaesIRLHQ--GASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 152 ILILDEAFSGLD-PVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK10261 189 VLIADEPTTALDvTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-214 |
7.37e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.10 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSKeLQhlmgyLPEERGLYPKVK----- 89
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK-LQ-----LDSWRSRLAVVSqtpfl 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 90 VSD----------------QIIYLAQLrgmsASEADKSLKywlerfdVPEYYNKKIEE----LSKGNQQKMGFVAAVVHK 149
Cdd:PRK10789 401 FSDtvannialgrpdatqqEIEHVARL----ASVHDDILR-------LPQGYDTEVGErgvmLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1133779397 150 PKILILDEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHRMEHVEElCRNITILDRSNTVVQGD 214
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-189 |
9.23e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 9.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 16 KTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLG-LIYPDE-------GSILYNGKPYSK----ELQHLMGYLPE--E 81
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAidapRLARLRAVLPQaaQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 82 RGLYPKVkvsDQIIYLAQL----RGMSASEADKSLKYW-LERFDVPEYYNKKIEELSKGNQQKMGF--VAAVVHK----- 149
Cdd:PRK13547 94 PAFAFSA---REIVLLGRYpharRAGALTHRDGEIAWQaLALAGATALVGRDVTTLSGGELARVQFarVLAQLWPphdaa 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1133779397 150 --PKILILDEAFSGLDPVNVELLKDTVREM-RDLGTSILFSTH 189
Cdd:PRK13547 171 qpPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVH 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-163 |
9.35e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 12 QYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPD--EGSILYNGKP-----YSKELQHLMGYLPEER-- 82
Cdd:NF040905 269 LHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRniSGTVFKDGKEvdvstVSDAIDAGLAYVTEDRkg 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 -GLypkvKVSDQI---IYLAQLRGMSAseadkslKYWL---ERFDVPEYYNKKI-----------EELSKGNQQKMgfva 144
Cdd:NF040905 349 yGL----NLIDDIkrnITLANLGKVSR-------RGVIdenEEIKVAEEYRKKMniktpsvfqkvGNLSGGNQQKV---- 413
|
170 180
....*....|....*....|....
gi 1133779397 145 aVVHK-----PKILILDEAFSGLD 163
Cdd:NF040905 414 -VLSKwlftdPDVLILDEPTRGID 436
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-163 |
1.31e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 22 ISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS-----KELQHLMGYLPEER---GLYPKVKVSDQ 93
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprDAIRAGIMLCPEDRkaeGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 94 IIYLAQLRGMSAS-------EADKSLKYwLERFDV----PEyynKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGL 162
Cdd:PRK11288 352 INISARRHHLRAGclinnrwEAENADRF-IRSLNIktpsRE---QLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
.
gi 1133779397 163 D 163
Cdd:PRK11288 428 D 428
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-205 |
1.34e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 3 ALQLKQVVKQY--GEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHLMG 76
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgltDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YLPEERGLY---------PKVKVSDQIIYLAQLRGMSASEADKSlkywleRFDVPEYYNKKIEELSKGNQQKMGFVAAVV 147
Cdd:PLN03232 1314 IIPQSPVLFsgtvrfnidPFSEHNDADLWEALERAHIKDVIDRN------PFGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1133779397 148 HKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTsILFSTHRMEHVEElCRNITILD 205
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCT-MLVIAHRLNTIID-CDKILVLS 1443
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-234 |
1.38e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.97 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKT----AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLI-YPDE---GSILYNG----KPYS 68
Cdd:PRK11022 1 MALLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYPGRvmaEKLEFNGqdlqRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 69 KELQHLMG------YLPEERGLYPKVKVSDQI-------------------IYLAQLRGMSASEAdkslkywleRFDVPE 123
Cdd:PRK11022 81 KERRNLVGaevamiFQDPMTSLNPCYTVGFQImeaikvhqggnkktrrqraIDLLNQVGIPDPAS---------RLDVYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 124 YynkkieELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPV----NVELLKDTVREMRdlgTSILFSTHRMEHVEELCR 199
Cdd:PRK11022 152 H------QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiqaqIIELLLELQQKEN---MALVLITHDLALVAEAAH 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 1133779397 200 NITILDRSNTVVQGDIREIKKG--YPREEVVLRTAGE 234
Cdd:PRK11022 223 KIIVMYAGQVVETGKAHDIFRAprHPYTQALLRALPE 259
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-223 |
1.50e-06 |
|
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: 48.70 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 22 ISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK-PYSKELQHLMGYLPEERGLYpkvKVS-DQIIYLAQ 99
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRiSFSSQFSWIMPGTIKENIIF---GVSyDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 100 LRGMSASEAdkslkywLERFdvPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILDEAFSGLD-PVNVELLKDTV 174
Cdd:cd03291 133 VKACQLEED-------ITKF--PEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDvFTEKEIFESCV 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1133779397 175 REMRDLGTSILFsTHRMEHVEElCRNITILDRSNTVVQGDIREIKKGYP 223
Cdd:cd03291 204 CKLMANKTRILV-TSKMEHLKK-ADKILILHEGSSYFYGTFSELQSLRP 250
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-253 |
1.72e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 13 YGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRM-------VLGLIYpdEGSILYNGKPYSK-----ELQHLMGYLPE 80
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVLLGGRSIFNyrdvlEFRRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 81 ERGLYPKVKVSD--------QIIYLAQLRGMSASEADKsLKYWLErfdVPEYYNKKIEELSKGNQQKMGFVAAVVHKPKI 152
Cdd:PRK14271 109 RPNPFPMSIMDNvlagvrahKLVPRKEFRGVAQARLTE-VGLWDA---VKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 153 LILDEAFSGLDPVNVELLKDTVREMRDLGTSILFsTHrmehveELCRNITILDRSNTVVQGdiREIKKGyPREEvVLRTA 232
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIV-TH------NLAQAARISDRAALFFDG--RLVEEG-PTEQ-LFSSP 253
|
250 260
....*....|....*....|..
gi 1133779397 233 GEVNGLTEIAGVTG-VQRQERG 253
Cdd:PRK14271 254 KHAETARYVAGLSGdVKDAKRG 275
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1-178 |
1.78e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAV---NGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGK------------ 65
Cdd:PTZ00265 380 IKKIQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwr 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 66 ---------------------PYS----KELQHLMGYLPEER---------------------GLYPKVKVSDQIIYLAQ 99
Cdd:PTZ00265 460 skigvvsqdpllfsnsiknniKYSlyslKDLEALSNYYNEDGndsqenknkrnscrakcagdlNDMSNTTDSNELIEMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 100 -LRGMSASEA-DKSLKYWLERF--DVPEYYNKKI----EELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLK 171
Cdd:PTZ00265 540 nYQTIKDSEVvDVSKKVLIHDFvsALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
....*..
gi 1133779397 172 DTVREMR 178
Cdd:PTZ00265 620 KTINNLK 626
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-213 |
1.78e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.95 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 22 ISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSkELQHlmgylpeeRGLYPKVKV--SDQII---- 95
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSH--------SVLRQGVAMvqQDPVVladt 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 96 YLAQLR-GMSASEAdkslKYW--LERF-------DVPEYYNKKIEE----LSKGNQQKMGFVAAVVHKPKILILDEAFSG 161
Cdd:PRK10790 431 FLANVTlGRDISEE----QVWqaLETVqlaelarSLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1133779397 162 LDPVNVELLKDTVREMRDLGTSILFStHRMEHVEElCRNITILDRSNTVVQG 213
Cdd:PRK10790 507 IDSGTEQAIQQALAAVREHTTLVVIA-HRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
121-212 |
2.58e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 121 VPEYYNKKI----EELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLG-TSILFSTHRMEHVE 195
Cdd:PTZ00265 1344 LPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIK 1423
|
90 100
....*....|....*....|..
gi 1133779397 196 elcRNITIL-----DRSNTVVQ 212
Cdd:PTZ00265 1424 ---RSDKIVvfnnpDRTGSFVQ 1442
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
9-220 |
2.67e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 48.69 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 9 VVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIyPDEGSILYNGKPYSkEL------QHLmGYLPEER 82
Cdd:PRK11174 356 EILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELR-ELdpeswrKHL-SWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 83 GLyPKVKVSDQIIylaqLRGMSASEADksLKYWLERFDVPEY-------YNKKIEE----LSKGNQQKMGFVAAVVHKPK 151
Cdd:PRK11174 433 QL-PHGTLRDNVL----LGNPDASDEQ--LQQALENAWVSEFlpllpqgLDTPIGDqaagLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1133779397 152 ILILDEAFSGLDPVNVELLKDTVREMRdLGTSILFSTHRMEHVEElCRNITILDRSNTVVQGDIREIKK 220
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQ 572
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-204 |
4.50e-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: 46.98 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 7 KQVVKQYGEktavNGISLK----VEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSilYNGKP-YSKELQHLMG----- 76
Cdd:cd03236 4 DEPVHRYGP----NSFKLHrlpvPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdWDEILDEFRGselqn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 77 YLpeERGLYPKVKVSDQIIYL----AQLRG-----MSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVV 147
Cdd:cd03236 78 YF--TKLLEGDVKVIVKPQYVdlipKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 148 HKPKILILDEAFSGLD---PVNVELLkdtVREMRDLGTSILFSTHRMEHVEELCRNITIL 204
Cdd:cd03236 156 RDADFYFFDEPSSYLDikqRLNAARL---IRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-163 |
5.92e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 18 AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYS-----KELQHLMGYLPEER---GLYPKVK 89
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnanEAINHGFALVTEERrstGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 90 VS-DQII-----YLAQLrGMSASEADKSLKYWL---ERFDVPEYYNkKIEELSKGNQQKMGFVAAVVHKPKILILDEAFS 160
Cdd:PRK10982 343 IGfNSLIsnirnYKNKV-GLLDNSRMKSDTQWVidsMRVKTPGHRT-QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
...
gi 1133779397 161 GLD 163
Cdd:PRK10982 421 GID 423
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-187 |
1.25e-05 |
|
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: 45.33 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 11 KQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPD---EGSILYNGKPYSKELQHLMG---YLPEERGL 84
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGeiiYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 85 YPKVKVSDQIIYLAQLRGmsaseadkslkywlerfdvpeyyNKKIEELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDP 164
Cdd:cd03233 95 FPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180
....*....|....*....|....*
gi 1133779397 165 VNV-ELLKdTVREMRD-LGTSILFS 187
Cdd:cd03233 152 STAlEILK-CIRTMADvLKTTTFVS 175
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-205 |
2.04e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.87 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 4 LQLKQVVKQY--GEKT--AVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNGKPYSK----ELQHL- 74
Cdd:PRK10535 5 LELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 75 ---MGYLPEERGLYPKVKVSDQIIYLAQLRGMSASEADKSLKYWLERFDVPEYYNKKIEELSKGNQQKMGFVAAVVHKPK 151
Cdd:PRK10535 85 rehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1133779397 152 ILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILD 205
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRD 218
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-95 |
3.89e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 12 QYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSIlyngkpySKELQHLMGYLPEERGLYPKVKVS 91
Cdd:PRK15064 10 QFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-------SLDPNERLGKLRQDQFAFEEFTVL 82
|
....
gi 1133779397 92 DQII 95
Cdd:PRK15064 83 DTVI 86
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-60 |
4.49e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 4.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1133779397 5 QLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSI 60
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-206 |
5.00e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 24 LKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYN-----------------GKPY---SKELQHLMGYLPEERG 83
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqdpprnveGTVYdfvAEGIEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 84 LYPKVKV--SDQII-YLAQLRGM----SASEADKSLKYWLERFDVPEyyNKKIEELSKGNQQKMGFVAAVVHKPKILILD 156
Cdd:PRK11147 104 ISHLVETdpSEKNLnELAKLQEQldhhNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1133779397 157 EAFSGLDPVNVELLKDTvreMRDLGTSILFSTHRMEHVEELCRNITILDR 206
Cdd:PRK11147 182 EPTNHLDIETIEWLEGF---LKTFQGSIIFISHDRSFIRNMATRIVDLDR 228
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
56-189 |
6.29e-05 |
|
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: 43.92 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 56 DEGSILYNGKPYSKELQHLMGYLPEERGLYPKVKVSDQIIYLAQLRGMSASeadkslkywLERFDVPEYYNKKIEELSKG 135
Cdd:pfam13304 170 DLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERG---------LILLENGGGGELPAFELSDG 240
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 136 NQQKMGFVAAV---VHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTH 189
Cdd:pfam13304 241 TKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-218 |
1.86e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 1 MEALQLKQVVKQYGEKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIypdegsILYNGKPYS----------KE 70
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGEL------PLLSGERQSqfshitrlsfEQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 71 LQHL------------MGYLPEERGlypkvKVSDQIIYlaqlrgMSASEADKSLKYwLERFDVPEYYNKKIEELSKGNQQ 138
Cdd:PRK10938 75 LQKLvsdewqrnntdmLSPGEDDTG-----RTTAEIIQ------DEVKDPARCEQL-AQQFGITALLDRRFKYLSTGETR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 139 KMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITILDRSNTVVQGDIREI 218
Cdd:PRK10938 143 KTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
152-204 |
1.90e-04 |
|
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: 41.19 E-value: 1.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1133779397 152 ILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFSTHRMEHVEELCRNITIL 204
Cdd:cd03227 102 LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-220 |
1.05e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 19 VNGIslkVEQGEIYGLLGANGAGKTTTMRMVLGLIY----PDEGSILYNGKPYSKELQHLMG---YLPEERGLYPKVKVS 91
Cdd:TIGR00956 80 MDGL---IKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRGdvvYNAETDVHFPHLTVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 92 DQIIYLA-----QLRGMSASE---ADKSLKYWLERFDVPEYYNKK-----IEELSKGNQQKMGFVAAVVHKPKILILDEA 158
Cdd:TIGR00956 157 ETLDFAArcktpQNRPDGVSReeyAKHIADVYMATYGLSHTRNTKvgndfVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1133779397 159 FSGLDPVN----VELLKDTVREmrdLGTSILFSTHR-MEHVEELCRNITILDRSNTVVQGDIREIKK 220
Cdd:TIGR00956 237 TRGLDSATalefIRALKTSANI---LDTTPLVAIYQcSQDAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-64 |
1.94e-03 |
|
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: 38.32 E-value: 1.94e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1133779397 26 VEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSILYNG 64
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG 60
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-241 |
2.59e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.57 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 15 EKTAVNGISLKVEQGEIYGLLGANGAGKTTTMRMVLGLIYPDEGSilyngkpySKELQHLMGYLPEERGLYpKVKVSDQI 94
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS--------SVVIRGSVAYVPQVSWIF-NATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 95 IYLAQLRGMSASEA--DKSLKYWLERF---DVPEYYNKKIeELSKGNQQKMGFVAAVVHKPKILILDEAFSGLDP-VNVE 168
Cdd:PLN03232 700 LFGSDFESERYWRAidVTALQHDLDLLpgrDLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQ 778
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133779397 169 LLKDTVREMRDLGTSILFSTHRmeHVEELCRNITILDRSNTVVQGDIREIKKGYPREEVVLRTAGEVNGLTEI 241
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQL--HFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEV 849
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
154-197 |
3.64e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 37.83 E-value: 3.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1133779397 154 ILDEAFSGLDPVNVELLKDTVREMRDlGTSILFSTHR---MEHVEEL 197
Cdd:cd03278 140 VLDEVDAALDDANVERFARLLKEFSK-ETQFIVITHRkgtMEAADRL 185
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
126-212 |
6.52e-03 |
|
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: 36.92 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1133779397 126 NKKIEELSKGNQQ--KMGFVAAVVHKPKILILDEAFSGLDPVNVELLKDTVREMRDLGTSILFsthrMEHveelcrNITI 203
Cdd:cd03238 82 GQKLSTLSGGELQrvKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVIL----IEH------NLDV 151
|
....*....
gi 1133779397 204 LDRSNTVVQ 212
Cdd:cd03238 152 LSSADWIID 160
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
112-168 |
7.14e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.29 E-value: 7.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1133779397 112 LKYWLERFDVPE---YYNKKIEELSKGNQQKMGFV---AAVV----------HKPKILILDEAFSGLDPVNVE 168
Cdd:pfam13558 10 LSFEVEVRDEDGsevETYRRSGGLSGGEKQLLAYLplaAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIR 82
|
|
| |
