|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-226 |
1.96e-98 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 289.27 E-value: 1.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:COG1131 7 TKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:COG1131 87 DLTVRENLRFFARLYGLPRKEArerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 171 IKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKK 226
Cdd:COG1131 167 RRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-218 |
1.06e-97 |
|
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: 286.42 E-value: 1.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKtEILKNIGAMVETPGFYS 93
Cdd:cd03268 7 TKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALIEAPGFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKENaIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:cd03268 86 NLTARENLRLLARLLGIRKKR-IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446716125 174 IRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNGVLLEEI 218
Cdd:cd03268 165 LRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-214 |
1.06e-78 |
|
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: 236.91 E-value: 1.06e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:cd03230 7 SKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLtinakilgiqkenaieevleivglasekvklfkNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:cd03230 87 NLTVRENL---------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446716125 174 IRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:cd03230 134 FWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
14-214 |
5.58e-76 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 231.90 E-value: 5.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKteiLKNIGAMVETPGFYS 93
Cdd:TIGR03740 7 SKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKD---LHKIGSLIESPPLYE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIqKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:TIGR03740 84 NLTARENLKVHTTLLGL-PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446716125 174 IRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:TIGR03740 163 LRELIRSFPE-QGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
14-226 |
8.80e-69 |
|
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: 213.95 E-value: 8.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:COG4555 8 SKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDERGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:COG4555 88 RLTVRENIRYFAELYGLFDEELkkrIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 171 IKEIRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKK 226
Cdd:COG4555 168 RRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-224 |
2.53e-64 |
|
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: 201.83 E-value: 2.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:cd03265 7 VKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:cd03265 87 ELTGWENLYIHARLYGVPGAERrerIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446716125 171 IKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLK 224
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-289 |
1.89e-62 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 199.56 E-value: 1.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESnktEILKNIGAMVETPGFYS 93
Cdd:COG4152 8 TKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRIGYLPEERGLYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:COG4152 85 KMKVGEQLVYLARLKGLSKAEAkrrADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 171 IKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNG--VL---LEEIMyeDLKKKNRQFISISVSDEEkvaclL 245
Cdd:COG4152 165 VELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGrkVLsgsVDEIR--RQFGRNTLRLEADGDAGW-----L 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446716125 246 ETNFGIYDYKIKENG-EFKIYSHIDRQQEINRLLVLNNIDVFQMR 289
Cdd:COG4152 237 RALPGVTVVEEDGDGaELKLEDGADAQELLRALLARGPVREFEEV 281
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
15-304 |
1.88e-58 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 189.52 E-value: 1.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSN 94
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGI 171
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAeerAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 172 KEIRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKK---------NRQFISISVSDEEKVA 242
Cdd:TIGR01188 161 RAIWDYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRlgkdtlesrPRDIQSLKVEVSMLIA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 243 CLLETNFGIYDYKiKENGEFKIYSHIDRQQ--EINRLLVLNNIDVFQMRVIEDNLETYFEDLVG 304
Cdd:TIGR01188 240 ELGETGLGLLAVT-VDSDRIKILVPDGDETvpEIVEAAIRNGIRIRSISTERPSLDDVFLKLTG 302
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-217 |
7.09e-56 |
|
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: 180.08 E-value: 7.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGqIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:cd03264 7 TKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGI---QKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:cd03264 86 NFTVREFLDYIAWLKGIpskEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446716125 171 IKEIRKLIKDLAQSRniTILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:cd03264 166 RIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
14-302 |
1.53e-55 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 182.28 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:TIGR03522 9 TKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIGYLPEHNPLYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQ---KENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:TIGR03522 89 DMYVREYLQFIAGIYGMKgqlLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTTGLDPNQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 171 IKEIRKLIKDLAQSRniTILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKKNRQFISISVSDEEKVACLLETNFG 250
Cdd:TIGR03522 169 LVEIRNVIKNIGKDK--TIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELSAANKKQVIEVEFEEQIDLQLFETLEE 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446716125 251 IYDYKIKENGEFKIY--SHIDRQQEINRLLVLNNIDVFQMRVIEDNLETYFEDL 302
Cdd:TIGR03522 247 ISSVKNTGGNTWKLTfeTPNDTRPEIFKLAQQKGLKLISLQQNEKNLEQVFREI 300
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
14-217 |
7.09e-52 |
|
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: 169.86 E-value: 7.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQY----GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETP 89
Cdd:cd03266 8 TKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 GFYSNLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:cd03266 88 GLYDRLTARENLEYFAGLYGLKGDELtarLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 167 DPIGIKEIRKLIKDLaQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:cd03266 168 DVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-215 |
8.86e-51 |
|
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: 167.30 E-value: 8.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGS--QIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAmveTPGF 91
Cdd:cd03263 7 TKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY---CPQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 ---YSNLTAKENLTINAKILGIQKENAIEEV---LEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:cd03263 84 dalFDELTVREHLRFYARLKGLPKSEIKEEVellLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446716125 166 LDPIGIKEIRKLIKDLAQSRniTILISSHILSEIEQLVDKVGIIHNGVLL 215
Cdd:cd03263 164 LDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-213 |
2.74e-49 |
|
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: 163.22 E-value: 2.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFEsnkTEILKNIGAMVETPGFYS 93
Cdd:cd03269 7 TKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPEERGLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:cd03269 84 KMKVIDQLVYLAQLKGLKKEEArrrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446716125 171 IKEIRKLIKDLAqSRNITILISSHILSEIEQLVDKVGIIHNGV 213
Cdd:cd03269 164 VELLKDVIRELA-RAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
14-200 |
8.96e-49 |
|
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: 161.49 E-value: 8.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:COG4133 9 SCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQK-ENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIK 172
Cdd:COG4133 89 ELTVRENLRFWAALYGLRAdREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVA 168
|
170 180
....*....|....*....|....*...
gi 446716125 173 EIRKLIKDLAQSRNItILISSHILSEIE 200
Cdd:COG4133 169 LLAELIAAHLARGGA-VLLTTHQPLELA 195
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
14-231 |
3.57e-48 |
|
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: 160.92 E-value: 3.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF----ESNKTEILKNIGaMVetp 89
Cdd:COG1127 12 TKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRRRIG-ML--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 gF-----YSNLTAKEN----LTINAKILGIQKENAIEEVLEIVGLA-------SEkvkLfknySLGMKQRLGIARALLHN 153
Cdd:COG1127 88 -FqggalFDSLTVFENvafpLREHTDLSEAEIRELVLEKLELVGLPgaadkmpSE---L----SGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 154 PELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKKN----RQ 229
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDdpwvRQ 239
|
..
gi 446716125 230 FI 231
Cdd:COG1127 240 FL 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-212 |
2.48e-47 |
|
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: 156.96 E-value: 2.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILK---NIGAMVETPG 90
Cdd:cd03229 7 SKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrrRIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENLTInakilgiqkenaieevleivGLasekvklfknySLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:cd03229 87 LFPHLTVLENIAL--------------------GL-----------SGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446716125 171 IKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:cd03229 136 RREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-296 |
1.50e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 159.48 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMvetpgF------YSNL 95
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVV-----FgqrsqlWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENLTINAKILGIQKENAIE------EVLEIVGLASEKV-KLfknySLGMKQRLGIARALLHNPELLILDEPTNGLDP 168
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAEYKKrldelvELLDLGELLDTPVrQL----SLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 169 IGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGvlleEIMY----EDLKKK--NRQFISISVSDEEKVA 242
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG----RIIYdgslEELKERfgPYKTIVLELAEPVPPL 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 243 CLLEtnfgiyDYKIKENGEFKIYSHIDRQQEINRLL--VLNNIDVFQMRVIEDNLE 296
Cdd:COG4586 264 ELPR------GGEVIEREGNRVRLEVDPRESLAEVLarLLARYPVRDLTIEEPPIE 313
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-230 |
5.59e-45 |
|
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: 152.66 E-value: 5.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF----ESNKTEILKNIGAMVETP 89
Cdd:cd03261 7 TKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 GFYSNLTAKENLTINAKILGIQKENAIEEV----LEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:cd03261 87 ALFDSLTVFENVAFPLREHTRLSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 166 LDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKKN----RQF 230
Cdd:cd03261 167 LDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDdplvRQF 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
14-217 |
3.93e-43 |
|
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: 147.73 E-value: 3.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQ----IAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF----ESNKTEILKNIGAM 85
Cdd:cd03258 8 SKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKARRRIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 86 VETPGFYSNLTAKENLTINAKILGIQK---ENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEP 162
Cdd:cd03258 88 FQHFNLLSSRTVFENVALPLEIAGVPKaeiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446716125 163 TNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:cd03258 168 TSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEE 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-215 |
1.21e-42 |
|
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: 146.71 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGA-MVETPGFYS 93
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvFGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARFkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446716125 171 IKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL 215
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-214 |
1.87e-42 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 156.05 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMveTPGF-- 91
Cdd:NF033858 273 TMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYM--SQAFsl 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSNLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDP 168
Cdd:NF033858 351 YGELTVRQNLELHARLFHLPAAEIaarVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446716125 169 IGIKEIRKLIKDLAQSRNITILISSHILSEIEQlVDKVGIIHNG-VL 214
Cdd:NF033858 431 VARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGrVL 476
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
22-217 |
2.43e-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: 152.75 E-value: 2.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF----ESNKTEILKNIGaMVetpgF---YSN 94
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsRRSLRELRRRVQ-MV----FqdpYSS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 L----TAKENLTINAKILGI----QKENAIEEVLEIVGLASEkvklFKNY-----SLGMKQRLGIARALLHNPELLILDE 161
Cdd:COG1123 355 LnprmTVGDIIAEPLRLHGLlsraERRERVAELLERVGLPPD----LADRyphelSGGQRQRVAIARALALEPKLLILDE 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
22-225 |
1.26e-41 |
|
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: 143.63 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKE-FESNKTEILKNIGaMV----ETPGFYSnlT 96
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDiTKKNLRELRRKVG-LVfqnpDDQLFAP--T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINAKILGIQKENA---IEEVLEIVGLASekvklFKNY-----SLGMKQRLGIARALLHNPELLILDEPTNGLDP 168
Cdd:COG1122 93 VEEDVAFGPENLGLPREEIrerVEEALELVGLEH-----LADRpphelSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 169 IGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVLL-----EEIM--YEDLKK 225
Cdd:COG1122 168 RGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVadgtpREVFsdYELLEE 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
17-206 |
1.55e-41 |
|
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: 143.06 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKefesNKTEILKNIGAMVETPGF--YSN 94
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK----PLEKERKRIGYVPQRRSIdrDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKE----NLTINAKILGIQKEN---AIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:cd03235 85 ISVRDvvlmGLYGHKGLFRRLSKAdkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 446716125 168 PIGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKV 206
Cdd:cd03235 165 PKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRV 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-225 |
2.32e-41 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 143.79 E-value: 2.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-ESNKTEILKNIGaMVetpgF-- 91
Cdd:COG1124 13 QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRVQ-MV----Fqd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 -YSNL----TAKENLTINAKILGI-QKENAIEEVLEIVGLASEkvkLFKNY----SLGMKQRLGIARALLHNPELLILDE 161
Cdd:COG1124 88 pYASLhprhTVDRILAEPLRIHGLpDREERIAELLEQVGLPPS---FLDRYphqlSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKK 225
Cdd:COG1124 165 PTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-217 |
2.64e-41 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 143.25 E-value: 2.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIfekefesNKTEI---------LKNIGAM 85
Cdd:COG1137 11 KSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL-------DGEDIthlpmhkraRLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 86 VETPGFYSNLTAKENLTINAKILGI---QKENAIEEVLEIVGLasEKVKLFKNYSL--GMKQRLGIARALLHNPELLILD 160
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELRKLskkEREERLEELLEEFGI--THLRKSKAYSLsgGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 161 EPTNGLDPIGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKE-RGIGVLITDHNVRETLGICDRAYIISEGKVLAE 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-214 |
3.40e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 143.31 E-value: 3.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKteilKNIG-----AMVEtPGF 91
Cdd:COG1121 16 YGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR----RRIGyvpqrAEVD-WDF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 --------YSNLTAKENLTinaKILGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:COG1121 91 pitvrdvvLMGRYGRRGLF---RRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 164 NGLDPIGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:COG1121 168 AGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-217 |
4.86e-41 |
|
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: 142.26 E-value: 4.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIG---AMVetpgF--- 91
Cdd:cd03257 16 GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkeiQMV----Fqdp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSNL----TAKENLTINAKILGI-----QKENAIEEVLEIVGLASEkvkLFKNY----SLGMKQRLGIARALLHNPELLI 158
Cdd:cd03257 92 MSSLnprmTIGEQIAEPLRIHGKlskkeARKEAVLLLLVGVGLPEE---VLNRYphelSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 159 LDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-212 |
5.65e-41 |
|
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: 141.45 E-value: 5.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKT-EILKNIGaMVetpgF----- 91
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVG-LV----Fqnpdd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 -YSNLTAKENLTINAKILGIQKE---NAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:cd03225 87 qFFGPTVEEEVAFGLENLGLPEEeieERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446716125 168 PIGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:cd03225 167 PAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-216 |
1.00e-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: 141.12 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFeSNKTEILKNIGAMVETPGFYS 93
Cdd:cd03259 7 SKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQDYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGI---QKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:cd03259 86 HLTVAENIAFGLKLRGVpkaEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446716125 171 IKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:cd03259 166 REELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-212 |
1.33e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 143.41 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSN 94
Cdd:PRK13537 15 KRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTINAKILGI---QKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPigi 171
Cdd:PRK13537 95 FTVRENLLVFGRYFGLsaaAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP--- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446716125 172 kEIRKLIKDLAQS---RNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK13537 172 -QARHLMWERLRSllaRGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
14-217 |
2.56e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 143.43 E-value: 2.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:PRK13536 48 SKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGI---QKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPig 170
Cdd:PRK13536 128 EFTVRENLLVFGRYFGMstrEIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP-- 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446716125 171 ikEIRKLIKDLAQS---RNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:PRK13536 206 --HARHLIWERLRSllaRGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-212 |
8.42e-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: 136.61 E-value: 8.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNigamvetpgfys 93
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 nltakenltinakilgiqkenaieEVLEIVGLasekvklfknySLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:cd00267 74 ------------------------RIGYVPQL-----------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 446716125 174 IRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:cd00267 119 LLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
15-217 |
2.98e-38 |
|
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: 134.98 E-value: 2.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIfekefesNKTEILK---------NIGAM 85
Cdd:cd03218 8 KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL-------DGQDITKlpmhkrarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 86 VETPGFYSNLTAKENLTINAKILGI---QKENAIEEVLEIVGLasEKVKLFKNYSL--GMKQRLGIARALLHNPELLILD 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLskkEREEKLEELLEEFHI--THLRKSKASSLsgGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 161 EPTNGLDPIGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
17-215 |
1.25e-37 |
|
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: 131.79 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEfesnkteilknigamvetpgfYSNLT 96
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD---------------------LASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKEnltiNAKILGIqkenaIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRK 176
Cdd:cd03214 68 PKE----LARKIAY-----VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 446716125 177 LIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL 215
Cdd:cd03214 139 LLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-164 |
6.63e-37 |
|
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: 128.92 E-value: 6.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIL-KNIGAMVETPGFYSNLTAKENL 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAKILGIQKENA---IEEVLE---IVGLASEKVKLF-KNYSLGMKQRLGIARALLHNPELLILDEPTN 164
Cdd:pfam00005 81 RLGLLLKGLSKREKdarAEEALEklgLGDLADRPVGERpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-217 |
8.75e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.05 E-value: 8.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQY----GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEIL---KNIGaM 85
Cdd:COG1135 8 SKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRaarRKIG-M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 86 VetpgFYS-NL----TAKENLTINAKILGIQKENA---IEEVLEIVGLASEKvklfKNY----SLGMKQRLGIARALLHN 153
Cdd:COG1135 87 I----FQHfNLlssrTVAENVALPLEIAGVPKAEIrkrVAELLELVGLSDKA----DAYpsqlSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 154 PELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-212 |
1.53e-36 |
|
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: 130.97 E-value: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGN-IKIFEKEFES-NKTEILKNIG----AMVETp 89
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGeDVWELRKRIGlvspALQLR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 gFYSNLTAKE--------NLTINAKILGIQKENAiEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDE 161
Cdd:COG1119 91 -FPRDETVLDvvlsgffdSIGLYREPTDEQRERA-RELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-214 |
1.87e-36 |
|
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: 129.92 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQI----AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF----ESNKTEI-LKNIGA 84
Cdd:cd03255 7 SKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFrRRHIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 85 MVETPGFYSNLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDE 161
Cdd:cd03255 87 VFQSFNLLPDLTALENVELPLLLAGVPKKERrerAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILsEIEQLVDKVGIIHNGVL 214
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-212 |
2.25e-36 |
|
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: 130.50 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQY-GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-ESNKTEILKNIGAMVETPGF 91
Cdd:cd03295 7 TKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIrEQDPVELRRKIGYVIQQIGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSNLTAKENLTINAKILGIQKENAIE---EVLEIVGLasEKVKLFKNY----SLGMKQRLGIARALLHNPELLILDEPTN 164
Cdd:cd03295 87 FPHMTVEENIALVPKLLKWPKEKIREradELLALVGL--DPAEFADRYphelSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446716125 165 GLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNG 212
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
15-217 |
5.62e-36 |
|
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: 129.32 E-value: 5.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIfekefesNKTEILK---------NIGAM 85
Cdd:TIGR04406 9 KSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILI-------DGQDITHlpmherarlGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 86 VETPGFYSNLTAKENLTInakILGIQK-------ENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLI 158
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMA---VLEIRKdldraerEERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 159 LDEPTNGLDPIGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKE-RGIGVLITDHNVRETLDICDRAYIISDGKVLAE 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
17-223 |
1.03e-35 |
|
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: 129.01 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAM---------- 85
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVpqeppapfgl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 86 -VE-------TP--GFYSNLTAKEnltinakilgiqkENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPE 155
Cdd:COG1120 91 tVRelvalgrYPhlGLFGRPSAED-------------REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446716125 156 LLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL-----EEIMYEDL 223
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVaqgppEEVLTPEL 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-214 |
2.03e-35 |
|
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: 127.26 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIL---KNIGaMVetpg 90
Cdd:cd03262 7 HKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrQKVG-MV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 F-----YSNLTAKENLTIN-AKILGIQKENAIE---EVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDE 161
Cdd:cd03262 82 FqqfnlFPHLTVLENITLApIKVKGMSKAEAEEralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:cd03262 162 PTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-216 |
2.56e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.09 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQY-GSQIAVNNLSITVESGQIYgFL-GRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILK---NIGaMVe 87
Cdd:COG2884 8 SKRYpGGREALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYlrrRIG-VV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 88 tpgFY-----SNLTAKENLTINAKILGIQKENA---IEEVLEIVGLaSEKVKLF-KNYSLGMKQRLGIARALLHNPELLI 158
Cdd:COG2884 85 ---FQdfrllPDRTVYENVALPLRVTGKSRKEIrrrVREVLDLVGL-SDKAKALpHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 159 LDEPTNGLDPIGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
14-194 |
3.82e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 127.48 E-value: 3.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQY-GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILK----NIGaMVE- 87
Cdd:COG3638 9 SKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrrRIG-MIFq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 88 TPGFYSNLTAKEN--------LTINAKILGI----QKENAIEeVLEIVGLASekvKLFK---NYSLGMKQRLGIARALLH 152
Cdd:COG3638 88 QFNLVPRLSVLTNvlagrlgrTSTWRSLLGLfppeDRERALE-ALERVGLAD---KAYQradQLSGGQQQRVAIARALVQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446716125 153 NPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSH 194
Cdd:COG3638 164 EPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLH 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
14-219 |
7.26e-35 |
|
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: 127.08 E-value: 7.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGaMVET---PG 90
Cdd:COG0411 11 TKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG-IARTfqnPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENLTI------NAKILGI--------QKENAI----EEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLH 152
Cdd:COG0411 90 LFPELTVLENVLVaaharlGRGLLAAllrlprarREEREAreraEELLERVGLADRADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446716125 153 NPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL-----EEIM 219
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIaegtpAEVR 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-217 |
8.98e-35 |
|
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: 131.95 E-value: 8.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPT---KGNIKIFEKEFESNKTEILKNIGAMVetpgFYSN 94
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGMV----FQDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTINAKI------LGIQKENA---IEEVLEIVGLAsekvKLFKNY----SLGMKQRLGIARALLHNPELLILDE 161
Cdd:COG1123 93 MTQLNPVTVGDQIaealenLGLSRAEArarVLELLEAVGLE----RRLDRYphqlSGGQRQRVAIAMALALDPDLLIADE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:COG1123 169 PTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
14-217 |
1.44e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 125.49 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILK---NIGaMVetpg 90
Cdd:COG1126 8 HKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlrrKVG-MV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 F-----YSNLTAKENLTInA--KILGIQKENAIE---EVLEIVGLAsEKVKlfkNY----SLGMKQRLGIARALLHNPEL 156
Cdd:COG1126 83 FqqfnlFPHLTVLENVTL-ApiKVKKMSKAEAEEramELLERVGLA-DKAD---AYpaqlSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 157 LILDEPTNGLDPIGIKEIRKLIKDLAQSrNITILISSHilsEIE---QLVDKVGIIHNGVLLEE 217
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTH---EMGfarEVADRVVFMDGGRIVEE 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-217 |
1.85e-34 |
|
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: 125.24 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGaMVET---PG 90
Cdd:cd03219 7 TKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG-IGRTfqiPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENL-----------TINAKILGIQKE--NAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELL 157
Cdd:cd03219 86 LFPELTVLENVmvaaqartgsgLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 158 ILDEPTNGLDPIGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-206 |
5.13e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.82 E-value: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQY----GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIlknigAMVetp 89
Cdd:COG1116 14 SKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR-----GVV--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 gF--YSNL---TAKENLTINAKILGIQKENA---IEEVLEIVGLASekvklFKNY-----SLGMKQRLGIARALLHNPEL 156
Cdd:COG1116 86 -FqePALLpwlTVLDNVALGLELRGVPKAERrerARELLELVGLAG-----FEDAyphqlSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446716125 157 LILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKV 206
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRV 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-216 |
6.91e-34 |
|
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: 123.44 E-value: 6.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIK-----PTKGNIKIFEKEFESNKTEIL---KNIGaM 85
Cdd:cd03260 7 NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLelrRRVG-M 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 86 V--ETPGFysNLTAKENLTINAKILGIQKENAI----EEVLEIVGLASE-KVKLFKNY-SLGMKQRLGIARALLHNPELL 157
Cdd:cd03260 86 VfqKPNPF--PGSIYDNVAYGLRLHGIKLKEELdervEEALRKAALWDEvKDRLHALGlSGGQQQRLCLARALANEPEVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 158 ILDEPTNGLDPIGIKEIRKLIKDLAqsRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-214 |
4.25e-33 |
|
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: 119.46 E-value: 4.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFEsnkteilknigamvetpgFYS 93
Cdd:cd03216 7 TKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------------------FAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKEnltinakiLGIqkenaieevlEIVglasekvklfknY--SLGMKQRLGIARALLHNPELLILDEPTNGLDPIGI 171
Cdd:cd03216 69 PRDARR--------AGI----------AMV------------YqlSVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446716125 172 KEIRKLIKDLaQSRNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:cd03216 119 ERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-219 |
6.58e-33 |
|
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: 122.37 E-value: 6.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEIL----KNIGAMVETP 89
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRelrrKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 GFYSNLTAKENLTINAKILGIQKENAIE---EVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGVPRAEREEraaEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 167 DPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL-----EEIM 219
Cdd:cd03294 192 DPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVqvgtpEEIL 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-192 |
8.63e-33 |
|
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: 120.05 E-value: 8.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFesNKTEILKNIGAMVETPG--FY 92
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERRKSIGYVMQDVDyqLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 93 SNlTAKENLTINAKILGiQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIK 172
Cdd:cd03226 86 TD-SVREELLLGLKELD-AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180
....*....|....*....|
gi 446716125 173 EIRKLIKDLAQSRNITILIS 192
Cdd:cd03226 164 RVGELIRELAAQGKAVIVIT 183
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-227 |
3.59e-32 |
|
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: 125.26 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAMVETPGFYsNLT 96
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVPQNPYLF-AGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTI---NAKilgiqkENAIEEVLEIVGLASEKVKLFKNY-----------SLGMKQRLGIARALLHNPELLILDEP 162
Cdd:COG4988 427 IRENLRLgrpDAS------DEELEAALEAAGLDEFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446716125 163 TNGLDPIGIKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKN 227
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-230 |
4.41e-32 |
|
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: 125.72 E-value: 4.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGaMVETPGFYSNLT 96
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIG-VVLQDVFLFSGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINAKILGIQKenaIEEVLEIVGLASEKVKLFKNY-----------SLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:COG2274 565 IRENITLGDPDATDEE---IIEAARLAGLHDFIEALPMGYdtvvgeggsnlSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446716125 166 LDPIGIKEIRKLIKDLAQsrNITILISSHILSEIeQLVDKVGIIHNGVLLEEIMYEDLKKKNRQF 230
Cdd:COG2274 642 LDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKGLY 703
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-212 |
6.10e-32 |
|
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: 118.31 E-value: 6.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIG-AMV-ETPGFYSN 94
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGiGYVpEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTINAKILGIQKENA-IEEVLEIVGLASEKVK-LFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIK 172
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKArLERVYELFPRLKERRKqLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446716125 173 EIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:cd03224 170 EIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-212 |
9.13e-32 |
|
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: 116.33 E-value: 9.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-ESNKTEILKNIGAMVETPGFYSNlT 96
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrDLDLESLRKNIAYVPQDPFLFSG-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENltinakILgiqkenaieevleivglasekvklfknySLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRK 176
Cdd:cd03228 92 IREN------IL----------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 446716125 177 LIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNG 212
Cdd:cd03228 138 ALRALAKGK--TVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
16-214 |
1.88e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.45 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNK-TEILKNIGAMVETPGFYSN 94
Cdd:COG4619 9 RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQVAYVPQEPALWGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 lTAKENLTINAKILGIQ-KENAIEEVLEIVGLASEKV-KLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIK 172
Cdd:COG4619 89 -TVRDNLPFPFQLRERKfDRERALELLERLGLPPDILdKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446716125 173 EIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:COG4619 168 RVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-211 |
1.92e-31 |
|
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: 116.80 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGS----QIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFesnkTEILKNIGAMVETP 89
Cdd:cd03293 7 SKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----TGPGPDRGYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 GFYSNLTAKENLTINAKILGIQKENAIEEV---LEIVGLASekvklFKNY-----SLGMKQRLGIARALLHNPELLILDE 161
Cdd:cd03293 83 ALLPWLTVLDNVALGLELQGVPKAEARERAeelLELVGLSG-----FENAyphqlSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHN 211
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-212 |
2.79e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 117.94 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 20 QIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNK----TEILKNIGaMV--------- 86
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkkklKDLRKKVG-LVfqfpehqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 87 ETpgfysnlTAKENLTINAKILGIQKENAIE---EVLEIVGLaSEKVKLFKNYSL--GMKQRLGIARALLHNPELLILDE 161
Cdd:TIGR04521 97 EE-------TVYKDIAFGPKNLGLSEEEAEErvkEALELVGL-DEEYLERSPFELsgGQMRRVAIAGVLAMEPEVLILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:TIGR04521 169 PTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKG 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
17-233 |
3.43e-31 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 116.47 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTE--ILKNIGAMVETPGFYSN 94
Cdd:TIGR03410 10 YGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHerARAGIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTINAKILGIQKENAIEEVLEivglasekvkLFK-----------NYSLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:TIGR03410 90 LTVEENLLTGLAALPRRSRKIPDEIYE----------LFPvlkemlgrrggDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446716125 164 NGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKK-KNRQFISI 233
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEdKVRRYLAV 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
14-218 |
4.25e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 116.30 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGS----QIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF----ESNKTEI-LKNIGa 84
Cdd:COG1136 11 TKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELARLrRRHIG- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 85 MVetpgFYS-----NLTAKENLTINAKILGIQKENA---IEEVLEIVGLAsEKVKLFKNY-SLGMKQRLGIARALLHNPE 155
Cdd:COG1136 90 FV----FQFfnllpELTALENVALPLLLAGVSRKERrerARELLERVGLG-DRLDHRPSQlSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446716125 156 LLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILsEIEQLVDKVGIIHNGVLLEEI 218
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVSDE 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-230 |
5.20e-31 |
|
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: 121.80 E-value: 5.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMV--ETPGFYSnl 95
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVpqRPHLFDT-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENLTI---NAKilgiqkENAIEEVLEIVGLASEKVKLFKNY-----------SLGMKQRLGIARALLHNPELLILDE 161
Cdd:COG4987 424 TLRENLRLarpDAT------DEELWAALERVGLGDWLAALPDGLdtwlgeggrrlSGGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKNRQF 230
Cdd:COG4987 498 PTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-217 |
6.68e-31 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 117.85 E-value: 6.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKP---TKGNIKIFEKEFESNKTEILKNI-G---AMVetpgFYSN 94
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIrGreiQMI----FQDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTA-----------KENLTINAKILGIQKENAIEEVLEIVGLASEKvKLFKNY----SLGMKQRLGIARALLHNPELLIL 159
Cdd:COG0444 96 MTSlnpvmtvgdqiAEPLRIHGGLSKAEARERAIELLERVGLPDPE-RRLDRYphelSGGMRQRVMIARALALEPKLLIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 160 DEPTNGLDPIgI-KEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:COG0444 175 DEPTTALDVT-IqAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-215 |
6.77e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.64 E-value: 6.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFesNKTEILK-NIgAMVetpgF- 91
Cdd:COG3839 10 SKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPPKDrNI-AMV----Fq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 ----YSNLTAKENLTINAKILGIQK---ENAIEEVLEIVGLAsekvKLFKNY----SLGMKQRLGIARALLHNPELLILD 160
Cdd:COG3839 83 syalYPHMTVYENIAFPLKLRKVPKaeiDRRVREAAELLGLE----DLLDRKpkqlSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 161 EPTNGLDPigiK---EIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL 215
Cdd:COG3839 159 EPLSNLDA---KlrvEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
14-221 |
8.22e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.66 E-value: 8.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES---NKteilKNIGaMVetpg 90
Cdd:COG3842 12 SKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppEK----RNVG-MV---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 F--YS---NLTAKENLTINAKILGIQKENA---IEEVLEIVGLAS-EKVK---LfknySLGMKQRLGIARALLHNPELLI 158
Cdd:COG3842 83 FqdYAlfpHLTVAENVAFGLRMRGVPKAEIrarVAELLELVGLEGlADRYphqL----SGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 159 LDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL-----EEImYE 221
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEqvgtpEEI-YE 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-212 |
1.97e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.75 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKE--FESNKTEILKNIGaMV----- 86
Cdd:COG3845 12 TKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrIRSPRDAIALGIG-MVhqhfm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 87 --EtpgfysNLTAKENLTI---NAKILGIQKENAIEEVLEI---VGLA---SEKVklfKNYSLGMKQRLGIARALLHNPE 155
Cdd:COG3845 91 lvP------NLTVAENIVLglePTKGGRLDRKAARARIRELserYGLDvdpDAKV---EDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 156 LLILDEPTNGLDPIGIKEIRKLIKDLAqSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLA-AEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-214 |
2.62e-30 |
|
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: 120.89 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLTAKENL 101
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLI 178
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAqleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|....*.
gi 446716125 179 KDLAQSRniTILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:TIGR01257 1105 LKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-194 |
2.75e-30 |
|
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: 114.59 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQ-IAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIL----KNIGAMVET 88
Cdd:cd03256 7 SKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlrRQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 PGFYSNLTAKENltINAKILG--------------IQKENAIEeVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNP 154
Cdd:cd03256 87 FNLIERLSVLEN--VLSGRLGrrstwrslfglfpkEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446716125 155 ELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSH 194
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLH 203
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-215 |
9.19e-30 |
|
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: 112.39 E-value: 9.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 32 SGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKE-FESNKTEIL----KNIGAMVETPGFYSNLTAKENLTINAK 106
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlFDSRKKINLppqqRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 107 ILG-IQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSR 185
Cdd:cd03297 102 RKRnREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNL 181
|
170 180 190
....*....|....*....|....*....|
gi 446716125 186 NITILISSHILSEIEQLVDKVGIIHNGVLL 215
Cdd:cd03297 182 NIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-214 |
1.10e-29 |
|
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: 111.96 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEK---EFESNKTEIlknigAMV-ETP 89
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtDLPPKDRDI-----AMVfQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 GFYSNLTAKENLTINAKILGIQKEN---AIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKLRKVPKDEideRVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446716125 167 DPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:cd03301 162 DAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-222 |
1.22e-29 |
|
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: 112.77 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIG-AMV-ETPGFYSN 94
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGiGYVpEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTINAKILGIQKENA--IEEVLEivglasekvkLF-------KNY----SLGMKQRLGIARALLHNPELLILDE 161
Cdd:COG0410 93 LTVEENLLLGAYARRDRAEVRadLERVYE----------LFprlkerrRQRagtlSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQsRNITILIsshilseIEQLVDKV-GIIHNGVLLE--EIMYED 222
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNR-EGVTILL-------VEQNARFAlEIADRAYVLErgRIVLEG 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-224 |
1.77e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.48 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKefesnkteilknIGAMVE-TPGFYSNLTAKEN 100
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------------VSALLElGAGFHPELTGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 101 LTINAKILGIQKEnAIEEVL-EIVGLA------SEKVklfKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:COG1134 109 IYLNGRLLGLSRK-EIDEKFdEIVEFAelgdfiDQPV---KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 174 IRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVLleeIMYEDLK 224
Cdd:COG1134 185 CLARIRELRE-SGRTVIFVSHSMGAVRRLCDRAIWLEKGRL---VMDGDPE 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-217 |
2.59e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 112.52 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQY--GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF--ESNKTEILKNIGaMV--- 86
Cdd:TIGR04520 7 SFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldEENLWEIRKKVG-MVfqn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 87 -----------ETPGFysnltAKENLTINAKIlgIQKEnaIEEVLEIVGLASekvklFKNY-----SLGMKQRLGIARAL 150
Cdd:TIGR04520 86 pdnqfvgatveDDVAF-----GLENLGVPREE--MRKR--VDEALKLVGMED-----FRDRephllSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 151 LHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQlVDKVGIIHNGVLLEE 217
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAE 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-217 |
9.00e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 112.97 E-value: 9.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQI-AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIL----KNIGaMVetp 89
Cdd:PRK11153 12 PQGGRTIhALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkarRQIG-MI--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 gF-YSNL----TAKENLTINAKILGIQKEN---AIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDE 161
Cdd:PRK11153 88 -FqHFNLlssrTVFDNVALPLELAGTPKAEikaRVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQ 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-212 |
9.42e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.68 E-value: 9.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNK---TEILKNIGAMVETPGF-YSNLTA 97
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFQYPEYqLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 KENLTINAKILGIQKE---NAIEEVLEIVGLASEKVKLFKNYSL--GMKQRLGIARALLHNPELLILDEPTNGLDPIGIK 172
Cdd:PRK13637 102 EKDIAFGPINLGLSEEeieNRVKRAMNIVGLDYEDYKDKSPFELsgGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446716125 173 EIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-219 |
1.10e-28 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 112.90 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 26 LSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIF-EKEFESNKTEIL----KNIGAMVETPGFYSNLTAKEN 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgRTLFDSRKGIFLppekRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 101 LTINAK-ILGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIK 179
Cdd:TIGR02142 96 LRYGMKrARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446716125 180 DLAQSRNITILISSHILSEIEQLVDKVGIIHNGVL-----LEEIM 219
Cdd:TIGR02142 176 RLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVaaagpIAEVW 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-215 |
1.61e-28 |
|
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: 109.28 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLI---KPTKGNIKIFEKEfeSNKTEILKNIGAMVETPG 90
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQP--RKPDQFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENLTINAKILG--IQKENAIEEVLEIVGL---ASEKV--KLFKNYSLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:cd03234 92 LLPGLTVRETLTYTAILRLprKSSDAIRKKRVEDVLLrdlALTRIggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446716125 164 NGLDPIGIKEIRKLIKDLAQsRNITILISSHI-LSEIEQLVDKVGIIHNGVLL 215
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLAR-RNRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-212 |
3.21e-28 |
|
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: 108.86 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES---NKteilKNIGAMVETPG 90
Cdd:cd03300 7 SKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHK----RPVNTVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENLTINAKILGIQK---ENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:cd03300 83 LFPHLTVFENIAFGLRLKKLPKaeiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446716125 168 PIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:cd03300 163 LKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-194 |
4.91e-28 |
|
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: 107.88 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQI-AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKE---FESNKTEILK-NIGAMVET 88
Cdd:cd03292 7 TKTYPNGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRrKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 PGFYSNLTAKENLTINAKILG-----IQKEnaIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:cd03292 87 FRLLPDRNVYENVAFALEVTGvppreIRKR--VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190
....*....|....*....|....*....|.
gi 446716125 164 NGLDPIGIKEIRKLIKDLAQsRNITILISSH 194
Cdd:cd03292 165 GNLDPDTTWEIMNLLKKINK-AGTTVVVATH 194
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
15-226 |
1.15e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.67 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFE--SNKTEILKNIGAMVETPGFY 92
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 93 SNLTAKEN----LTINAKILGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDP 168
Cdd:PRK10895 91 RRLSVYDNlmavLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446716125 169 IGIKEIRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNGVLL-----EEIMYEDLKKK 226
Cdd:PRK10895 171 ISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIahgtpTEILQDEHVKR 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-217 |
2.38e-27 |
|
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: 106.08 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkifekefesnktEILKNIGAMVE-TPGFYSNLTAKEN 100
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------------TVRGRVSSLLGlGGGFNPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 101 LTINAKILGIQKENAIEEVLEIVGLaSEKVKLF----KNYSLGMKQRLGIARALLHNPELLILDEPTNGLDP-IGIKEIR 175
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKIDEIIEF-SELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAaFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446716125 176 KLIKDLAQSRniTILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:cd03220 184 RLRELLKQGK--TVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-212 |
3.15e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.49 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIG-AMV--EtPG 90
Cdd:COG1129 11 SKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGiAIIhqE-LN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENLTI-----NAKILGIQKENAI-EEVLEIVGL---ASEKVKlfkNYSLGMKQRLGIARALLHNPELLILDE 161
Cdd:COG1129 90 LVPNLSVAENIFLgreprRGGLIDWRAMRRRaRELLARLGLdidPDTPVG---DLSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446716125 162 PTNGLDPigiKEIRKL---IKDLaQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:COG1129 167 PTASLTE---REVERLfriIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDG 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-227 |
5.23e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.64 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGaMV--ETPGFysN 94
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIG-VVpqDTFLF--S 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTinakiLGiqKENA----IEEVLEIVGlASEKVKLFKN-Y-----------SLGMKQRLGIARALLHNPELLI 158
Cdd:COG1132 428 GTIRENIR-----YG--RPDAtdeeVEEAAKAAQ-AHEFIEALPDgYdtvvgergvnlSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 159 LDEPTNGLDPIGIKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKN 227
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLARG 565
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-217 |
9.73e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.93 E-value: 9.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIL---KNIGAMVETPG---FYSnl 95
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevrKTVGIVFQNPDdqlFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENLTINAKILGIQK---ENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIK 172
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKeevEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446716125 173 EIRKLIKDLaQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:PRK13639 175 QIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
14-222 |
1.52e-26 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 104.69 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQI-AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF----ESNKTEILKNIGAMVET 88
Cdd:TIGR02315 8 SKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrGKKLRKLRRRIGMIFQH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 PGFYSNLTAKENLTINA--------KILGI----QKENAIEeVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPEL 156
Cdd:TIGR02315 88 YNLIERLTVLENVLHGRlgykptwrSLLGRfseeDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 157 LILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGvlleEIMYED 222
Cdd:TIGR02315 167 ILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAG----EIVFDG 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-212 |
3.62e-26 |
|
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: 103.57 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:cd03296 9 SKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFGGEDATDVPVQERNVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGI-------QKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:cd03296 88 HMTVFDNVAFGLRVKPRserppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446716125 167 DPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
15-217 |
4.58e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-------ESNKTEILKNIGAMVE 87
Cdd:COG4161 10 CFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQKVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 88 TPGFYSNLTAKENLtINA--KILGIQKENAIEEVLEIvgLA----SEKVKLFKNY-SLGMKQRLGIARALLHNPELLILD 160
Cdd:COG4161 90 QYNLWPHLTVMENL-IEApcKVLGLSKEQAREKAMKL--LArlrlTDKADRFPLHlSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 161 EPTNGLDPIGIKEIRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
22-194 |
5.84e-26 |
|
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: 101.73 E-value: 5.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNK---TEILKNIGAMVETPG---FYSnl 95
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkglLERRQRVGLVFQDPDdqlFAA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIK 172
Cdd:TIGR01166 85 DVDQDVAFGPLNLGLSEAEVerrVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|..
gi 446716125 173 EIRKLIKDLAQSRNiTILISSH 194
Cdd:TIGR01166 165 QMLAILRRLRAEGM-TVVISTH 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-202 |
6.36e-26 |
|
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: 101.67 E-value: 6.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLTA 97
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 KENLTINAKILGiQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKL 177
Cdd:TIGR01189 91 LENLHFWAAIHG-GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170 180
....*....|....*....|....*...
gi 446716125 178 IKDLAQSRNITILiSSHI---LSEIEQL 202
Cdd:TIGR01189 170 LRAHLARGGIVLL-TTHQdlgLVEAREL 196
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-217 |
9.99e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 102.50 E-value: 9.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKifekeFESnkTEILK---------NIGAMVETPGFY 92
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVL-----FGG--TDLTGldeheiarlGIGRKFQKPTVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 93 SNLTAKENL------------TINAKILGIQKENaIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILD 160
Cdd:COG4674 98 EELTVFENLelalkgdrgvfaSLFARLTAEERDR-IEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 161 EPTNGLDPIGIKEIRKLIKDLAQSRniTILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:COG4674 177 EPVAGMTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSVLAE 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
14-219 |
1.03e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.80 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIfEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:PRK11432 13 TKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-DGEDVTHRSIQQRDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKE---NAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:PRK11432 92 HMSLGENVGYGLKMLGVPKEerkQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446716125 171 IKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGvlleEIM 219
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKG----KIM 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-226 |
1.25e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.00 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIL---KNIGAMVETPG--FYSnLT 96
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMklrESVGMVFQDPDnqLFS-AS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVrkrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446716125 174 IRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG-VLLEEIMYEDLKKK 226
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGrVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-234 |
1.28e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.76 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 19 SQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAMVETP-GFYSNLT 96
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKeNLKEIRKKIGIIFQNPdNQFIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTI---NAKILGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:PRK13632 101 VEDDIAFgleNKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 174 IRKLIKDLAQSRNITILISSHILSEIeQLVDKVGIIHNGVLL-----EEIMyedlkkKNRQFISIS 234
Cdd:PRK13632 181 IKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIaqgkpKEIL------NNKEILEKA 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
14-212 |
1.32e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.45 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGnikifekefesnktEILKNIGAMVEtpgfys 93
Cdd:PRK11247 19 SKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--------------ELLAGTAPLAE------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 nltAKENLTI---NAKIL--------------GIQKENAiEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPEL 156
Cdd:PRK11247 79 ---AREDTRLmfqDARLLpwkkvidnvglglkGQWRDAA-LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 157 LILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-195 |
1.46e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.10 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFE-SNKTEILKNIG---AMvetpgfYSNLTAKEN 100
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLGhrnAM------KPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 101 LTINAKILGiQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKD 180
Cdd:PRK13539 94 LEFWAAFLG-GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
170
....*....|....*.
gi 446716125 181 -LAQsrNITILISSHI 195
Cdd:PRK13539 173 hLAQ--GGIVIAATHI 186
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-212 |
1.83e-25 |
|
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: 101.13 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-ESNKTEILKNIGAMVETPG-FYSNLtaKE 99
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrQLDPADLRRNIGYVPQDVTlFYGTL--RD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 100 NLTINAkilGIQKENAIEEVLEIVGLASEKVKLFKNYSL-----------GMKQRLGIARALLHNPELLILDEPTNGLDp 168
Cdd:cd03245 97 NITLGA---PLADDERILRAAELAGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDEPTSAMD- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446716125 169 igIKEIRKLIKDLAQS-RNITILISSHILSeIEQLVDKVGIIHNG 212
Cdd:cd03245 173 --MNSEERLKERLRQLlGDKTLIIITHRPS-LLDLVDRIIVMDSG 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-251 |
2.34e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.41 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGS---QIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTE-----ILKNIGAM 85
Cdd:PRK13634 11 RYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkpLRKKVGIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 86 VETPgfYSNL---TAKENLTINAKILGIQKENAIE---EVLEIVGLaSEKVKLFKNYSL--GMKQRLGIARALLHNPELL 157
Cdd:PRK13634 91 FQFP--EHQLfeeTVEKDICFGPMNFGVSEEDAKQkarEMIELVGL-PEELLARSPFELsgGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 158 ILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL-----EEIMY--EDLKKknrqf 230
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFlqgtpREIFAdpDELEA----- 242
|
250 260
....*....|....*....|.
gi 446716125 231 ISISVSDEEKVACLLETNFGI 251
Cdd:PRK13634 243 IGLDLPETVKFKRALEEKFGI 263
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-214 |
5.59e-25 |
|
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: 105.48 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYG--SQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGF 91
Cdd:TIGR01257 1944 TKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSNLTAKENLTINAKILGIQKENaIEEV----LEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:TIGR01257 2024 DDLLTGREHLYLYARLRGVPAEE-IEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446716125 168 PIGIKEIRKLIKDLAQSRNITILiSSHILSEIEQLVDKVGIIHNGVL 214
Cdd:TIGR01257 2103 PQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCTRLAIMVKGAF 2148
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-216 |
6.42e-25 |
|
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: 100.10 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkIFEKEFESNKTEILKNIGAMVETPGFYSNLTAKENLTIN 104
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-LLNGKDITNLPPEKRDISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 105 AKILGIQKENAIEEVLEIVGLASEKVKLFKN---YSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDL 181
Cdd:cd03299 96 LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKpetLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKI 175
|
170 180 190
....*....|....*....|....*....|....*
gi 446716125 182 AQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:cd03299 176 RKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-206 |
6.78e-25 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 104.29 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-ESNKTEILKNIGAMVETPGFYSNlT 96
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLaDADADSWRDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINAKIlgiQKENAIEEVLEIVGLASEKVKLFKNY-----------SLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:TIGR02857 412 IAENIRLARPD---ASDAEIREALERAGLDEFVAALPQGLdtpigeggaglSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446716125 166 LDPIGIKEIRKLIKDLAQSRniTILISSHILSEIEqLVDKV 206
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQGR--TVLLVTHRLALAA-LADRI 526
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-216 |
2.18e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.93 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFE-SNKT------EILKNIGAMVETP 89
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfSKTPsdkairELRRNVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 GFYSNLTAKENLtINA--KILGIQKENAIEEVLEIvgLA----SEKVKLFK-NYSLGMKQRLGIARALLHNPELLILDEP 162
Cdd:PRK11124 92 NLWPHLTVQQNL-IEApcRVLGLSKDQALARAEKL--LErlrlKPYADRFPlHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446716125 163 TNGLDPIGIKEIRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-217 |
2.19e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.70 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 19 SQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-ESNKTEILKNIGAMVETP-GFYSNLT 96
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLsEETVWDVRRQVGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINAKILGIQKENAIEEV---LEIVGLAS----EKVKLfknySLGMKQRLGIARALLHNPELLILDEPTNGLDPI 169
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVdqaLRQVGMEDflnrEPHRL----SGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446716125 170 GIKEIRKLIKDLAQSRNITILISSHILSEIEQlVDKVGIIHNGVLLEE 217
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-206 |
4.67e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.80 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKN---IGamvETPGFYSNLTAKENL 101
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllyLG---HQPGIKTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAKILGIQKENAIEEVLEIVGLAS-EKVkLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKD 180
Cdd:PRK13538 96 RFYQRLHGPGDDEALWEALAQVGLAGfEDV-PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
170 180
....*....|....*....|....*.
gi 446716125 181 LAQSRNITILISSHILSEIEQLVDKV 206
Cdd:PRK13538 175 HAEQGGMVILTTHQDLPVASDKVRKL 200
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-227 |
8.55e-24 |
|
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: 96.91 E-value: 8.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 21 IAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAMVETPGFYSNlTAKE 99
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 100 NLTINAKIlgiQKENAIEEVLEIVGLASEKVKLFKNY-----------SLGMKQRLGIARALLHNPELLILDEPTNGLDP 168
Cdd:cd03254 96 NIRLGRPN---ATDEEVIEAAKEAGAHDFIMKLPNGYdtvlgenggnlSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 169 IGIKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKN 227
Cdd:cd03254 173 ETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-232 |
1.27e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.13 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKT---------EILKNIGA 84
Cdd:PRK11264 10 VKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkglirQLRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 85 MVETPGFYSNLTAKENLTINAKIL-GIQKENAIE---EVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILD 160
Cdd:PRK11264 90 VFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATArarELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 161 EPTNGLDPIGIKEIRKLIKDLAQSRNiTILISSHILSEIEQLVDKVGIIHNGVLLE-----EIMYEDLKKKNRQFIS 232
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEqgpakALFADPQQPRTRQFLE 245
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-212 |
1.39e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIF-EKEFESNKTEILKNIGAMVETPG--FYSN 94
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRgEPITKENIREVRKFVGLVFQNPDdqIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 lTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGI 171
Cdd:PRK13652 95 -TVEQDIAFGPINLGLDEETVahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446716125 172 KEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKG 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-217 |
2.08e-23 |
|
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: 94.30 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 19 SQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNlTAK 98
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 99 ENLtinakilGIQkenaieevleivglasekvklfknYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLI 178
Cdd:cd03247 93 NNL-------GRR------------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 446716125 179 kdLAQSRNITILISSHILSEIEQlVDKVGIIHNGVLLEE 217
Cdd:cd03247 142 --FEVLKDKTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
22-216 |
2.59e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 96.44 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTE--------ILK----------NIG 83
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKyrckhirmIFQdpntslnprlNIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 84 AMVETPgfysnltakenLTINAKILGIQKENAIEEVLEIVGLASEKVKLFKN-YSLGMKQRLGIARALLHNPELLILDEP 162
Cdd:COG4167 108 QILEEP-----------LRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHmLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446716125 163 TNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:COG4167 177 LAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-270 |
4.84e-23 |
|
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: 98.72 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGL--IKPTKGNI--------------------------- 64
Cdd:TIGR03269 7 TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 65 ---KIFEKEF----ESNKTEILKNIGAMVE-TPGFYSNLTAKENLTINAKILGIQKENAIE---EVLEIVGLASEKVKLF 133
Cdd:TIGR03269 87 gtlEPEEVDFwnlsDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGravDLIEMVQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 134 KNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGV 213
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGE 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 214 LLEEIMYEDLKKKNRQfisiSVSDEEKvacllETNFGIYDYKIKENGEFKIYSHIDR 270
Cdd:TIGR03269 247 IKEEGTPDEVVAVFME----GVSEVEK-----ECEVEVGEPIIKVRNVSKRYISVDR 294
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-217 |
6.79e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.54 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 19 SQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKI--FEKEFESNKTEILKNIGAMVETPGfySNLT 96
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgLDTSDEENLWDIRNKAGMVFQNPD--NQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 A---KENLTINAKILGIQKEnaieEVLEIVGLASEKVKLF--KNY-----SLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:PRK13633 100 AtivEEDVAFGPENLGIPPE----EIRERVDESLKKVGMYeyRRHaphllSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 167 DPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQlVDKVGIIHNGVLLEE 217
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-212 |
9.39e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.67 E-value: 9.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGaMVETpgF----- 91
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG-VVRT--Fqhvrl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSNLTAKENLTI------NAKIL-GIQK--------ENAIEEV---LEIVGLASEKVKLFKNYSLGMKQRLGIARALLHN 153
Cdd:PRK11300 92 FREMTVIENLLVaqhqqlKTGLFsGLLKtpafrraeSEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 154 PELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-215 |
1.32e-22 |
|
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: 92.61 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKP--TKGNIKIfeKEFESNKTEILKNIGAMVETPGFYSNLTAKEN 100
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLI--NGRPLDKRSFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 101 LTINAKILGIqkenaieevleivglasekvklfknySLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKD 180
Cdd:cd03213 103 LMFAAKLRGL--------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 446716125 181 LAQSrNITILISSHILS-EIEQLVDKVGIIHNGVLL 215
Cdd:cd03213 157 LADT-GRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-194 |
2.75e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIF----------EKEFESNKT------- 76
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkglrigylpqEPPLDDDLTvldtvld 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 77 ------EILKNIGAMVETPGFYSNLTAK--ENLTINAKILGIQKENAIEEVLEIVGLASEKV-KLFKNYSLGMKQRLGIA 147
Cdd:COG0488 85 gdaelrALEAELEELEAKLAEPDEDLERlaELQEEFEALGGWEAEARAEEILSGLGFPEEDLdRPVSELSGGWRRRVALA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446716125 148 RALLHNPELLILDEPTNGLDpigIKEIRKLIKDLAQSRNiTILISSH 194
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHLD---LESIEWLEEFLKNYPG-TVLVVSH 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
22-217 |
3.06e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.65 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-ESNKTEILKNIGAMVETPG---FYSnlTA 97
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGLVFQDPDdqvFSS--TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 KENLTINAKILGIQK---ENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEI 174
Cdd:PRK13647 98 WDDVAFGPVNMGLDKdevERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446716125 175 RKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:PRK13647 178 MEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-216 |
4.68e-22 |
|
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: 96.02 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKI--------FEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdMTKPGPDGRGRAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTiNAKILGIQKENAIEE---VLEIVGLASEKV-----KLFKNYSLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:TIGR03269 379 HRTVLDNLT-EAIGLELPDELARMKaviTLKMVGFDEEKAeeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 166 LDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-216 |
5.40e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 92.79 E-value: 5.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRML---LGLIkP---TKGNIKIFEKEFESNK---TEILKNIGaMV- 86
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLI-PgarVEGEILLDGEDIYDPDvdvVELRRRVG-MVf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 87 ETPgfysNLTAK---ENLTINAKILGIQK----ENAIEEVLEIVGLASE-KVKLFKN-YSL--GMKQRLGIARALLHNPE 155
Cdd:COG1117 99 QKP----NPFPKsiyDNVAYGLRLHGIKSkselDEIVEESLRKAALWDEvKDRLKKSaLGLsgGQQQRLCIARALAVEPE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446716125 156 LLILDEPTNGLDPIGIKEIRKLIKDLAQsrNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:COG1117 175 VLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVTHNMQQAARVSDYTAFFYLGELVE 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-212 |
5.89e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.13 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAvnNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIfekefesNKTEILK-NIG----AMVet 88
Cdd:COG3840 8 TYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW-------NGQDLTAlPPAerpvSML-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 pgFYSN-----LTAKENLTinakiLGI---------QKEnAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNP 154
Cdd:COG3840 77 --FQENnlfphLTVAQNIG-----LGLrpglkltaeQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 155 ELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-218 |
7.18e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 7.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNI---------------KIFEKE----FESNKTEI 78
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaklnraqrKAFRRDiqmvFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 79 --LKNIGAMVETPgfysnltAKENLTINAKilgiQKENAIEEVLEIVGLASEKV-KLFKNYSLGMKQRLGIARALLHNPE 155
Cdd:PRK10419 103 npRKTVREIIREP-------LRHLLSLDKA----ERLARASEMLRAVDLDDSVLdKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446716125 156 LLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEI 218
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-212 |
7.27e-22 |
|
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: 90.57 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIG-AMVetP------GFYSN 94
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGiAYV--PedrkreGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTINAkILgiqkenaieevleivglasekvklfknySLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEI 174
Cdd:cd03215 93 LSVAENIALSS-LL----------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 446716125 175 RKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:cd03215 144 YRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-220 |
1.02e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 93.26 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIK-----------------------IFEKEFES-N--K 75
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqditglsgrelrplrrrmqmVFQDPYASlNprM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 76 TeilknIGAMVETPgfysnltakenLTINAKILGIQKENAIEEVLEIVGLASEkvklFKN-----YSLGMKQRLGIARAL 150
Cdd:COG4608 113 T-----VGDIIAEP-----------LRIHGLASKAERRERVAELLELVGLRPE----HADrypheFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 151 LHNPELLILDEPTNGLDpigiKEIRK----LIKDLAQSRNITILISSHILSEIEQLVDKVGiihngvlleeIMY 220
Cdd:COG4608 173 ALNPKLIVCDEPVSALD----VSIQAqvlnLLEDLQDELGLTYLFISHDLSVVRHISDRVA----------VMY 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-206 |
1.16e-21 |
|
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: 90.63 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 26 LSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLTAKENLTINA 105
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 106 KILGiqkENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSR 185
Cdd:cd03231 99 ADHS---DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARG 175
|
170 180
....*....|....*....|.
gi 446716125 186 NITILISSHILSEIEQLVDKV 206
Cdd:cd03231 176 GMVVLTTHQDLGLSEAGAREL 196
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-212 |
1.20e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 90.99 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkifekefesnkteILKniGAMVETPG-----FYSN--- 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV-------------ILE--GKQITEPGpdrmvVFQNysl 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 ---LTAKENLT-----INAKILGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:TIGR01184 66 lpwLTVRENIAlavdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446716125 167 DPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-216 |
1.22e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.94 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKI----FEKEFESNKTEILKNIGAMV-ETPGFY 92
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIdgvdIAKISDAELREVRRKKIAMVfQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 93 SNLTAKENLTINAKILGIQKENAIEEVLEI---VGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPI 169
Cdd:PRK10070 119 PHMTVLDNTAFGMELAGINAEERREKALDAlrqVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446716125 170 GIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-194 |
2.30e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.02 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 24 NNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIK--PTKGNIKIFEKEFESNKTeILKNIGAmvetpgfysnltakeNL 101
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREAS-LIDAIGR---------------KG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAKIlgiqkenaieEVLEIVGLASEK--VKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIK 179
Cdd:COG2401 111 DFKDAV----------ELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQ 180
|
170
....*....|....*
gi 446716125 180 DLAQSRNITILISSH 194
Cdd:COG2401 181 KLARRAGITLVVATH 195
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-223 |
2.35e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.12 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTtirmLLGLI----KPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLtrawDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGiqkENAIEEVLEIVGLAsekvKLFKNY--------------SLGMKQRLGIARALLHNPELLIL 159
Cdd:PRK11160 427 SATLRDNLLLAAPNAS---DEALIEVLQQVGLE----KLLEDDkglnawlgeggrqlSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 160 DEPTNGLDPIGIKEIRKLIKDLAQSRniTILISSHILSEIEQLvDKVGIIHNGVLLEEIMYEDL 223
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-216 |
2.85e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.67 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIK-----PTKGNIKIFEKEFES---NKTEILKNIGAMVET 88
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSpdvDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 PGFYSNLTAKENLTINAKILGIQKENaiEEVLEIVGLASEKVKLFK-----------NYSLGMKQRLGIARALLHNPELL 157
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLVKSK--KELDERVEWALKKAALWDevkdrlndypsNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 158 ILDEPTNGLDPIGIKEIRKLIKDLaqSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-212 |
2.94e-21 |
|
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: 89.47 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 26 LSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEiLKNIGAMVETPGFYSNLTAKEN--LTI 103
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-DRPVSMLFQENNLFAHLTVEQNvgLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 104 NAKI-LGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLA 182
Cdd:cd03298 96 SPGLkLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|
gi 446716125 183 QSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-218 |
3.68e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.13 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:COG1118 9 SKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVFQHYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKENA---IEEVLEIVGLASekvkLFKNY----SLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:COG1118 89 HMTVAENIAFGLRVRPPSKAEIrarVEELLELVQLEG----LADRYpsqlSGGQRQRVALARALAVEPEVLLLDEPFGAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446716125 167 DPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVlLEEI 218
Cdd:COG1118 165 DAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR-IEQV 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-227 |
3.91e-21 |
|
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: 89.91 E-value: 3.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 20 QIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAMVETPGFYSNlTAK 98
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 99 ENLTinakiLGiqKENAI-EEVLEIVGLASEK---VKLFKNY-----------SLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:cd03249 95 ENIR-----YG--KPDATdEEVEEAAKKANIHdfiMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 164 NGLDPIGIKEIRKLIKDLAQSRniTILISSHILSEIeQLVDKVGIIHNGVLLEEIMYEDLKKKN 227
Cdd:cd03249 168 SALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTI-RNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-221 |
4.40e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.21 E-value: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:PRK11607 26 TKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGVDLSHVPPYQRPINMMFQSYALFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQK---ENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDpig 170
Cdd:PRK11607 105 HMTVEQNIAFGLKQDKLPKaeiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD--- 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 171 iKEIRKLIK----DLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL-----EEImYE 221
Cdd:PRK11607 182 -KKLRDRMQlevvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVqigepEEI-YE 239
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-214 |
6.32e-21 |
|
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: 87.66 E-value: 6.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIfekefesnkteilknIGAMVETpgfysnltakenlt 102
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL---------------DGADISQ-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 103 INAKILGiqkenaieevlEIVGLASEKVKLFKN------YSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRK 176
Cdd:cd03246 69 WDPNELG-----------DHVGYLPQDDELFSGsiaeniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 446716125 177 LIKDLaQSRNITILISSHILSEIEQlVDKVGIIHNGVL 214
Cdd:cd03246 138 AIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-212 |
9.11e-21 |
|
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: 86.35 E-value: 9.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKefesnkteilknigamvETPGFYS 93
Cdd:cd03221 7 SKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------------VKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLtakenltinakilgiqkenaieevleivglasekvklfknySLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:cd03221 70 QL-----------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190
....*....|....*....|....*....|....*....
gi 446716125 174 IRKLIKDLaqsrNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:cd03221 109 LEEALKEY----PGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-216 |
9.14e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.34 E-value: 9.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKI------FEKE-FESNKTEILKNIGAMVETPGFYSNL 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyFGKDiFQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENLTINAKILGIQKENAI----EEVLEIVGLASEKVKLFKN----YSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIkkivEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446716125 168 PIGIKEIRKLIKDLaqSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:PRK14246 186 IVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-212 |
1.32e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.41 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-ESNKTEILKNIGAMVETP-GFYSNLTAKEN 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLtEENVWDIRHKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 101 LTINAKILGIQKENAIEEV---LEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKL 177
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVneaLELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190
....*....|....*....|....*....|....*
gi 446716125 178 IKDLAQSRNITILISSHILSEIeQLVDKVGIIHNG 212
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNG 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-217 |
1.41e-20 |
|
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: 91.67 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIkPTKGNIKIFEKEFESNKTEILK--------------------- 80
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRplrrrmqvvfqdpfgslsprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 81 NIGAMVEtpgfysnltakENLTINAKIL-GIQKENAIEEVLEIVGLASEkvkLFKNY----SLGMKQRLGIARALLHNPE 155
Cdd:COG4172 380 TVGQIIA-----------EGLRVHGPGLsAAERRARVAEALEEVGLDPA---ARHRYphefSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446716125 156 LLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQ 507
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-227 |
1.64e-20 |
|
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: 88.06 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLTAKENL 101
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAkiLGIQKEnAIEEVLEIVGLASEKVKLFKNY-----------SLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:cd03251 97 AYGR--PGATRE-EVEEAARAANAHEFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 171 IKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKN 227
Cdd:cd03251 174 ERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-217 |
1.72e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIkPTKGNIKIFEKEFES-NKTEIL---KNIGAMVETPgfYS 93
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNlNRRQLLpvrHRIQVVFQDP--NS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAK--------ENLTINAKIL-GIQKENAIEEVLEIVGLASEKVKLF-KNYSLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:PRK15134 374 SLNPRlnvlqiieEGLRVHQPTLsAAQREQQVIAVMEEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446716125 164 NGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQ 507
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-215 |
1.78e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.03 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES---NK--TEILKNIGAMVETPgfYSNL- 95
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStskNKdiKQIRKKVGLVFQFP--ESQLf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 --TAKENLTINAKILGIQKENA---IEEVLEIVGLASEkvkLF-KN---YSLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:PRK13649 100 eeTVLKDVAFGPQNFGVSQEEAealAREKLALVGISES---LFeKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446716125 167 DPIGIKEIRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNGVLL 215
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
15-217 |
2.79e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKE-------------FESNKTEILKN 81
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 82 IGAMV-ETPGFYSNLTAKEN-LTINAKILGIQKENAIEEV---LEIVGL-ASEKVKLFKNYSLGMKQRLGIARALLHNPE 155
Cdd:PRK10619 93 RLTMVfQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAvkyLAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446716125 156 LLILDEPTNGLDPIGIKEIRKLIKDLAQSRNiTILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-227 |
2.81e-20 |
|
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: 87.67 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 24 NNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIL-KNIGaMV--ETPGF--------- 91
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLrRAIG-VVpqDTVLFndtigynir 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSNLTAKENLTINAKilgiqKENAIEEVLE--------IVGlasEK-VKLfknySLGMKQRLGIARALLHNPELLILDEP 162
Cdd:cd03253 97 YGRPDATDEEVIEAA-----KAAQIHDKIMrfpdgydtIVG---ERgLKL----SGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446716125 163 TNGLDPIGIKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKN 227
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
16-217 |
5.08e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.86 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKT-EILKNIGAMV-ETPGFYS 93
Cdd:PRK11614 14 HYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVpEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQK-ENAIEEVLEIVG-LASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGI 171
Cdd:PRK11614 94 RMTVEENLAMGGFFAERDQfQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446716125 172 KEIRKLIKDLaQSRNITILISSHILSEIEQLVDKVGIIHNG-VLLEE 217
Cdd:PRK11614 174 QQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGhVVLED 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-216 |
9.65e-20 |
|
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: 85.62 E-value: 9.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIL-KNIGAMVETPGFYSNlT 96
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLrSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLtinaKILGIQKENAIEEVLEIVGLASEKVKLFK-----------NYSLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:cd03244 94 IRSNL----DPFGEYSDEELWQALERVGLKEFVESLPGgldtvveeggeNLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 166 LDPIGIKEIRKLIKDlaQSRNITILISSHILSEIEQlVDKVGIIHNGVLLE 216
Cdd:cd03244 170 VDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
14-219 |
1.15e-19 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 87.85 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGS-QIAVNnlsITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEI-----LKNIGAMVE 87
Cdd:COG4148 8 RLRRGGfTLDVD---FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflpphRRRIGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 88 TPGFYSNLTAKENLTINAKILGIQKENA-IEEVLEIVGLASekvkLFKNY----SLGMKQRLGIARALLHNPELLILDEP 162
Cdd:COG4148 85 EARLFPHLSVRGNLLYGRKRAPRAERRIsFDEVVELLGIGH----LLDRRpatlSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446716125 163 TNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG-VL----LEEIM 219
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGrVVasgpLAEVL 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-212 |
1.20e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFE--SNKTEILKNIGAMVETPGF 91
Cdd:PRK09700 12 GKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGIIYQELSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSNLTAKENLTIN----AKILGIQ-------KENAiEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILD 160
Cdd:PRK09700 92 IDELTVLENLYIGrhltKKVCGVNiidwremRVRA-AMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446716125 161 EPTNGLDPigiKEIRKLIKDLAQSRN--ITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK09700 171 EPTSSLTN---KEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-212 |
2.06e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.33 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTE-----ILKNIGAMVETPgfYSNL- 95
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQFP--ESQLf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 --TAKENLTINAKILGIQKENA---IEEVLEIVGLASE--KVKLFKnYSLGMKQRLGIARALLHNPELLILDEPTNGLDP 168
Cdd:PRK13643 99 eeTVLKDVAFGPQNFGIPKEKAekiAAEKLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446716125 169 IGIKEIRKLIKDLAQSRNITILIsSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLV-THLMDDVADYADYVYLLEKG 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-194 |
4.39e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.91 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGnikifekefesnktEILKNiGAMVETPG------F 91
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSG--------------EITLD-GVPVTGPGadrgvvF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSN-----LTAKENLTINAKILGI---QKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:COG4525 83 QKDallpwLNVLDNVAFGLRLRGVpkaERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170 180 190
....*....|....*....|....*....|.
gi 446716125 164 NGLDPIGIKEIRKLIKDLAQSRNITILISSH 194
Cdd:COG4525 163 GALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-216 |
4.87e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.84 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFE------------------SNKTEILKNIG 83
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysyrsqrirmifqdpSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 84 AMVETPgfysnltakenLTINAKILGIQKENAIEEVLEIVGLASEKVKLFKN-YSLGMKQRLGIARALLHNPELLILDEP 162
Cdd:PRK15112 108 QILDFP-----------LRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446716125 163 TNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
16-203 |
6.97e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.98 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIlkniGAMVETPGFYSNL 95
Cdd:PRK11248 10 DYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----GVVFQNEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENLTINAKILGI---QKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIK 172
Cdd:PRK11248 86 NVQDNVAFGLQLAGVekmQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190
....*....|....*....|....*....|.
gi 446716125 173 EIRKLIKDLAQSRNITILISSHilsEIEQLV 203
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITH---DIEEAV 193
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-210 |
7.82e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.32 E-value: 7.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTI----RM--LLGLIKpTKGNIKIFEK---EFESNKTEILKNIGAMVE 87
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnRMneLESEVR-VEGRVEFFNQniyERRVNLNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 88 TPGFYSnLTAKENLTINAKILGIQKENAIEEVLEIVGLASE-----KVKLFK---NYSLGMKQRLGIARALLHNPELLIL 159
Cdd:PRK14258 96 KPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADlwdeiKHKIHKsalDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 160 DEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIH 210
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
14-212 |
8.83e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.67 E-value: 8.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETpgfYS 93
Cdd:PRK13548 9 SVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQ---HS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NL----TAKENLTINAKILGI---QKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARAL--LHNPE----LLILD 160
Cdd:PRK13548 86 SLsfpfTVEEVVAMGRAPHGLsraEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqLWEPDgpprWLLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446716125 161 EPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQG 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
23-235 |
1.04e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.99 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKI-FEKEFESNKTEILKNIGAMVETP-GFYSNLTAKEN 100
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 101 LTINAKILGIQKENAI---EEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKL 177
Cdd:PRK13642 103 VAFGMENQGIPREEMIkrvDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 178 IKDLAQSRNITILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKNRQFISISV 235
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEIGL 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-229 |
1.11e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.06 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFeSNKTE------ILKNIGAMVETPgfYSNL 95
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITI-THKTKdkyirpVRKRIGMVFQFP--ESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 ---TAKENLTINAKILGIQKENAIEEVLEIV---GLASEKVKL--FKnYSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PRK13646 99 fedTVEREIIFGPKNFKMNLDEVKNYAHRLLmdlGFSRDVMSQspFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446716125 168 PIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKKNRQ 229
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-212 |
1.15e-18 |
|
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: 85.96 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAV-NNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAM---VET-PGf 91
Cdd:COG4618 342 GSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLpqdVELfDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 ysnlTAKENltinakILGIQKENAiEEVLE----------IVGLAsekvklfKNY-----------SLGMKQRLGIARAL 150
Cdd:COG4618 421 ----TIAEN------IARFGDADP-EKVVAaaklagvhemILRLP-------DGYdtrigeggarlSGGQRQRIGLARAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446716125 151 LHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQsRNITILISSHILSeIEQLVDKVGIIHNG 212
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPS-LLAAVDKLLVLRDG 542
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-212 |
1.17e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.93 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 40 GRNGAGKTTTIRMLLGLIKPTKGNIKIFEKE-FESNKTEIL----KNIGAMVETPGFYSNLTAKENLTinakiLGIQKEN 114
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGICLppekRRIGYVFQDARLFPHYKVRGNLR-----YGMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 115 AiEEVLEIVGLASEKvKLFKNY----SLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITIL 190
Cdd:PRK11144 106 V-AQFDKIVALLGIE-PLLDRYpgslSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPIL 183
|
170 180
....*....|....*....|..
gi 446716125 191 ISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK11144 184 YVSHSLDEILRLADRVVVLEQG 205
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-223 |
1.22e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 84.85 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLikpTKGNIKIFEKEFESNKTEILK------------NIGAMVETP 89
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMRFDDIDLLRlsprerrklvghNVSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 gfYSNLTAKENL---TINA-----------KILGIQKENAIEeVLEIVGLASEKvKLFKNYSL----GMKQRLGIARALL 151
Cdd:PRK15093 99 --QSCLDPSERVgrqLMQNipgwtykgrwwQRFGWRKRRAIE-LLHRVGIKDHK-DAMRSFPYelteGECQKVMIAIALA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446716125 152 HNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDL 223
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-215 |
1.30e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.90 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEIL---KNIGAMVETPG-- 90
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLalrQQVATVFQDPEqq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 -FYSNLTAkeNLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:PRK13638 90 iFYTDIDS--DIAFSLRNLGVPEAEItrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446716125 167 DPIGIKEIRKLIKDLAQSRNiTILISSHILSEIEQLVDKVGIIHNGVLL 215
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-223 |
1.57e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFEsnkteiLKNIGAMVE-----------TPG 90
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR------IRSPRDAIRagiayvpedrkGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENLTI-------NAKILGIQKENAI-EEVLEIVGL--ASEKVKLfKNYSLGMKQRLGIARALLHNPELLILD 160
Cdd:COG1129 341 LVLDLSIRENITLasldrlsRGGLLDRRRERALaEEYIKRLRIktPSPEQPV-GNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 161 EPTNGLDpIGIK-EIRKLIKDLAQSRNITILISSHiLSEIEQLVDKVGIIHNGVLLEEIMYEDL 223
Cdd:COG1129 420 EPTRGID-VGAKaEIYRLIRELAAEGKAVIVISSE-LPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-214 |
2.03e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGaMVETP------GFYSNLTAK 98
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARG-LVYLPedrqssGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 99 EN---LTINAKILGIQ--KENAI-EEVLEIVGLA-SEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGI 171
Cdd:PRK15439 360 WNvcaLTHNRRGFWIKpaRENAVlERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR 439
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446716125 172 KEIRKLIKDLAQSRNITILISSHiLSEIEQLVDKVGIIHNGVL 214
Cdd:PRK15439 440 NDIYQLIRSIAAQNVAVLFISSD-LEEIEQMADRVLVMHQGEI 481
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
17-206 |
2.04e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.85 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKifekefesnKTEILKnIGAMVETpgfySNLT 96
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR-IGYVPQK----LYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINAKIL---GIQKENaIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:PRK09544 80 TTLPLTVNRFLRlrpGTKKED-ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180 190
....*....|....*....|....*....|...
gi 446716125 174 IRKLIKDLAQSRNITILISSHILSEIEQLVDKV 206
Cdd:PRK09544 159 LYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-194 |
2.54e-18 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 85.10 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAMVETPGFYSNlT 96
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINAkilGIQKENAIEEVLEIVGLAS--------------EKVKLFknySLGMKQRLGIARALLHNPELLILDEP 162
Cdd:TIGR02868 425 VRENLRLAR---PDATDEELWAALERVGLADwlralpdgldtvlgEGGARL---SGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....
gi 446716125 163 TNGLDPIGIKEirkLIKDL--AQSRNITILISSH 194
Cdd:TIGR02868 499 TEHLDAETADE---LLEDLlaALSGRTVVLITHH 529
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-233 |
3.40e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.49 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQ--IAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkIFEKEF--ESNKTEILKNIGAMVETPgf 91
Cdd:PRK13648 16 QYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAitDDNFEKLRKHIGIVFQNP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 ysnltakENLTINAKI---LGIQKENAI---EEVLEIVGLASEKVKLF-------KNYSLGMKQRLGIARALLHNPELLI 158
Cdd:PRK13648 93 -------DNQFVGSIVkydVAFGLENHAvpyDEMHRRVSEALKQVDMLeradyepNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446716125 159 LDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKNRQFISI 233
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTRI 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-261 |
3.70e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKE--FESNKTEILKNIGAMVETPGFYSNLTAKE 99
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrFASTTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 100 NLtinakILG--------IQKENAIEEV---LEIVGL---ASEKVKLFknySLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:PRK11288 99 NL-----YLGqlphkggiVNRRLLNYEAreqLEHLGVdidPDTPLKYL---SIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 166 LDPIGIKEIRKLIKDL-AQSRniTILISSHILSEIEQLVDKVGIIHNGvlleeimyedlkKKNRQFISIS-VSDEEKVAC 243
Cdd:PRK11288 171 LSAREIEQLFRVIRELrAEGR--VILYVSHRMEEIFALCDAITVFKDG------------RYVATFDDMAqVDRDQLVQA 236
|
250
....*....|....*....
gi 446716125 244 LLETNFG-IYDYKIKENGE 261
Cdd:PRK11288 237 MVGREIGdIYGYRPRPLGE 255
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-206 |
3.78e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 83.09 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVE----TPgfYSNL-- 95
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQivfqNP--YGSLnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 ------TAKENLTINAKILGIQKENAIEEVLEIVGLASEKVKLFKN-YSLGMKQRLGIARALLHNPELLILDEPTNGLDp 168
Cdd:PRK11308 108 rkkvgqILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHmFSGGQRQRIAIARALMLDPDVVVADEPVSALD- 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 446716125 169 IGIK-EIRKLIKDLAQSRNITILISSHILSEIEQLVDKV 206
Cdd:PRK11308 187 VSVQaQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEV 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-230 |
3.97e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 84.51 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 20 QIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIkPTKGNIKIFEKEF-ESNKTEILKNIGAMVETPgfysNL--- 95
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELrELDPESWRKHLSWVGQNP----QLphg 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENLTINAKILGiqkENAIEEVLEIVGlASEKVKLFKN------------YSLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:PRK11174 438 TLRDNVLLGNPDAS---DEQLQQALENAW-VSEFLPLLPQgldtpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 164 NGLDpigIKEIRKLIKDLAQ-SRNITILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKNRQF 230
Cdd:PRK11174 514 ASLD---AHSEQLVMQALNAaSRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGGLF 577
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-227 |
4.20e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 81.76 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLTAKENL 101
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAKILGIQKenaIEEVLEIVGLASEKVKLFKNY-----------SLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:cd03252 97 ALADPGMSMER---VIEAAKLAGAHDFISELPEGYdtivgeqgaglSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 171 IKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKN 227
Cdd:cd03252 174 EHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-212 |
4.34e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.21 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGlIKPT---KGNIkIFE---------KEFESNKTEILKN 81
Cdd:PRK13549 12 TKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEI-IFEgeelqasniRDTERAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 82 IGAMVEtpgfysNLTAKENLTINAKIL--GIQKENAI----EEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPE 155
Cdd:PRK13549 90 ELALVK------ELSVLENIFLGNEITpgGIMDYDAMylraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 156 LLILDEPTNGLDPIGIKEIRKLIKDLaQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
17-205 |
5.28e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.75 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIR---MLLGLIKPTK--GNIKIFEKEF---ESNKTEILKNIGAMVET 88
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGFRveGKVTFHGKNLyapDVDPVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 PGFYSNlTAKENLTINAKILGIQK--ENAIEEVLEIVGLASE-KVKLFKN---YSLGMKQRLGIARALLHNPELLILDEP 162
Cdd:PRK14243 100 PNPFPK-SIYDNIAYGARINGYKGdmDELVERSLRQAALWDEvKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446716125 163 TNGLDPIGIKEIRKLIKDLaqSRNITILISSHILSEIEQLVDK 205
Cdd:PRK14243 179 CSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDM 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-230 |
6.06e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAMVETPGFYsNLT 96
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLF-NRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINakilgiqKENAI-EEVLEIVGLASEKVKLFKN--------------YSLGMKQRLGIARALLHNPELLILDE 161
Cdd:PRK13657 425 IEDNIRVG-------RPDATdEEMRAAAERAQAHDFIERKpdgydtvvgergrqLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKNRQF 230
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGGRF 563
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-178 |
6.68e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 80.66 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 26 LSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKefeSNKT-EILKNIGAMVETPGFYSNLTAKENLTIN 104
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRgDRSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 105 AKILGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLI 178
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-215 |
8.36e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.21 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKI----------FEKEFESNKTEILKNIGA 84
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 85 MVETPGFYSNL--------TAKENLTINAKILGIQKENAIEEV---LEIVGLASE--KVKLFKnYSLGMKQRLGIARALL 151
Cdd:PRK13631 114 LRRRVSMVFQFpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAkfyLNKMGLDDSylERSPFG-LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 152 HNPELLILDEPTNGLDPIGIKEIRKLIKDlAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL 215
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
22-227 |
8.51e-18 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 83.61 E-value: 8.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLTAKENL 101
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAkiLGIQKENAIEEVLEIVGLASEKVKLFK-----------NYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:TIGR02203 427 AYGR--TEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 171 IKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKN 227
Cdd:TIGR02203 505 ERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLARN 558
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-217 |
9.48e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.73 E-value: 9.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIK-----PTKGNIKIFEKE-FESNKTEILKNIGAMVETP 89
Cdd:PRK14247 12 SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDiFKMDVIELRRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 GFYSNLTAKENLTINAKILGIQKENAieEVLEIVGLASEKVKLF---KN--------YSLGMKQRLGIARALLHNPELLI 158
Cdd:PRK14247 92 NPIPNLSIFENVALGLKLNRLVKSKK--ELQERVRWALEKAQLWdevKDrldapagkLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 159 LDEPTNGLDPIGIKEIRKLIKDLaqSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
14-216 |
1.45e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKifekefesnkteilknIGAMVETpGFYS 93
Cdd:COG0488 322 SKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK----------------LGETVKI-GYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 --NLTAKENLTINAKILGIQKENAIEEVLEIVGL-------ASEKVKLFknySLGMKQRLGIARALLHNPELLILDEPTN 164
Cdd:COG0488 385 qhQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRflfsgddAFKPVGVL---SGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446716125 165 GLDPigikEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:COG0488 462 HLDI----ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-214 |
1.59e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF---ESNKTEILkNIGAMVETPGF 91
Cdd:PRK15439 19 KQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarlTPAKAHQL-GIYLVPQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSNLTAKENLtinakILGIQKENAIEEVLEIVgLASEKVKLFKNYSLGM-----KQRLGIARALLHNPELLILDEPTNGL 166
Cdd:PRK15439 98 FPNLSVKENI-----LFGLPKRQASMQKMKQL-LAALGCQLDLDSSAGSlevadRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446716125 167 DPIGIKEIRKLIKDLaQSRNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:PRK15439 172 TPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-231 |
1.95e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkIFEKE-----FESNKTEILKNIGAMVETPGFY 92
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGEnipamSRSRLYTVRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 93 SNLTAKENLTINAKilgiQKENAIEEV--------LEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTN 164
Cdd:PRK11831 97 TDMNVFDNVAYPLR----EHTQLPAPLlhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446716125 165 GLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKKN----RQFI 231
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPdprvRQFL 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-214 |
2.83e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.90 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKiFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:PRK10851 9 KKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIR-FHGTDVSRLHARDRKVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKIL---------GIQKEnaIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTN 164
Cdd:PRK10851 88 HMTVFDNIAFGLTVLprrerpnaaAIKAK--VTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446716125 165 GLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
17-232 |
3.16e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.43 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRML--LGLIKP---TKGNIKIFEKEFESNKT---EILKNIGAMVET 88
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPRTdtvDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 PGFYSnLTAKENLTINAKILGIQKENAIEEVLE--IVGLAS-EKVK--LFKN---YSLGMKQRLGIARALLHNPELLILD 160
Cdd:PRK14239 95 PNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEksLKGASIwDEVKdrLHDSalgLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 161 EPTNGLDPIGIKEIRKLIKDLAQsrNITILISSHILSEIEQLVDKVGIIHNGVLLE-----EIMYEDLKKKNRQFIS 232
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEyndtkQMFMNPKHKETEDYIS 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-192 |
3.28e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.09 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTtirmLLGLI----KPTKGNIKIFEKEFESNK--TEILKNIGAMVETP 89
Cdd:NF033858 10 RYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIagarKIQQGRVEVLGGDMADARhrRAVCPRIAYMPQGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 G--FYSNLTAKENLTINAKILGI---QKENAIEEVLEIVGLASekvklFKN-----YSLGMKQRLGIARALLHNPELLIL 159
Cdd:NF033858 86 GknLYPTLSVFENLDFFGRLFGQdaaERRRRIDELLRATGLAP-----FADrpagkLSGGMKQKLGLCCALIHDPDLLIL 160
|
170 180 190
....*....|....*....|....*....|....
gi 446716125 160 DEPTNGLDPIGIKEIRKLIKDL-AQSRNITILIS 192
Cdd:NF033858 161 DEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVA 194
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-212 |
4.65e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.74 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIF---------EKEFESNKTEI---------LKNIG 83
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkkTKEKEKVLEKLviqktrfkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 84 AMVETPG----------FYSnlTAKENLTINAKILGIQKENAIE---EVLEIVGLASEKVKLFK-NYSLGMKQRLGIARA 149
Cdd:PRK13651 102 EIRRRVGvvfqfaeyqlFEQ--TIEKDIIFGPVSMGVSKEEAKKraaKYIELVGLDESYLQRSPfELSGGQKRRVALAGI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446716125 150 LLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-212 |
5.01e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.60 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNI---KIFEKEFESNKTEILKNIGAMVETPG 90
Cdd:PRK09493 8 SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdGLKVNDPKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENLTINA-KILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:PRK09493 88 LFPHLTALENVMFGPlRVRGASKEEAekqARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446716125 167 DPIGIKEIRKLIKDLAQSrNITILISSHILSEIEQL------VDKVGIIHNG 212
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVasrlifIDKGRIAEDG 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-221 |
5.81e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.77 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKP---TKGNIKIFEKEF------ESNK---TEIlknigAM 85
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpekELNKlraEQI-----SM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 86 VetpgFYSNLTA-------KENLTinaKIL----GIQKENAIEE---VLEIVGL--ASEKVKLFKN-YSLGMKQRLGIAR 148
Cdd:PRK09473 102 I----FQDPMTSlnpymrvGEQLM---EVLmlhkGMSKAEAFEEsvrMLDAVKMpeARKRMKMYPHeFSGGMRQRVMIAM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 149 ALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE-----EIMYE 221
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEygnarDVFYQ 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-212 |
5.98e-17 |
|
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: 81.02 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGlIKPT---KGNIKIFEKEFESN---KTEiLKNIGAMVE 87
Cdd:TIGR02633 8 VKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASnirDTE-RAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 88 TPGFYSNLTAKENLTINAKIL---GIQKENAI----EEVLEIVGL-ASEKVKLFKNYSLGMKQRLGIARALLHNPELLIL 159
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITlpgGRMAYNAMylraKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446716125 160 DEPTNGLDPIGIKEIRKLIKDLaQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-259 |
6.95e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.10 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 21 IAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKT-----EILKNIGAMVETP--GFYS 93
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlkKLRKKVSLVFQFPeaQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NlTAKENLTINAKILGIQKENAIEEVLEI---VGLASEKV-KLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPI 169
Cdd:PRK13641 101 N-TVLKDVEFGPKNFGFSEDEAKEKALKWlkkVGLSEDLIsKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 170 GIKEIRKLIKDLAQSRNITILIsSHILSEIEQLVDKVGIIHNGVLLE----EIMYEDLKKKNRQFISisvsdeEKVACLL 245
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILV-THNMDDVAEYADDVLVLEHGKLIKhaspKEIFSDKEWLKKHYLD------EPATSRF 252
|
250
....*....|....
gi 446716125 246 ETNFGIYDYKIKEN 259
Cdd:PRK13641 253 ASKLEKGGFKFSEM 266
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
15-226 |
7.70e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 79.78 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIrMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVET-PGFYS 93
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVr*GRRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSRKDArarADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 171 IK----EIRKLIKDLAqsrniTILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKK 226
Cdd:NF000106 180 RNevwdEVRSMVRDGA-----TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-222 |
1.44e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.66 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKT-EILKN----IGAMVETPGFYSNLTA 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqDGLANgivyISEDRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 KENLTINA------KILGIQKENAIEEVLEIVGLASEKV----KLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PRK10762 348 KENMSLTAlryfsrAGGSLKHADEQQAVSDFIRLFNIKTpsmeQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446716125 168 PIGIKEIRKLIKDLAQSRNITILISSHiLSEIEQLVDKVGIIHNGVLLEEIMYED 222
Cdd:PRK10762 428 VGAKKEIYQLINQFKAEGLSIILVSSE-MPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-206 |
1.50e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKP---TKGNIKIFEKEFESNKteiLKNIGAMV-ETP 89
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKE---MRAISAYVqQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 GFYSNLTAKENLTINA------KILGIQKENAIEEVLEIVGLAS------EKVKLFKNYSLGMKQRLGIARALLHNPELL 157
Cdd:TIGR00955 109 LFIPTLTVREHLMFQAhlrmprRVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446716125 158 ILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKV 206
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKI 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-201 |
1.80e-16 |
|
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: 76.74 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMV-ETPGFYS---------N 94
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVgQEPVLFArslqdniayG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTINAKILGIQKENAIEEV-LEIVGLASEKVKLFknySLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:cd03248 112 LQSCSFECVKEAAQKAHAHSFISELaSGYDTEVGEKGSQL---SGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180
....*....|....*....|....*...
gi 446716125 174 IRKLIKDLAQSRniTILISSHILSEIEQ 201
Cdd:cd03248 189 VQQALYDWPERR--TVLVIAHRLSTVER 214
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-226 |
2.82e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.02 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPtkgNIKIFEKEFESNKTEILK------------NIGAMVETP 89
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD---NWHVTADRFRWNGIDLLKlsprerrkiigrEIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 GFYSNLTAKENLTINAKILGIQ------------KENAIEeVLEIVGLASEKvKLFKNY----SLGMKQRLGIARALLHN 153
Cdd:COG4170 99 SSCLDPSAKIGDQLIEAIPSWTfkgkwwqrfkwrKKRAIE-LLHRVGIKDHK-DIMNSYphelTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446716125 154 PELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKK 226
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
14-194 |
3.36e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.98 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTK---------GNIKIFEKEFESNKTEILKNIGA 84
Cdd:PRK09984 11 AKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRKSRANTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 85 MVETPGFYSNLTAKENLTINAkiLG--------------IQKENAIEeVLEIVGLASEKVKLFKNYSLGMKQRLGIARAL 150
Cdd:PRK09984 91 IFQQFNLVNRLSVLENVLIGA--LGstpfwrtcfswftrEQKQRALQ-ALTRVGMVHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446716125 151 LHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSH 194
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLH 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
25-197 |
3.66e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkIFE-----KEFESNKTEiLKN--IGAMVETPGFYSNLTA 97
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNgqpmsKLSSAAKAE-LRNqkLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 KENLTINAKILGIQKENAIE---EVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEI 174
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSralEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180
....*....|....*....|...
gi 446716125 175 RKLIKDLAQSRNITILISSHILS 197
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQ 207
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-216 |
5.97e-16 |
|
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: 75.14 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKN-IGAMVETPGFYSNlTAKEN 100
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSsLTIIPQDPTLFSG-TIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 101 LtinaKILGIQKENAIEEVLEIVGLASekvklfkNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKD 180
Cdd:cd03369 102 L----DPFDEYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 446716125 181 LAQsrNITILISSHILSEIEQLvDKVGIIHNGVLLE 216
Cdd:cd03369 171 EFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-226 |
8.14e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.84 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-ESNKTEILKNIGAMVETPGFYSNlTAKENL-- 101
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvQYDHHYLHRQVALVGQEPVLFSG-SVRENIay 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 ----TINAKILGIQKE-NAIEEVLEIV-GLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDpigiKEIR 175
Cdd:TIGR00958 578 gltdTPDEEIMAAAKAaNAHDFIMEFPnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECE 653
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 176 KLIKDLAQSRNITILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKK 226
Cdd:TIGR00958 654 QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
15-217 |
9.81e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 75.22 E-value: 9.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 15 KQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGA---------- 84
Cdd:COG4598 16 KSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPAdrrqlqrirt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 85 ---MVetpgF-----YSNLTAKENLtINAKI--LGIQKENAIEE---VLEIVGLASEKVKLFKNYSLGMKQRLGIARALL 151
Cdd:COG4598 96 rlgMV----FqsfnlWSHMTVLENV-IEAPVhvLGRPKAEAIERaeaLLAKVGLADKRDAYPAHLSGGQQQRAAIARALA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 152 HNPELLILDEPTNGLDPIGIKEIRKLIKDLAQS-RniTILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:COG4598 171 MEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEgR--TMLVVTHEMGFARDVSSHVVFLHQGRIEEQ 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-217 |
1.16e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.61 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKP---TKGNIKIFEKEF-ESNKTEILKNIGAMVETP-GFYSNLT 96
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLtAKTVWDIREKVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINAKILGIQKENAIE---EVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446716125 174 IRKLIKDLAQSRNITILISSHILSEIEQlVDKVGIIHNGVLLEE 217
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQ 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-216 |
1.48e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.74 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKP----TKGNIKIFEKEFESNKTEilkniGAMVET------PGFY 92
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR-----GRKIATimqnprSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 93 SNLT----AKENLtinaKILGIQKENA-IEEVLEIVGLASEKvKLFKNY----SLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:PRK10418 94 PLHTmhthARETC----LALGKPADDAtLTAALEAVGLENAA-RVLKLYpfemSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446716125 164 NGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-212 |
1.61e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFesNKTEILK-NIGAMVETPGFY 92
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM--NDVPPAErGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 93 SNLTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPI 169
Cdd:PRK11000 88 PHLSVAENMSFGLKLAGAKKEEInqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446716125 170 GIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-216 |
3.11e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.66 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEI------LKNIGAMVETPGF-YSN 94
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVFQFPEYqLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTINAKILGIQKENA---IEEVLEIVGLASEKVKLFK-NYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAykkVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446716125 171 IKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-217 |
4.00e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIkPT------KGNIKiFEKEFESNKTE-----ILKNIGAMVetpgF 91
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIR-FHGESLLHASEqtlrgVRGNKIAMI----F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSNLTAKENLTINAKIL--------GIQKENAIEEV---LEIVGLASEKVKLfKNY----SLGMKQRLGIARALLHNPEL 156
Cdd:PRK15134 99 QEPMVSLNPLHTLEKQLyevlslhrGMRREAARGEIlncLDRVGIRQAAKRL-TDYphqlSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446716125 157 LILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-216 |
4.57e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.87 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKI--FEKEFESNKTEILKNIGAMVETPGF-YSNLTAK 98
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgIDTGDFSKLQGIRKLVGIVFQNPETqFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 99 ENLTINAKIL---GIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIR 175
Cdd:PRK13644 97 EDLAFGPENLclpPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446716125 176 KLIKDLaQSRNITILISSHILSEIeQLVDKVGIIHNG-VLLE 216
Cdd:PRK13644 177 ERIKKL-HEKGKTIVYITHNLEEL-HDADRIIVMDRGkIVLE 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-214 |
5.87e-15 |
|
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: 74.86 E-value: 5.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGlIKPTKGNIKIFEKEFESNKTEILKNIG---AMV----ETPGFYSNL 95
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVFINGKPVDIRNPAQAIRagiAMVpedrKRHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENLTINA--KILGIQKENAIEEvLEIVGLASEKVKL--------FKNYSLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:TIGR02633 355 GVGKNITLSVlkSFCFKMRIDAAAE-LQIIGSAIQRLKVktaspflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446716125 166 LDpIGIK-EIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:TIGR02633 434 VD-VGAKyEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-216 |
5.90e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkIFEKE----FESNKTEILK-NIGAMVETPgfYSNLT 96
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI-IFNGQridtLSPGKLQALRrDIQFIFQDP--YASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AK--------ENLTINAKILGIQKENAIEEVLEIVGLASEKVKLFKN-YSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PRK10261 416 PRqtvgdsimEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446716125 168 pIGIK-EIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:PRK10261 496 -VSIRgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-206 |
8.36e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF----ESNKTEILKNIGAMVETPgfYSNLTA 97
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQDP--LASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 KENL-TINAKILGI-QKENAIEEVLEIVGLASEKVKLFKN--------YSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PRK15079 114 RMTIgEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNlinrypheFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446716125 168 pIGIK-EIRKLIKDLAQSRNITILISSHILSEIEQLVDKV 206
Cdd:PRK15079 194 -VSIQaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRV 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-223 |
1.08e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 20 QIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVE------TPGFYS 93
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQqdpvvlADTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTinakilgiqkENAIEEVLEIVGLAsEKVKLF------------KNYSLGMKQRLGIARALLHNPELLILDE 161
Cdd:PRK10790 434 NVTLGRDIS----------EEQVWQALETVQLA-ELARSLpdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446716125 162 PTNGLDPIGIKEIRKLIKDLAQsrNITILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDL 223
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-225 |
2.30e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.39 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIfekefesNKTEILKNIGAmvetpGFYSNLTAKENL 101
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-------KGSAALIAISS-----GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAKILGIQKENAIE---EVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLI 178
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEiipEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446716125 179 KDLaQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEeimYEDLKK 225
Cdd:PRK13545 187 NEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE---YGDIKE 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-227 |
2.98e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 73.24 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIaVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAMVETPGFYSNl 95
Cdd:TIGR01193 485 YGSNI-LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENLTINAKILGIQKEnaIEEVLEIVGLASEKVKLFKNY-----------SLGMKQRLGIARALLHNPELLILDEPTN 164
Cdd:TIGR01193 563 SILENLLLGAKENVSQDE--IWAACEIAEIKDDIENMPLGYqtelseegssiSGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446716125 165 GLDPIgikEIRKLIKDLAQSRNITILISSHILSeIEQLVDKVGIIHNGVLLEEIMYEDLKKKN 227
Cdd:TIGR01193 641 NLDTI---TEKKIVNNLLNLQDKTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDELLDRN 699
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-192 |
3.33e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.74 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTtirmLLGLI-----KPTKGNIKIFEKEFESNKT--EILKNIGamvet 88
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKST----LLSLItgdhpQGYSNDLTLFGRRRGSGETiwDIKKHIG----- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 pgFYSN---LTAKENLTINAKIL-------GI-------QKENAiEEVLEIVGLASEKVKL-FKNYSLGmKQRLG-IARA 149
Cdd:PRK10938 340 --YVSSslhLDYRVSTSVRNVILsgffdsiGIyqavsdrQQKLA-QQWLDILGIDKRTADApFHSLSWG-QQRLAlIVRA 415
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446716125 150 LLHNPELLILDEPTNGLDPIGikeiRKLIKdlaqsRNITILIS 192
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPLN----RQLVR-----RFVDVLIS 449
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-194 |
4.79e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 26 LSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVEtpgfySNLTAKENLTINA 105
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP-----QQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 106 KI-------------LGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIK 172
Cdd:PRK10575 105 LVaigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180
....*....|....*....|..
gi 446716125 173 EIRKLIKDLAQSRNITILISSH 194
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLH 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-218 |
6.10e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFE--SNKTEILKNIGAMVET---PGFYSNLTA 97
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMAYITESrrdNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 KENLTINAKI--------LGI---QKENAI-EEVLEIVGLASEKVKL-FKNYSLGMKQRLGIARALLHNPELLILDEPTN 164
Cdd:PRK09700 359 AQNMAISRSLkdggykgaMGLfheVDEQRTaENQRELLALKCHSVNQnITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446716125 165 GLDpIGIK-EIRKLIKDLAQSRNITILISSHiLSEIEQLVDKVGIIHNGVLLEEI 218
Cdd:PRK09700 439 GID-VGAKaEIYKVMRQLADDGKVILMVSSE-LPEIITVCDRIAVFCEGRLTQIL 491
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-217 |
6.67e-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: 71.64 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKP----TKGNIKiFEKEfesnktEILK------------N 81
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSIL-FDGQ------DLLGlserelrrirgnR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 82 IgAMVetpgFYSNLTA-----------KENLTINAKILGIQKENAIEEVLEIVGLASEKVKLfKNY----SLGMKQRLGI 146
Cdd:COG4172 94 I-AMI----FQEPMTSlnplhtigkqiAEVLRLHRGLSGAAARARALELLERVGIPDPERRL-DAYphqlSGGQRQRVMI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446716125 147 ARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEE 217
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-214 |
6.91e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTK-GNIKIFEKEFE-SNKTEILKNIGAMV----ETPGFYSNLT 96
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKiRNPQQAIAQGIAMVpedrKRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTInAKILGIQKENAIEEVLEIVGLASE----KVKLF------KNYSLGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:PRK13549 358 VGKNITL-AALDRFTGGSRIDDAAELKTILESiqrlKVKTAspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446716125 167 DpIGIK-EIRKLIKDLAQSRNITILISSHiLSEIEQLVDKVGIIHNGVL 214
Cdd:PRK13549 437 D-VGAKyEIYKLINQLVQQGVAIIVISSE-LPEVLGLSDRVLVMHEGKL 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-194 |
7.99e-14 |
|
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: 72.25 E-value: 7.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKpTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLTA 97
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 KENLTINAKilgiQKENAIEEVLEIVGLAS--EKVKLFKNYSL---------GMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:TIGR01271 1309 RKNLDPYEQ----WSDEEIWKVAEEVGLKSviEQFPDKLDFVLvdggyvlsnGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180
....*....|....*....|....*....
gi 446716125 167 DPIGIKEIRKLIKdlaQS-RNITILISSH 194
Cdd:TIGR01271 1385 DPVTLQIIRKTLK---QSfSNCTVILSEH 1410
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
14-213 |
1.05e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 70.75 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkIFEKEFESNKTEILKNIGAMVETPGFYS 93
Cdd:PRK09452 21 SKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-MLDGQDITHVPAENRHVNTVFQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLtinAKILGIQK------ENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PRK09452 100 HMTVFENV---AFGLRMQKtpaaeiTPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446716125 168 PIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGV 213
Cdd:PRK09452 177 YKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-206 |
1.26e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGsqiavnNLSITVESGQIY-----GFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEK----------EFESNKTEI 78
Cdd:PRK13409 347 TKKLG------DFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqyikpDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 79 LKNIGAMVETPGFYSNLTAKENLtinakilgiqkenaiEEVLEivglasekvKLFKNYSLGMKQRLGIARALLHNPELLI 158
Cdd:PRK13409 421 LRSITDDLGSSYYKSEIIKPLQL---------------ERLLD---------KNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446716125 159 LDEPTNGLDpigiKEIR----KLIKDLAQSRNITILISSHILSEIEQLVDKV 206
Cdd:PRK13409 477 LDEPSAHLD----VEQRlavaKAIRRIAEEREATALVVDHDIYMIDYISDRL 524
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-221 |
1.41e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESnkteilKNIGAMVET-----P------G 90
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG------LSPRERRRLgvayiPedrlgrG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENLtinakIL-----------GIQKENAIEEvleivgLASEKVKLF-----------KNYSLGMKQRLGIAR 148
Cdd:COG3845 347 LVPDMSVAENL-----ILgryrrppfsrgGFLDRKAIRA------FAEELIEEFdvrtpgpdtpaRSLSGGNQQKVILAR 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446716125 149 ALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGvlleEIMYE 221
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLDEILALSDRIAVMYEG----RIVGE 483
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-231 |
1.87e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.07 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkifEKEFESNKTEIlknigamveTPGFYSNLTAKENL 101
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---DRNGEVSVIAI---------SAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAKILGIQKENAIE---EVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLI 178
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAmtpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446716125 179 KDLaQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKKNRQFI 231
Cdd:PRK13546 187 YEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFL 238
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-194 |
2.21e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLT 96
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINakilgIQKENAIEEVLEIVGLAseKVKLFKNY-----SLGMKQRLGIARALLHNPELLILDEPTNGLDPIGI 171
Cdd:PRK13540 91 LRENCLYD-----IHFSPGAVGITELCRLF--SLEHLIDYpcgllSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|...
gi 446716125 172 KEIRKLIKDlAQSRNITILISSH 194
Cdd:PRK13540 164 LTIITKIQE-HRAKGGAVLLTSH 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-212 |
2.32e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 70.29 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKtEILKNIGAMVETPGFYS 93
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTK-QILKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINA-----KILGIQ-KENAIEEVLEIVGLASEKVKLFKN-----YSLGMKQRLGIARALLHNPELLILDEP 162
Cdd:PLN03211 154 HLTVRETLVFCSllrlpKSLTKQeKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 163 TNGLDPIGIKEIRKLIKDLAQsRNITILISSH-ILSEIEQLVDKVGIIHNG 212
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHqPSSRVYQMFDSVLVLSEG 283
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-227 |
3.53e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 69.66 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLTAKENL 101
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAKilGIQKENAIEEVLEiVGLASEKVKLFKN------------YSLGMKQRLGIARALLHNPELLILDEPTNGLDPI 169
Cdd:PRK11176 438 AYART--EQYSREQIEEAAR-MAYAMDFINKMDNgldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 170 GIKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKN 227
Cdd:PRK11176 515 SERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQN 569
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-194 |
4.60e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.15 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKE-----------FESNK------- 75
Cdd:PRK15064 8 TMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNErlgklrqdqfaFEEFTvldtvim 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 76 --TEILKnigAMVETPGFYSNLTAKENLTINAKIL--------GIQKENAIEEVLEIVGLASEK-VKLFKNYSLGMKQRL 144
Cdd:PRK15064 88 ghTELWE---VKQERDRIYALPEMSEEDGMKVADLevkfaemdGYTAEARAGELLLGVGIPEEQhYGLMSEVAPGWKLRV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446716125 145 GIARALLHNPELLILDEPTNGLDpigIKEIRKLIKDLAQsRNITILISSH 194
Cdd:PRK15064 165 LLAQALFSNPDILLLDEPTNNLD---INTIRWLEDVLNE-RNSTMIIISH 210
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-228 |
5.60e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.23 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIK-PTK---------GN--IKIFEKEfesnKTEILKNIGAMVetp 89
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaeklefnGQdlQRISEKE----RRNLVGAEVAMI--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 gFYSNLTA-KENLTINAKIL-----------GIQKENAIEeVLEIVGLASEKVKLfKNY----SLGMKQRLGIARALLHN 153
Cdd:PRK11022 95 -FQDPMTSlNPCYTVGFQIMeaikvhqggnkKTRRQRAID-LLNQVGIPDPASRL-DVYphqlSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446716125 154 PELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLKKKNR 228
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
16-167 |
6.15e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.71 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGA---------- 84
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASvpqdtslsfe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 85 --------MVETP--GFYSNLTAKEnltinakilgiqkENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNP 154
Cdd:PRK09536 92 fdvrqvveMGRTPhrSRFDTWTETD-------------RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170
....*....|...
gi 446716125 155 ELLILDEPTNGLD 167
Cdd:PRK09536 159 PVLLLDEPTASLD 171
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-216 |
6.94e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.89 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 27 SITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNI----------------KIFEKEFESNKTEILkniGAMVETPG 90
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfshitrlsfeqlqKLVSDEWQRNNTDML---SPGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 fysnLTAKEnlTINakiLGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:PRK10938 100 ----RTTAE--IIQ---DEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446716125 171 IKEIRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:PRK10938 171 RQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-226 |
7.98e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.96 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVetPgfySNLT 96
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL--P---QHHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINAKI-------------LGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:PRK11231 87 TPEGITVRELVaygrspwlslwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 164 NGLDPIGIKEIRKLIKDLAQSRN--ITILissHILSEIEQLVDKVGIIHNGVLL-----EEIMYEDLKKK 226
Cdd:PRK11231 167 TYLDINHQVELMRLMRELNTQGKtvVTVL---HDLNQASRYCDHLVVLANGHVMaqgtpEEVMTPGLLRT 233
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-222 |
7.98e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 19 SQIAVNN----LSITVESGQIYGFLGRNGAGKTTTIRMLLGLIkPTKGNIKIFEKEFESNKTEILKNIGAMV---ETPGF 91
Cdd:PRK03695 4 NDVAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLsqqQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 ----YSNLTakenLTINAKILGIQKENAIEEVLEIVGLASekvKLFKN---YSLGMKQRLGIARALLH-----NPE--LL 157
Cdd:PRK03695 83 ampvFQYLT----LHQPDKTRTEAVASALNEVAEALGLDD---KLGRSvnqLSGGEWQRVRLAAVVLQvwpdiNPAgqLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 158 ILDEPTNGLDPIGIKEIRKLIKDLAQSrNITILISSHILSEIEQLVDKVGIIHNGVLL-----EEIMYED 222
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLasgrrDEVLTPE 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
26-194 |
1.23e-12 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 65.92 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 26 LSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEfesnkteilknIGAMVETP---------GF----- 91
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD-----------LFALDEDArarlrarhvGFvfqsf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 --YSNLTAKENLTINAKILGIQ--KENAiEEVLEIVGLAsekvKLFKNY----SLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:COG4181 100 qlLPTLTALENVMLPLELAGRRdaRARA-RALLERVGLG----HRLDHYpaqlSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190
....*....|....*....|....*....|.
gi 446716125 164 NGLDPIGIKEIRKLIKDLAQSRNITILISSH 194
Cdd:COG4181 175 GNLDAATGEQIIDLLFELNRERGTTLVLVTH 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-201 |
1.23e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.05 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQY-GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTE----ILKNIGAMVET 88
Cdd:PRK10908 8 SKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 PGFYSNLTAKENLTINAKILGIQKENAIEEV---LEIVGLAsEKVKLFK-NYSLGMKQRLGIARALLHNPELLILDEPTN 164
Cdd:PRK10908 88 HHLLMDRTVYDNVAIPLIIAGASGDDIRRRVsaaLDKVGLL-DKAKNFPiQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 446716125 165 GLDPIGIKEIRKLIKDLAQSrNITILISSHILSEIEQ 201
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISR 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-206 |
1.38e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkIFE-KEFESNKTEIL-KNIGAMVETPGFYS 93
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-LFEgEDISTLKPEIYrQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NlTAKENLTINAKILGIQ-KENAIEEVLEIVGLASEKV-KLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGI 171
Cdd:PRK10247 95 D-TVYDNLIFPWQIRNQQpDPAIFLDDLERFALPDTILtKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190
....*....|....*....|....*....|....*
gi 446716125 172 KEIRKLIKDLAQSRNITILISSHILSEIEQlVDKV 206
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-236 |
1.49e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 20 QIAV-NNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEK---EFESNKTEILK--NIGAMVETPGFYS 93
Cdd:PRK10535 20 QVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvaTLDADALAQLRreHFGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKILGIQKENAIE---EVLEIVGLAsEKVKLFKN-YSLGMKQRLGIARALLHNPELLILDEPTNGLDPI 169
Cdd:PRK10535 100 HLTAAQNVEVPAVYAGLERKQRLLraqELLQRLGLE-DRVEYQPSqLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 170 GIKEIRKLIKDLaQSRNITILISSHIlSEIEQLVDKVGIIHNGvlleEIMYEDLKKKNRQFISISVS 236
Cdd:PRK10535 179 SGEEVMAILHQL-RDRGHTVIIVTHD-PQVAAQAERVIEIRDG----EIVRNPPAQEKVNVAGGTEP 239
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-212 |
1.91e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.76 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 27 SITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFesNKTEILKNIGAMV-ETPGFYSNLTAKENLTI-- 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDH--TTTPPSRRPVSMLfQENNLFSHLTVAQNIGLgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 104 --NAKILGIQKEnAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDL 181
Cdd:PRK10771 97 npGLKLNAAQRE-KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190
....*....|....*....|....*....|.
gi 446716125 182 AQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK10771 176 CQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-204 |
1.98e-12 |
|
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: 66.03 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKpTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLTA 97
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 KENLTINAKilgiQKENAIEEVLEIVGLAS---------EKVKLFKNYSL--GMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:cd03289 94 RKNLDPYGK----WSDEEIWKVAEEVGLKSvieqfpgqlDFVLVDGGCVLshGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 446716125 167 DPIGIKEIRKLIKDlaQSRNITILISSHilsEIEQLVD 204
Cdd:cd03289 170 DPITYQVIRKTLKQ--AFADCTVILSEH---RIEAMLE 202
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-212 |
2.87e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.04 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMV-ETPGFYSNLTAken 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVsQTPFLFSDTVA--- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 101 ltiNAKILGiqKENA----IEEVLEIVGLASEKVKLFKNY-----------SLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:PRK10789 407 ---NNIALG--RPDAtqqeIEHVARLASVHDDILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446716125 166 LDpiGIKEiRKLIKDLAQ-SRNITILISSHILSEI----EQLVDKVG-IIHNG 212
Cdd:PRK10789 482 VD--GRTE-HQILHNLRQwGEGRTVIISAHRLSALteasEILVMQHGhIAQRG 531
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-199 |
3.13e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 66.77 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 24 NNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKI--------------------------FekefesNKTe 77
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdgqdirdvtqaslraaigivpqdtvlF------NDT- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 78 ILKNIGamvetpgfYSNLTAKEnltinakilgiqkenaiEEVLEIVGLAS-----------------EK-VKLfknySLG 139
Cdd:COG5265 448 IAYNIA--------YGRPDASE-----------------EEVEAAARAAQihdfieslpdgydtrvgERgLKL----SGG 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 140 MKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRniTILISSHILSEI 199
Cdd:COG5265 499 EKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTI 556
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-223 |
5.20e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.12 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKG----------NIKIFEKEfesNKTEILKNIG 83
Cdd:PRK14271 28 TLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllgGRSIFNYR---DVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 84 AMVETPGFYSnLTAKENLT--INAKILGIQKE--NAIEEVLEIVGL-ASEKVKLFKN---YSLGMKQRLGIARALLHNPE 155
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLagVRAHKLVPRKEfrGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 156 LLILDEPTNGLDPIGIKEIRKLIKDLAQsrNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYEDL 223
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-198 |
7.89e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKT-EILKNIGAMVE---TP 89
Cdd:PRK10253 14 TLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVARRIGLLAQnatTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 G--FYSNLTAKENLTINAKILGIQKEN--AIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:PRK10253 94 GdiTVQELVARGRYPHQPLFTRWRKEDeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190
....*....|....*....|....*....|...
gi 446716125 166 LDPIGIKEIRKLIKDLAQSRNITILISSHILSE 198
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQ 206
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-206 |
1.20e-11 |
|
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: 65.19 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGsqiavnNLSITVESGQIY-----GFLGRNGAGKTTTIRMLLGLIKPTKGNI----KIFEK----EFESNKT--EI 78
Cdd:COG1245 348 TKSYG------GFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlKISYKpqyiSPDYDGTveEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 79 LKN-IGAMVETPGFYSNLtakenltinAKILGIQKenaieeVLEivglasekvKLFKNYSLGMKQRLGIARALLHNPELL 157
Cdd:COG1245 422 LRSaNTDDFGSSYYKTEI---------IKPLGLEK------LLD---------KNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446716125 158 ILDEPTNGLDpigiKEIR----KLIKDLAQSRNITILISSHILSEIEQLVDKV 206
Cdd:COG1245 478 LLDEPSAHLD----VEQRlavaKAIRRFAENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-206 |
1.22e-11 |
|
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: 63.58 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 24 NNLSITVESG-----QIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIF-----------EKEFESNKTEILKNIgamve 87
Cdd:cd03237 11 GEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEldtvsykpqyiKADYEGTVRDLLSSI----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 88 TPGFYSNLTAKENLtinAKILGIqkENAIE-EVLEIVGlasekvklfknyslGMKQRLGIARALLHNPELLILDEPTNGL 166
Cdd:cd03237 86 TKDFYTHPYFKTEI---AKPLQI--EQILDrEVPELSG--------------GELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446716125 167 DpigiKEIR----KLIKDLAQSRNITILISSHILSEIEQLVDKV 206
Cdd:cd03237 147 D----VEQRlmasKVIRRFAENNEKTAFVVEHDIIMIDYLADRL 186
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-167 |
1.55e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.88 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIR-MLLGLIKPTKGNIKIF--EKEFESNKTEILKNI------------ 82
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRyMAMHAIDGIPKNCQILhvEQEVVGDDTTALQCVlntdiertqlle 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 83 --------GAMVETPGFYSNLTAKENLTINAKILGiQKENAIEEVLEIV--------------GL---ASEKVKLFKNYS 137
Cdd:PLN03073 268 eeaqlvaqQRELEFETETGKGKGANKDGVDKDAVS-QRLEEIYKRLELIdaytaearaasilaGLsftPEMQVKATKTFS 346
|
170 180 190
....*....|....*....|....*....|
gi 446716125 138 LGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PLN03073 347 GGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-216 |
1.70e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.88 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILK---------------NIGAMV 86
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgaDMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 87 ETPGFYSN--LTAKENLTINAKI-LGIQKENAIEE---VLEIVGLASEKVKLFK---NYSLGMKQRLGIARALLHNPELL 157
Cdd:PRK10261 111 QEPMTSLNpvFTVGEQIAESIRLhQGASREEAMVEakrMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 158 ILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLLE 216
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-194 |
2.49e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEK-----------EFESNKTeILKNIGa 84
Cdd:PRK11147 328 QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlevayfdqhraELDPEKT-VMDNLA- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 85 mvetpgfysnlTAKENLTINAK---ILGIqkenaIEEVLEIVGLASEKVKLFknySLGMKQRLGIARALLHNPELLILDE 161
Cdd:PRK11147 406 -----------EGKQEVMVNGRprhVLGY-----LQDFLFHPKRAMTPVKAL---SGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|...
gi 446716125 162 PTNGLDpigiKEIRKLIKDLAQSRNITILISSH 194
Cdd:PRK11147 467 PTNDLD----VETLELLEELLDSYQGTVLLVSH 495
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-223 |
3.38e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAMVETPGFYSNlTAKENL 101
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSG-TVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TI-----NAKILGIQKENAIEEVLE--IVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEI 174
Cdd:PLN03232 1331 DPfsehnDADLWEALERAHIKDVIDrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446716125 175 RKLIKDlaQSRNITILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDL 223
Cdd:PLN03232 1411 QRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-212 |
3.41e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKE--FESNKtEILKNIGAMVETPgfySNLTAKE 99
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidFKSSK-EALENGISMVHQE---LNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 100 NLTINAkILG--------------IQKENAIEEVLEIVGLASEKVklfKNYSLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:PRK10982 89 SVMDNM-WLGryptkgmfvdqdkmYRDTKAIFDELDIDIDPRAKV---ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446716125 166 LDPIGIKEIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKE-RGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-194 |
3.70e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQiyGFL--GRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEfesnktEILknigamvetpgF-----YSNL 95
Cdd:COG4178 379 LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA------RVL-----------FlpqrpYLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 -TAKENLTINAKILGIQKEnAIEEVLEIVGLA--SEKVKLFKNY----SLGMKQRLGIARALLHNPELLILDEPTNGLDP 168
Cdd:COG4178 440 gTLREALLYPATAEAFSDA-ELREALEAVGLGhlAERLDEEADWdqvlSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180
....*....|....*....|....*...
gi 446716125 169 IGIKEIRKLIKD-LAQsrniTILIS-SH 194
Cdd:COG4178 519 ENEAALYQLLREeLPG----TTVISvGH 542
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-194 |
4.68e-11 |
|
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: 60.25 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 19 SQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEfesnkteilkNIGAMVETPGFysnltak 98
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----------DLLFLPQRPYL------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 99 enltinakILGIQKENAI---EEVLeivglasekvklfknySLGMKQRLGIARALLHNPELLILDEPTNGLDPigikEIR 175
Cdd:cd03223 76 --------PLGTLREQLIypwDDVL----------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESE 127
|
170
....*....|....*....
gi 446716125 176 KLIKDLAQSRNITILISSH 194
Cdd:cd03223 128 DRLYQLLKELGITVISVGH 146
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-214 |
5.42e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEkefESNKTEILKNIGAMV----ETPGFYSNLTa 97
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG---QPTRQALQKNLVAYVpqseEVDWSFPVLV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 kENLTINAK-----ILGIQKEN---AIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPI 169
Cdd:PRK15056 98 -EDVVMMGRyghmgWLRRAKKRdrqIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446716125 170 GIKEIRKLIKDLaQSRNITILISSHILSEIEQLVDKVGIIHNGVL 214
Cdd:PRK15056 177 TEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-167 |
5.80e-11 |
|
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: 63.03 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEkefesnkTEILknigAMVEtpgfys 93
Cdd:TIGR03719 329 TKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-------TVKL----AYVD------ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 nlTAKENLTINakilgiqkENAIEEV---LEIVGLASEKV-----------------KLFKNYSLGMKQRLGIARALLHN 153
Cdd:TIGR03719 392 --QSRDALDPN--------KTVWEEIsggLDIIKLGKREIpsrayvgrfnfkgsdqqKKVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....
gi 446716125 154 PELLILDEPTNGLD 167
Cdd:TIGR03719 462 GNVLLLDEPTNDLD 475
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-199 |
6.29e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIfekefesNKTEILKN---------IGAMVETPGFYSNl 95
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII-------NDSHNLKDinlkwwrskIGVVSQDPLLFSN- 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENltINAKILGIQKENAIEEVLEIVGLAS----------------------------EKVKLFKNY----------- 136
Cdd:PTZ00265 475 SIKNN--IKYSLYSLKDLEALSNYYNEDGNDSqenknkrnscrakcagdlndmsnttdsnELIEMRKNYqtikdsevvdv 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 137 ----------------------------SLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNIT 188
Cdd:PTZ00265 553 skkvlihdfvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632
|
250
....*....|.
gi 446716125 189 ILISSHILSEI 199
Cdd:PTZ00265 633 TIIIAHRLSTI 643
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-212 |
6.46e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 20 QIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFE-SNKTEILKNIGAMV----ETPGFYSN 94
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANEAINHGFALVteerRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTI-NAKI----LGIQKENAIEEVLEIVgLASEKVK------LFKNYSLGMKQRLGIARALLHNPELLILDEPT 163
Cdd:PRK10982 341 LDIGFNSLIsNIRNyknkVGLLDNSRMKSDTQWV-IDSMRVKtpghrtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446716125 164 NGLDpIGIK-EIRKLIKDLAQSRNITILISSHiLSEIEQLVDKVGIIHNG 212
Cdd:PRK10982 420 RGID-VGAKfEIYQLIAELAKKDKGIIIISSE-MPELLGITDRILVMSNG 467
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
24-194 |
6.76e-11 |
|
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: 60.33 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 24 NNLSITVESGQIYGFLGRNGAGKTTTIRML-----LGLIKptkGNIKIFEKEfesNKTEILKNIGAMVETPGFYSNLTAK 98
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILINGRP---LDKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 99 ENLTINAKILGIqkenaieevleivglasekvklfknySLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLI 178
Cdd:cd03232 98 EALRFSALLRGL--------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
170
....*....|....*.
gi 446716125 179 KDLAQSrNITILISSH 194
Cdd:cd03232 152 KKLADS-GQAILCTIH 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-271 |
6.88e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.22 E-value: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTkgnikifekefeSNKTEILKNIGAMVETPGFYSNLTAKENLTIN 104
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPR------------SDASVVIRGTVAYVPQVSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 105 AKILGIQKENAIEEV-----LEIV--GLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDP-IGIKEIRK 176
Cdd:PLN03130 703 SPFDPERYERAIDVTalqhdLDLLpgGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDK 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 177 LIKD-LAQSRNITILISSHILSEieqlVDKVGIIHNGVLLEEIMYEDLKKKNRQFisisvsdeekvACLLEtNFGIYDYK 255
Cdd:PLN03130 783 CIKDeLRGKTRVLVTNQLHFLSQ----VDRIILVHEGMIKEEGTYEELSNNGPLF-----------QKLME-NAGKMEEY 846
|
250
....*....|....*.
gi 446716125 256 IKENGEFKIYSHIDRQ 271
Cdd:PLN03130 847 VEENGEEEDDQTSSKP 862
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
14-167 |
7.23e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFEsnkteiLKNIGAMVET----- 88
Cdd:PRK11701 13 TKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQ------LRDLYALSEAerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 -----------P--GFYSNLTAKEN-----LTINAKILGIQKENAIEEvLEIVGLASEKV-KLFKNYSLGMKQRLGIARA 149
Cdd:PRK11701 87 lrtewgfvhqhPrdGLRMQVSAGGNigerlMAVGARHYGDIRATAGDW-LERVEIDAARIdDLPTTFSGGMQQRLQIARN 165
|
170
....*....|....*...
gi 446716125 150 LLHNPELLILDEPTNGLD 167
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLD 183
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-217 |
8.78e-11 |
|
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: 60.23 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGL--IKPTKGNIkIFEKEfesnkteilkNIGAMveTPgfysNLTAKEN 100
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEI-LFKGE----------DITDL--PP----EERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 101 LTinakiLGIQKENAIEEVleivglaseKVKLF-----KNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIR 175
Cdd:cd03217 79 IF-----LAFQYPPEIPGV---------KNADFlryvnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446716125 176 KLIKDLAqSRNITILISSH---ILSEIEqlVDKVGIIHNGVLLEE 217
Cdd:cd03217 145 EVINKLR-EEGKSVLIITHyqrLLDYIK--PDRVHVLYDGRIVKS 186
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-167 |
9.36e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.49 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFE----KEFESNKTEILKnigaMVETPgfy 92
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiklGYFAQHQLEFLR----ADESP--- 394
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 93 snltakenLTINAKILGIQKENAIEEVLEIVGLASEKV-KLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PRK10636 395 --------LQHLARLAPQELEQKLRDYLGGFGFQGDKVtEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-209 |
1.06e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 28 ITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGN----------IK---------IFEKEFESNKTEILKNigAMVET 88
Cdd:PRK13409 94 PIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdevLKrfrgtelqnYFKKLYNGEIKVVHKP--QYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 PGFYSNLTAKENLTinakilGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDp 168
Cdd:PRK13409 172 IPKVFKGKVRELLK------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD- 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446716125 169 igIKE---IRKLIKDLAQSRniTILISSHILSEIEQLVDKVGII 209
Cdd:PRK13409 245 --IRQrlnVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIA 284
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-210 |
1.64e-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: 61.72 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 29 TVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkifekEFESNKTEILKnigamvetpgFYSNLTAKENLT--INAK 106
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-----DEEPSWDEVLK----------RFRGTELQDYFKklANGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 107 ILGIQKENAIE-----------EVLEIV---GLASEKVKLF----------KNYSLGMKQRLGIARALLHNPELLILDEP 162
Cdd:COG1245 160 IKVAHKPQYVDlipkvfkgtvrELLEKVderGKLDELAEKLglenildrdiSELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 163 TNGLDpigIKE-IR--KLIKDLAQSrNITILISSHILSEIEQLVDKVGIIH 210
Cdd:COG1245 240 SSYLD---IYQrLNvaRLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-212 |
1.81e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.34 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGlIKPT---KGNIkIFEKE---FES-NKTE--------- 77
Cdd:NF040905 8 TKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEI-LFDGEvcrFKDiRDSEalgiviihq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 78 ---------ILKNIgamvetpgFYSNLTAKENLtINAKilgiQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIAR 148
Cdd:NF040905 86 elalipylsIAENI--------FLGNERAKRGV-IDWN----ETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 149 ALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLaQSRNITILISSHILSEIEQLVDKVGIIHNG 212
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-216 |
1.91e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 26 LSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFES-NKTEILKNIGAMVETPGFYSNlTAKENLtin 104
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFSG-TVRFNL--- 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 105 aKILGIQKENAIEEVLE-----------IVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKE 173
Cdd:PLN03130 1334 -DPFNEHNDADLWESLErahlkdvirrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446716125 174 IRKLIKDlaQSRNITILISSHILSEIEQlVDKVGIIHNGVLLE 216
Cdd:PLN03130 1413 IQKTIRE--EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-225 |
2.37e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 59.70 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 24 NNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIK--PTKGNIkIFEKEfesnkteilkNIGAM---------------- 85
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSI-LLDGE----------DILELspderaragiflafqy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 86 -VETPG--FYSNLTAKENLTINAKILGIQKENAIEEVLEIVGLASEKVK--LFKNYSLGMKQRLGIARALLHNPELLILD 160
Cdd:COG0396 86 pVEIPGvsVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDryVNEGFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 161 EPTNGLDPIGIKEIRKLIKDLaQSRNITILISSH---ILSEIEqlVDKVGIIHNGV--------LLEEIM---YEDLKK 225
Cdd:COG0396 166 ETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHyqrILDYIK--PDFVHVLVDGRivksggkeLALELEeegYDWLKE 241
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-194 |
5.12e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.64 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 28 ITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF----ESNKTEI-LKNIGAMVETPGFYSNLTAKENLT 102
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLrAKHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 103 INAKILGIQ----KENAIEeVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLI 178
Cdd:PRK10584 111 LPALLRGESsrqsRNGAKA-LLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170
....*....|....*.
gi 446716125 179 KDLAQSRNITILISSH 194
Cdd:PRK10584 190 FSLNREHGTTLILVTH 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-247 |
5.68e-10 |
|
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: 60.31 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEK-EFESNKTEILknigamvetPGfysnlTAKENLti 103
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSPQTSWIM---------PG-----TIKDNI-- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 104 nakILGIQ-KENAIEEVLEIVGLaSEKVKLFKN------------YSLGMKQRLGIARALLHNPELLILDEPTNGLDPIG 170
Cdd:TIGR01271 508 ---IFGLSyDEYRYTSVIKACQL-EEDIALFPEkdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 171 IKEI--RKLIKDLAQSRNITilisshILSEIEQL--VDKVGIIHNGVLLEEIMYEDLKKKNRQFISI--------SVSDE 238
Cdd:TIGR01271 584 EKEIfeSCLCKLMSNKTRIL------VTSKLEHLkkADKILLLHEGVCYFYGTFSELQAKRPDFSSLllgleafdNFSAE 657
|
....*....
gi 446716125 239 EKVACLLET 247
Cdd:TIGR01271 658 RRNSILTET 666
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-194 |
6.48e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.56 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 21 IAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFeSNKTE--ILKNIGAMVETP--GFYSNLT 96
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEykRAKYIGRVFQDPmmGTAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 AKENLTINAK-------ILGIQKEN--AIEEVLEIVGLASE-----KVKLFknySLGMKQRLGIARALLHNPELLILDEP 162
Cdd:COG1101 99 IEENLALAYRrgkrrglRRGLTKKRreLFRELLATLGLGLEnrldtKVGLL---SGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190
....*....|....*....|....*....|..
gi 446716125 163 TNGLDPIGIKEIRKLIKDLAQSRNITILISSH 194
Cdd:COG1101 176 TAALDPKTAALVLELTEKIVEENNLTTLMVTH 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-206 |
8.56e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 57.83 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkifekefesnkteILKNIGAMV--------------- 86
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-------------LVRHDGGWVdlaqaspreilalrr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 87 ETPGFYSN-------LTAkenLTINAKIL---GIQKENAIEEVLEIvgLASEKV--KLFKNY----SLGMKQRLGIARAL 150
Cdd:COG4778 93 RTIGYVSQflrviprVSA---LDVVAEPLlerGVDREEARARAREL--LARLNLpeRLWDLPpatfSGGEQQRVNIARGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446716125 151 LHNPELLILDEPTNGLDPIGIKEIRKLIKDlAQSRNITILISSHILSEIEQLVDKV 206
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDEEVREAVADRV 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-212 |
2.04e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 56.32 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 24 NNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFekefesnkteilKNIGAMVETPgFYSNLTAKENlti 103
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP------------GSIAYVSQEP-WIQNGTIREN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 104 nakILGIQKENA--IEEVLEIVGLaSEKVKLFK------------NYSLGMKQRLGIARALLHNPELLILDEPTNGLDP- 168
Cdd:cd03250 86 ---ILFGKPFDEerYEKVIKACAL-EPDLEILPdgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAh 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446716125 169 IGIKEIRKLI-KDLAQSRniTILISSHILSEIEQlVDKVGIIHNG 212
Cdd:cd03250 162 VGRHIFENCIlGLLLNNK--TRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-224 |
3.22e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKE--FESNKTEILKNIGAMVETPGFYSNLTAKE 99
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEvtFNGPKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 100 NLtinakILGIQKENAI------------EEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PRK10762 99 NI-----FLGREFVNRFgridwkkmyaeaDKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 168 PIGIKEIRKLIKDL-AQSRNITILisSHILSEIEQLVDKVGIIHNGVLLEEIMYEDLK 224
Cdd:PRK10762 174 DTETESLFRVIRELkSQGRGIVYI--SHRLKEIFEICDDVTVFRDGQFIAEREVADLT 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-222 |
4.51e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 27 SITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMV-----ETPGFYSNLTAKENL 101
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLcpedrKAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINAK--------IL--GIQKENAIEEVleivglASEKVK------LFKNYSLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:PRK11288 353 NISARrhhlragcLInnRWEAENADRFI------RSLNIKtpsreqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 166 LDpIGIK-EIRKLIKDLAQsRNITILISSHILSEIEQLVDKVGIIHNGVLLEEIMYED 222
Cdd:PRK11288 427 ID-VGAKhEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-167 |
4.88e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKefesnkteilknigamvETPGFYS 93
Cdd:PRK15064 326 TKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN-----------------ANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKE---NLTINAKILGIQKENAIEEVLE-IVGL----ASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:PRK15064 389 QDHAYDfenDLTLFDWMSQWRQEGDDEQAVRgTLGRllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNH 468
|
..
gi 446716125 166 LD 167
Cdd:PRK15064 469 MD 470
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-211 |
5.09e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 5.09e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446716125 134 KNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQlVDKVGIIHN 211
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-221 |
7.52e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKI--------------------------FEKEF 71
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgnwqlawvnqetpalpqpaleyvidGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 72 ESNKTEIL----KNIGAMVETpgFYSNLTAKENLTINAKI------LGIQKENAIEEVleivglasekvklfKNYSLGMK 141
Cdd:PRK10636 92 RQLEAQLHdaneRNDGHAIAT--IHGKLDAIDAWTIRSRAasllhgLGFSNEQLERPV--------------SDFSGGWR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 142 QRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKdlaqSRNITILISSHILSEIEQLVDKvgIIHngvLLEEIMYE 221
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK----SYQGTLILISHDRDFLDPIVDK--IIH---IEQQSLFE 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-66 |
8.45e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 8.45e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446716125 14 TKQYGSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKI 66
Cdd:PRK11819 331 SKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-192 |
8.78e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLG--LIKPTKGNIKIFEKEFESNKTEILKNIGAM------VETPGFySN 94
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIFlafqypIEIPGV-SN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKEnLTINAKilgiQKENAIEEV--LEIVGLASEKVKLFK------------NYSLGMKQRLGIARALLHNPELLILD 160
Cdd:CHL00131 102 ADFLR-LAYNSK----RKFQGLPELdpLEFLEIINEKLKLVGmdpsflsrnvneGFSGGEKKRNEILQMALLDSELAILD 176
|
170 180 190
....*....|....*....|....*....|..
gi 446716125 161 EPTNGLDPIGIKEIRKLIKDLAQSRNITILIS 192
Cdd:CHL00131 177 ETDSGLDIDALKIIAEGINKLMTSENSIILIT 208
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
25-199 |
1.36e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.72 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVetpGFYSNLTAKENLTIN 104
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNL---GLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 105 AKIL-GIQKENAIEEVLEIVGLASEKVklfKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDpigiKEIRKLIKDL-- 181
Cdd:PRK13541 95 SEIYnSAETLYAAIHYFKLHDLLDEKC---YSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS----KENRDLLNNLiv 167
|
170 180
....*....|....*....|
gi 446716125 182 --AQSRNItILISSHILSEI 199
Cdd:PRK13541 168 mkANSGGI-VLLSSHLESSI 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-194 |
2.79e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLI-----------------------KPTKGNIKIFEKEFESNKTEILKN 81
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVllddgriiyeqdlivarlqqdppRNVEGTVYDFVAEGIEEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 82 ---IGAMVETPGFYSNLTAKENLTINAKILGI-QKENAIEEVLEIVGLASEKvkLFKNYSLGMKQRLGIARALLHNPELL 157
Cdd:PRK11147 101 yhdISHLVETDPSEKNLNELAKLQEQLDHHNLwQLENRINEVLAQLGLDPDA--ALSSLSGGWLRKAALGRALVSNPDVL 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 446716125 158 ILDEPTNGLDPIGIKEIRKLIKDLAQSrnitILISSH 194
Cdd:PRK11147 179 LLDEPTNHLDIETIEWLEGFLKTFQGS----IIFISH 211
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-167 |
5.14e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.47 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 33 GQIYGFLGRNGAGKTTTIRMLLGliKPT----KGNIKI--FEKefesnKTEILKNIGAMVETPGFYS-NLTAKENLTINA 105
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRIsgFPK-----KQETFARISGYCEQNDIHSpQVTVRESLIYSA 978
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446716125 106 kILGIQKENAIEEVLEIVGLASEKVKL--FKNYSLGM----------KQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PLN03140 979 -FLRLPKEVSKEEKMMFVDEVMELVELdnLKDAIVGLpgvtglsteqRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-212 |
6.80e-08 |
|
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: 51.88 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPT---KGNIKI----FEKEFESNKTEILKNigamVETPGFYSNL 95
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYngipYKEFAEKYPGEIIYV----SEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 96 TAKENLTINAKILGiqkeNAIeevleivglasekvklFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIR 175
Cdd:cd03233 99 TVRETLDFALRCKG----NEF----------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 446716125 176 KLIKDLAQSRNITILISSHILS-EIEQLVDKVGIIHNG 212
Cdd:cd03233 159 KCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEG 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-230 |
9.19e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTkgnikifekefESNKTEILKNIGAMVETPGFYsNLTAKENLT 102
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA-----------ETSSVVIRGSVAYVPQVSWIF-NATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 103 INAKILGIQKENAIEevleiVGLASEKVKLFK------------NYSLGMKQRLGIARALLHNPELLILDEPTNGLDP-I 169
Cdd:PLN03232 701 FGSDFESERYWRAID-----VTALQHDLDLLPgrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhV 775
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446716125 170 GIKEIRKLIKDLAQSRNITILISS-HILSeieqLVDKVGIIHNGVLLEEIMYEDLKKKNRQF 230
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQlHFLP----LMDRIILVSEGMIKEEGTFAELSKSGSLF 833
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-230 |
1.68e-07 |
|
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: 52.64 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIfekefesnkteilKNIGAMVETPGFYSNLTAKENLT 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-------------KGSVAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 103 INAKIlgiqKENAIEEVLEIVGL--------ASEKVKLFK---NYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGI 171
Cdd:TIGR00957 721 FGKAL----NEKYYQQVLEACALlpdleilpSGDRTEIGEkgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 172 KEI-RKLIKDLAQSRNITILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDLKKKNRQF 230
Cdd:TIGR00957 797 KHIfEHVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-167 |
2.28e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.79 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 17 YGSQIA-VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKG-----NIKIFEKEFESNKTEILKNIGAMVETPg 90
Cdd:cd03290 10 WGSGLAtLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwsNKNESEPSFEATRSRNRYSVAYAAQKP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENLTINAKiLGIQKENAIEEVLEI--------VGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEP 162
Cdd:cd03290 89 WLLNATVEENITFGSP-FNKQRYKAVTDACSLqpdidllpFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
....*
gi 446716125 163 TNGLD 167
Cdd:cd03290 168 FSALD 172
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-216 |
3.98e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.48 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILK-NIGAMVETPGFYSNlt 96
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRfKITIIPQDPVLFSG-- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 97 akeNLTINAKILGIQKENAIEEVLEIV-----------GLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNG 165
Cdd:TIGR00957 1375 ---SLRMNLDPFSQYSDEEVWWALELAhlktfvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446716125 166 LDPIGIKEIRKLIKdlAQSRNITILISSHILSEIEQLVdKVGIIHNGVLLE 216
Cdd:TIGR00957 1452 VDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAE 1499
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-212 |
5.68e-07 |
|
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: 49.86 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 25 NLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEK-EFESNKTEILknigamvetPGfysnlTAKENLTI 103
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRiSFSSQFSWIM---------PG-----TIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 104 NA-----KILGIQKENAIEEvlEIVGLASEKVKLFK----NYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEI 174
Cdd:cd03291 121 GVsydeyRYKSVVKACQLEE--DITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446716125 175 RK--LIKDLAQSRNITilisshILSEIEQL--VDKVGIIHNG 212
Cdd:cd03291 199 FEscVCKLMANKTRIL------VTSKMEHLkkADKILILHEG 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-199 |
5.82e-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: 48.14 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 32 SGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEfesnkteilknigamvetpgfysnltakenltinakilgiq 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 112 kenAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLI-----KDLAQSRN 186
Cdd:smart00382 40 ---DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEKN 116
|
170
....*....|...
gi 446716125 187 ITILISSHILSEI 199
Cdd:smart00382 117 LTVILTTNDEKDL 129
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-210 |
6.63e-07 |
|
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: 48.72 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 30 VESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIkifekefesnkteilknigamvETPGfysnltakenLTINAKilg 109
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND----------------------EWDG----------ITPVYK--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 110 iqkenaieevleivglaSEKVKLfknySLGMKQRLGIARALLHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITI 189
Cdd:cd03222 67 -----------------PQYIDL----SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTA 125
|
170 180
....*....|....*....|.
gi 446716125 190 LISSHILSEIEQLVDKVGIIH 210
Cdd:cd03222 126 LVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-167 |
1.16e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 37 GFLGRNGAGKTTTIRMLLGLIKPTKG------NIKIF----EKEFESNKT----------EI------LKNIGAMVETPG 90
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGearpapGIKVGylpqEPQLDPEKTvrenveegvaEVkaaldrFNEIYAAYAEPD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 91 FYSNLTAKENLTINAKIlgiQKENA--IEEVLEIVGLA------SEKVKlfkNYSLGMKQRLGIARALLHNPELLILDEP 162
Cdd:PRK11819 117 ADFDALAAEQGELQEII---DAADAwdLDSQLEIAMDAlrcppwDAKVT---KLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
....*
gi 446716125 163 TNGLD 167
Cdd:PRK11819 191 TNHLD 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-167 |
1.19e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 37 GFLGRNGAGKTTTIRMLLGLIKPTKGnikifEKEFESNKTeilknIGAMVETPGFYSNLTAKENLTIN-AKILGIQKE-N 114
Cdd:TIGR03719 35 GVLGLNGAGKSTLLRIMAGVDKDFNG-----EARPQPGIK-----VGYLPQEPQLDPTKTVRENVEEGvAEIKDALDRfN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 115 AI-----EEVLEIVGLASEKVKL-------------------------------FKNYSLGMKQRLGIARALLHNPELLI 158
Cdd:TIGR03719 105 EIsakyaEPDADFDKLAAEQAELqeiidaadawdldsqleiamdalrcppwdadVTKLSGGERRRVALCRLLLSKPDMLL 184
|
....*....
gi 446716125 159 LDEPTNGLD 167
Cdd:TIGR03719 185 LDEPTNHLD 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-182 |
1.46e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 24 NNLSITVESGQIYGFLGRNGAGKTTTI-----RMLLGLIkpTKG----NIKIFEKEFEsnkteilKNIGAMVETPGFYSN 94
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLnvlaeRVTTGVI--TGGdrlvNGRPLDSSFQ-------RSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 95 LTAKENLTINA------KILGIQKENAIEEVLEIVGLASEKVKLFKNYSLGM----KQRLGIARALLHNPELLI-LDEPT 163
Cdd:TIGR00956 851 STVRESLRFSAylrqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPT 930
|
170
....*....|....*....
gi 446716125 164 NGLDPIGIKEIRKLIKDLA 182
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLA 949
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-194 |
2.05e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.81 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 16 QYGSQ-IAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEF-ESNKTEILKNIGAMVETPGFYS 93
Cdd:PRK10522 331 AYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLFSAVFTDFHLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 94 NLTAKENLTINAKilgiqkenAIEEVLEIVGLAsEKVKLFKN------YSLGMKQRLGIARALLHNPELLILDEPTNGLD 167
Cdd:PRK10522 411 QLLGPEGKPANPA--------LVEKWLERLKMA-HKLELEDGrisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180
....*....|....*....|....*..
gi 446716125 168 PIGIKEIRKLIKDLAQSRNITILISSH 194
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-210 |
2.32e-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: 48.13 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 29 TVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGN----------IKIFEKEFESNKTEILKNIGAMVETPGFYSNLTAK 98
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeiLDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 99 enlTINAKILGIQKE-------NAIEEVLEIVGLASEKVklfKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDpigI 171
Cdd:cd03236 102 ---AVKGKVGELLKKkdergklDELVDQLELRHVLDRNI---DQLSGGELQRVAIAAALARDADFYFFDEPSSYLD---I 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446716125 172 KE---IRKLIKDLAQSRNiTILISSHILSEIEQLVDKVGIIH 210
Cdd:cd03236 173 KQrlnAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-177 |
2.51e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 48.30 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 14 TKQY-GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEK---EFESNKTEIlknigAMVetp 89
Cdd:PRK11650 10 RKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELEPADRDI-----AMV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 gF-----YSNLTAKENLTINAKILGIQKEnAIEE-------VLEIVGLASEK-VKLfknySLGMKQRLGIARALLHNPEL 156
Cdd:PRK11650 82 -FqnyalYPHMSVRENMAYGLKIRGMPKA-EIEErvaeaarILELEPLLDRKpREL----SGGQRQRVAMGRAIVREPAV 155
|
170 180
....*....|....*....|....*...
gi 446716125 157 LILDEPTNGLDPigiK-------EIRKL 177
Cdd:PRK11650 156 FLFDEPLSNLDA---KlrvqmrlEIQRL 180
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
39-212 |
5.76e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 39 LGRNGAGKTTtirmllgLIKPTKGNIKIFEKEFESNKT-------EILKNIGAMV----ETPGFYSNLTAKENL------ 101
Cdd:TIGR00956 93 LGRPGSGCST-------LLKTIASNTDGFHIGVEGVITydgitpeEIKKHYRGDVvynaETDVHFPHLTVGETLdfaarc 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 -TINAKILGIQKENAIEEV----LEIVGLA---SEKV--KLFKNYSLGMKQRLGIARALLHNPELLILDEPTNGLDPIGI 171
Cdd:TIGR00956 166 kTPQNRPDGVSREEYAKHIadvyMATYGLShtrNTKVgnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATA 245
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446716125 172 KEIRKLIKDLAQSRNITILISSHILSE-IEQLVDKVGIIHNG 212
Cdd:TIGR00956 246 LEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEG 287
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-194 |
9.97e-06 |
|
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: 47.05 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 20 QIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGL--------IKPTKGniKIFekefesnkteilknigaMVETPGF 91
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKG--KLF-----------------YVPQRPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 YSNLTAKENLTINAKILGIQK----ENAIEEVLEIVGLAS--------EKVKLFKN-YSLGMKQRLGIARALLHNPELLI 158
Cdd:TIGR00954 526 MTLGTLRDQIIYPDSSEDMKRrglsDKDLEQILDNVQLTHilereggwSAVQDWMDvLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 446716125 159 LDEPTNGLDPigikEIRKLIKDLAQSRNITILISSH 194
Cdd:TIGR00954 606 LDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-216 |
1.37e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYSNLTA 97
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 98 KENLTinaKILgiqkENAIEEV---LEIVGL----ASEK-------VKLFKNYSLGMKQRLGIARALLHNPELLIL-DEP 162
Cdd:PTZ00243 1401 RQNVD---PFL----EASSAEVwaaLELVGLrervASESegidsrvLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEA 1473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446716125 163 TNGLDPIGIKEIRKLIkdLAQSRNITILISSHILSEIEQLvDKVGIIHNGVLLE 216
Cdd:PTZ00243 1474 TANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAE 1524
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-193 |
1.43e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLGLIKPTK--GNIKIFEKEFESNK------------TEILKNIGAmvet 88
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNisGTVFKDGKEVDVSTvsdaidaglayvTEDRKGYGL---- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 89 pgfysNL--TAKENLTInAKILGIQKENAIEEVLEIVgLASEKVKLFK-----------NYSLGMKQRLGIARALLHNPE 155
Cdd:NF040905 352 -----NLidDIKRNITL-ANLGKVSRRGVIDENEEIK-VAEEYRKKMNiktpsvfqkvgNLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190
....*....|....*....|....*....|....*....
gi 446716125 156 LLILDEPTNGLDpIGIK-EIRKLIKDLAQSRNITILISS 193
Cdd:NF040905 425 VLILDEPTRGID-VGAKyEIYTIINELAAEGKGVIVISS 462
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-215 |
5.33e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.05 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGQIYGFLGRNGAGKTTTIRMLLG-LIKP-------TKGNIKIFEK---EFESNKTEILKNIGAMVETPGF 91
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEplaAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 92 ysNLTAKENLTIN-------AKILGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQRLGIARAL--LH-------NPE 155
Cdd:PRK13547 97 --AFSAREIVLLGrypharrAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqLWpphdaaqPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 156 LLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSHILSEIEQLVDKVGIIHNGVLL 215
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-204 |
1.54e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 22 AVNNLSITVESGQIYGFLGRNGAGKTTTIrmLLGLIKPTKGNIKIFEKEFESNKTEILKNIGAMVETPGFYsnltakenL 101
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDVGLGY--------L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 102 TINakilgiQKENAIeevleivglasekvklfknySLGMKQRLGIARALLHNPE--LLILDEPTNGLDPIGIKEIRKLIK 179
Cdd:cd03238 80 TLG------QKLSTL--------------------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIK 133
|
170 180
....*....|....*....|....*..
gi 446716125 180 DLAQSRNITILISSH--ILSEIEQLVD 204
Cdd:cd03238 134 GLIDLGNTVILIEHNldVLSSADWIID 160
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
144-194 |
1.65e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.61 E-value: 1.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446716125 144 LGIARALLHN--PELLILDEPTNGLDPIGIKEIRKLIKDLaqSRNITILISSH 194
Cdd:COG4637 267 LALLAALLSPrpPPLLCIEEPENGLHPDLLPALAELLREA--SERTQVIVTTH 317
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
135-200 |
1.67e-04 |
|
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: 42.76 E-value: 1.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446716125 135 NYSLGMKQRLGIARALL---HNPELLILDEPTNGLDPIGIKEIRKLIKDLAQsRNITILISSHILSEIE 200
Cdd:pfam13304 236 ELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSR-NGAQLILTTHSPLLLD 303
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-238 |
6.34e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 40.66 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 18 GSQIAVNNLSITVES---------------GQIYGFLGRNGAGKTTTIRMLLGLIKPTKGNIKIFEKEFESNKTEILKN- 81
Cdd:cd03288 17 GGEIKIHDLCVRYENnlkpvlkhvkayikpGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 82 IGAMVETPGFYSNlTAKENLTINAKIlgiqKENAIEEVLEIV-----------GLASEKVKLFKNYSLGMKQRLGIARAL 150
Cdd:cd03288 97 LSIILQDPILFSG-SIRFNLDPECKC----TDDRLWEALEIAqlknmvkslpgGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 151 LHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRniTILISSHILSEIEQlVDKVGIIHNGVLLEEIMYEDL-KKKNRQ 229
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLlAQEDGV 248
|
....*....
gi 446716125 230 FISISVSDE 238
Cdd:cd03288 249 FASLVRTDK 257
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
23-194 |
9.77e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.37 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 23 VNNLSITVESGqIYGFLGRNGAGKTTTIRmLLGLIKPTKGNIKIFEKEFESNK-------------TEILKNIGAMVETP 89
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILE-ALRLLLGPSSSRKFDEEDFYLGDdpdlpeieieltfGSLLSRLLRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 90 GFYSNLTAK-ENL---------TINAKILGIQKENAIEEVLEIVGLASEKVKLFKNYSLGMKQR---------LGIARAL 150
Cdd:COG3593 92 EDKEELEEAlEELneelkealkALNELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGkelpldrlgSGFQRLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446716125 151 L-------------HNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSrNITILISSH 194
Cdd:COG3593 172 LlallsalaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEK-PNQVIITTH 227
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
143-206 |
1.02e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.51 E-value: 1.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446716125 143 RLGIARALLHNPELLILDEPTNGLDPIGIKE-IRKLIKDLAQSRNITILISSHIlSEIEQLVDKV 206
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHD-EELVDAADHI 192
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|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
133-209 |
2.03e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 39.26 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446716125 133 FKNYSLGMKQRLGIARAL---LHNPELLILDEPTNGLDPIGIKEIRKLIKDLAQSRNITILISSH---ILSEIEQLVDKV 206
Cdd:COG1106 200 LSEESDGTKRLLALAGALldaLAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHsteLLDAFLELLRRD 279
|
...
gi 446716125 207 GII 209
Cdd:COG1106 280 QIW 282
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| |
