|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-214 |
9.32e-111 |
|
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: 319.14 E-value: 9.32e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR-EIRKIIGYLPQD 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPqKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAG 163
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517427119 164 LDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-223 |
1.19e-104 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 304.29 E-value: 1.19e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-DNDREIRKIIGYLPQ 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGeIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVaRDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517427119 163 GLDPEERVRFRNLLSETAKD-RIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEA 223
Cdd:COG1131 161 GLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-222 |
1.20e-76 |
|
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: 233.60 E-value: 1.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND-REIRKIIGYLPQ 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEpREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517427119 163 GLDPEERVRFRNLLSETAK-DRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:COG4555 162 GLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-266 |
1.08e-75 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 233.08 E-value: 1.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDndREIRKIIGYLPQD 83
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGeIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAG 163
Cdd:COG4152 80 RGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 164 LDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAGRIYSAqVSRMELESIRD 242
Cdd:COG4152 160 LDPVNVELLKDVIRElAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRL-EADGDAGWLRA 238
|
250 260
....*....|....*....|....
gi 517427119 243 HYTVTSMMMQGNHASVRLISDEKP 266
Cdd:COG4152 239 LPGVTVVEEDGDGAELKLEDGADA 262
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-210 |
3.89e-75 |
|
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: 227.28 E-value: 3.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-DNDREIRKIIGYLPQ 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGeIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIkKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYlgvlsglsgparkeripslleqvnltddvktkvramSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517427119 163 GLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRGCV 210
Cdd:cd03230 125 GLDPESRREFWELLRElKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
5-219 |
5.18e-69 |
|
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: 216.18 E-value: 5.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-DNDREIRKIIGYLPQ 82
Cdd:TIGR03522 3 IRVSSLTKLYGTQNALDEVSFEAQKGrIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVlQNPKEVQRNIGYLPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:TIGR03522 83 HNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 163 GLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:TIGR03522 163 GLDPNQLVEIRNVIKNIGKDKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDEL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-219 |
5.16e-67 |
|
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: 208.13 E-value: 5.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQ--ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR-EIRKIIGYL 80
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGeIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRkAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 161 TAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-214 |
2.51e-61 |
|
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: 193.20 E-value: 2.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGYLPQD 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGeIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVYEAMDYLGVLSGLsgpaRKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAG 163
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517427119 164 LDPEERVRFRNLLSETAKDRI-VILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGItVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-219 |
1.18e-60 |
|
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: 191.81 E-value: 1.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND-REIRKIIGYLPQ 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGeIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREpREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 163 GLDPEERVRFRNLLSETAK--DRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-265 |
1.03e-57 |
|
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: 187.21 E-value: 1.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 12 KTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-DNDREIRKIIGYLPQDFSMYGN 89
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGeVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 90 MSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEER 169
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 170 VRFRNLLSETAKDRI-VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAGR-IYSAQVSRMELESIRDHYTVT 247
Cdd:TIGR01188 161 RAIWDYIRALKEEGVtILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDtLESRPRDIQSLKVEVSMLIAE 240
|
250
....*....|....*...
gi 517427119 248 SMMMQGNHASVRLISDEK 265
Cdd:TIGR01188 241 LGETGLGLLAVTVDSDRI 258
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-236 |
7.19e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 180.67 E-value: 7.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIdndREIRKIIGY 79
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGeFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP---RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYGN--MSVYEAmdylgVLSGLSG---------PARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQAL 148
Cdd:COG1121 80 VPQRAEVDWDfpITVRDV-----VLMGRYGrrglfrrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 149 LHDPKVLIVDEPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRGcVLFQGTVTELL-EEAAGR 226
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLtPENLSR 233
|
250
....*....|
gi 517427119 227 IYSAQVSRME 236
Cdd:COG1121 234 AYGGPVALLA 243
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-214 |
1.07e-55 |
|
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: 179.01 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNdrEIRKIIGYLPQDFS 85
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGeIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI--AARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 86 MYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517427119 166 PEERVRFRNLLSETA-KDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03269 161 PVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
5-225 |
1.65e-55 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 179.41 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND-REIRKIIGYLPQ 82
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFvALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRApRAALARLGVVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:TIGR03864 82 QPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 163 GLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATcEDIAVLNRGCVLFQGTVTELLEEAAG 225
Cdd:TIGR03864 162 GLDPASRAAITAHVRALARDQglSVLWATHLVDEIEAS-DRLVVLHRGRVLADGAAAELRGATGG 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-190 |
6.71e-54 |
|
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: 174.60 E-value: 6.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG----KKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKI--- 76
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFvAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 ---IGYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPK 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 517427119 154 VLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTH 190
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTH 199
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-223 |
1.12e-51 |
|
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: 169.05 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND--REIRKIIGYL 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFvAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnlRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQD-----FSMygnmSVYE--AmdyLGVL-SGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDP 152
Cdd:COG1122 81 FQNpddqlFAP----TVEEdvA---FGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517427119 153 KVLIVDEPTAGLDPEERVRFRNLLSETAKDRI-VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEA 223
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-231 |
2.79e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 168.70 E-value: 2.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKI---I 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFvALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalRGRALRRLrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQDFSMYGNMSVYE-----AMDYLGVLSGLSG---PARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALL 149
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTnvlagRLGRTSTWRSLLGlfpPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 150 HDPKVLIVDEPTAGLDPE--ERVrfRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAG 225
Cdd:COG3638 163 QEPKLILADEPVASLDPKtaRQV--MDLLRRIAREDgiTVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAVLR 240
|
....*.
gi 517427119 226 RIYSAQ 231
Cdd:COG3638 241 EIYGGE 246
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-190 |
3.03e-51 |
|
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: 167.27 E-value: 3.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDRE-IRKIIGYLPQ 82
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGeALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREdYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYLGVLSGLSGPArkERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180
....*....|....*....|....*....
gi 517427119 163 GLDPEERVRFRNLLSE-TAKDRIVILSTH 190
Cdd:COG4133 161 ALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-214 |
3.34e-51 |
|
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: 167.54 E-value: 3.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKK----QALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-DNDREIRKIIG 78
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGeVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVD 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 159 EPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-221 |
6.69e-51 |
|
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: 174.71 E-value: 6.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-----GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN-----DREI 73
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGeTLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 74 RKIIGYLPQD-FSMYgN--MSVYEAMDY-LGVLSGLSGPARKERIPSLLEQVNLTDDVKTK-VRAMSGGMRRRLGIAQAL 148
Cdd:COG1123 341 RRRVQMVFQDpYSSL-NprMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 149 LHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR----IVIlsTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLE 221
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgltyLFI--SHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-245 |
8.38e-51 |
|
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: 167.91 E-value: 8.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREIRKIIGYLP 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVtALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 QDFSMYGNMSVYE--AM---DYLGVLSGLSgPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLI 156
Cdd:COG1120 82 QEPPAPFGLTVRElvALgryPHLGLFGRPS-AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 157 VDEPTAGLDPEERVRFRNLLSETAKD--RIVILSTHivgDVE---ATCEDIAVLNRGCVLFQGTVTELL-EEAAGRIYsa 230
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLH---DLNlaaRYADRLVLLKDGRIVAQGPPEEVLtPELLEEVY-- 235
|
250
....*....|....*
gi 517427119 231 qvsRMELESIRDHYT 245
Cdd:COG1120 236 ---GVEARVIEDPVT 247
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-211 |
2.46e-50 |
|
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: 165.39 E-value: 2.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGYLPQD 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGeFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAG 163
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517427119 164 LDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVL 211
Cdd:cd03259 161 LDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-222 |
2.72e-50 |
|
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: 165.65 E-value: 2.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHvcginIDNDREIRKI---IGYL 80
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNsVYGLLGPNGAGKSTLLKMITGILRPTSGEII-----FDGHPWTRKDlhkIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYEAMDYLGVLSGLSgparKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEP 160
Cdd:TIGR03740 76 IESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 161 TAGLDPEERVRFRNLL-SETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTV--TELLEE 222
Cdd:TIGR03740 152 TNGLDPIGIQELRELIrSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKInkSENLEK 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-214 |
2.27e-49 |
|
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: 162.70 E-value: 2.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDReirKIIGYLPQ--D 83
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFlAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---KRIGYVPQrrS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVYE--AMDYLGVLSGLSGP--ARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:cd03235 79 IDRDFPISVRDvvLMGLYGHKGLFRRLskADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517427119 160 PTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRGcVLFQG 214
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-221 |
2.90e-49 |
|
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: 163.23 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN-----DREIR 74
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGeILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekeLYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQDFSMYGNMSVYE--AMdYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDP 152
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFEnvAF-PLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517427119 153 KVLIVDEPTAGLDPEERVRFRNLLSETAKDR----IVIlsTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLE 221
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELgltsVVV--THDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-228 |
1.19e-48 |
|
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: 161.97 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG-KKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND-----REIRKII 77
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGeFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQDFSMYGNMSVYE--------AMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALL 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLEnvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 150 HDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAGRI 227
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
.
gi 517427119 228 Y 228
Cdd:cd03256 241 Y 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-208 |
1.52e-48 |
|
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: 160.71 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 6 VIKNLSKTY--GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGYL 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFvLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTklSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQD-FSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:cd03225 81 FQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517427119 160 PTAGLDPEERVRFRNLLSETAKDRI-VILSTHIVGDVEATCEDIAVLNRG 208
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-223 |
1.01e-47 |
|
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: 160.69 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGK-----KQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND-----REI 73
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFvAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkkklKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 74 RKIIGYL---P--QDFS-------MYG--NMsvyeamdylgvlsGLSGPARKERIPSLLEQVNLTDDVKTKVR-AMSGGM 138
Cdd:TIGR04521 81 RKKVGLVfqfPehQLFEetvykdiAFGpkNL-------------GLSEEEAEERVKEALELVGLDEEYLERSPfELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 139 RRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTV 216
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTP 227
|
....*..
gi 517427119 217 TELLEEA 223
Cdd:TIGR04521 228 REVFSDV 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-190 |
3.89e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.51 E-value: 3.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKK----QALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREI 73
Cdd:COG1136 1 MSPLLELRNLTKSYGTGegevTALRGVSLSIEAGEFvAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 74 RKI----IGYLPQDFSMYGNMSVYE----AMdylgVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIA 145
Cdd:COG1136 81 ARLrrrhIGFVFQFFNLLPELTALEnvalPL----LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517427119 146 QALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD--RIVILSTH 190
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTH 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-219 |
5.07e-47 |
|
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: 157.28 E-value: 5.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN-----DREIRKIIG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGeILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYGNMSVYEAMDY-LGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFpLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517427119 158 DEPTAGLDPEERVRFRNLLSET--AKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-228 |
6.01e-46 |
|
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: 154.76 E-value: 6.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGK-KQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND-----REIRKII 77
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFvAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkklRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQDFSMYGNMSVYE--------AMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALL 149
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLEnvlhgrlgYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 150 HDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAGRI 227
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVLRHI 241
|
.
gi 517427119 228 Y 228
Cdd:TIGR02315 242 Y 242
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-208 |
3.92e-45 |
|
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: 150.09 E-value: 3.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND--REIRKIIGYLPQd 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGeIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLplEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 fsmygnmsvyeamdylgvlsglsgparkeripslleqvnltddvktkvraMSGGMRRRLGIAQALLHDPKVLIVDEPTAG 163
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517427119 164 LDPEERVRFRNLLSETAKD-RIVILSTHIVGDVEATCEDIAVLNRG 208
Cdd:cd00267 111 LDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-221 |
4.91e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 154.86 E-value: 4.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-------G--------------KKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHV 62
Cdd:COG4586 2 IEVENLSKTYrvyekepGlkgalkglfrreyrEVEAVDDISFTIEPGeIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 63 CGINIDNDR-EIRKIIGylpqdfSMYGN-------MSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAM 134
Cdd:COG4586 82 LGYVPFKRRkEFARRIG------VVFGQrsqlwwdLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 135 SGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLF 212
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVIDHGRIIY 235
|
....*....
gi 517427119 213 QGTVTELLE 221
Cdd:COG4586 236 DGSLEELKE 244
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-228 |
6.07e-45 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 152.11 E-value: 6.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN---DREIRKIIGY 79
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYGNMSVYEAMdyLGVL--SGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:COG1137 83 LPQEASIFRKLTVEDNI--LAVLelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 158 DEPTAGLDP---EErvrFRNLLSEtAKDR-IVILST-HIVGDVEATCEDIAVLNRGCVLFQGTVTELLE-EAAGRIY 228
Cdd:COG1137 161 DEPFAGVDPiavAD---IQKIIRH-LKERgIGVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNnPLVRKVY 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-225 |
9.38e-45 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 153.81 E-value: 9.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-DNDREIRKIIGYLPQ 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGEcFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 163 GLDPEER----VRFRNLLsetAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAG 225
Cdd:PRK13537 168 GLDPQARhlmwERLRSLL---ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIG 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-220 |
1.26e-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: 148.50 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG----KKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID-----NDREIR 74
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGeIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKV 154
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 155 LIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-228 |
1.31e-43 |
|
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: 148.46 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN---DREIRKIIGYL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGeIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEP 160
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 161 TAGLDPEERVRFRNLLSETAKDRIVILST-HIVGDVEATCEDIAVLNRGCVLFQGTVTELLE-EAAGRIY 228
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAnELVRKVY 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
2.58e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 150.75 E-value: 2.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-DNDREIRKIIGY 79
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGeCFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQ------DFSMYGNMSVYeamdylGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPK 153
Cdd:PRK13536 119 VPQfdnldlEFTVRENLLVF------GRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517427119 154 VLIVDEPTAGLDPEER----VRFRNLLsetAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAG 225
Cdd:PRK13536 193 LLILDEPTTGLDPHARhliwERLRSLL---ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIG 265
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-214 |
2.72e-43 |
|
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: 147.86 E-value: 2.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 14 YGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG-INIDNDREIRKIIGY-LPQDFSMYGNM 90
Cdd:cd03267 31 YREVEALKGISFTIEKGeIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRKKFLRRIGVvFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 91 SVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERV 170
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517427119 171 RFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03267 191 NIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-190 |
3.81e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.12 E-value: 3.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GKKQALKHVDLTIHKGMFGLL-GPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREI---RKII 77
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkRREIpylRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQDFSMYGNMSVYE----AMDYLGVlsglSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPK 153
Cdd:COG2884 82 GVVFQDFRLLPDRTVYEnvalPLRVTGK----SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517427119 154 VLIVDEPTAGLDPEERVRFRNLLSE-----TAkdriVILSTH 190
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEinrrgTT----VLIATH 195
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-208 |
4.09e-43 |
|
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: 145.41 E-value: 4.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID----NDREIRKIIGY 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGeIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYGNMSVYEamdylgvlsglsgparkeripslleqvNLTddvktkvRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLE---------------------------NIA-------LGLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517427119 160 PTAGLDPEERVRFRNLLsETAKDRI---VILSTHIVGDVEATCEDIAVLNRG 208
Cdd:cd03229 127 PTSALDPITRREVRALL-KSLQAQLgitVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-218 |
7.87e-43 |
|
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: 146.43 E-value: 7.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN---DREIRKIIGYLPQ 82
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGeIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlppHEIARLGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDyLGVLSGLSGPAR-----------KERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHD 151
Cdd:cd03219 83 IPRLFPELTVLENVM-VAAQARTGSGLLlararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSETAKDRI-VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTE 218
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-196 |
1.04e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 147.16 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTY----GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIdndREIRK 75
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFvALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV---TGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 IIGYLPQDFSMYGNMSVYE--AmdyLGV-LSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDP 152
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDnvA---LGLeLRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 153 KVLIVDEPTAGLDPEERVRFRNLL----SETAK----------------DRIVILSTH---IVGDVE 196
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELlrlwQETGKtvlfvthdvdeavflaDRVVVLSARpgrIVEEID 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-214 |
2.61e-42 |
|
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: 144.96 E-value: 2.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTY----GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-DNDREIRKI---- 76
Cdd:cd03257 4 VKNLSVSFptggGSVKALDDVSFSIKKGeTLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlKLSRRLRKIrrke 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQD--FSMYGNMSVY----EAMDYLGVLSGLSgpARKERIPSLLEQVNLTDDVKTK-VRAMSGGMRRRLGIAQALL 149
Cdd:cd03257 84 IQMVFQDpmSSLNPRMTIGeqiaEPLRIHGKLSKKE--ARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 150 HDPKVLIVDEPTAGLDPEERVRFRNLLSE--TAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKlqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-162 |
3.26e-42 |
|
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: 142.40 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 20 LKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI--DNDREIRKIIGYLPQDFSMYGNMSVYEAM 96
Cdd:pfam00005 1 LKNVSLTLNPGeILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 97 DYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRA----MSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-214 |
3.41e-42 |
|
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: 143.34 E-value: 3.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREIRKIIGYLPQd 83
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGeIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlsPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 fsmygnmsvyeAMDYLGVLsglsgparkeripSLLEQVnltddvktkVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAG 163
Cdd:cd03214 81 -----------ALELLGLA-------------HLADRP---------FNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517427119 164 LDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03214 128 LDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-190 |
6.48e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.42 E-value: 6.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR--EIRKIIGYLP 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECvAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 QDFSMYGNmSVYEAMDYlgVLSGLSGPARKERIPSLLEQVNLTDDVKTK-VRAMSGGMRRRLGIAQALLHDPKVLIVDEP 160
Cdd:COG4619 81 QEPALWGG-TVRDNLPF--PFQLRERKFDRERALELLERLGLPPDILDKpVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|..
gi 517427119 161 TAGLDPEERVRFRNLLSE--TAKDRIVILSTH 190
Cdd:COG4619 158 TSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-220 |
8.87e-42 |
|
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: 144.46 E-value: 8.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEG-DIHVCG-----INIdndREIRKII 77
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHwAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrggEDV---WELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GY----LPQDFsmYGNMSVYEAmdylgVLSGLSG---------PARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGI 144
Cdd:COG1119 81 GLvspaLQLRF--PRDETVLDV-----VLSGFFDsiglyreptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 145 AQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRI--VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAptLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-223 |
1.56e-41 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 152.59 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID-NDREIRKIIGYLPQ 82
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGeIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIATRRRVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:NF033858 347 AFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517427119 163 GLDPEERVRFRNLLSETA-KDRIVI-LSTHIVGdvEAT-CEDIAVLNRGCVLFQGTVTEL--------LEEA 223
Cdd:NF033858 427 GVDPVARDMFWRLLIELSrEDGVTIfISTHFMN--EAErCDRISLMHAGRVLASDTPAALvaargaatLEEA 496
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-208 |
3.42e-41 |
|
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: 140.21 E-value: 3.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG--KKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGY 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKvAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYgNMSVYEamdylgvlsglsgparkeripslleqvNLtddvktkvraMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:cd03228 81 VPQDPFLF-SGTIRE---------------------------NI----------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517427119 160 PTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEAtCEDIAVLNRG 208
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-220 |
7.46e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.45 E-value: 7.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKK----QALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIaTLLQK-TEGDIHVCGINID--NDREIRKI 76
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGeIFGIIGYSGAGKSTLIRCI-NLLERpTSGSVLVDGVDLTalSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 ---IGYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPK 153
Cdd:COG1135 81 rrkIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517427119 154 VLIVDEPTAGLDPEERVRFRNLLsetakDRI-------VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLL-----KDInrelgltIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVF 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
1.34e-40 |
|
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: 141.33 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN---DREIRKI 76
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGeIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlppHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQDFSMYGNMSVYEAM----------DYLGVLSGLSGPARKERIPS-----LLEQVNLTDDVKTKVRAMSGGMRRR 141
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVlvaaharlgrGLLAALLRLPRARREEREAReraeeLLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 142 LGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRI--VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTE 218
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGitILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.46e-40 |
|
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: 147.36 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTY--GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKT---EGDIHVCGINID--NDRE 72
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETvALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLelSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 73 IRKIIGYLPQDFSMYGNM-SVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHD 151
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNPvTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAG 225
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-221 |
2.16e-40 |
|
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: 148.83 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG--KKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGY 79
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERvAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYgNMSVYE--AMDYLGvlsglsgpARKERIPSLLEQVNLTDDVK-------TKV----RAMSGGMRRRLGIAQ 146
Cdd:COG2274 554 VLQDVFLF-SGTIREniTLGDPD--------ATDEEIIEAARLAGLHDFIEalpmgydTVVgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 147 ALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTH---IVGDveatCEDIAVLNRGCVLFQGTVTELLE 221
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRL----ADRIIVLDKGRIVEDGTHEELLA 698
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-223 |
2.33e-40 |
|
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: 140.71 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKK----QALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREIRKII 77
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGeSFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQDF--SMYGNMSVYEAMDYLGVLSGLsgPARKERIPSLLEQVNLTDDVKTK-VRAMSGGMRRRLGIAQALLHDPKV 154
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517427119 155 LIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEA 223
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
1.14e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.77 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID----NDREIrk 75
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGeFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglppEKRNV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 iiGYLPQDFSMYGNMSVYEAMDY-LGVLsGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKV 154
Cdd:COG3842 80 --GMVFQDYALFPHLTVAENVAFgLRMR-GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517427119 155 LIVDEPTAGLDPEERVRFRNLLSETAKDR-I-VILSTHivgDVE---ATCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELgItFIYVTH---DQEealALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-228 |
2.33e-39 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 137.79 E-value: 2.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN---DREIRKIIGYL 80
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGeIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlpmHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYE-AMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:TIGR04406 82 PQEASIFRKLTVEEnIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517427119 160 PTAGLDPEERVRFRNLLSETAKDRIVILST-HIVGDVEATCEDIAVLNRGCVLFQGTVTELLE-EAAGRIY 228
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVAnEKVRRVY 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-219 |
2.46e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 140.59 E-value: 2.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 3 TKIVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIdNDREIRKI-IGYL 80
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFlVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYEAMDY-LgVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:COG3839 81 FQSYALYPHMTVYENIAFpL-KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 160 PTAGLDPEERVRFRNLLSETAKDR--IVILSTHivgD-VEA-TCED-IAVLNRGCVLFQGTVTEL 219
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLgtTTIYVTH---DqVEAmTLADrIAVMNDGRIQQVGTPEEL 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-222 |
3.53e-39 |
|
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: 144.14 E-value: 3.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY--GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGY 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGeRVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQD---FsmygNMSVYE--------AMDylgvlsglsgparkERIPSLLEQVNLTDDVK-------TKV----RAMSGG 137
Cdd:COG4987 414 VPQRphlF----DTTLREnlrlarpdATD--------------EELWAALERVGLGDWLAalpdgldTWLgeggRRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 138 MRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEdIAVLNRGCVLFQGTVT 217
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDR-ILVLEDGRIVEQGTHE 554
|
....*
gi 517427119 218 ELLEE 222
Cdd:COG4987 555 ELLAQ 559
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-211 |
7.81e-39 |
|
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: 135.68 E-value: 7.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG----KKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIdndREIRKIIGY 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFvALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV---TGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYGNMSVYE-AMdyLGV-LSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:cd03293 78 VFQQDALLPWLTVLDnVA--LGLeLQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517427119 158 DEPTAGLDPEERVRFRNLLSETAKDRI--VILSTHivgDVEatcEDIAVLNRGCVL 211
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWRETGktVLLVTH---DID---EAVFLADRVVVL 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-210 |
8.54e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 142.09 E-value: 8.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDRE-IRKI 76
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGeIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDaIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQDFSMYGNMSVYE--AMDYLGVLSGLSGPAR-KERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPK 153
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAEniVLGLEPTKGGRLDRKAaRARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 154 VLIVDEPTAGLDPEERVR-FRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCV 210
Cdd:COG3845 162 ILILDEPTAVLTPQEADElFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-222 |
1.89e-38 |
|
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: 142.20 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREIRKIIGYL 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGeRVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDldPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQD---FsmygNMSVYEAMDylgvlsgLSGP-ARKERIPSLLEQVNLTDDVK-------TKV----RAMSGGMRRRLGIA 145
Cdd:COG4988 417 PQNpylF----AGTIRENLR-------LGRPdASDEELEAALEAAGLDEFVAalpdgldTPLgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 146 QALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEAtCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-219 |
3.31e-37 |
|
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: 131.92 E-value: 3.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLL-----QKTEGDIHVCGINIDNDR----EIR 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEiTALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDvdvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQDFSMYgNMSVYEAMDYLGVLSG-LSGPARKERIPSLLEQVNLTDDVK--TKVRAMSGGMRRRLGIAQALLHD 151
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-221 |
6.91e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 134.12 E-value: 6.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKI-IGYLPQ 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGeLVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERrVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDY-LGVLsGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPT 161
Cdd:COG1118 83 HYALFPHMTVAENIAFgLRVR-PPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 162 AGLD----PEERVRFRNLLSETakDRIVILSTHivgDVE---ATCEDIAVLNRGCVLFQGTVTELLE 221
Cdd:COG1118 162 GALDakvrKELRRWLRRLHDEL--GGTTVFVTH---DQEealELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-220 |
7.93e-37 |
|
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: 131.27 E-value: 7.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGK-KQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGYL 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFlVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLtDDVKTKVR---AMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGL-DPAEFADRyphELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 158 DEPTAGLDPEERVR----FRNLLSETAKdrIVILSTHivgDV-EATC--EDIAVLNRGCVLFQGTVTELL 220
Cdd:cd03295 160 DEPFGALDPITRDQlqeeFKRLQQELGK--TIVFVTH---DIdEAFRlaDRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-224 |
2.10e-35 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 134.87 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATL--LQktEGDIHVCGINIDNDREIRKI---IG 78
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGcMVGLIGPDGVGKSSLLSLIAGArkIQ--QGRVEVLGGDMADARHRRAVcprIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDF--SMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLI 156
Cdd:NF033858 80 YMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 157 VDEPTAGLDPEERVRFRNLLsetakDRI--------VILSTHIVGdvEATCED-IAVLNRGCVLFQGTVTELLEEAA 224
Cdd:NF033858 160 LDEPTTGVDPLSRRQFWELI-----DRIraerpgmsVLVATAYME--EAERFDwLVAMDAGRVLATGTPAELLARTG 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-226 |
2.32e-35 |
|
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: 126.97 E-value: 2.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGYLPQD 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFfTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAG 163
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 164 LDPEER----VRFRNLLSETAKdrIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAGR 226
Cdd:cd03300 161 LDLKLRkdmqLELKRLQKELGI--TFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-222 |
3.25e-35 |
|
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: 126.39 E-value: 3.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN---DREIRKIIGYLPQ 82
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGeIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppHERARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDyLGvLSGLSGPARKERIPSLLEQV-NLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPT 161
Cdd:cd03224 83 GRRIFPELTVEENLL-LG-AYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517427119 162 AGLDP--EERVrFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:cd03224 161 EGLAPkiVEEI-FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-214 |
1.06e-34 |
|
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: 125.08 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 16 KKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQK---TEGDIHVCGINIDNDrEIRKIIGYLPQDFSMYGNMS 91
Cdd:cd03234 19 YARILNDVSLHVESGqVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPD-QFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 92 VYEAMDYLGVLSG---LSGPARKERIP-SLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPE 167
Cdd:cd03234 98 VRETLTYTAILRLprkSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517427119 168 ERVRFRNLLSETAK-DRIVILSTHIVG-DVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03234 178 TALNLVSTLSQLARrNRIVILTIHQPRsDLFRLFDRILLLSSGEIVYSG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-205 |
1.25e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDREIRKI- 76
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGeVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQDFSMYGNMSVYEAMdYLGVLSGLSG----PARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDP 152
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENI-FLGREPRRGGlidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517427119 153 KVLIVDEPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVL 205
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRlKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-224 |
5.83e-34 |
|
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: 125.55 E-value: 5.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTY----GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQK---TEGDIHVCGINIDN--DREIRKI 76
Cdd:COG0444 4 VRNLKVYFptrrGVVKAVDGVSFDVRRGeTLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 ----IGYLPQDFSMYGN--MSVY----EAMDYLGvlsGLSGPARKERIPSLLEQVNLTDDVKTKVR---AMSGGMRRRLG 143
Cdd:COG0444 84 rgreIQMIFQDPMTSLNpvMTVGdqiaEPLRIHG---GLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 144 IAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRI--VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLE 221
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGlaILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
...
gi 517427119 222 EAA 224
Cdd:COG0444 241 NPR 243
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-210 |
6.03e-34 |
|
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: 121.38 E-value: 6.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDRE-IRKIIGYL 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGeVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRDaRRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQdfsmygnmsvyeamdylgvlsglsgparkeripslleqvnltddvktkvraMSGGMRRRLGIAQALLHDPKVLIVDEP 160
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517427119 161 TAGLDPEERVRFRNLLSETAKDRI-VILSTHIVGDVEATCEDIAVLNRGCV 210
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVaVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-167 |
3.14e-33 |
|
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: 121.10 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR----EIRKIIGY 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkninELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYGNMSVYE-AMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLEnITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
....*....
gi 517427119 159 EPTAGLDPE 167
Cdd:cd03262 161 EPTSALDPE 169
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-235 |
6.94e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 120.77 E-value: 6.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIhvcgiNIDND--------REIRK 75
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGeIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI-----IIDDEdisllplhARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 IIGYLPQDFSMYGNMSVYE-AMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKV 154
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDnLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 155 LIVDEPTAGLDPEERVRFRNLLsETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL-EEAAGRIYSAQ 231
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRII-EHLRDSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILqDEHVKRVYLGE 237
|
....
gi 517427119 232 VSRM 235
Cdd:PRK10895 238 DFRL 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-221 |
1.04e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.56 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVcGINIDndreirkiIGYLPQD 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDrIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------IGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 F-SMYGNMSVYEAMdylgvlSGLSGPARKERIPSLLEQVNLT-DDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPT 161
Cdd:COG0488 387 QeELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 162 AGLDPEERVRFRNLLSE---TakdriVILSTHivgD---VEATCEDI-AVLNRGCVLFQGTVTELLE 221
Cdd:COG0488 461 NHLDIETLEALEEALDDfpgT-----VLLVSH---DryfLDRVATRIlEFEDGGVREYPGGYDDYLE 519
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-208 |
1.30e-32 |
|
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: 119.28 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID----NDREIRKIIgy 79
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFvVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdlppKDRDIAMVF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 lpQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:cd03301 79 --QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517427119 160 PTAGLDPEERVRFRNLLSETAK--DRIVILSTHivGDVEA-TCED-IAVLNRG 208
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTH--DQVEAmTMADrIAVMNDG 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-214 |
1.68e-32 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 118.42 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKT------YGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIA--TLLQKTEGDIHVCGINIDnDREIRK 75
Cdd:cd03213 4 LSFRNLTVTvksspsKSGKQLLKNVSGKAKPGeLTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD-KRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 IIGYLPQDFSMYGNMSVYEAMDYLGVLSGLsgparkeripslleqvnltddvktkvramSGGMRRRLGIAQALLHDPKVL 155
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517427119 156 IVDEPTAGLDPEERVRFRNLLSETAKD-RIVILSTHIV-GDVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-228 |
3.67e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 124.89 E-value: 3.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGYL 80
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGeTVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdlTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYgNMSVYEAMDYlgvlsGLSGpARKERIPSLLEQVNLTDDVK-------TKV----RAMSGGMRRRLGIAQALL 149
Cdd:COG1132 420 PQDTFLF-SGTIRENIRY-----GRPD-ATDEEVEEAAKAAQAHEFIEalpdgydTVVgergVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 150 HDPKVLIVDEPTAGLDPE-ERVRFRNlLSETAKDRIVILSTHIVgdveATCED---IAVLNRGCVLFQGTVTELLeeAAG 225
Cdd:COG1132 493 KDPPILILDEATSALDTEtEALIQEA-LERLMKGRTTIVIAHRL----STIRNadrILVLDDGRIVEQGTHEELL--ARG 565
|
...
gi 517427119 226 RIY 228
Cdd:COG1132 566 GLY 568
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-221 |
6.47e-32 |
|
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: 118.21 E-value: 6.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQaLKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGYLPQD 83
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGdYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAG 163
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 164 LDPEERVRFRNLLSETAK--DRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLE 221
Cdd:cd03299 160 LDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-165 |
9.49e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.25 E-value: 9.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVcginidnDREIRkiIGYLPQDFS 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDrIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------PKGLR--IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 86 MYGNMSVYEAmdylgVLSGLSGPARKE-------------------------------------RIPSLLEQVNLT-DDV 127
Cdd:COG0488 72 LDDDLTVLDT-----VLDGDAELRALEaeleeleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPeEDL 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 517427119 128 KTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-223 |
1.02e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.00 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGK-----KQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID----NDREIR 74
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFvGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQ--DFSMYGNmSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLT-DDVKTKVR-AMSGGMRRRLGIAQALLH 150
Cdd:PRK13637 83 KKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPfELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 151 DPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEA 223
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEV 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-236 |
1.04e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 118.58 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLL---QKTEGDIHVCGINIDND----RE 72
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGeMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREgrlaRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 73 IRKI---IGYLPQDFSMYGNMSVYEamdylGVLSGLSG-------------PARKERIPSLLEQVNLTDDVKTKVRAMSG 136
Cdd:PRK09984 81 IRKSranTGYIFQQFNLVNRLSVLE-----NVLIGALGstpfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 137 GMRRRLGIAQALLHDPKVLIVDEPTAGLDPEE-RVRFRNLLSETAKDRI-VILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESaRIVMDTLRDINQNDGItVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
250 260
....*....|....*....|..
gi 517427119 215 TVTELLEEAAGRIYSAqVSRME 236
Cdd:PRK09984 236 SSQQFDNERFDHLYRS-INRVE 256
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-221 |
1.49e-31 |
|
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: 117.44 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGYLPQD 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGeLVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVYEAMDY-LGVLSGLSGPAR---KERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:cd03296 83 YALFRHMTVFDNVAFgLRVKPRSERPPEaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 160 PTAGLDPEERVRFRNLLSETaKDRIVILSTHIVGDVEATCE---DIAVLNRGCVLFQGTVTELLE 221
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRL-HDELHVTTVFVTHDQEEALEvadRVVVMNKGRIEQVGTPDEVYD 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-167 |
1.63e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.02 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-DNDREIRKI---IGY 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGeVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtDSKKDINKLrrkVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYGNMSVYE-AMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVD 158
Cdd:COG1126 82 VFQQFNLFPHLTVLEnVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
....*....
gi 517427119 159 EPTAGLDPE 167
Cdd:COG1126 162 EPTSALDPE 170
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-208 |
1.85e-31 |
|
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: 116.35 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKK-QALKHVDLTIHKGMFG-LLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREI---RKII 77
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVfLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrGRAIpylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517427119 158 DEPTAGLDPEERVRFRNLLSETAK-DRIVILSTHIVGDVEATCEDIAVLNRG 208
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-205 |
3.25e-31 |
|
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: 115.43 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQ-ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNdREIRKIIGYLPQD- 83
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGeIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KERRKSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 -FSMYGNmSVYEAMDylgvLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:cd03226 81 dYQLFTD-SVREELL----LGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517427119 163 GLDPEERVRFRNLLSE-TAKDRIVILSTHivgDVE--ATCEDIAVL 205
Cdd:cd03226 156 GLDYKNMERVGELIRElAAQGKAVIVITH---DYEflAKVCDRVLL 198
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-218 |
3.67e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 116.37 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRkI----IGYLP 81
Cdd:COG4674 13 VEDLTVSFDGFKALNDLSLYVDPGeLRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHE-IarlgIGRKF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 QDFSMYGNMSVYEAMD-----YLGVLSGLS---GPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPK 153
Cdd:COG4674 92 QKPTVFEELTVFENLElalkgDRGVFASLFarlTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 154 VLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTE 218
Cdd:COG4674 172 LLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDE 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-220 |
1.86e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 114.62 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 3 TKIVIKNLSKTYGKKQALKHVDLTI-HKGMFGLLGPNGAGKTTLMKIIATLLQ-----KTEGDIHVCGINI--DNDREIR 74
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIpDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIfkMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARK--ERIPSLLEQVNLTDDVKTKVRA----MSGGMRRRLGIAQAL 148
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517427119 149 LHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-190 |
3.02e-30 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 114.36 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLL-----QKTEGDIHVCGINIDNDR--- 71
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKvTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDIYDPDvdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 72 -EIRKIIGYLPQD---FSMygnmSVYEAMDYlGV-LSGLSGPAR-KERIPSLLEQVNLTDDVKTKVR----AMSGGMRRR 141
Cdd:COG1117 88 vELRRRVGMVFQKpnpFPK----SIYDNVAY-GLrLHGIKSKSElDEIVEESLRKAALWDEVKDRLKksalGLSGGQQQR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517427119 142 LGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTH 190
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTH 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-220 |
4.37e-30 |
|
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: 114.06 E-value: 4.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY--GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND---REIRKIIG 78
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFvAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEenlWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQD---------------FSMYgNMSV-YEAMdylgvlsglsgparKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRL 142
Cdd:TIGR04520 81 MVFQNpdnqfvgatveddvaFGLE-NLGVpREEM--------------RKRVDEALKLVGMEDFRDREPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 143 GIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHivgDVE--ATCEDIAVLNRGCVLFQGTVTE 218
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITH---DMEeaVLADRVIVMNKGKIVAEGTPRE 222
|
..
gi 517427119 219 LL 220
Cdd:TIGR04520 223 IF 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-166 |
6.57e-30 |
|
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: 6.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN---DREIRKIIGYLPQ 82
Cdd:COG0410 6 VENLHAGYGGIHVLHGVSLEVEEGeIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlppHRIARLGIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMdylgvLSGLSGPARKERIPSLLEQV-----NLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:COG0410 86 GRRIFPSLTVEENL-----LLGAYARRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
....*....
gi 517427119 158 DEPTAGLDP 166
Cdd:COG0410 161 DEPSLGLAP 169
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-226 |
9.16e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.20 E-value: 9.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIdNDREIR-KIIGYLPQ 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGtMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQqRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 163 GLDPEERVRFRNLLSETAKdRIVILS---THIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAGR 226
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQ-QFNITSlyvTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
1.88e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 111.71 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTY----------------------GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTE 57
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGeSVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 58 GDIHVCGinidndrEIRKIIGylpqdFS--MYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMS 135
Cdd:COG1134 81 GRVEVNG-------RVSALLE-----LGagFHPELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 136 GGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRElRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDG 228
|
....*...
gi 517427119 215 TVTELLEE 222
Cdd:COG1134 229 DPEEVIAA 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-215 |
2.51e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.64 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--------INIDNDREIRK 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGeTLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 IIGYLPQDFSMYGNMSVyeaMDYL-----GVLsGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLH 150
Cdd:COG4161 83 KVGMVFQQYNLWPHLTV---MENLieapcKVL-GLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 151 DPKVLIVDEPTAGLDPE---ERVRFRNLLSETAKDRIVIlsTHIVGDVEATCEDIAVLNRGCVLFQGT 215
Cdd:COG4161 159 EPQVLLFDEPTAALDPEitaQVVEIIRELSQTGITQVIV--THEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-215 |
4.59e-29 |
|
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: 116.65 E-value: 4.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGK--KQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDRE-IRKIIGYL 80
Cdd:TIGR01257 929 VCVKNLVKIFEPsgRPAVDRLNITFYENQItAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDaVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEP 160
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 161 TAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGT 215
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-214 |
4.72e-29 |
|
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: 110.08 E-value: 4.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 23 VDLTIHKGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG-------INIDNDREIRKIiGYLPQDFSMYGNMSVYEA 95
Cdd:cd03297 17 IDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQRKI-GLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 96 MDYlgVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNL 175
Cdd:cd03297 96 LAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517427119 176 LSETAKD--RIVILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03297 174 LKQIKKNlnIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-249 |
4.95e-29 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 115.91 E-value: 4.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 15 GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQK---TEGDIHVCGINIDNdREIRKIIGYLPQDFSMYGNM 90
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGeLLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDA-KEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 91 SVYEAMDYLGVL---SGLSGPARKERIPSLLEQVNLTDDVKTK------VRAMSGGMRRRLGIAQALLHDPKVLIVDEPT 161
Cdd:TIGR00955 115 TVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 162 AGLDPEERVRFRNLLSETA-KDRIVILSTHivgdvEATCE------DIAVLNRGCVLFQGTVTEL--------------- 219
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAqKGKTIICTIH-----QPSSElfelfdKIILMAEGRVAYLGSPDQAvpffsdlghpcpeny 269
|
250 260 270
....*....|....*....|....*....|....*.
gi 517427119 220 ------LEEAAGRIYSAQVSRMELESIRDHYTVTSM 249
Cdd:TIGR00955 270 npadfyVQVLAVIPGSENESRERIEKICDSFAVSDI 305
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-224 |
6.87e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 110.23 E-value: 6.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGkkQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGYLPQD 83
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRFDLTIAAGERvAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVYEAMdYLGVLSGLS-GPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:COG3840 80 NNLFPHLTVAQNI-GLGLRPGLKlTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517427119 163 GLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAA 224
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-190 |
1.19e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.93 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTI-HKGMFGLLGPNGAGKTTLMKIIATLLQ-----KTEGDIHVCGINIDNDR--- 71
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIpQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDvdp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 72 -EIRKIIGYLPQDFSMYGNMSVYEAMDyLGV-LSGLSGPARK--ERIPSLLEQVNLTDDVKTKVR----AMSGGMRRRLG 143
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFPHLTIYDNVA-IGVkLNGLVKSKKEldERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517427119 144 IAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTH 190
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-220 |
1.31e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 113.01 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREIRKIIGYLP 81
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLvGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlsARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 QDFSMYGNMSVYEAMD-----YLGVLSGLsGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLI 156
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEmgrtpHRSRFDTW-TETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 157 VDEPTAGLDPEERVRFRNLLSETAKD-RIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-214 |
2.67e-28 |
|
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: 108.06 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTY--GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIG 78
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGeKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSM-YGnmSVYEAMDyLGVLSglsgpARKERIPSLLEQVNLTDDVKT-----------KVRAMSGGMRRRLGIAQ 146
Cdd:cd03245 82 YVPQDVTLfYG--TLRDNIT-LGAPL-----ADDERILRAAELAGVTDFVNKhpngldlqigeRGRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 147 ALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGdVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-218 |
3.12e-28 |
|
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: 108.00 E-value: 3.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGinidndreirKIIGYLPQ 82
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGeRIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:cd03220 92 GGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 163 GLDPEER----VRFRNLLSetaKDRIVILSTHIVGDVEATCediavlNRGCVLFQGTVTE 218
Cdd:cd03220 172 VGDAAFQekcqRRLRELLK---QGKTVILVSHDPSSIKRLC------DRALVLEKGKIRF 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-232 |
5.92e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 108.32 E-value: 5.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGYLP 81
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGeVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 QDFSMYGNMSVYE--AMdylGVLSGLSGPARKERIP-SLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALL------HDP 152
Cdd:PRK13548 83 QHSSLSFPFTVEEvvAM---GRAPHGLSRAEDDALVaAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 153 KVLIVDEPTAGLDPEERVRFRNLLSETAKDR----IVILstHivgDVEAT---CEDIAVLNRGCVLFQGTVTELL-EEAA 224
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHERglavIVVL--H---DLNLAaryADRIVLLHQGRLVADGTPAEVLtPETL 234
|
....*...
gi 517427119 225 GRIYSAQV 232
Cdd:PRK13548 235 RRVYGADV 242
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-197 |
8.16e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.80 E-value: 8.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQ---KTEGDIHVcginidNDREIRKI------ 76
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGeILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLL------NGRRLTALpaeqrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQDFSMYGNMSVYEAMDYlGVLSGLSGPARKERIPSLLEQVNLTD----DVKTkvraMSGGMRRRLGIAQALLHDP 152
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGfadrDPAT----LSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517427119 153 KVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEA 197
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFEQIRQRgiPALLVTHDEEDAPA 199
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-215 |
1.87e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.64 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID-----NDREIRKI-- 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGeTLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktpSDKAIRELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 -IGYLPQDFSMYGNMSVyeaMDYL-----GVLsGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLH 150
Cdd:PRK11124 83 nVGMVFQQYNLWPHLTV---QQNLieapcRVL-GLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 151 DPKVLIVDEPTAGLDPE---ERVRFRNLLSETAKDRIVIlsTHIVGDVEATCEDIAVLNRGCVLFQGT 215
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEitaQIVSIIRELAETGITQVIV--THEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-218 |
7.22e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 107.19 E-value: 7.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY----GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI---DND--REIR 74
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGeIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKelRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKV 154
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 155 LIVDEPTAGLDPEERVRFRNLLSETAKD---RIViLSTHIVGDVEATCEDIAVLNRGCVLFQGTVTE 218
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRElglTIV-LITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-229 |
1.37e-26 |
|
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: 104.23 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQ--ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIdndREI-----RKI 76
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGeTVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYtlaslRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQDFSMYgNMSVYEAMDYlgvlsGLSGPARkERIPSLLEQVNLTD---------DVKTKVRA--MSGGMRRRLGIA 145
Cdd:cd03251 78 IGLVSQDVFLF-NDTVAENIAY-----GRPGATR-EEVEEAARAANAHEfimelpegyDTVIGERGvkLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 146 QALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEaTCEDIAVLNRGCVLFQGTVTELLeeAAG 225
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIE-NADRIVVLEDGKIVERGTHEELL--AQG 227
|
....
gi 517427119 226 RIYS 229
Cdd:cd03251 228 GVYA 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
1.48e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTYGK-KQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR----EIRK 75
Cdd:PRK13636 3 DYILKVEELNYNYSDgTHALKGININIKKGeVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 IIGYLPQD-----FSMygnmSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLH 150
Cdd:PRK13636 83 SVGMVFQDpdnqlFSA----SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517427119 151 DPKVLIVDEPTAGLDPEERVRFRNLLSETAK--DRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-219 |
1.65e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.88 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GKKQALKHVDLTI-HKGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDREIRKIIGYL 80
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIApRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQD-----FSMygnmSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:PRK13652 84 FQNpddqiFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 156 IVDEPTAGLDPE---ERVRFRNLLSETAkDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:PRK13652 160 VLDEPTAGLDPQgvkELIDFLNDLPETY-GMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-235 |
1.66e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.43 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGYLP 81
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGeLTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 QDFSMYGNMSVYE--AMdylGVLSGLSGPARKERIPSL-LEQVNLTDDVKTKVRAMSGGMRRRLGIAQAL--LHD----- 151
Cdd:COG4559 82 QHSSLAFPFTVEEvvAL---GRAPHGSSAAQDRQIVREaLALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEpvdgg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSthIVGDVEAT---CEDIAVLNRGCVLFQGTVTELLEEAA-GRI 227
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVA--VLHDLNLAaqyADRILLLHQGRLVAQGTPEEVLTDELlERV 236
|
....*...
gi 517427119 228 YSAQVSRM 235
Cdd:COG4559 237 YGADLRVL 244
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-231 |
2.56e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.46 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGYLPQDFS 85
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGeIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 86 MYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 166 PEERvrfrnllsetakDRIVILSTHIVGDVEATC-------ED-------IAVLNRGCVLFQGTVTELLEEAAGRiYSAQ 231
Cdd:PRK11607 182 KKLR------------DRMQLEVVDILERVGVTCvmvthdqEEamtmagrIAIMNRGKFVQIGEPEEIYEHPTTR-YSAE 248
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-238 |
2.92e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.79 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGK----KQALKHVDLTIHKGMFG-LLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI---DNDReirki 76
Cdd:COG4525 4 LTVRHVSVRYPGggqpQPALQDVSLTIESGEFVvALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpGADR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 iGYLPQDFSMYGNMSVYEAMDyLGV-LSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVA-FGLrLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 156 IVDEPTAGLDPEERVRFRNLL----SETAKdrIVILSTHivgDVEATcediavlnrgcvLFQGTVTELLEEAAGRIysaq 231
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLldvwQRTGK--GVFLITH---SVEEA------------LFLATRLVVMSPGPGRI---- 215
|
....*..
gi 517427119 232 VSRMELE 238
Cdd:COG4525 216 VERLELD 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-169 |
2.97e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.25 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID----NDREIRKIIGY 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGeVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYGNMSVYEAMDYLGV-LSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVD 158
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170
....*....|.
gi 517427119 159 EPTAGLDPEER 169
Cdd:PRK09493 162 EPTSALDPELR 172
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-219 |
3.41e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.48 E-value: 3.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTYGK-----KQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND------R 71
Cdd:PRK13646 2 TIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYyAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyiR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 72 EIRKIIGYL--------------------PQDFsmygNMSVYEAmdylgvlsglsgparKERIPSLLEQVNLTDDVKTKV 131
Cdd:PRK13646 82 PVRKRIGMVfqfpesqlfedtvereiifgPKNF----KMNLDEV---------------KNYAHRLLMDLGFSRDVMSQS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 132 R-AMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSE--TAKDRIVILSTHIVGDVEATCEDIAVLNRG 208
Cdd:PRK13646 143 PfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
250
....*....|.
gi 517427119 209 CVLFQGTVTEL 219
Cdd:PRK13646 223 SIVSQTSPKEL 233
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-208 |
3.56e-26 |
|
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: 100.22 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVcGINIDndreirkiIGYLPQd 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGdRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK--------IGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 fsmygnmsvyeamdylgvlsglsgparkeripslleqvnltddvktkvraMSGGMRRRLGIAQALLHDPKVLIVDEPTAG 163
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517427119 164 LDPEERVRFRNLLSEtaKDRIVILSTHivgD---VEATCEDIAVLNRG 208
Cdd:cd03221 101 LDLESIEALEEALKE--YPGTVILVSH---DryfLDQVATKIIELEDG 143
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-192 |
4.73e-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: 101.35 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 15 GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR----EIRKIIGYLPQD-----F 84
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGeVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkgllERRQRVGLVFQDpddqlF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 85 SMygnmSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGL 164
Cdd:TIGR01166 83 AA----DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180
....*....|....*....|....*....
gi 517427119 165 DPEERVRFRNLLSE-TAKDRIVILSTHIV 192
Cdd:TIGR01166 159 DPAGREQMLAILRRlRAEGMTVVISTHDV 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-210 |
5.34e-26 |
|
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: 100.75 E-value: 5.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQA--LKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGY 79
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGeSLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDfsmygnmsvyeamDYLgvLSGlsgparkeripSLLEQVnltddvktkvraMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:cd03246 81 LPQD-------------DEL--FSG-----------SIAENI------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517427119 160 PTAGLDPE-ERVRFRNLLSETAKDRIVILSTHIVGdVEATCEDIAVLNRGCV 210
Cdd:cd03246 123 PNSHLDVEgERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-190 |
6.92e-26 |
|
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: 106.60 E-value: 6.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGYL 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGeRVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYgNMSVYEamdylGVLSGLSGPARKErIPSLLEQVNLTDDVK-------TKV----RAMSGGMRRRLGIAQALL 149
Cdd:TIGR02857 402 PQHPFLF-AGTIAE-----NIRLARPDASDAE-IREALERAGLDEFVAalpqgldTPIgeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517427119 150 HDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTH 190
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-226 |
7.43e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.78 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN----DREirkiIGY 79
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGqMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlharDRK----VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYGNMSVYEAMDY-LGVL---SGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFgLTVLprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 156 IVDEPTAGLDPEERVRFRNL---LSETAKDRIVILsTHivgDVEATCE---DIAVLNRGCVLFQGTVTELLEEAAGR 226
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWlrqLHEELKFTSVFV-TH---DQEEAMEvadRVVVMSQGNIEQAGTPDQVWREPATR 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-221 |
8.27e-26 |
|
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: 101.92 E-value: 8.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTY-GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIdNDREI---RKIIG 78
Cdd:cd03254 2 EIEFENVNFSYdEKKPVLKDINFSIKPGETvAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-RDISRkslRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYgNMSVYEAMDYlgvlsglSGP-ARKERIPSLLEQVN-------LTDDVKTKVR----AMSGGMRRRLGIAQ 146
Cdd:cd03254 81 VVLQDTFLF-SGTIMENIRL-------GRPnATDEEVIEAAKEAGahdfimkLPNGYDTVLGenggNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 147 ALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVgdveATCED---IAVLNRGCVLFQGTVTELLE 221
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL----STIKNadkILVLDDGKIIEEGTHDELLA 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-220 |
8.83e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.52 E-value: 8.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND----------REI 73
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGeVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkgliRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 74 RKIIGYLPQDFSMYGNMSVYEamdylGVLSG---LSGPARKE---RIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQA 147
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLE-----NIIEGpviVKGEPKEEataRARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517427119 148 LLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD-RIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-210 |
9.88e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.73 E-value: 9.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 3 TKIVIKNLSKTYGKKQALKHVDLTIHKGMFGL-LGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIdNDREIRKI-IGYL 80
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVfVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERgVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEP 160
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517427119 161 TAGLDPEERVRFRNLLSETAK--DRIVILSTHivGDVEA-TCED-IAVLNRGCV 210
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRLHKrlGRTMIYVTH--DQVEAmTLADkIVVLDAGRV 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-219 |
1.05e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.85 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 8 KNLSKTYGK-KQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR----EIRKIIGYLP 81
Cdd:PRK13639 5 RDLKYSYPDgTEALKGINFKAEKGeMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksllEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 Q--DFSMYGNmSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:PRK13639 85 QnpDDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517427119 160 PTAGLDPEERVRFRNLLSETAKDRI-VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:PRK13639 164 PTSGLDPMGASQIMKLLYDLNKEGItIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-214 |
1.05e-25 |
|
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: 100.08 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG--KKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN-DREIRKIIGYL 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEkIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDlEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNmsvyeamdylgvlsglsgparkeripSLLEQVNltddvktkvRAMSGGMRRRLGIAQALLHDPKVLIVDEP 160
Cdd:cd03247 81 NQRPYLFDT--------------------------TLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517427119 161 TAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATcEDIAVLNRGCVLFQG 214
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-249 |
1.08e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.40 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 3 TKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDREIRKIIGY 79
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGkITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYGNMSVYEAMDY--------LGVLSGlsgpARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHD 151
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYgrspwlslWGRLSA----EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAGRiysa 230
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRElNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLR---- 232
|
250
....*....|....*....
gi 517427119 231 QVSRMELESIRDHYTVTSM 249
Cdd:PRK11231 233 TVFDVEAEIHPEPVSGTPM 251
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-224 |
1.25e-25 |
|
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: 102.34 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQ------------------------ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGD 59
Cdd:cd03294 1 IKIKGLYKIFGKNPqkafkllakgkskeeilkktgqtvGVNDVSLDVREGeIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 60 IHVCGINID--NDREIRKI----IGYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRA 133
Cdd:cd03294 81 VLIDGQDIAamSRKELRELrrkkISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 134 MSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD--RIVILSTHIVGDVEATCEDIAVLNRGCVL 211
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElqKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250
....*....|...
gi 517427119 212 FQGTVTELLEEAA 224
Cdd:cd03294 241 QVGTPEEILTNPA 253
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-190 |
1.92e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.00 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 14 YGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGinidndreiRKIIGYLPQDFSMYGNM-- 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGsLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------GARVAYVPQRSEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 91 SVYEAMDyLGVLS--GLSGPARKE---RIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:NF040873 73 TVRDLVA-MGRWArrGLWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180
....*....|....*....|....*.
gi 517427119 166 PEERVRFRNLLSE-TAKDRIVILSTH 190
Cdd:NF040873 152 AESRERIIALLAEeHARGATVVVVTH 177
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
2.20e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGK-KQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDREIRKI 76
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGsKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGreVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQD-----FSMygnmSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHD 151
Cdd:PRK13647 81 VGLVFQDpddqvFSS----TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEA 223
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-220 |
2.85e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.20 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI----DND------ 70
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGdVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrDKDgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 71 -----REIRKIIGYLPQDFSMYGNMSVYE-AMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRA-MSGGMRRRLG 143
Cdd:PRK10619 83 dknqlRLLRTRLTMVFQHFNLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 144 IAQALLHDPKVLIVDEPTAGLDPE---ERVRFRNLLSETAKDRIVIlsTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVV--THEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
3.21e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDtkIVIKNLSKTYGKK-----QALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHV------CGINID 68
Cdd:PRK13634 1 MD--ITFQKVEHRYQYKtpferRALYDVNVSIPSGSYvAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 69 NDREIRKIIGYL--------------------PQDFSMygnmSVYEAmdylgvlsglsgparKERIPSLLEQVNLTDDVK 128
Cdd:PRK13634 79 KLKPLRKKVGIVfqfpehqlfeetvekdicfgPMNFGV----SEEDA---------------KQKAREMIELVGLPEELL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 129 TKVR-AMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVR----FRNLLSEtaKDRIVILSTHIVGDVEATCEDIA 203
Cdd:PRK13634 140 ARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEmmemFYKLHKE--KGLTTVLVTHSMEDAARYADQIV 217
|
250 260
....*....|....*....|.
gi 517427119 204 VLNRGCVLFQGTVTELLEEAA 224
Cdd:PRK13634 218 VMHKGTVFLQGTPREIFADPD 238
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-173 |
8.05e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.84 E-value: 8.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTY-GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN----DREIRKII 77
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFiVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepaDRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 gylpQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:PRK11650 83 ----QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170
....*....|....*.
gi 517427119 158 DEPTAGLDPEERVRFR 173
Cdd:PRK11650 159 DEPLSNLDAKLRVQMR 174
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-197 |
9.42e-25 |
|
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: 98.20 E-value: 9.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 8 KNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIR-KIIGYLPQDFS 85
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGeALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 86 MYGNMSVYEAMDYLgvlSGLSGPARKErIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:TIGR01189 84 LKPELSALENLHFW---AAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180 190
....*....|....*....|....*....|....
gi 517427119 166 PEERVRFRNLLSE-TAKDRIVILSTHI-VGDVEA 197
Cdd:TIGR01189 160 KAGVALLAGLLRAhLARGGIVLLTTHQdLGLVEA 193
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-208 |
9.96e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.79 E-value: 9.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREI---RKII 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGeMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlKNREVpflRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517427119 158 DEPTAGLDPEERVRFRNLLSETAKDRI-VILSTHIVGDVEATCEDIAVLNRG 208
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVtVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-166 |
1.03e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.78 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGK-----KQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIR--KI 76
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFvTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKraKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQDFSM--YGNMSVYE--AMDYL-----GVLSGLSgPARKERIPSLLEQVN--LTDDVKTKVRAMSGGMRRRLGIA 145
Cdd:COG1101 82 IGRVFQDPMMgtAPSMTIEEnlALAYRrgkrrGLRRGLT-KKRRELFRELLATLGlgLENRLDTKVGLLSGGQRQALSLL 160
|
170 180
....*....|....*....|.
gi 517427119 146 QALLHDPKVLIVDEPTAGLDP 166
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDP 181
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-214 |
1.98e-24 |
|
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: 97.95 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 22 HVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGYLPQDFSMYGNMSVYEAMDyLG 100
Cdd:cd03298 16 HFDLTFAQGeITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVG-LG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 101 VLSGLS-GPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSET 179
Cdd:cd03298 95 LSPGLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 517427119 180 AKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:cd03298 175 HAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
3.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.67 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQA--LKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDREIRKIIGY 79
Cdd:PRK13648 8 IVFKNVSFQYQSDASftLKDVSFNIPKGQWtSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQD---------------FSMYGNMSVYEAMdylgvlsglsgparKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGI 144
Cdd:PRK13648 88 VFQNpdnqfvgsivkydvaFGLENHAVPYDEM--------------HRRVSEALKQVDMLERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 145 AQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR-IVILS-THIVgdVEATCED-IAVLNRGCVLFQGTVTELLE 221
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHnITIISiTHDL--SEAMEADhVIVMNKGTVYKEGTPTEIFD 231
|
....
gi 517427119 222 EAAG 225
Cdd:PRK13648 232 HAEE 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-222 |
4.91e-24 |
|
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: 97.30 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG-KKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIdndREI-----RKII 77
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGkKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVtldslRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQDFSM----------YGNMS-----VYEAmdylgvlsglsgpARKERIPSLLEqvNLTDDVKTKV--RA--MSGGM 138
Cdd:cd03253 78 GVVPQDTVLfndtigynirYGRPDatdeeVIEA-------------AKAAQIHDKIM--RFPDGYDTIVgeRGlkLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 139 RRRLGIAQALLHDPKVLIVDEPTAGLDPE-ERVRFRNlLSETAKDRIVILSTHIVGDVeATCEDIAVLNRGCVLFQGTVT 217
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHtEREIQAA-LRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHE 220
|
....*
gi 517427119 218 ELLEE 222
Cdd:cd03253 221 ELLAK 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-190 |
1.43e-23 |
|
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: 100.13 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR--EIRKIIGYL 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGeRVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqdEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNmSVYEamdylGVLSGlSGPARKERIPSLLEQVNLTDDVK-------TKV----RAMSGGMRRRLGIAQALL 149
Cdd:TIGR02868 415 AQDAHLFDT-TVRE-----NLRLA-RPDATDEELWAALERVGLADWLRalpdgldTVLgeggARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517427119 150 HDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTH 190
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-229 |
3.01e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.13 E-value: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY--GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGY 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKvALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdySEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQdfsmygnmSVYeamdylgVLSG-------LSGP-ARKERIPSLLEQVNLTDDVKTKV----------RAMSGGMRRR 141
Cdd:PRK11160 419 VSQ--------RVH-------LFSAtlrdnllLAAPnASDEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 142 LGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATcEDIAVLNRGCVLFQGTVTELLE 221
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLA 562
|
....*...
gi 517427119 222 EaAGRIYS 229
Cdd:PRK11160 563 Q-QGRYYQ 569
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-224 |
4.94e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.33 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN----DREIRKIIgy 79
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFlTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaeNRHVNTVF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 lpQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:PRK09452 93 --QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 160 PTAGLDPEERVRFRNLLSETAKDRIV--ILSTHivgDVE---ATCEDIAVLNRGCVLFQGTVTELLEEAA 224
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGItfVFVTH---DQEealTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-190 |
9.71e-23 |
|
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: 93.65 E-value: 9.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY----GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN-DREIR---- 74
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESvAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAlDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 -KIIGYLPQDFSMYGNMSvyeAMDYLGV---LSGLSGPARKERipSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLH 150
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLT---ALENVMLpleLAGRRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517427119 151 DPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTH 190
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTH 205
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-219 |
1.13e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.16 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVcgINIDNDREIRKI-----IG 78
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGeIHALLGENGAGKSTLMKVLSGIHEPTKGTITI--NNINYNKLDHKLaaqlgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYGNMSVYEAMdYLGVLsglsgPARK-------------ERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIA 145
Cdd:PRK09700 84 IIYQELSVIDELTVLENL-YIGRH-----LTKKvcgvniidwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517427119 146 QALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD--RIVILStHIVGDVEATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgtAIVYIS-HKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-235 |
1.21e-22 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 95.96 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTtlmkiiatllqKTEGDIHVCGINID-----------NDRE 72
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGtVLGVLGP*GAA**-----------RGALPAHV*GPDAGrrpwrf*twcaNRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 73 IRKIIG-YLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHD 151
Cdd:NF000106 83 LRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSETAKD-RIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEAAGRI--- 227
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTlqi 242
|
250
....*....|.
gi 517427119 228 ---YSAQVSRM 235
Cdd:NF000106 243 rpaHAAELDRM 253
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-208 |
1.96e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.13 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG-----KKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID------NDRE 72
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFvALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 73 IRKIIGYLPQ--DFSMYGNmSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVR-AMSGGMRRRLGIAQALL 149
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 150 HDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD-RIVILSTHIVGDVEATCEDIAVLNRG 208
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-222 |
2.01e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.90 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG--KKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI--DNDREIRKIIGY 79
Cdd:PRK13632 8 IKVENVSFSYPnsENNALKNVSFEINEGEYvAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIskENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQD---------------FSMYGNMSVYEAMdylgvlsglsgparKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGI 144
Cdd:PRK13632 88 IFQNpdnqfigatveddiaFGLENKKVPPKKM--------------KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 145 AQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHivgDV-EATCED-IAVLNRGCVLFQGTVTELL 220
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITH---DMdEAILADkVIVFSEGKLIAQGKPKEIL 230
|
..
gi 517427119 221 EE 222
Cdd:PRK13632 231 NN 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-222 |
2.10e-22 |
|
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: 92.99 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKK---QALKHVDLTIHKGMF-GLLGPNGAGKTTlmkiIATLLQK----TEGDIHVCGINID--NDREIR 74
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTvALVGSSGCGKST----VVSLLERfydpTSGEILLDGVDIRdlNLRWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQDFSMYgNMSVYEAMDYlgvlsGLSGPARKERIpSLLEQVN-------LTDDVKTKVRA----MSGGMRRRLG 143
Cdd:cd03249 77 SQIGLVSQEPVLF-DGTIAENIRY-----GKPDATDEEVE-EAAKKANihdfimsLPDGYDTLVGErgsqLSGGQKQRIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 144 IAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEAtCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-238 |
2.52e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.23 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRkiiGYLPQDFS 85
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGeLLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 86 MYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 166 PEERVRFRNLL----SETAKDriVILSTHivgDVEATcediavlnrgcvLFQGTVTELLEEAAGRIysaqVSRMELE 238
Cdd:PRK11248 161 AFTREQMQTLLlklwQETGKQ--VLLITH---DIEEA------------VFMATELVLLSPGPGRV----VERLPLN 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-222 |
2.88e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.64 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 18 QALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND------REIRKIIGYLPQ-DFSMYGN 89
Cdd:PRK13643 20 RALFDIDLEVKKGSYtALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeiKPVRKKVGVVFQfPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 90 MSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVR-AMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEE 168
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 169 RVRFRNLLSETAKD-RIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:PRK13643 180 RIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-219 |
2.91e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREIRKIIGYL- 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGeVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltPAKAHQLGIYLv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYEamdylGVLSGLSGPAR-KERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:PRK15439 92 PQEPLLFPNLSVKE-----NILFGLPKRQAsMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517427119 160 PTAGLDPEERVR-FRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:PRK15439 167 PTASLTPAETERlFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-197 |
4.27e-22 |
|
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: 91.40 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 8 KNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR-EIRKIIGYLPQDFS 85
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGeALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdSIARGLLYLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 86 MYGNMSVYEAMDYLGVLSGlsgparKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:cd03231 84 IKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190
....*....|....*....|....*....|....
gi 517427119 166 PEERVRFRNLL-SETAKDRIVILSTHI-VGDVEA 197
Cdd:cd03231 158 KAGVARFAEAMaGHCARGGMVVLTTHQdLGLSEA 191
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-258 |
1.21e-21 |
|
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: 93.25 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 6 VIKNLSKTYGKKQaLKhVDLTIH-KGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREI------RKIIG 78
Cdd:TIGR02142 1 LSARFSKRLGDFS-LD-ADFTLPgQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiflppeKRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYGNMSVYEAMDYlgvlsGLS---GPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:TIGR02142 79 YVFQEARLFPHLSVRGNLRY-----GMKrarPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 156 IVDEPTAGLDPEERVR----FRNLLSETakdRI-VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL---------E 221
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEilpyLERLHAEF---GIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWaspdlpwlaR 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 517427119 222 EAAGRIYSAQVsrmelESIRDHYTVTSMMMQGNHASV 258
Cdd:TIGR02142 231 EDQGSLIEGVV-----AEHDQHYGLTALRLGGGHLWV 262
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-190 |
1.60e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.99 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIH-KGMFGLLGPNGAGKTTLMKIIATLLQ-----KTEGDIHVCGINIDNDR--- 71
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYpNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 72 -EIRKIIGYL---PQDFSMygnmSVYEAMDYLGVLSGLSGPAR-KERIPSLLEQVNLTDDVKTKVR----AMSGGMRRRL 142
Cdd:PRK14239 82 vDLRKEIGMVfqqPNPFPM----SIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDEVKDRLHdsalGLSGGQQQRV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517427119 143 GIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTH 190
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-191 |
1.72e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTYGKKQALKhvdltihkgmfgLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDReIRKIIGYL-PQ 82
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALV------------LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD-VAEACHYLgHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFsMYGNMSVYEAM----DYLGvlsglsgpARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVD 158
Cdd:PRK13539 82 NA-MKPALTVAENLefwaAFLG--------GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|....
gi 517427119 159 EPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHI 191
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-222 |
1.89e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.69 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTYGKK-----QALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND------- 70
Cdd:PRK13651 2 QIKVKNIVKIFNKKlptelKALDNVSVEINQGEFiAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 71 -------------------REIRKIIGYLPQdFSMYgnmSVYEAM---DYL-GVLS-GLSGPARKERIPSLLEQVNLTDD 126
Cdd:PRK13651 82 kvleklviqktrfkkikkiKEIRRRVGVVFQ-FAEY---QLFEQTiekDIIfGPVSmGVSKEEAKKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 127 -VKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD-RIVILSTHIVGDVEATCEDIAV 204
Cdd:PRK13651 158 yLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIF 237
|
250
....*....|....*...
gi 517427119 205 LNRGCVLFQGTVTELLEE 222
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD 255
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-190 |
2.10e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 22 HVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREirkiigylpqDFsmygnmsvYEAMDYLG 100
Cdd:PRK13538 19 GLSFTLNAGeLVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD----------EY--------HQDLLYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 101 VLSG----------------LSGPARKERIPSLLEQVNL--TDDVktKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:PRK13538 81 HQPGikteltalenlrfyqrLHGPGDDEALWEALAQVGLagFEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*....
gi 517427119 163 GLDPEERVRFRNLLSE-TAKDRIVILSTH 190
Cdd:PRK13538 159 AIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-221 |
2.14e-21 |
|
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: 93.60 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 10 LSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKiiATL-LQKTEGDIHVCGINID--NDREIRKiigyLPQDFS 85
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGeTLGLVGESGSGKSTLGL--ALLrLIPSEGEIRFDGQDLDglSRRALRP----LRRRMQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 86 M-----YGNMS--------VYEAMDYLGVlsGLSGPARKERIPSLLEQVNLTDDVKTK-VRAMSGGMRRRLGIAQALLHD 151
Cdd:COG4172 366 VvfqdpFGSLSprmtvgqiIAEGLRVHGP--GLSAAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSETAKDR----IVIlsTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLE 221
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDLQREHglayLFI--SHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-224 |
2.31e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.79 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGK--KQALKHVD----------------------LTIHKG-MFGLLGPNGAGKTTLMKIIATLLQK 55
Cdd:PRK10070 1 MAIKLEIKNLYKIFGEhpQRAFKYIEqglskeqilektglslgvkdasLAIEEGeIFVIMGLSGSGKSTMVRLLNRLIEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 56 TEGDIHVCGINID--NDREIRKI----IGYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKT 129
Cdd:PRK10070 81 TRGQVLIDGVDIAkiSDAELREVrrkkIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 130 KVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLS--ETAKDRIVILSTHIVGDVEATCEDIAVLNR 207
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVklQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
250
....*....|....*..
gi 517427119 208 GCVLFQGTVTELLEEAA 224
Cdd:PRK10070 241 GEVVQVGTPDEILNNPA 257
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-219 |
2.80e-21 |
|
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: 93.92 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 32 FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-DNDREIRKIIGYLPQDFSMYGNMSVYEAMDYLGVLSGLsgPAR 110
Cdd:TIGR01257 1968 FGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGV--PAE 2045
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 111 K-ERIPSL-LEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRN-LLSETAKDRIVIL 187
Cdd:TIGR01257 2046 EiEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNtIVSIIREGRAVVL 2125
|
170 180 190
....*....|....*....|....*....|..
gi 517427119 188 STHIVGDVEATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:TIGR01257 2126 TSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-220 |
3.58e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.84 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKK-----QALKHVDLTIHKGMFG-LLGPNGAGKTTLMKIIATLL-----QKTEGDIHV-CGIN-IDNDR 71
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTcVIGTTGSGKSTMIQLTNGLIisetgQTIVGDYAIpANLKkIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 72 EIRKIIGYLPQ--DFSMYGNmSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDD-VKTKVRAMSGGMRRRLGIAQAL 148
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 149 LHDPKVLIVDEPTAGLDPEERVRFRNL---LSETAKDRIvILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRI-IMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-221 |
4.10e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.46 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTY--GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGI--NIDNDREIRK 75
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWvAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 IIGYLPQ--DFSMYGNmSVYEamdylGVLSGL--SGPARKE---RIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQAL 148
Cdd:PRK13635 82 QVGMVFQnpDNQFVGA-TVQD-----DVAFGLenIGVPREEmveRVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 149 LHDPKVLIVDEPTAGLDPEERVR----FRNLLSETakdRIVILS-THivgDVE--ATCEDIAVLNRGCVLFQGTVTELLE 221
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREvletVRQLKEQK---GITVLSiTH---DLDeaAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-228 |
5.74e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 89.37 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREIRKIIGYLP 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGItALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtpSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 QDFSMYGNMSVYEamdyL----------GVLSglsgPARKERIPSLLEQVNLTD------DvktkvrAMSGGMRRRLGIA 145
Cdd:COG4604 82 QENHINSRLTVRE----LvafgrfpyskGRLT----AEDREIIDEAIAYLDLEDladrylD------ELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 146 QALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD--RIVILSTHivgDVE-ATC--EDIAVLNRGCVLFQGTVTELL 220
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLH---DINfASCyaDHIVAMKDGRVVAQGTPEEII 224
|
....*....
gi 517427119 221 EEAA-GRIY 228
Cdd:COG4604 225 TPEVlSDIY 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-215 |
8.60e-21 |
|
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: 88.32 E-value: 8.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTY--GKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIG 78
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEkVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkiGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQD---FSmyGnmSVYEAMDYLGVLSglsgparKERIPSLLEQVNLTDDVKTKVRAM-----------SGGMRRRLGI 144
Cdd:cd03244 82 IIPQDpvlFS--G--TIRSNLDPFGEYS-------DEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517427119 145 AQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVeATCEDIAVLNRGCVLFQGT 215
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVVEFDS 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-165 |
9.95e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 90.18 E-value: 9.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKK-----------QALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--ND 70
Cdd:COG4608 8 LEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGeTLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITglSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 71 REIRKiigyLPQDFSM-----YG--N--MSVY----EAMDYLGVLSGlsgPARKERIPSLLEQVNLTDDVKTKVRAM-SG 136
Cdd:COG4608 88 RELRP----LRRRMQMvfqdpYAslNprMTVGdiiaEPLRIHGLASK---AERRERVAELLELVGLRPEHADRYPHEfSG 160
|
170 180
....*....|....*....|....*....
gi 517427119 137 GMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-221 |
1.36e-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: 91.28 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIV--IKNLSKTYGK----KQALKHVDLTIHKG-MFGLLGPNGAGKT----TLMKIIATLLQKTEGDIHVCGINIDN 69
Cdd:COG4172 1 MMSMPLlsVEDLSVAFGQgggtVEAVKGVSFDIAAGeTLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 70 --DREIRKIIGylpQDFSMygnmsVY-EAMDYLG-----------VLS---GLSGPARKERIPSLLEQVNLTDDvKTKVR 132
Cdd:COG4172 81 lsERELRRIRG---NRIAM-----IFqEPMTSLNplhtigkqiaeVLRlhrGLSGAAARARALELLERVGIPDP-ERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 133 A----MSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLN 206
Cdd:COG4172 152 AyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFADRVAVMR 231
|
250
....*....|....*
gi 517427119 207 RGCVLFQGTVTELLE 221
Cdd:COG4172 232 QGEIVEQGPTAELFA 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-222 |
1.43e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 91.71 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTY---GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIR 74
Cdd:TIGR00958 475 LEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGeVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqyDHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQDFSMYGNmSVYEAMDYlgvlsGLSgPARKERIPSLLEQVNLTD-----------DVKTKVRAMSGGMRRRLG 143
Cdd:TIGR00958 555 RQVALVGQEPVLFSG-SVRENIAY-----GLT-DTPDEEIMAAAKAANAHDfimefpngydtEVGEKGSQLSGGQKQRIA 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 144 IAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSetAKDRIVILSTHIVGDVEaTCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMED 703
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-190 |
1.47e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.69 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQ-----KTEGDIHVCGINIDNDR---- 71
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNqITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDvdpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 72 EIRKIIGYL---PQDFSMygnmSVYEAMDYLGVLSGLSGPArKERIPSLLEQVNLTDDVKTKVR----AMSGGMRRRLGI 144
Cdd:PRK14243 88 EVRRRIGMVfqkPNPFPK----SIYDNIAYGARINGYKGDM-DELVERSLRQAALWDEVKDKLKqsglSLSGGQQQRLCI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517427119 145 AQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTH 190
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-192 |
2.30e-20 |
|
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: 87.14 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 20 LKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGylpQDFSMYGNMSVYE--AM 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFiSLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF---QNYSLLPWLTVREniAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 97 DYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLL 176
Cdd:TIGR01184 78 AVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170
....*....|....*...
gi 517427119 177 SETAKDR--IVILSTHIV 192
Cdd:TIGR01184 158 MQIWEEHrvTVLMVTHDV 175
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-222 |
3.06e-20 |
|
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: 90.25 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-----GKKQALKHVDLTI-HKGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHV---------CGINIDN 69
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVkEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 70 DREIRKIIGYLPQDFSMYGNMSVyeaMDYLGVLSGLSGPARKERIPSL--LEQVNLTDDVKTKV-----RAMSGGMRRRL 142
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPHRTV---LDNLTEAIGLELPDELARMKAVitLKMVGFDEEKAEEIldkypDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 143 GIAQALLHDPKVLIVDEPTAGLDPEERVRFRN--LLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsiLKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
..
gi 517427119 221 EE 222
Cdd:TIGR03269 517 EE 518
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-207 |
5.19e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 3 TKIVIKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDRE-IRKIIgyl 80
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFvAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdTRLMF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 pQDFSMYGNMSVyeaMDYLGVlsGLSGPARKERIPSlLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEP 160
Cdd:PRK11247 88 -QDARLLPWKKV---IDNVGL--GLKGQWRDAALQA-LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517427119 161 TAGLDPEERVRFRNLLSETAKDR--IVILSTHivgDVEatcEDIAVLNR 207
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHgfTVLLVTH---DVS---EAVAMADR 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-234 |
5.66e-20 |
|
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: 88.23 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 23 VDLTIH-KGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG-INIDNDREI-----RKIIGYLPQDFSMYGNMSVYEA 95
Cdd:COG4148 18 VDFTLPgRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGeVLQDSARGIflpphRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 96 MDYlgVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPE-------- 167
Cdd:COG4148 98 LLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLArkaeilpy 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 168 -ERVRfrnllsetakDRI---VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL----------EEAAGRIYSAQVS 233
Cdd:COG4148 176 lERLR----------DELdipILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLsrpdllplagGEEAGSVLEATVA 245
|
.
gi 517427119 234 R 234
Cdd:COG4148 246 A 246
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-207 |
5.82e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 86.71 E-value: 5.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIhvcginidnDREIRKIIGY 79
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGkILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYGNM--SVYEAMDylgvlsgLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:PRK09544 72 VPQKLYLDTTLplTVNRFLR-------LRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517427119 158 DEPTAGLDPEERVRFRNLLSE--TAKDRIVILSTHIVGDVEATCEDIAVLNR 207
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQlrRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
34-238 |
1.61e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.28 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 34 LLGPNGAGKTTLMKIIATLLQkTEGDIHVCGINID--NDREIRKIIGYLPQDFSMYGNMSVYEAMDyLGVLSGLSGPARK 111
Cdd:COG4138 27 LIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSdwSAAELARHRAYLSQQQSPPFAMPVFQYLA-LHQPAGASSEAVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 112 ERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLH-------DPKVLIVDEPTAGLDPEERVRFRNLLSE-TAKDR 183
Cdd:COG4138 105 QLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRElCQQGI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 184 IVILSTHivgDVEATC---EDIAVLNRGCVLFQGTVTELLEEAA-GRIYSAQVSRMELE 238
Cdd:COG4138 185 TVVMSSH---DLNHTLrhaDRVWLLKQGKLVASGETAEVMTPENlSEVFGVKFRRLEVE 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-222 |
1.85e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.01 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTY--GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGD---IHVCGINIDNDR--EI 73
Cdd:PRK13640 3 DNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWtALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTvwDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 74 RKIIGYLPQ--DFSMYGnMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHD 151
Cdd:PRK13640 83 REKVGIVFQnpDNQFVG-ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVgDVEATCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDI-DEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-215 |
1.91e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.43 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREI-RKIIGYLPQ 82
Cdd:PRK11300 8 VSGLMMRFGGLLAVNNVNLEVREQeIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpGHQIaRMGVVRTFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAM-----DYL--GVLSGL-SGPA-RK------ERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQA 147
Cdd:PRK11300 88 HVRLFREMTVIENLlvaqhQQLktGLFSGLlKTPAfRRaesealDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 148 LLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGT 215
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-222 |
1.96e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGK------KQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGI---NIDND 70
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFlVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtsDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 71 REIRKIIGYLPQ--DFSMYGNMsVYEAMDY----LGVLSglsgPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGI 144
Cdd:PRK13633 81 WDIRNKAGMVFQnpDNQIVATI-VEEDVAFgpenLGIPP----EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 145 AQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVeATCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-222 |
1.98e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 87.79 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 15 GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN-DRE-IRKIIGYLPQDFSMY-GNM 90
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEAlAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDREtFGKHIGYLPQDVELFpGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 91 --------------SVYEAMDYLGVlsglsgparKERIpslleqVNLTDDVKTKV----RAMSGGMRRRLGIAQALLHDP 152
Cdd:TIGR01842 409 aeniarfgenadpeKIIEAAKLAGV---------HELI------LRLPDGYDTVIgpggATLSGGQRQRIALARALYGDP 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517427119 153 KVLIVDEPTAGLDPEERVRFRN-LLSETAKDRIVILSTHIVGDVEatCED-IAVLNRGCVLFQGTVTELLEE 222
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANaIKALKARGITVVVITHRPSLLG--CVDkILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-208 |
2.31e-19 |
|
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: 83.25 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKtygkKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDRE-IRKIIGYLPQ 82
Cdd:cd03215 7 VRGLSV----KGAVRDVSFEVRAGeIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDaIRAGIAYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYG---NMSVYEAMdylgvlsglsgparkeRIPSLLeqvnltddvktkvramSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:cd03215 83 DRKREGlvlDLSVAENI----------------ALSSLL----------------SGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517427119 160 PTAGLDPEERVRFRNLLSETAKDR--IVILSThivgDVE---ATCEDIAVLNRG 208
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADAGkaVLLISS----ELDellGLCDRILVMYEG 180
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-222 |
2.79e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.18 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG-----KKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND------RE 72
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYtAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 73 IRKIIGYLPQdfsmYGNMSVYEAMdylgVLSGLS-GP----ARKERIPSL----LEQVNLTDDVKTKVR-AMSGGMRRRL 142
Cdd:PRK13649 83 IRKKVGLVFQ----FPESQLFEET----VLKDVAfGPqnfgVSQEEAEALarekLALVGISESLFEKNPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 143 GIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVI-LSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLE 221
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIvLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
.
gi 517427119 222 E 222
Cdd:PRK13649 235 D 235
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-228 |
3.32e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 8 KNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREIRKIIGYLPQDF 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFtAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 85 SMYGNMSVYEAmdylgVLSG------LSGPARKE---RIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:PRK10253 91 TTPGDITVQEL-----VARGryphqpLFTRWRKEdeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 156 IVDEPTAGLDPEERVRFRNLLSETAKDRIVILSThIVGDVEATCE---DIAVLNRGCVLFQGTVTELLE-EAAGRIY 228
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAA-VLHDLNQACRyasHLIALREGKIVAQGAPKEIVTaELIERIY 241
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-183 |
3.81e-19 |
|
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: 84.02 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTY------GKK-QALKHVDLTIHKGMF-GLLGPNGAGKTTLMKII-ATLLqKTEGDIHVCGIN--ID- 68
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECvALTGPSGAGKSTLLKCIyGNYL-PDSGSILVRHDGgwVDl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 69 ---NDREI----RKIIGYLPQdfsmygnmsvyeamdYLGVLsglsgParkeRIP-------SLLEQVNLTDDVKTKVRAM 134
Cdd:COG4778 80 aqaSPREIlalrRRTIGYVSQ---------------FLRVI-----P----RVSaldvvaePLLERGVDREEARARAREL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 135 ------------------SGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLsETAKDR 183
Cdd:COG4778 136 larlnlperlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELI-EEAKAR 201
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-190 |
4.72e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.09 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTY--GKKQ--ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI---DND---REIRK 75
Cdd:PRK10535 7 LKDIRRSYpsGEEQveVLKGISLDIYAGeMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatlDADalaQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 IIGYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 517427119 156 IVDEPTAGLDPEERVRFRNLLSE-TAKDRIVILSTH 190
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTH 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-165 |
5.02e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.61 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKtygkKQALKHVDLTIHKG----MFGLLGpngAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDRE-IRKIIGY 79
Cdd:COG1129 259 VEGLSV----GGVVRDVSFSVRAGeilgIAGLVG---AGRTELARALFGADPADSGEIRLDGkpVRIRSPRDaIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYG---NMSVYE-----AMDYLGVLSGLSGPARKERIPSLLEQVNL-TDDVKTKVRAMSGGMRRRLGIAQALLH 150
Cdd:COG1129 332 VPEDRKGEGlvlDLSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLAT 411
|
170
....*....|....*
gi 517427119 151 DPKVLIVDEPTAGLD 165
Cdd:COG1129 412 DPKVLILDEPTRGID 426
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-226 |
1.18e-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: 85.57 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 15 GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGYLPQD---F---- 84
Cdd:COG4618 343 SKRPILRGVSFSLEPGeVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDREELGRHIGYLPQDvelFdgti 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 85 ----SMYGNMS---VYEAmdylgvlsglsgpARK----ERIpslleqVNLTDDVKTKV----RAMSGGMRRRLGIAQALL 149
Cdd:COG4618 423 aeniARFGDADpekVVAA-------------AKLagvhEMI------LRLPDGYDTRIgeggARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 150 HDPKVLIVDEPTAGLDPEERVRFRNLLSEtAKDR--IVILSTHIVGdVEATCEDIAVLNRGCVLFQGTVTELLEEAAGR 226
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKARgaTVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLARLARP 560
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
36-167 |
1.98e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 81.82 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 36 GPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKI--IGYLPqdfSMYGNMSVYEAMDYLGVLSGlsgpARKER 113
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMayLGHLP---GLKADLSTLENLHFLCGLHG----RRAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 114 IP-SLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPE 167
Cdd:PRK13543 117 MPgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-208 |
2.28e-18 |
|
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: 84.88 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQ--KTEGDIHVCG--INIDNDREI-RKIIGYL 80
Cdd:TIGR02633 4 MKGIVKTFGGVKALDGIDLEVRPGeCVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGspLKASNIRDTeRAGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYEAMdYLGVLSGLSG-----PARKERIPSLLEQVNLTDDVKTK-VRAMSGGMRRRLGIAQALLHDPKV 154
Cdd:TIGR02633 84 HQELTLVPELSVAENI-FLGNEITLPGgrmayNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 155 LIVDEPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRG 208
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
2.42e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.36 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTYGKKQ-----ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGI---------- 65
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQenelvALNNISYTFEKNkIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 66 --------NIDNDREIRKIIGYLPQ--DFSMYGNmSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDD-VKTKVRAM 134
Cdd:PRK13631 99 litnpyskKIKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 135 SGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPE-ERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQ 213
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKgEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
....*.
gi 517427119 214 GTVTEL 219
Cdd:PRK13631 258 GTPYEI 263
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-221 |
3.58e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.08 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATL--LQKTEGDI--HV----------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGeVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyHValcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 63 ----CG----------INIDND--REIRKIIGYLPQ-DFSMYGNMSVYE----AMDYLGvlsgLSGPARKERIPSLLEQV 121
Cdd:TIGR03269 81 pcpvCGgtlepeevdfWNLSDKlrRRIRKRIAIMLQrTFALYGDDTVLDnvleALEEIG----YEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 122 NLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATC 199
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|..
gi 517427119 200 EDIAVLNRGCVLFQGTVTELLE 221
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVA 258
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-167 |
4.30e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 81.77 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID------------ND 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGdVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpaDR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 71 REIRKI---IGYLPQDFSMYGNMSVYE-AMDY-LGVLsGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIA 145
Cdd:COG4598 88 RQLQRIrtrLGMVFQSFNLWSHMTVLEnVIEApVHVL-GRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180
....*....|....*....|..
gi 517427119 146 QALLHDPKVLIVDEPTAGLDPE 167
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPE 188
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-222 |
6.00e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 80.99 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYG--KKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN-DRE-IRKIIGY 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGeVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAwLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMYgNMSVYE-------AMDYLGVLSGLSGPARKERIPSLLEQVNLTddVKTKVRAMSGGMRRRLGIAQALLHDP 152
Cdd:cd03252 81 VLQENVLF-NRSIRDnialadpGMSMERVIEAAKLAGAHDFISELPEGYDTI--VGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517427119 153 KVLIVDEPTAGLDPE-ERVRFRNlLSETAKDRIVILSTHIVGDVEaTCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:cd03252 158 RILIFDEATSALDYEsEHAIMRN-MHDICAGRTVIIIAHRLSTVK-NADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-208 |
6.07e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 8 KNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQ--KTEGDIHVCG--INIDNDREI-RKIIGYLP 81
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGeIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGeeLQASNIRDTeRAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 QDFSMYGNMSVYEAMdYLGVLSGLSG----PARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:PRK13549 89 QELALVKELSVLENI-FLGNEITPGGimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517427119 158 DEPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRG 208
Cdd:PRK13549 168 DEPTASLTESETAVLLDIIRDlKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
8-167 |
6.98e-18 |
|
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: 79.59 E-value: 6.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 8 KNLSKT----YGKKQALKHVDLTIHKGMFG-LLGPNGAGKTTLMKIIAtlLQKT----EGDIHVCGINIDndREIRKIIG 78
Cdd:cd03232 7 KNLNYTvpvkGGKRQLLNNISGYVKPGTLTaLMGESGAGKTTLLDVLA--GRKTagviTGEILINGRPLD--KNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYGNMSVYEAMDYLGVLSGLSgparkeripslLEQvnltddvktkvramsggmRRRLGIAQALLHDPKVLIVD 158
Cdd:cd03232 83 YVEQQDVHSPNLTVREALRFSALLRGLS-----------VEQ------------------RKRLTIGVELAAKPSILFLD 133
|
....*....
gi 517427119 159 EPTAGLDPE 167
Cdd:cd03232 134 EPTSGLDSQ 142
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
5-267 |
7.84e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.08 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDndREIRK-IIGYLP 81
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGsIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR--QALQKnLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 Q----DFSMYGNMSVYEAMDYLGVLSGLSGPARKER--IPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:PRK15056 85 QseevDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRqiVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 156 IVDEPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCeDIAVLNRGCVLFQG-TVTELLEEAAGRIYSAQVS 233
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFC-DYTVMVKGTVLASGpTETTFTAENLELAFSGVLR 243
|
250 260 270
....*....|....*....|....*....|....
gi 517427119 234 RMELESIRDHYtvtsmmmqgnhasvrLISDEKPF 267
Cdd:PRK15056 244 HVALNGSEESI---------------ITDDERPF 262
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-220 |
9.61e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.86 E-value: 9.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 9 NLSKTY---GKKQALKHVDLTI-HKGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREI--------RKI 76
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIpNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfqidaiklRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERI-PSLLEQVNLTDDVKTKVRA----MSGGMRRRLGIAQALLHD 151
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIvEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-228 |
1.15e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIG 78
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGkVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYGNMSVYEAM-----DYLGVLsGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPK 153
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVaigryPWHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 154 VLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLE-EAAGRIY 228
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRgETLEQIY 245
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-166 |
1.68e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.54 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN---DREIRKI 76
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGeIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQDFSMYGNMSVYEAMDYLGVLSGLSG-PARKERIPSLLEQvnLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170
....*....|.
gi 517427119 156 IVDEPTAGLDP 166
Cdd:PRK11614 160 LLDEPSLGLAP 170
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-222 |
2.11e-17 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 79.33 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 22 HVDLTIHKG-MFGLLGPNGAGKTT----LMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGYLPQD--------FSMYG 88
Cdd:TIGR02770 4 DLNLSLKRGeVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprtafnplFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 89 NMsvyeaMDYLGVLSGLSGPARKeRIPSLLEQVNLtDDVKTKVRA----MSGGMRRRLGIAQALLHDPKVLIVDEPTAGL 164
Cdd:TIGR02770 84 HA-----IETLRSLGKLSKQARA-LILEALEAVGL-PDPEEVLKKypfqLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 165 DPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFgtGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYN 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-226 |
2.32e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 79.73 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 9 NLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIH-----VCGINIDNDREIRKIIGYLPQ 82
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGeTVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgepLAKLNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGN------MSVYEAMDYLgvlSGLSGPARKERIPSLLEQVNLTDDVKTKVRA-MSGGMRRRLGIAQALLHDPKVL 155
Cdd:PRK10419 97 DSISAVNprktvrEIIREPLRHL---LSLDKAERLARASEMLRAVDLDDSVLDKRPPqLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 156 IVDEPTAGLDPEERVRFRNLLSE------TAkdriVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL--EEAAGR 226
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKlqqqfgTA----CLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLtfSSPAGR 248
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-176 |
3.08e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.31 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQ-----KTEGDIHVCGINIdndREIRKIIG 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSkVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNI---YERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYGN------MSVYEAMDYLGVLSGLSGPARKERI-PSLLEQVNLTDDVKTKVRA----MSGGMRRRLGIAQA 147
Cdd:PRK14258 85 RLRRQVSMVHPkpnlfpMSVYDNVAYGVKIVGWRPKLEIDDIvESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARA 164
|
170 180
....*....|....*....|....*....
gi 517427119 148 LLHDPKVLIVDEPTAGLDPEERVRFRNLL 176
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLI 193
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-208 |
3.46e-17 |
|
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: 78.67 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKK---QALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDREIR 74
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRpdtLVLQDVSFTLHPGeVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQDFSMYGNmSVYEAMDY------LGVLSGLSGPARKERIPSLLEQVNLTDdVKTKVRAMSGGMRRRLGIAQAL 148
Cdd:cd03248 88 SKVSLVGQEPVLFAR-SLQDNIAYglqscsFECVKEAAQKAHAHSFISELASGYDTE-VGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 149 LHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATcEDIAVLNRG 208
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERA-DQILVLDGG 224
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-222 |
5.57e-17 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 78.33 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIH-----------VCGINIDNDREIR 74
Cdd:TIGR02323 6 VSGLSKSYGGGKGCRDVSFDLYPGeVLGIVGESGSGKSTLLGCLAGRLAPDHGTATyimrsgaelelYQLSEAERRRLMR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQ--------DFSMYGNMSvyEAMDYLGVLSglSGPARKERIpSLLEQVNL----TDDvktKVRAMSGGMRRRL 142
Cdd:TIGR02323 86 TEWGFVHQnprdglrmRVSAGANIG--ERLMAIGARH--YGNIRATAQ-DWLEEVEIdptrIDD---LPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 143 GIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVL 237
|
..
gi 517427119 221 EE 222
Cdd:TIGR02323 238 DD 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-208 |
7.25e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 9 NLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDRE-IRKIIGYLPQDF 84
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGqVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFASTTAaLAAGVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 85 SMYGNMSVYEAMdYLGVLSGLSGPARK----ERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEP 160
Cdd:PRK11288 89 HLVPEMTVAENL-YLGQLPHKGGIVNRrllnYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517427119 161 TAGLD-PEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRG 208
Cdd:PRK11288 168 TSSLSaREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-229 |
8.75e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.01 E-value: 8.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 15 GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMkiiaTLLQK----TEGDIHVCGINID--NDREIRKIIGYLPQD---F 84
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGqTVAIVGPTGAGKSTLI----NLLQRvfdpQSGRILIDGTDIRtvTRASLRRNIAVVFQDaglF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 85 --SMYGNMSV-------YEAMDYLGVLSGLSGPARKERipslleqvNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:PRK13657 422 nrSIEDNIRVgrpdatdEEMRAAAERAQAHDFIERKPD--------GYDTVVGERGRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 156 IVDEPTAGLDPEERVRFRNLLSETAKDRivilSTHIVGDVEATCED---IAVLNRGCVLFQGTVTELLEEaAGRIYS 229
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMKGR----TTFIIAHRLSTVRNadrILVFDNGRVVESGSFDELVAR-GGRFAA 565
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-166 |
9.60e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 78.27 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI---DNDR--EIRKIIG 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGkITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRlyTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYGNMSVYEAMDY-LGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYpLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
....*....
gi 517427119 158 DEPTAGLDP 166
Cdd:PRK11831 168 DEPFVGQDP 176
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-220 |
1.02e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKK---------QALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID-- 68
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQtLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 69 ----NDREIRKIIgylpQDFSMYGN--MSVYEAMDY-LGVLSGLSGPARKERIPSLLEQVNL-TDDVKTKVRAMSGGMRR 140
Cdd:PRK15112 81 dysyRSQRIRMIF----QDPSTSLNprQRISQILDFpLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 141 RLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSE-TAKDRIV-ILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTE 218
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLElQEKQGISyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
..
gi 517427119 219 LL 220
Cdd:PRK15112 237 VL 238
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-190 |
1.17e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.13 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQA----LKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN-DREIR-----K 75
Cdd:PRK10584 9 VHHLKKSVGQGEHelsiLTGVELVVKRGeTIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmDEEARaklraK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 IIGYLPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:PRK10584 89 HVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 517427119 156 IVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTH 190
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-214 |
2.81e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.77 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 31 MFGLLGPNGAGKTTLMKIIATLLQKTegdiHVCGINIDNDREIRKII----GYLPQDFSMYGNMSVYEAMDYLGVLSGLS 106
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGRIQGN----NFTGTILANNRKPTKQIlkrtGFVTQDDILYPHLTVRETLVFCSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 107 GPARKERI---PSLLEQVNLTDDVKTKV-----RAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSE 178
Cdd:PLN03211 172 SLTKQEKIlvaESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190
....*....|....*....|....*....|....*...
gi 517427119 179 TA-KDRIVILSTHIVGD-VEATCEDIAVLNRGCVLFQG 214
Cdd:PLN03211 252 LAqKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-239 |
5.67e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 5.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 34 LLGPNGAGKTTLMKIIATLLQkTEGDIHVCGINID--NDREIRKIIGYLPQDFSMYGNMSVYEamdYLgvlsGLSGPA-- 109
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEawSAAELARHRAYLSQQQTPPFAMPVFQ---YL----TLHQPDkt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 110 ----RKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLH-------DPKVLIVDEPTAGLDPEERVRFRNLLSE 178
Cdd:PRK03695 99 rteaVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517427119 179 TAKDRI-VILSTHivgDVEATCED---IAVLNRGCVLFQGTVTELL-EEAAGRIYSAQVSRMELES 239
Cdd:PRK03695 179 LCQQGIaVVMSSH---DLNHTLRHadrVWLLKQGKLLASGRRDEVLtPENLAQVFGVNFRRLDVEG 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-190 |
1.03e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.37 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 15 GKKQALKHVDLTIHKGMFGLL-GPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGYLPQDFSMYGNmS 91
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIYRQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 92 VYEAMDYLGVLSGLSgPARKeRIPSLLEQVNLTDDVKTK-VRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERV 170
Cdd:PRK10247 97 VYDNLIFPWQIRNQQ-PDPA-IFLDDLERFALPDTILTKnIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180
....*....|....*....|..
gi 517427119 171 RFRNLLSETAKDR--IVILSTH 190
Cdd:PRK10247 175 NVNEIIHRYVREQniAVLWVTH 196
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-223 |
1.04e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 14 YGKKQALK--HVDLTIHkGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDRE----IRKIIGYLPQD---- 83
Cdd:PRK13638 11 YQDEPVLKglNLDFSLS-PVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllaLRQQVATVFQDpeqq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 -FSMYGNMSVYEAMDYLGVlsglsgpARKE---RIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:PRK13638 90 iFYTDIDSDIAFSLRNLGV-------PEAEitrRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517427119 160 PTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQG------TVTELLEEA 223
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGapgevfACTEAMEQA 233
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-165 |
1.10e-15 |
|
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: 73.84 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQ---KTEGDIHVCGINIDNDREI--R 74
Cdd:cd03233 4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGeMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKypG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIgYLPQDFSMYGNMSVYEAMDYLGVLSGlsgparkeripslleqvnltDDVktkVRAMSGGMRRRLGIAQALLHDPKV 154
Cdd:cd03233 84 EII-YVSEEDVHFPTLTVRETLDFALRCKG--------------------NEF---VRGISGGERKRVSIAEALVSRASV 139
|
170
....*....|.
gi 517427119 155 LIVDEPTAGLD 165
Cdd:cd03233 140 LCWDNSTRGLD 150
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-220 |
1.28e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.23 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 22 HVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDREIRKIIGYLPQDFSMYGNMSVYEAMDyLG 100
Cdd:PRK10771 17 RFDLTVERGeRVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIG-LG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 101 VLSGLS-GPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSET 179
Cdd:PRK10771 96 LNPGLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517427119 180 AKDRIVIL--STHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:PRK10771 176 CQERQLTLlmVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
2-166 |
1.41e-15 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 75.91 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTYGK--KQALKHVD----------------------LTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKT 56
Cdd:COG4175 1 MPKIEVRNLYKIFGKrpERALKLLDqgkskdeilektgqtvgvndasFDVEEGeIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 57 EGDIHVCGINID--NDREIRKI----IGYLPQDFSMYGNMSVYEAMDYlGV-LSGLSGPARKERIPSLLEQVNLTDDVKT 129
Cdd:COG4175 81 AGEVLIDGEDITklSKKELRELrrkkMSMVFQHFALLPHRTVLENVAF-GLeIQGVPKAERRERAREALELVGLAGWEDS 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 517427119 130 KVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDP 166
Cdd:COG4175 160 YPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP 196
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-237 |
1.56e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.60 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY-GK-KQALKHVDLTIHKG-MFGLLGPNGAGKTTlmkiIATLLQK----TEGDIHVCGINID-----NDRE 72
Cdd:PRK11176 342 IEFRNVTFTYpGKeVPALRNINFKIPAGkTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGHDLRdytlaSLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 73 ---------------IRKIIGYLPQDFsmYGNMSVYEA------MDYLgvlsglsgparkERIPSLLEQVNLTDDVktkv 131
Cdd:PRK11176 418 qvalvsqnvhlfndtIANNIAYARTEQ--YSREQIEEAarmayaMDFI------------NKMDNGLDTVIGENGV---- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 132 rAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEdIAVLNRGCVL 211
Cdd:PRK11176 480 -LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADE-ILVVEDGEIV 557
|
250 260
....*....|....*....|....*.
gi 517427119 212 FQGTVTELLEEAAgrIYsAQVSRMEL 237
Cdd:PRK11176 558 ERGTHAELLAQNG--VY-AQLHKMQF 580
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-167 |
2.42e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 75.70 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCginiDNDReirkiIGYLPQD 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGeRLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS----ENAN-----IGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMY--GNMSVYEAMDYLgvlsglsgpaRKER-----IPSLLEQVNLT-DDVKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:PRK15064 391 HAYDfeNDLTLFDWMSQW----------RQEGddeqaVRGTLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170
....*....|..
gi 517427119 156 IVDEPTAGLDPE 167
Cdd:PRK15064 461 VMDEPTNHMDME 472
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
2.71e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.00 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQ---ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDREIR 74
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGeWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdlLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQ--DFSMYGnMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTdDVKTKVRA-MSGGMRRRLGIAQALLHD 151
Cdd:PRK13650 81 HKIGMVFQnpDNQFVG-ATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQ-DFKEREPArLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 152 PKVLIVDEPTAGLDPEERVRFRNLLSETAKDR--IVILSTHIVGDVeATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-165 |
3.06e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 72.56 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATL--LQKTEGDIHVCGINIDndreirkiigylp 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEvHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 qdfsmygNMSVYEAMDyLGVLSGLSGPARKE--RIPSLLEQVNLTddvktkvraMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:cd03217 68 -------DLPPEERAR-LGIFLAFQYPPEIPgvKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDE 130
|
....*.
gi 517427119 160 PTAGLD 165
Cdd:cd03217 131 PDSGLD 136
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-186 |
3.14e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTYGKKQaLKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIhvcginidnDREIRkiIGYL 80
Cdd:PRK13409 338 ETLVEYPDLTKKLGDFS-LEVEGGEIYEGeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---------DPELK--ISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYeamDYL-GVLSGLSGP------ARKERIPSLLEQvnltddvktKVRAMSGGMRRRLGIAQALLHDPK 153
Cdd:PRK13409 406 PQYIKPDYDGTVE---DLLrSITDDLGSSyykseiIKPLQLERLLDK---------NVKDLSGGELQRVAIAACLSRDAD 473
|
170 180 190
....*....|....*....|....*....|....*..
gi 517427119 154 VLIVDEPTAGLDPEERVR----FRNLLSETAKDRIVI 186
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAvakaIRRIAEEREATALVV 510
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-167 |
6.42e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIV--IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHvCGINI-----DNDREI-- 73
Cdd:PRK11147 317 KIVfeMENVNYQIDGKQLVKDFSAQVQRGdKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLevayfDQHRAEld 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 74 ----------------------RKIIGYLpQDFsmygnmsvyeamdylgvlsgLSGPARkeripslleqvnltddVKTKV 131
Cdd:PRK11147 396 pektvmdnlaegkqevmvngrpRHVLGYL-QDF--------------------LFHPKR----------------AMTPV 438
|
170 180 190
....*....|....*....|....*....|....*.
gi 517427119 132 RAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPE 167
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-243 |
6.92e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.10 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGK-KQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND---REIRKIIGY 79
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYiGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsklQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQD-FSMYGNMSVYEAMDYlgvlsglsGPAR--------KERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLH 150
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAF--------GPENlclppieiRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 151 DPKVLIVDEPTAGLDPEE-RVRFRNLLSETAKDRIVILSTHIVGDVEATcEDIAVLNRGCVLFQGTVTELLEEAAGRIYS 229
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSDVSLQTLG 232
|
250
....*....|....*.
gi 517427119 230 -AQVSRMEL-ESIRDH 243
Cdd:PRK13644 233 lTPPSLIELaENLKMH 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-241 |
1.18e-14 |
|
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: 73.82 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTY-GKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVC-GINidndreirkiIGYLPQD 83
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAkIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIK----------VGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVYE-----------AMDYLGVLSG-LSGP--------ARKERIPSLLEQVNLTD-DVK-------------- 128
Cdd:TIGR03719 77 PQLDPTKTVREnveegvaeikdALDRFNEISAkYAEPdadfdklaAEQAELQEIIDAADAWDlDSQleiamdalrcppwd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 129 TKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKdrIVILSTHIVGDVEATCEDIAVLNRG 208
Cdd:TIGR03719 157 ADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTHDRYFLDNVAGWILELDRG 234
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 517427119 209 -CVLFQGTVTELLEEAAGRIY---SAQVSRM-----ELESIR 241
Cdd:TIGR03719 235 rGIPWEGNYSSWLEQKQKRLEqeeKEESARQktlkrELEWVR 276
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-190 |
1.29e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.69 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLS-KTYGKKQALKHVDLTIHKGMfGLL--GPNGAGKTTLMKIIATLLQKTEGDIHVCginiDNDReirkiIG 78
Cdd:COG4178 360 DGALALEDLTlRTPDGRPLLEDLSLSLKPGE-RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARP----AGAR-----VL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQdfsmygnmSVY-------EAMDYlgvlsglsgPARKERIP-----SLLEQVNLT------DDVKTKVRAMSGGMRR 140
Cdd:COG4178 430 FLPQ--------RPYlplgtlrEALLY---------PATAEAFSdaelrEALEAVGLGhlaerlDEEADWDQVLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517427119 141 RLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTH 190
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-167 |
1.62e-14 |
|
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: 73.43 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVcGINIDndreirkiIGYLPQD 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGgIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK--------LAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 F-SMYGNMSVYEAM----DYLgVLSGLSGPARkeripSLLEQVNLT-DDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIV 157
Cdd:TIGR03719 394 RdALDPNKTVWEEIsgglDII-KLGKREIPSR-----AYVGRFNFKgSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
170
....*....|
gi 517427119 158 DEPTAGLDPE 167
Cdd:TIGR03719 468 DEPTNDLDVE 477
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-165 |
1.67e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 71.25 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIA--TLLQKTEGDIHVCGINIdNDREI----RKIIGY 79
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVhAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDI-LELSPderaRAGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 L---PQDFSMYGNM----SVYEAMDylgvLSGLSGPARKERIPSLLEQVNLTDDVKTkvRAM----SGGMRRRLGIAQAL 148
Cdd:COG0396 82 AfqyPVEIPGVSVSnflrTALNARR----GEELSAREFLKLLKEKMKELGLDEDFLD--RYVnegfSGGEKKRNEILQML 155
|
170
....*....|....*..
gi 517427119 149 LHDPKVLIVDEPTAGLD 165
Cdd:COG0396 156 LLEPKLAILDETDSGLD 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-214 |
1.72e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 10 LSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTT----LMKIIATllqktEGDIHVCGINIDN-DRE----IRKIIGY 79
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGeTLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNlNRRqllpVRHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDfsmyGNMSVYEAMDYLGVLS--------GLSGPARKERIPSLLEQVNLtdDVKTKVR---AMSGGMRRRLGIAQAL 148
Cdd:PRK15134 367 VFQD----PNSSLNPRLNVLQIIEeglrvhqpTLSAAQREQQVIAVMEEVGL--DPETRHRypaEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 149 LHDPKVLIVDEPTAGLDPEERVRFRNLL-SETAKDRIV-ILSTHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLkSLQQKHQLAyLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-220 |
2.31e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 9 NLSKTYGKKQALKHVDLTI-HKGMFGLLGPNGAGKTTLMKIIATLLQKTEG-----DIHVCGINIDNDR---EIRKIIGY 79
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFpARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRdvlEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 L---PQDFSMygnmsvyEAMDylGVLSGLSG----PARKER--IPSLLEQVNLTDDVKTKVR----AMSGGMRRRLGIAQ 146
Cdd:PRK14271 106 LfqrPNPFPM-------SIMD--NVLAGVRAhklvPRKEFRgvAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517427119 147 ALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-171 |
2.48e-14 |
|
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: 70.90 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 16 KKQALKHVDLTIHKGMF------GLLGPNGAGKTTLMKIIATLLQKTEGDIhvcgiNIDNDReirkiIGYLPQDFSMYGN 89
Cdd:cd03237 6 MKKTLGEFTLEVEGGSIseseviGILGPNGIGKTTFIKMLAGVLKPDEGDI-----EIELDT-----VSYKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 90 MSVYEAMdyLGVLSGL-SGPARKERI--PSLLEQVnltddVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDP 166
Cdd:cd03237 76 GTVRDLL--SSITKDFyTHPYFKTEIakPLQIEQI-----LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
....*
gi 517427119 167 EERVR 171
Cdd:cd03237 149 EQRLM 153
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-186 |
2.55e-14 |
|
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: 72.89 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 26 TIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIhvcginidnDREIRkiIGYLPQDFSMYGNMSVYEamdylgVLSG 104
Cdd:COG1245 362 EIREGeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---------DEDLK--ISYKPQYISPDYDGTVEE------FLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 105 lsgpARKERIPS------LLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVR----FRN 174
Cdd:COG1245 425 ----ANTDDFGSsyykteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAvakaIRR 500
|
170
....*....|..
gi 517427119 175 LLSETAKDRIVI 186
Cdd:COG1245 501 FAENRGKTAMVV 512
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-182 |
4.73e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 71.28 E-value: 4.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 16 KKQALKHVD---LTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDI-----HVCGINIDNDREIRKIIGYLPQD--F 84
Cdd:PRK15079 30 PPKTLKAVDgvtLRLYEGeTLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkDLLGMKDDEWRAVRSDIQMIFQDplA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 85 SMYGNMSVYEAmdylgvlsgLSGPARKERiPSLLEQvnltdDVKTKVRAM------------------SGGMRRRLGIAQ 146
Cdd:PRK15079 110 SLNPRMTIGEI---------IAEPLRTYH-PKLSRQ-----EVKDRVKAMmlkvgllpnlinryphefSGGQCQRIGIAR 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 517427119 147 ALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD 182
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRE 210
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-210 |
6.31e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 68.98 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTYGKK--QALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND--REIRKI 76
Cdd:cd03369 4 HGEIEVENLSVRYAPDlpPVLKNVSFKVKAGeKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIplEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQD--------------FSMYGNMSVYEAmdyLGVLSGLSgparkeripslleqvNLtddvktkvramSGGMRRRL 142
Cdd:cd03369 84 LTIIPQDptlfsgtirsnldpFDEYSDEEIYGA---LRVSEGGL---------------NL-----------SQGQRQLL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 143 GIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVeATCEDIAVLNRGCV 210
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTI-IDYDKILVMDAGEV 201
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-165 |
7.23e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.67 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIA--TLLQKTEGDIHVCGINI-DNDREIR-------- 74
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGeIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESIlDLEPEERahlgifla 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 -----KIIGYLPQDFSM--YGNMSVYEAMDYLGVLSGLsgparkERIPSLLEQVN-----LTDDVKtkvRAMSGGMRRRL 142
Cdd:CHL00131 90 fqypiEIPGVSNADFLRlaYNSKRKFQGLPELDPLEFL------EIINEKLKLVGmdpsfLSRNVN---EGFSGGEKKRN 160
|
170 180
....*....|....*....|...
gi 517427119 143 GIAQALLHDPKVLIVDEPTAGLD 165
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLD 183
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-223 |
9.43e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.28 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 17 KQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDI-----HVCGINIDNDREIRKIIGYLPQDFS--MYG 88
Cdd:PRK10789 328 HPALENVNFTLKPGqMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdiPLTKLQLDSWRSRLAVVSQTPFLFSdtVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 89 NMSvyeamdylgvlsgLSGP-ARKERIPSLLEQVNLTDDV-------KTKV--RA--MSGGMRRRLGIAQALLHDPKVLI 156
Cdd:PRK10789 408 NIA-------------LGRPdATQQEIEHVARLASVHDDIlrlpqgyDTEVgeRGvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 157 VDEPTAGLDPEERVRFRNLLSETAKDRIVILSTH-IVGDVEATceDIAVLNRGCVLFQGTVTELLEEA 223
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHrLSALTEAS--EILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-238 |
9.79e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 9.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDREIRKI- 76
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGrVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSSQEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQDFSMYGNMSVYEAMdYLG-----VLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHD 151
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENI-FLGrefvnRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 152 PKVLIVDEPTAGL-DPEERVRFRNLLSETAKDR-IVILStHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEA-----A 224
Cdd:PRK10762 160 SKVIIMDEPTDALtDTETESLFRVIRELKSQGRgIVYIS-HRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSliemmV 238
|
250
....*....|....
gi 517427119 225 GRIYSAQVSRMELE 238
Cdd:PRK10762 239 GRKLEDQYPRLDKA 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-190 |
1.09e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTY--GKKQALKHVDLTIHKGMFGLL-GPNGAGKTTLMKIIATLL--QKTEGDIHVCGINIDNDREIRK 75
Cdd:COG2401 25 ERVAIVLEAFGVELrvVERYVLRDLNLEIEPGEIVLIvGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 IIGYLPqdfsmygnmSVYEAMDYLGVlSGLSGPArkeripsLLeqvnltddvKTKVRAMSGGMRRRLGIAQALLHDPKVL 155
Cdd:COG2401 105 AIGRKG---------DFKDAVELLNA-VGLSDAV-------LW---------LRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 517427119 156 IVDEPTAGLDPE-ERVRFRNLLSETAKDRI-VILSTH 190
Cdd:COG2401 159 VIDEFCSHLDRQtAKRVARNLQKLARRAGItLVVATH 195
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-214 |
1.10e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.18 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 6 VIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVcginIDNDREIRKII------- 77
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGeVLGIVGESGSGKTTLLNALSARLAPDAGEVHY----RMRDGQLRDLYalseaer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 --------GYLPQD--------FSMYGN-----MSV---------YEAMDYLGvlsglsgpaRKERIPSLLeqvnltDDV 127
Cdd:PRK11701 84 rrllrtewGFVHQHprdglrmqVSAGGNigerlMAVgarhygdirATAGDWLE---------RVEIDAARI------DDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 128 KtkvRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRF----RNLLSETakDRIVILSTHIVGDVEATCEDIA 203
Cdd:PRK11701 149 P---TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLldllRGLVREL--GLAVVIVTHDLAVARLLAHRLL 223
|
250
....*....|.
gi 517427119 204 VLNRGCVLFQG 214
Cdd:PRK11701 224 VMKQGRVVESG 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-228 |
1.15e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.90 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTYGK-KQALKHVDLTI-HKGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIGY 79
Cdd:PRK10790 340 RIDIDNVSFAYRDdNLVLQNINLSVpSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQD-----FSMYGNMSvyeamdylgvlsgLSGPARKERIPSLLEQVNLTDdvktKVRAMSGGMRRRLG----------- 143
Cdd:PRK10790 420 VQQDpvvlaDTFLANVT-------------LGRDISEEQVWQALETVQLAE----LARSLPDGLYTPLGeqgnnlsvgqk 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 144 ----IAQALLHDPKVLIVDEPTAGLDP--EERVRfRNLLSETAKDRIVILSTHIVGDVEAtcEDIAVLNRGCVLFQGTVT 217
Cdd:PRK10790 483 qllaLARVLVQTPQILILDEATANIDSgtEQAIQ-QALAAVREHTTLVVIAHRLSTIVEA--DTILVLHRGQAVEQGTHQ 559
|
250
....*....|.
gi 517427119 218 ELLeEAAGRIY 228
Cdd:PRK10790 560 QLL-AAQGRYW 569
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-208 |
1.18e-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: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLS-KTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND--REIRKI- 76
Cdd:COG3845 255 EVVLEVENLSvRDDRGVPALKDVSLEVRAGeILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLspRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IGYLPQD---FSMYGNMSVYEAMdylgVLSGLSGPA-------RKERIPSLLEQVN-----LTDDVKTKVRAMSGGMRRR 141
Cdd:COG3845 335 VAYIPEDrlgRGLVPDMSVAENL----ILGRYRRPPfsrggflDRKAIRAFAEELIeefdvRTPGPDTPARSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 142 LGIAQALLHDPKVLIVDEPTAGLDPE--ERVRFRnLLSetAKDR---IVILSThivgDVE---ATCEDIAVLNRG 208
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGaiEFIHQR-LLE--LRDAgaaVLLISE----DLDeilALSDRIAVMYEG 478
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
102-239 |
1.22e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.96 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 102 LSGLSGPARKERIPSLLEQVNLtDDVKTKVRA----MSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLS 177
Cdd:PRK10418 106 CLALGKPADDATLTAALEAVGL-ENAARVLKLypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLE 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 178 ETAKDRI--VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLE----EAAGRIYSAQVS--RMELES 239
Cdd:PRK10418 185 SIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNapkhAVTRSLVSAHLAlyGMELAS 254
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
7-219 |
1.24e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.14 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTY----GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQK---TEGDIHVCGINIDN--DREIRKI 76
Cdd:PRK09473 15 VKDLRVTFstpdGDVTAVNDLNFSLRAGeTLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNlpEKELNKL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 ----IGYLPQD--FSMYGNMSVYEA-MDYLGVLSGLSgpaRKEripSLLEQVNLTDDVKT----KVRAM-----SGGMRR 140
Cdd:PRK09473 95 raeqISMIFQDpmTSLNPYMRVGEQlMEVLMLHKGMS---KAE---AFEESVRMLDAVKMpearKRMKMyphefSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 141 RLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD--RIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTE 218
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
.
gi 517427119 219 L 219
Cdd:PRK09473 249 V 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-178 |
1.61e-13 |
|
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: 67.18 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 20 LKHVDLTIHKGMFGLL-GPNGAGKTTLMKIIATLLQKTEGDIHVCGiniDNDreirkiIGYLPQdfsmygnmsvyeaMDY 98
Cdd:cd03223 17 LKDLSFEIKPGDRLLItGPSGTGKSSLFRALAGLWPWGSGRIGMPE---GED------LLFLPQ-------------RPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 99 LGVLSglsgparkeripsLLEQVNLT-DDVktkvraMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLS 177
Cdd:cd03223 75 LPLGT-------------LREQLIYPwDDV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
.
gi 517427119 178 E 178
Cdd:cd03223 136 E 136
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-165 |
2.33e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLSKTygkkqALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDRE-IRKII 77
Cdd:PRK10762 255 EVRLKVDNLSGP-----GVNDVSFTLRKGeILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQDgLANGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQDFSMYG---NMSVYEAMDY--LGVLSGLSGPARKERipsllEQVNLTD-----DVKTKVRA-----MSGGMRRRL 142
Cdd:PRK10762 330 VYISEDRKRDGlvlGMSVKENMSLtaLRYFSRAGGSLKHAD-----EQQAVSDfirlfNIKTPSMEqaiglLSGGNQQKV 404
|
170 180
....*....|....*....|...
gi 517427119 143 GIAQALLHDPKVLIVDEPTAGLD 165
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVD 427
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-224 |
2.70e-13 |
|
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: 70.32 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTY--GKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQkTEGDIHVCGINIDND--REIRKIIG 78
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQrVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVtlQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQD--------------FSMYGNMSVYEAMDYLGVLSGLsgparkERIPSLLEQVnLTDDVKTkvraMSGGMRRRLGI 144
Cdd:TIGR01271 1296 VIPQKvfifsgtfrknldpYEQWSDEEIWKVAEEVGLKSVI------EQFPDKLDFV-LVDGGYV----LSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 145 AQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHivgDVEA--TCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH---RVEAllECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
..
gi 517427119 223 AA 224
Cdd:TIGR01271 1442 TS 1443
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
34-208 |
3.70e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 34 LLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN-----DREIRKIIGYLPQD--FSMYGNMSV-YEAMDYLGVLSGL 105
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgkLQALRRDIQFIFQDpyASLDPRQTVgDSIMEPLRVHGLL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 106 SGPARKERIPSLLEQVNLTDDVKTKV-RAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRI 184
Cdd:PRK10261 435 PGKAAAARVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFG 514
|
170 180
....*....|....*....|....*.
gi 517427119 185 V--ILSTHIVGDVEATCEDIAVLNRG 208
Cdd:PRK10261 515 IayLFISHDMAVVERISHRVAVMYLG 540
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-219 |
4.48e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.10 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLS-KTYGKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLqKTEGDIHVCGINIdndREI-----RKII 77
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRiALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIEL---RELdpeswRKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYL---PQDF--SMYGNMSvyeamdylgvlsgLSGP-ARKERIPSLLEQVNLTD-----------DVKTKVRAMSGGMRR 140
Cdd:PRK11174 426 SWVgqnPQLPhgTLRDNVL-------------LGNPdASDEQLQQALENAWVSEflpllpqgldtPIGDQAAGLSVGQAQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 141 RLGIAQALLHDPKVLIVDEPTAGLD--PEERVrfRNLLSETAKDRIVILSTHIVGDVEAtCEDIAVLNRGCVLFQGTVTE 218
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDahSEQLV--MQALNAASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
|
.
gi 517427119 219 L 219
Cdd:PRK11174 570 L 570
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-190 |
4.57e-13 |
|
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: 66.72 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQ-----ALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGInidndreirkiIG 78
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELvAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------IA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQdFSMYGNMSVYEamdylGVLSGLsgPARKERIPSLLEQVNLTDDVK-------TKV----RAMSGGMRRRLGIAQA 147
Cdd:cd03250 70 YVSQ-EPWIQNGTIRE-----NILFGK--PFDEERYEKVIKACALEPDLEilpdgdlTEIgekgINLSGGQKQRISLARA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517427119 148 LLHDPKVLIVDEPTAGLDPE-ERVRFRN-LLSETAKDRIVILSTH 190
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHvGRHIFENcILGLLLNNKTRILVTH 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-167 |
6.80e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIV--IKNLSKTYG-KKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVC-GINidndreirk 75
Cdd:PRK11819 1 MMAQYIytMNRVSKVVPpKKQILKDISLSFFPGAkIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIK--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 76 iIGYLPQ------DFSMYGN--MSVYEAMDYL----GVLSGLSGP--------ARKERIPSLLEQVNLTD-DVK------ 128
Cdd:PRK11819 72 -VGYLPQepqldpEKTVRENveEGVAEVKAALdrfnEIYAAYAEPdadfdalaAEQGELQEIIDAADAWDlDSQleiamd 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517427119 129 --------TKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPE 167
Cdd:PRK11819 151 alrcppwdAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-214 |
1.35e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.83 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYgKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIAT----LLQKTEGDIHVCGINIDN-DREIRKIIGYL 80
Cdd:TIGR00956 65 LKKFRDTK-TFDILKPMDGLIKPGeLTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEiKKHYRGDVVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQDFSMYGNMSVYEAMDYLGVLSG----LSGPARKERIPSLLEQV----NLTDDVKTKV-----RAMSGGMRRRLGIAQA 147
Cdd:TIGR00956 144 AETDVHFPHLTVGETLDFAARCKTpqnrPDGVSREEYAKHIADVYmatyGLSHTRNTKVgndfvRGVSGGERKRVSIAEA 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 148 LLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAkdriVIL-STHIVGDVEATCEDIAVLNRGCVLFQG 214
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKTSA----NILdTTPLVAIYQCSQDAYELFDKVIVLYEG 287
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-239 |
1.67e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.12 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 8 KNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIA------TLlqktEGDIH----VCGINIDNDREIRKI 76
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGeIHALCGENGAGKSTLMKVLSgvyphgSY----EGEILfdgeVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 77 IgYLPQDFSMYGNMSVYEAMdYLGVLSGLSG----PARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDP 152
Cdd:NF040905 81 V-IIHQELALIPYLSIAENI-FLGNERAKRGvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 153 KVLIVDEPTAGLDPEERVRFRNLLSETAKDRIV-ILSTHIVGDVEATCEDIAVLNRGCV-----LFQGTVTElleeaaGR 226
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITsIIISHKLNEIRRVADSITVLRDGRTietldCRADEVTE------DR 232
|
250
....*....|...
gi 517427119 227 IYSAQVSRmELES 239
Cdd:NF040905 233 IIRGMVGR-DLED 244
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-178 |
2.68e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.84 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 9 NLSKTY--GKKQA--LKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID-----NDREIR-KII 77
Cdd:PRK11629 10 NLCKRYqeGSVQTdvLHNVSFSIGEGeMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQ------DFSMYGNMsvyeAMDylgVLSGLSGPAR-KERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLH 150
Cdd:PRK11629 90 GFIYQfhhllpDFTALENV----AMP---LLIGKKKPAEiNSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180
....*....|....*....|....*...
gi 517427119 151 DPKVLIVDEPTAGLDPEERVRFRNLLSE 178
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGE 190
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-165 |
2.98e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIhvcgiNIDNDReirkIIGYLPQD 83
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNeRVCLVGRNGAGKSTLMKILNGEVLLDDGRI-----IYEQDL----IVARLQQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGNMSVY--------EAMDYL--------------------------GVLSGLSGPARKERIPSLLEQVNLTDDvkT 129
Cdd:PRK11147 75 PPRNVEGTVYdfvaegieEQAEYLkryhdishlvetdpseknlnelaklqEQLDHHNLWQLENRINEVLAQLGLDPD--A 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 517427119 130 KVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:PRK11147 153 ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-220 |
3.10e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.50 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKK---QALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDREIR 74
Cdd:PRK13642 1 MNKILEVENLVFKYEKEsdvNQLNGVSFSITKGEWvSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQD-FSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPK 153
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 154 VLIVDEPTAGLDPEERVRFRNLLSETA-KDRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELL 220
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-208 |
3.97e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.84 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTY----------------GKKQ----ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGd 59
Cdd:PRK13546 1 MNVSVNIKNVTKEYriyrtnkermkdalipKHKNktffALDDISLKAYEGdVIGLVGINGSGKSTLSNIIGGSLSPTVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 60 ihvcgiNIDNDREIRKIigylPQDFSMYGNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMR 139
Cdd:PRK13546 80 ------KVDRNGEVSVI----AISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 140 RRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSE-TAKDRIVILSTHIVGDVEATCEDIAVLNRG 208
Cdd:PRK13546 150 AKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEfKEQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-176 |
4.15e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 1 MDTKIVIKNLSKTYGKK----------QALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINI-D 68
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKrglfkperlvKALDGVSFTLERGkTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 69 NDREIRKIigyLPQDFSM-----YGNM-------SVYEamDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAM-S 135
Cdd:PRK11308 82 ADPEAQKL---LRQKIQIvfqnpYGSLnprkkvgQILE--EPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMfS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517427119 136 GGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLL 176
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-205 |
8.28e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 33 GLLGPNGAGKTTLMKIIATLLQKTEGdihvcgiNIDNDREIRKIIGYlpqdFSmyGNmsvyEAMDYL-GVLSGLSGPARK 111
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLG-------DYEEEPSWDEVLKR----FR--GT----ELQNYFkKLYNGEIKVVHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 112 ----ERIP---------------------SLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDP 166
Cdd:PRK13409 166 pqyvDLIPkvfkgkvrellkkvdergkldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190
....*....|....*....|....*....|....*....
gi 517427119 167 EERVRFRNLLSETAKDRIVILSTHivgdveatceDIAVL 205
Cdd:PRK13409 246 RQRLNVARLIRELAEGKYVLVVEH----------DLAVL 274
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-222 |
8.80e-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: 64.11 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTY--GKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQkTEGDIHVCGINIDND--REIRKIIG 78
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQrVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVplQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYgnmsvyeamdylgvlsglSGPARKERIP----SLLEQVNLTDDVKTKV-----------------RAMSGG 137
Cdd:cd03289 81 VIPQKVFIF------------------SGTFRKNLDPygkwSDEEIWKVAEEVGLKSvieqfpgqldfvlvdggCVLSHG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 138 MRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHivgDVEAT--CEDIAVLNRGCVLFQGT 215
Cdd:cd03289 143 HKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEH---RIEAMleCQRFLVIEENKVRQYDS 219
|
....*..
gi 517427119 216 VTELLEE 222
Cdd:cd03289 220 IQKLLNE 226
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-190 |
9.98e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.58 E-value: 9.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 36 GPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNdreIRK-IIGYLPQDFSMYGNMSVYEAMDYLGVLSGLSgparkERI 114
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN---IAKpYCTYIGHNLGLKLEMTVFENLKFWSEIYNSA-----ETL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 115 PSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD-RIVILSTH 190
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSgGIVLLSSH 181
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-165 |
1.47e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.87 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 18 QALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATllQKT----EGDIHVCGINIDNDREIRkIIGYLPQDFSMYGNMSV 92
Cdd:PLN03140 894 QLLREVTGAFRPGVLtALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKKQETFAR-ISGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 93 YEAMDYLGVLSgLSGPARKE-------RIPSLLEQVNLTDDVK--TKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAG 163
Cdd:PLN03140 971 RESLIYSAFLR-LPKEVSKEekmmfvdEVMELVELDNLKDAIVglPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
..
gi 517427119 164 LD 165
Cdd:PLN03140 1050 LD 1051
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-176 |
2.24e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.84 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTYGKKQ-ALKHVDLTIHKG--MFgLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINID--NDREIRKIIG 78
Cdd:PRK10522 322 TLELRNVTFAYQDNGfSVGPINLTIKRGelLF-LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYgnmsvyeamDYLgvLSGLSGPARKERIPSLLEQVNLTDDVK--------TKvraMSGGMRRRLGIAQALLH 150
Cdd:PRK10522 401 AVFTDFHLF---------DQL--LGPEGKPANPALVEKWLERLKMAHKLEledgrisnLK---LSKGQKKRLALLLALAE 466
|
170 180
....*....|....*....|....*..
gi 517427119 151 DPKVLIVDEPTAGLDPE-ERVRFRNLL 176
Cdd:PRK10522 467 ERDILLLDEWAADQDPHfRREFYQVLL 493
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-165 |
2.29e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 15 GKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQK---TEGDIHVCGINIDNDREirKIIGYLPQD------- 83
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGtLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQ--RSIGYVQQQdlhlpts 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 -------FSMY----GNMSVYEAMDYLgvlsglsgparkERIPSLLEQVNLTDD-VKTKVRAMSGGMRRRLGIAQALLHD 151
Cdd:TIGR00956 852 tvreslrFSAYlrqpKSVSKSEKMEYV------------EEVIKLLEMESYADAvVGVPGEGLNVEQRKRLTIGVELVAK 919
|
170
....*....|....*
gi 517427119 152 PKVLI-VDEPTAGLD 165
Cdd:TIGR00956 920 PKLLLfLDEPTSGLD 934
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
17-255 |
3.08e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.97 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 17 KQALKHVDLTIH-----KGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVcginidNDR-------------EIRKIiG 78
Cdd:PRK11144 7 KQQLGDLCLTVNltlpaQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVL------NGRvlfdaekgiclppEKRRI-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQD---FSMY---GN----MSVYEAMDYLGVLSGLSgparkerIPSLLEQVNLTddvktkvraMSGGMRRRLGIAQAL 148
Cdd:PRK11144 80 YVFQDarlFPHYkvrGNlrygMAKSMVAQFDKIVALLG-------IEPLLDRYPGS---------LSGGEKQRVAIGRAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 149 LHDPKVLIVDEPTAGLD-PeervRFRNL---LSETAKD-RIVIL-STHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEE 222
Cdd:PRK11144 144 LTAPELLLMDEPLASLDlP----RKRELlpyLERLAREiNIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWAS 219
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 517427119 223 AAGRiysAQVSRMELESI--------RDHYTVTSMMMQGNH 255
Cdd:PRK11144 220 SAMR---PWLPKEEQSSIlkvtvlehHPHYAMTALALGDQH 257
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-232 |
3.77e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 59 DIHVCGINIDNDREIRKIIGYLPQDFsmygNMSVYEAMDYLGVLSGLSGPARKERIPSLLEQV-NLTDDVKTKV----RA 133
Cdd:PTZ00265 1283 GVDICDYNLKDLRNLFSIVSQEPMLF----NMSIYENIKFGKEDATREDVKRACKFAAIDEFIeSLPNKYDTNVgpygKS 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 134 MSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDP-EERVRFRNLLSETAK-DRIVILSTHIVGDVEATcEDIAVLNR---- 207
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSnSEKLIEKTIVDIKDKaDKTIITIAHRIASIKRS-DKIVVFNNpdrt 1437
|
170 180
....*....|....*....|....*.
gi 517427119 208 -GCVLFQGTVTELLEEAAGrIYSAQV 232
Cdd:PTZ00265 1438 gSFVQAHGTHEELLSVQDG-VYKKYV 1462
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
7-219 |
4.72e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.45 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQA-LKHVD---LTIHKG-MFGLLGPNGAGKT----TLM-------KIIATLLQKTEGDIHVCginidND 70
Cdd:PRK11022 6 VDKLSVHFGDESApFRAVDrisYSVKQGeVVGIVGESGSGKSvsslAIMglidypgRVMAEKLEFNGQDLQRI-----SE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 71 REIRKIIG----YLPQD--FSMYGNMSV-YEAMDYLGVLSGLSGPARKERIPSLLEQVNLTD-----DVKTkvRAMSGGM 138
Cdd:PRK11022 81 KERRNLVGaevaMIFQDpmTSLNPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasrlDVYP--HQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 139 RRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAK--DRIVILSTHIVGDVEATCEDIAVLNRGCVLFQGTV 216
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
...
gi 517427119 217 TEL 219
Cdd:PRK11022 239 HDI 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-205 |
5.27e-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: 62.88 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 33 GLLGPNGAGKTTLMKIIATLLQKTEGdihvcgiNIDNDREIRKIIGYlpqdFSmyGNmsvyEAMDYL-GVLSGLSGPARK 111
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLG-------DYDEEPSWDEVLKR----FR--GT----ELQDYFkKLANGEIKVAHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 112 ----ERIP---------------------SLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDP 166
Cdd:COG1245 166 pqyvDLIPkvfkgtvrellekvdergkldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517427119 167 EERVRFRNLLSETAK-DRIVILSTHivgdveatceDIAVL 205
Cdd:COG1245 246 YQRLNVARLIRELAEeGKYVLVVEH----------DLAIL 275
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-208 |
9.34e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDRE-IRKIIGYLPQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHsIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEaLENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 DFSMYGNMSVYEAMdYLG--VLSGLSGPARK--ERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVD 158
Cdd:PRK10982 81 ELNLVLQRSVMDNM-WLGryPTKGMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517427119 159 EPTAGLDpEERVRFRNLLSETAKDR---IVILStHIVGDVEATCEDIAVLNRG 208
Cdd:PRK10982 160 EPTSSLT-EKEVNHLFTIIRKLKERgcgIVYIS-HKMEEIFQLCDEITILRDG 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-229 |
9.64e-11 |
|
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: 62.27 E-value: 9.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 20 LKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND--REIRKIIGYLPQD------------- 83
Cdd:TIGR00957 1302 LRHINVTIHGGeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIglHDLRFKITIIPQDpvlfsgslrmnld 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 -FSMYGNMSVYEAMDylgvLSGLsgparKERIPSLLEQVNLtdDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:TIGR00957 1382 pFSQYSDEEVWWALE----LAHL-----KTFVSALPDKLDH--ECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 163 GLDPEErvrfRNLLSETAKDRIVILSTHIVGDVEATCED---IAVLNRGCVLFQGTVTELLeEAAGRIYS 229
Cdd:TIGR00957 1451 AVDLET----DNLIQSTIRTQFEDCTVLTIAHRLNTIMDytrVIVLDKGEVAEFGAPSNLL-QQRGIFYS 1515
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-224 |
1.55e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 21 KHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR---EIRKIIGYLPQDFSMYG-NMSVYEA 95
Cdd:PRK15439 280 RNISLEVRAGeILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqRLARGLVYLPEDRQSSGlYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 96 MDYLGVLSGLSG----PARKERIpslLEQ----VNLT-DDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDP 166
Cdd:PRK15439 360 WNVCALTHNRRGfwikPARENAV---LERyrraLNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 167 EERVRFRNLLSETAKDRIVILstHIVGDVEatcEDIAVLNRGCVLFQGTVTELLEEAA 224
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVL--FISSDLE---EIEQMADRVLVMHQGEISGALTGAA 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-167 |
2.25e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVcGinidndrEIRKiIGYLPQ- 82
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGgIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-------ETVK-LAYVDQs 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 -DfSMYGNMSVYEAM----DYLGVlsglsgpARKErIPS--LLEQVNL--TDDVKtKVRAMSGGMRRRLGIAQALLHDPK 153
Cdd:PRK11819 396 rD-ALDPNKTVWEEIsgglDIIKV-------GNRE-IPSraYVGRFNFkgGDQQK-KVGVLSGGERNRLHLAKTLKQGGN 465
|
170
....*....|....
gi 517427119 154 VLIVDEPTAGLDPE 167
Cdd:PRK11819 466 VLLLDEPTNDLDVE 479
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-190 |
4.20e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 9 NLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDR-EIRKIIGYLPQDFSM 86
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGgLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLcTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 87 YGNMSVYEAMDY-LGVLSGLSGparkerIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:PRK13540 86 NPYLTLRENCLYdIHFSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180
....*....|....*....|....*...
gi 517427119 166 peER---VRFRNLLSETAKDRIVILSTH 190
Cdd:PRK13540 160 --ELsllTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-169 |
8.18e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 8.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIAtllqkteGDiHVCGINidND-------R----- 71
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEhWQIVGPNGAGKSTLLSLIT-------GD-HPQGYS--NDltlfgrrRgsget 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 72 --EIRKIIGYLPQDFSM-YG-NMSVYEAM-----DYLGVLSGLSGPARKeRIPSLLEQVNLTDDV-KTKVRAMSGGMRRR 141
Cdd:PRK10938 331 iwDIKKHIGYVSSSLHLdYRvSTSVRNVIlsgffDSIGIYQAVSDRQQK-LAQQWLDILGIDKRTaDAPFHSLSWGQQRL 409
|
170 180
....*....|....*....|....*...
gi 517427119 142 LGIAQALLHDPKVLIVDEPTAGLDPEER 169
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLDPLNR 437
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-159 |
1.36e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.75 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 19 ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG----INIDNdreirkiigylpqdfSMYGNMSVY 93
Cdd:PRK13545 39 ALNNISFEVPEGeIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsaalIAISS---------------GLNGQLTGI 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517427119 94 EAMDYLGVLSGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDE 159
Cdd:PRK13545 104 ENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-190 |
3.64e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTYGKKQAL---KHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCgiNIDNDREI-----R 74
Cdd:PTZ00265 382 KIQFKNVRFHYDTRKDVeiyKDLNFTLTEGkTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDInlkwwR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIIGYLPQDFSMYGN-------MSVY-----EAM-DYL----------------------GVLSGLSGPARKERIPSLLE 119
Cdd:PTZ00265 460 SKIGVVSQDPLLFSNsiknnikYSLYslkdlEALsNYYnedgndsqenknkrnscrakcaGDLNDMSNTTDSNELIEMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 120 QVNLTDD--------------------------VKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFR 173
Cdd:PTZ00265 540 NYQTIKDsevvdvskkvlihdfvsalpdkyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250
....*....|....*....
gi 517427119 174 NLLSETA--KDRIVILSTH 190
Cdd:PTZ00265 620 KTINNLKgnENRITIIIAH 638
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-165 |
4.31e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 23 VDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQ-KTEGDIHVCG--INIDNDRE-IRKIIGYLPQDFSMYG---NMSVYE 94
Cdd:PRK13549 281 VSFSLRRGeILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQaIAQGIAMVPEDRKRDGivpVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 95 AMdylgVLSGLSGPARKERIPSLLEQVNLTDDVKT-KVRA---------MSGGMRRRLGIAQALLHDPKVLIVDEPTAGL 164
Cdd:PRK13549 361 NI----TLAALDRFTGGSRIDDAAELKTILESIQRlKVKTaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
.
gi 517427119 165 D 165
Cdd:PRK13549 437 D 437
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-194 |
4.40e-09 |
|
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: 54.30 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 33 GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGInidndreirkiigylpqdfsmygnmsvyeamdylgvlsglsgparkE 112
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDG----------------------------------------------E 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 113 RIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETA-------KDRIV 185
Cdd:smart00382 40 DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkseKNLTV 119
|
....*....
gi 517427119 186 ILSTHIVGD 194
Cdd:smart00382 120 ILTTNDEKD 128
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-165 |
8.97e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 8.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG------IN----------- 66
Cdd:PRK10636 2 IVFSSLQIRRGVRVLLDNATATINPGQkVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawVNqetpalpqpal 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 67 ---IDNDREIRKiigyLPQDFSMYGNMSVYEAMDYL-GVLSGLSGPARKERIPSLLEQVNLTDD-VKTKVRAMSGGMRRR 141
Cdd:PRK10636 82 eyvIDGDREYRQ----LEAQLHDANERNDGHAIATIhGKLDAIDAWTIRSRAASLLHGLGFSNEqLERPVSDFSGGWRMR 157
|
170 180
....*....|....*....|....
gi 517427119 142 LGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:PRK10636 158 LNLAQALICRSDLLLLDEPTNHLD 181
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-208 |
1.04e-08 |
|
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: 55.39 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 3 TKIVIKNLsktygkkQALKHVDLTIHKGMFGLLGPNGAGKTTLMKIIATLLQK------TEGDIHVCGINIDNDREI--- 73
Cdd:COG3593 4 EKIKIKNF-------RSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPsssrkfDEEDFYLGDDPDLPEIEIelt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 74 -----RKIIGYLPQDfSMYGNMS------------------------VYEAMDYLGVLSGLSGPARKERIPSLleQVNLT 124
Cdd:COG3593 77 fgsllSRLLRLLLKE-EDKEELEealeelneelkealkalnellseyLKELLDGLDLELELSLDELEDLLKSL--SLRIE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 125 DDVKTKVRAMSGGMRRRLGIA--QALLH-----DPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRI-VILSTH---IVG 193
Cdd:COG3593 154 DGKELPLDRLGSGFQRLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVIITTHsphLLS 233
|
250
....*....|....*
gi 517427119 194 DVEAtcEDIAVLNRG 208
Cdd:COG3593 234 EVPL--ENIRRLRRD 246
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-189 |
1.50e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 10 LSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVC-GINidndreirkiIGYLPQ----- 82
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGsRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIK----------LGYFAQhqlef 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 ---DFSMYGNMS-----VYEAM--DYLGVLsGLSGparkeripslleqvnltDDVKTKVRAMSGGMRRRLGIAQALLHDP 152
Cdd:PRK10636 388 lraDESPLQHLArlapqELEQKlrDYLGGF-GFQG-----------------DKVTEETRRFSGGEKARLVLALIVWQRP 449
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517427119 153 KVLIVDEPTAGLDPEER-------VRFRNLLSETAKDRIVILST 189
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRqaltealIDFEGALVVVSHDRHLLRST 493
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-221 |
3.06e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKqaLKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDNDRE---IRKIIGYLPQ 82
Cdd:PRK09700 268 VRNVTSRDRKK--VRDISFSVCRGeILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldaVKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 83 ---------DFSMYGNMSVYEAMDyLGVLSGLSG--PARKERIPSLLEQVNLT---DDVKTKVRAMSGGMRRRLGIAQAL 148
Cdd:PRK09700 346 srrdngffpNFSIAQNMAISRSLK-DGGYKGAMGlfHEVDEQRTAENQRELLAlkcHSVNQNITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517427119 149 LHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVIL--STHIVgdveatcEDIAVLNRGCVLFQGTVTELLE 221
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILmvSSELP-------EIITVCDRIAVFCEGRLTQILT 492
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-219 |
3.92e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 20 LKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGinidndreirkIIGYLPQ-DFSMYGNMSVyeamd 97
Cdd:TIGR01271 442 LKNISFKLEKGqLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------RISFSPQtSWIMPGTIKD----- 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 98 ylGVLSGLSgpARKERIPSLLEQVNLTDDV-----KTKVRAM------SGGMRRRLGIAQALLHDPKVLIVDEPTAGLD- 165
Cdd:TIGR01271 506 --NIIFGLS--YDEYRYTSVIKACQLEEDIalfpeKDKTVLGeggitlSGGQRARISLARAVYKDADLYLLDSPFTHLDv 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 166 PEERVRFRNLLSE--TAKDRIVILST--HIvgdveATCEDIAVLNRGCVLFQGTVTEL 219
Cdd:TIGR01271 582 VTEKEIFESCLCKlmSNKTRILVTSKleHL-----KKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-206 |
5.24e-08 |
|
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: 52.75 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 33 GLLGPNGAGKTTLMKIIATLLQKTEGdihvcgiNIDNDREIRKIIGYLpqdfsmYGNmsvyEAMDYL-GVLSGLSGPARK 111
Cdd:cd03236 30 GLVGPNGIGKSTALKILAGKLKPNLG-------KFDDPPDWDEILDEF------RGS----ELQNYFtKLLEGDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 112 ----ERIPS---------------------LLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDP 166
Cdd:cd03236 93 pqyvDLIPKavkgkvgellkkkdergkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517427119 167 EERVRFRNLLSETAKD-RIVILSTHivgdveatceDIAVLN 206
Cdd:cd03236 173 KQRLNAARLIRELAEDdNYVLVVEH----------DLAVLD 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-210 |
7.30e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 2 DTKIVIKNLskTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN----------- 69
Cdd:PRK10982 248 EVILEVRNL--TSLRQPSIRDVSFDLHKGeILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgf 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 70 -----DREIRKIIGYLPQDF-SMYGNMSvyeamDYLGVLSGLSGPARKERIPSLLEQVNL-TDDVKTKVRAMSGGMRRRL 142
Cdd:PRK10982 326 alvteERRSTGIYAYLDIGFnSLISNIR-----NYKNKVGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKV 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 143 GIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETA-KDRIVILSTHIVGDVEATCEDIAVLNRGCV 210
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-165 |
7.58e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 32 FGLLGPNGAGKTTLMKIIATLLQKTEGDIHvcginID-NDReirkiIGYLPQDFSMYGNMSVYEAmdylgVLSGLSG--- 107
Cdd:PRK15064 30 YGLIGANGCGKSTFMKILGGDLEPSAGNVS-----LDpNER-----LGKLRQDQFAFEEFTVLDT-----VIMGHTElwe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 108 -PARKERIPSLLEqvnLTDDVKTKV-----------------RA-----------------MSG---GMRRRLGIAQALL 149
Cdd:PRK15064 95 vKQERDRIYALPE---MSEEDGMKVadlevkfaemdgytaeaRAgelllgvgipeeqhyglMSEvapGWKLRVLLAQALF 171
|
170
....*....|....*.
gi 517427119 150 HDPKVLIVDEPTAGLD 165
Cdd:PRK15064 172 SNPDILLLDEPTNNLD 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-219 |
7.68e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQ----ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIH------------VCGINI 67
Cdd:PRK10261 13 LAVENLNIAFMQEQqkiaAVRNLSFSLQRGeTLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqVIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 68 DNDREIRKIIGylpQDFSMYgnmsVYEAMDYLGVL--------------SGLSGPARKERIPSLLEQVNLTDDVKTKVR- 132
Cdd:PRK10261 93 QSAAQMRHVRG---ADMAMI----FQEPMTSLNPVftvgeqiaesirlhQGASREEAMVEAKRMLDQVRIPEAQTILSRy 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 133 --AMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRI--VILSTHIVGDVEATCEDIAVLNRG 208
Cdd:PRK10261 166 phQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQG 245
|
250
....*....|.
gi 517427119 209 CVLFQGTVTEL 219
Cdd:PRK10261 246 EAVETGSVEQI 256
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
3-190 |
8.64e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 52.28 E-value: 8.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 3 TKIVIKNLsKTYgKKQALKHVDLTIhkgmfgLLGPNGAGKTTLMKIIATLLQktegdIHVcgINIDNDRE-IRKIIGYLP 81
Cdd:COG4938 2 KSISIKNF-GPF-KEAELELKPLTL------LIGPNGSGKSTLIQALLLLLQ-----SNF--IYLPAERSgPARLYPSLV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 QDFSMYGNMSVYeAMDYLGVLSGLSGPARKEriPSLLEQVN---------------LTDDVKTKVRAMSGGMRRRL---- 142
Cdd:COG4938 67 RELSDLGSRGEY-TADFLAELENLEILDDKS--KELLEQVEewlekifpgkvevdaSSDLVRLVFRPSGNGKRIPLsnvg 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 143 -GIAQ------ALLHDPK---VLIVDEPTAGLDPEERVRFRNLLSETAKDRI-VILSTH 190
Cdd:COG4938 144 sGVSEllpillALLSAAKpgsLLIIEEPEAHLHPKAQSALAELLAELANSGVqVIIETH 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-187 |
1.04e-07 |
|
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: 52.90 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 23 VDLTIHKG-MFGLLGPNGAGKTTLMK-IIATLLQKTEGDIHVCG--INIDN-DREIRKIIGYLPQDFSMYGNMSVyeamd 97
Cdd:TIGR02633 279 VSFSLRRGeILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGkpVDIRNpAQAIRAGIAMVPEDRKRHGIVPI----- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 98 yLGV-----LSGLSGPARKERIPSLLEQVNLTDDVKT-KVRA---------MSGGMRRRLGIAQALLHDPKVLIVDEPTA 162
Cdd:TIGR02633 354 -LGVgknitLSVLKSFCFKMRIDAAAELQIIGSAIQRlKVKTaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180
....*....|....*....|....*
gi 517427119 163 GLDPEERVRFRNLLSETAKDRIVIL 187
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAII 457
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-220 |
1.11e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 33 GLLGPNGAGKTTLMKIIATLLQKTEGDIHV--CGINIDNDREIRKIIGYLPQDFSMYG-----NMSVYEAMDYLGVLSGL 105
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIddCDVAKFGLTDLRRVLSIIPQSPVLFSgtvrfNIDPFSEHNDADLWEAL 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 106 SGPARKERIPSllEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDpeerVRFRNLLSETAKDRIV 185
Cdd:PLN03232 1346 ERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD----VRTDSLIQRTIREEFK 1419
|
170 180 190
....*....|....*....|....*....|....*...
gi 517427119 186 ILSTHIVGDVEAT---CEDIAVLNRGCVLFQGTVTELL 220
Cdd:PLN03232 1420 SCTMLVIAHRLNTiidCDKILVLSSGQVLEYDSPQELL 1457
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-236 |
1.37e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.75 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 20 LKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQ--------KTEGDIHVCG---INIDNDREIRkIIGYLPQDFSMY 87
Cdd:PRK13547 17 LRDLSLRIEPGrVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGeplAAIDAPRLAR-LRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 88 GNMSVYEAMdYLGVL-----SGLSGPARKERIPSLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQAL--LH-------DPK 153
Cdd:PRK13547 96 FAFSAREIV-LLGRYpharrAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqLWpphdaaqPPR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 154 VLIVDEPTAGLDPEERVRFRNLLSETAKD-RIVILSthIVGDVEAT---CEDIAVLNRGCVLFQGTVTELLEEA-AGRIY 228
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLA--IVHDPNLAarhADRIAMLADGAIVAHGAPADVLTPAhIARCY 252
|
....*...
gi 517427119 229 SAQVSRME 236
Cdd:PRK13547 253 GFAVRLVD 260
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-221 |
1.83e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 21 KHVDLTIHKGMFG---------LLGPNGAGKTTLMKIIATLLQ---KTEGDIHVCGINIdNDREIRKIIGYLPQDFSMYG 88
Cdd:PLN03140 174 KKTKLTILKDASGiikpsrmtlLLGPPSSGKTTLLLALAGKLDpslKVSGEITYNGYRL-NEFVPRKTSAYISQNDVHVG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 89 NMSVYEAMDYLGVLSG-------LSGPARKERIPSLLEQV----------------NLTDDVKTKV-------------- 131
Cdd:PLN03140 253 VMTVKETLDFSARCQGvgtrydlLSELARREKDAGIFPEAevdlfmkatamegvksSLITDYTLKIlgldickdtivgde 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 132 --RAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDpeervrfrnllSETAKdRIVILSTHIVGDVEATC---------- 199
Cdd:PLN03140 333 miRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLD-----------SSTTY-QIVKCLQQIVHLTEATVlmsllqpape 400
|
250 260
....*....|....*....|....*..
gi 517427119 200 -----EDIAVLNRGCVLFQGTVTELLE 221
Cdd:PLN03140 401 tfdlfDDIILLSEGQIVYQGPRDHILE 427
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
124-190 |
2.43e-07 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 51.24 E-value: 2.43e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517427119 124 TDDVKTKVRAMSGGMRRRLGIAQALLHDPK---VLIVDEPTAGLDPEERVRFRNLLSETAKDRI-VILSTH 190
Cdd:pfam13304 227 GGGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-220 |
3.57e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHV----DLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQK-----TEGDIHVCGINI--DNDREIR 74
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVvndvSLQIEAGeTLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLlhASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 75 KIigylpqdfsmYGN---MSVYEAMDYLG-----------VLS---GLSGPARKERIPSLLEQVNLTDdVKTKVRA---- 133
Cdd:PRK15134 88 GV----------RGNkiaMIFQEPMVSLNplhtlekqlyeVLSlhrGMRREAARGEILNCLDRVGIRQ-AAKRLTDyphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 134 MSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAK--DRIVILSTHIVGDVEATCEDIAVLNRGCVL 211
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
....*....
gi 517427119 212 FQGTVTELL 220
Cdd:PRK15134 237 EQNRAATLF 245
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
10-186 |
1.02e-06 |
|
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: 47.95 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 10 LSKTYGKKQALKHVDLTIHKGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINidndreirkiIGYLPQDFSmygn 89
Cdd:cd03222 6 CVKRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT----------PVYKPQYID---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 90 msvyeamdylgvlsglsgparkeripslleqvnltddvktkvraMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEER 169
Cdd:cd03222 72 --------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR 107
|
170 180
....*....|....*....|.
gi 517427119 170 VR----FRNLLSETAKDRIVI 186
Cdd:cd03222 108 LNaaraIRRLSEEGKKTALVV 128
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-165 |
1.03e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIAtlLQKTEG------DIHV-------------CG 64
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRhYGLVGRNGTGKTTFLRYMA--MHAIDGipkncqILHVeqevvgddttalqCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 65 INIDNDR------EIRKIIGYLPQDFSMYGNMSvyeAMDYLGVLSGLSGPARKERIPSLLEQVN---------------- 122
Cdd:PLN03073 256 LNTDIERtqlleeEAQLVAQQRELEFETETGKG---KGANKDGVDKDAVSQRLEEIYKRLELIDaytaearaasilagls 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517427119 123 LTDDVKTK-VRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:PLN03073 333 FTPEMQVKaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-221 |
1.46e-06 |
|
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: 49.56 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTYGKKQ--ALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGInidndreirkiIGYLP 81
Cdd:TIGR00957 637 ITVHNATFTWARDLppTLNGITFSIPEGaLVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------VAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 82 QDfSMYGNMSVYEamdylGVLSGlsGPARKERIPSLLEQVNLTDDVKT-----------KVRAMSGGMRRRLGIAQALLH 150
Cdd:TIGR00957 706 QQ-AWIQNDSLRE-----NILFG--KALNEKYYQQVLEACALLPDLEIlpsgdrteigeKGVNLSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517427119 151 DPKVLIVDEPTAGLDPE-ERVRFRNLLSETA--KDRIVILSTHIVGDVEATcEDIAVLNRGCVLFQGTVTELLE 221
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHvGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-225 |
1.82e-06 |
|
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: 48.37 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 4 KIVIKNLSKTYGK--KQALKHVDLTIHKGM-FGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDN--DREIRKIIG 78
Cdd:cd03288 19 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQkVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlpLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 79 YLPQDFSMYGNmSVYEAMDylgvlsglsgPARKERIPSLLEQVNLTdDVKTKVRAMSGGM---------------RRRLG 143
Cdd:cd03288 99 IILQDPILFSG-SIRFNLD----------PECKCTDDRLWEALEIA-QLKNMVKSLPGGLdavvteggenfsvgqRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 144 IAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTHIVGDVeATCEDIAVLNRGCVLFQGTVTELLEEA 223
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENLLAQE 245
|
..
gi 517427119 224 AG 225
Cdd:cd03288 246 DG 247
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-190 |
2.42e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 47.33 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 20 LKHVDLTIHKGMFGLL-GPNGAGKTTLMKIIATLLQKTEGDIHVCGIN------IDNDREIRKIIGYLPQDfSMYGNMSV 92
Cdd:cd03290 17 LSNINIRIPTGQLTMIvGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsfEATRSRNRYSVAYAAQK-PWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 93 YEAMDYlgvlsglSGPARKERIPSLLEQVNLTDDV-------KTKVRA----MSGGMRRRLGIAQALLHDPKVLIVDEPT 161
Cdd:cd03290 96 EENITF-------GSPFNKQRYKAVTDACSLQPDIdllpfgdQTEIGErginLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|..
gi 517427119 162 AGLDPE--ERVRFRNLLSETAKD-RIVILSTH 190
Cdd:cd03290 169 SALDIHlsDHLMQEGILKFLQDDkRTLVLVTH 200
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-220 |
2.72e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 33 GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND--REIRKIIGYLPQD--------------FSMYGNMSVYEAm 96
Cdd:PLN03130 1269 GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFglMDLRKVLGIIPQApvlfsgtvrfnldpFNEHNDADLWES- 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 97 dylgvlsglsgparkeripslLEQVNLTDDVKTKVRAM-----------SGGMRRRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:PLN03130 1348 ---------------------LERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517427119 166 peerVRFRNLLSETAKDR------IVI---LSTHIvgdveaTCEDIAVLNRGCVLFQGTVTELL 220
Cdd:PLN03130 1407 ----VRTDALIQKTIREEfksctmLIIahrLNTII------DCDRILVLDAGRVVEFDTPENLL 1460
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-187 |
4.15e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 23 VDLTIHKG-MFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG--INIDNDRE-IRKIIGYLPQDFSMYG---------- 88
Cdd:PRK11288 272 ISFSVRAGeIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDaIRAGIMLCPEDRKAEGiipvhsvadn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 89 -NMSVYEAMDYLGVLsgLSGPARKERIPSLLEQVNL-TDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDP 166
Cdd:PRK11288 352 iNISARRHHLRAGCL--INNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180
....*....|....*....|.
gi 517427119 167 EERVRFRNLLSETAKDRIVIL 187
Cdd:PRK11288 430 GAKHEIYNVIYELAAQGVAVL 450
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-191 |
1.15e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 3 TKIVIKNLsKTYGKKQalkHVDLTihKGMFGLLGPNGAGKTTLMKIIATLL---QKTEGDIHVCGINIDNDR-------- 71
Cdd:COG0419 3 LRLRLENF-RSYRDTE---TIDFD--DGLNLIVGPNGAGKSTILEAIRYALygkARSRSKLRSDLINVGSEEasvelefe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 72 -------------EIRKIIGYLPQD-----FSMYGNMSVYEAMDYLGVLsglsgparKERIPSLLEQVNLTDDVKTK--- 130
Cdd:COG0419 77 hggkryrierrqgEFAEFLEAKPSErkealKRLLGLEIYEELKERLKEL--------EEALESALEELAELQKLKQEila 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517427119 131 -------VRAMSGGMRRRLGIAQALlhdpkVLIVDepTAGLDPEERVRFRNLLsetakDRIVILSTHI 191
Cdd:COG0419 149 qlsgldpIETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDAL-----EELAIITHVI 204
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
24-190 |
2.40e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 24 DLTIHKGMFGLL-GPNGAGKTTLMKiiATLLqktegdihVCGINIDNDREirkiigylpqdfsmygnmsvyeamdYLGVL 102
Cdd:cd03227 15 DVTFGEGSLTIItGPNGSGKSTILD--AIGL--------ALGGAQSATRR-------------------------RSGVK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 103 SGLSGPARKERIPSLLEQvnltddvktkvraMSGGMRRRLGIAQAL---LHDPKVL-IVDEPTAGLDPEERVRFRNLLSE 178
Cdd:cd03227 60 AGCIVAAVSAELIFTRLQ-------------LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAILE 126
|
170
....*....|...
gi 517427119 179 TA-KDRIVILSTH 190
Cdd:cd03227 127 HLvKGAQVIVITH 139
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-165 |
2.40e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 7 IKNLSKTYGKKQALKHVDLTIHKG-MFGLLGPNGAGKTTLMKIIATL--LQKTEGDIHVCGinidndreiRKIIGYLPQD 83
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGeVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKG---------KDLLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 84 FSMYGnmsVYEAMDYLGVLSGLSG---------PARKERIPSLLEQVNLTDDVKTKVRAM---------------SGGMR 139
Cdd:PRK09580 75 RAGEG---IFMAFQYPVEIPGVSNqfflqtalnAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEK 151
|
170 180
....*....|....*....|....*.
gi 517427119 140 RRLGIAQALLHDPKVLIVDEPTAGLD 165
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLD 177
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
101-223 |
2.40e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 101 VLSGLSGPARKERipsLLEQVNLTDDVKTKVRAMSGGMRRRLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETA 180
Cdd:PRK10938 106 IQDEVKDPARCEQ---LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH 182
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 517427119 181 KDRI-VILSTHIVGDVEATCEDIAVLNRGCVLFQGTVTELLEEA 223
Cdd:PRK10938 183 QSGItLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQA 226
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-207 |
1.06e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 43.06 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 3 TKIVIKNLsktYGKKQAlkHVDLTIHKGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVCG-----INIDNDREIRKII 77
Cdd:COG3950 4 KSLTIENF---RGFEDL--EIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKfrkllIRNGEFGDSAKLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 78 GYLPQ-------DFSMYGNMSVYEAMDYLGVLSGLSGPAR-------------------KERIPSLLEQVN--------- 122
Cdd:COG3950 79 LYYGTsrllldgPLKKLERLKEEYFSRLDGYDSLLDEDSNlreflewlreyledlenklSDELDEKLEAVRealnkllpd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 123 ----------------LTDDVKTKVRAMSGGMRRRLGIA--------------QALLHDPKVLIVDEPTAGLDPEERVRF 172
Cdd:COG3950 159 fkdiridrdpgrlvilDKNGEELPLNQLSDGERSLLALVgdlarrlaelnpalENPLEGEGIVLIDEIDLHLHPKWQRRI 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 517427119 173 RNLLSETAKDRIVILSTH---IVGDVEAtcEDIAVLNR 207
Cdd:COG3950 239 LPDLRKIFPNIQFIVTTHsplILSSLED--EEVIVLER 274
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
132-190 |
1.61e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.61 E-value: 1.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517427119 132 RAMSGGMRRRLGIAqALLHDPK---VLIVDEPTAGLDPEERVRFRNLLSETAKDRIVILSTH 190
Cdd:COG4637 257 RELSDGTLRFLALL-AALLSPRpppLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTH 317
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
133-190 |
5.32e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 5.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 133 AMSGGMRR------RLGIAQALLHDPKVLIVDEPTAGLDPEERVRFRNLLSETAKD-----RIVILSTH 190
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDssdipQVIMISHH 869
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-232 |
5.85e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 33 GLLGPNGAGKTTLMKIIATLLQKTEGDIHVCGINIDND--REIRKIIGYLPQD--------------FSMYGNMSVYEAM 96
Cdd:PTZ00243 1340 GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYglRELRRQFSMIPQDpvlfdgtvrqnvdpFLEASSAEVWAAL 1419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 97 DYLGVlsglsgparKERIPSllEQVNLTDDVKTKVRAMSGGMRRRLGIAQALL-HDPKVLIVDEPTAGLDPEERVRFRNL 175
Cdd:PTZ00243 1420 ELVGL---------RERVAS--ESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQAT 1488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517427119 176 LSETAKDRIVILSTHIVGDVeATCEDIAVLNRGCVLFQGTVTELLE----------EAAGRIYSAQV 232
Cdd:PTZ00243 1489 VMSAFSAYTVITIAHRLHTV-AQYDKIIVMDHGAVAEMGSPRELVMnrqsifhsmvEALGRSEAKRF 1554
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-227 |
6.21e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLSKTY---GKKQALKHVDLTIHKGMF-GLLGPNGAGKTTLMKIIATLLQKTEGDIHVcginidndreIRKIIGYL 80
Cdd:PLN03130 615 ISIKNGYFSWdskAERPTLSNINLDVPVGSLvAIVGSTGEGKTSLISAMLGELPPRSDASVV----------IRGTVAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 81 PQdFSMYGNMSVYEamdylGVLSGLS-GPARKERIP---------SLLEQVNLTDDVKTKVRaMSGGMRRRLGIAQALLH 150
Cdd:PLN03130 685 PQ-VSWIFNATVRD-----NILFGSPfDPERYERAIdvtalqhdlDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 151 DPKVLIVDEPTAGLDPE-ERVRFRNLLSETAKDRIVILST---HIVGDVEAtcedIAVLNRGCVLFQGTVTEL------- 219
Cdd:PLN03130 758 NSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTnqlHFLSQVDR----IILVHEGMIKEEGTYEELsnngplf 833
|
250
....*....|
gi 517427119 220 --LEEAAGRI 227
Cdd:PLN03130 834 qkLMENAGKM 843
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
5-77 |
7.99e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.79 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 5 IVIKNLsktygkkQALKHVDLTIHKGMFGLLGPNGAGKTTLMKIIATLL--------QKTEGDIHVCGINIDNDREIRKI 76
Cdd:pfam13476 1 LTIENF-------RSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALygktsrlkRKSGGGFVKGDIRIGLEGKGKAY 73
|
.
gi 517427119 77 I 77
Cdd:pfam13476 74 V 74
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
22-80 |
8.08e-04 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 40.70 E-value: 8.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 517427119 22 HVDLTihKGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVcginIDNDREIRKIIGYL 80
Cdd:COG3451 199 HDGLD--NGNTLILGPSGSGKSFLLKLLLLQLLRYGARIVI----FDPGGSYEILVRAL 251
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-190 |
1.63e-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: 38.74 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 3 TKIVIKNLSKTYgkkqalKHVDLTIHKGMFGLLGPNGAGKTTlmkIIATLLQKTEGDIHVCGINIDNDRE-IRK--IIGY 79
Cdd:cd03240 2 DKLSIRNIRSFH------ERSEIEFFSPLTLIVGQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPKlIREgeVRAQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 80 LPQDFSMY--GNMSVYEAMD-YLGVLSglsgpARKERIPSLLEQvnltddvktKVRAMSGGMRR------RLGIAQALLH 150
Cdd:cd03240 73 VKLAFENAngKKYTITRSLAiLENVIF-----CHQGESNWPLLD---------MRGRCSGGEKVlasliiRLALAETFGS 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517427119 151 DPKVLIVDEPTAGLDPEER-VRFRNLLSETAKDRI--VILSTH 190
Cdd:cd03240 139 NCGILALDEPTTNLDEENIeESLAEIIEERKSQKNfqLIVITH 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-165 |
2.75e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 17 KQALKHVDLTIHKG-MFGLLGPNGAGKTTL-MKIIA-TLLQKTEGDIHVCGINIDN---DREIRKIIGYLPQDFSMYG-- 88
Cdd:NF040905 273 RKVVDDVSLNVRRGeIVGIAGLMGAGRTELaMSVFGrSYGRNISGTVFKDGKEVDVstvSDAIDAGLAYVTEDRKGYGln 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517427119 89 -------NMSvyeamdylgvLSGLSGPARKERIPSLLE---------QVNL-TDDVKTKVRAMSGGMRRRLGIAQALLHD 151
Cdd:NF040905 353 liddikrNIT----------LANLGKVSRRGVIDENEEikvaeeyrkKMNIkTPSVFQKVGNLSGGNQQKVVLSKWLFTD 422
|
170
....*....|....
gi 517427119 152 PKVLIVDEPTAGLD 165
Cdd:NF040905 423 PDVLILDEPTRGID 436
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
29-53 |
4.06e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 4.06e-03
|
| AAA_30 |
pfam13604 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
15-63 |
4.20e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.
Pssm-ID: 433343 [Multi-domain] Cd Length: 191 Bit Score: 37.54 E-value: 4.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 517427119 15 GKKQALKHVdLTIHKGMFGLLGPNGAGKTTLMKIIATLLQKTEGDIHVC 63
Cdd:pfam13604 5 EQAAAVRAL-LTSGDRVAVLVGPAGTGKTTALKALREAWEAAGYRVIGL 52
|
|
| |
